UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
|---|---|---|
Q9P1Y1 | MNITNCTTEASMAIRPKTITEKMLICMTLVVITTLTTLLNLAVIMAIGTTKKLHQPANYLICSLAVTDLLVAVLVMPLSIIYIVMDRWKLGYFLCEVWLSVDMTCCTCSILHLCVIALDRYWAITNAIEYARKRTAKRAALMILTVWTISIFISMPPLFWRSHRRLSPPPSQCTIQHDHVIYTIYSTLGAFYIPLTLILILYYRIYHAAKSLYQKRGSSRHLSNRSTDSQNSFASCKLTQTFCVSDFSTSDPTTEFEKFHASIRIPPFDNDLDHPGERQQISSTRERKAARILGLILGAFILSWLPFFIKELIVGLSIYT... | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, su... |
Q9N2B6 | MNITNCTTEASMAIRPKTITEKMLICMTLVVITTLTTLLNLAVIMAIGTTKKLHQPANYLICSLAVTDLLVAVLVMPLSIIYIVMDRWKLGYFLCEVWLSVDMTCCTCSILHLCVIALDRYWAITNAIEYARKRTAKRAALMILTVWTISIFISMPPLFWRSHRRLSPPPSQCTIQHDHVIYTIYSTLGAFYIPLTLILILYYRIYHAAKSLYQKRGSSRHLSNRSTDSQNSFASCKLTQTFCVSDFSTSDPTTEFEKFHASIRIPPFDNDLDHPGERQQISSTRERKAARILGLILGAFILSWLPFFIKELIVGLSIYT... | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, su... |
Q29003 | HQPANYLICSLAVTDLLVAVLVMPLSIMYIVMDSWRLGYFICEVWLSVDMTCCTCSILHLCVIALDRYWAITNAIEYARKRTAKRAGLMILTVWTISIFISMPPLFWRSHRQLSPPPSQCAIQHDHVIYTIYSTLGAFYIPLTLILILY | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, su... |
O08890 | MDFLNSSDQNLTSEELLHRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVLCDIWLSVDIICCTCSILHLSAIALDRYRAITDAVEYARKRTPKQAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLVLILILYYKIYKAAKTLYHKRQASRIAKEELNGQVLLESGEKSIKMVSTTYVPEKSLSDPSTDFDKIHNTVKSPRCKLRHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCE... | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, su... |
P30939 | MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCD... | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, su... |
Q02284 | MDFLNASDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVLCDIWLSVDIICCTCSILHLSAIALDRYRAITDAVEYARKRTPRHAGIMITIVWVISVFISMPPLFWRHQGTSRDDECVIKHDHIVSTIYSTFGAFYIPLVLILILYYKIYRAARTLYHKRQASRMIKEELNGQVFLESGEKSIKLVSTSYMLEKSLSDPSTDFDRIHSTVKSPRSELKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCE... | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, su... |
P70715 | MNYITFPTAQHAVEKIAQEFVIYSQLNHPAHISLSGGSTPKLLFKTLAQSPYAEQINWRNLHFWWGDDRMVSPSDPESNYGEVQKLLFDHIQIPAENIHRIRGENEPHFELKRFQAELSAVISDGVFDWIILGMGADGHTSSLFPHQTNFDDENLAVIAKHPESGQIRISKTAKLIEQAKRITYLVTGEGKAEILKEIQSTPAENLPYPAAKIYAKNGVTEWYLDKDAAKLL | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the glucosamine/galactosamine-6-phosphate isome... |
D4B0N9 | MKTVPFLSLLQAGILTSGIVAQNIAFVGSNANAIATVSFDTKTGTFKVTGNNTDSSTPSWQEVSRDGKLLYSIEETSTEHALTSYSIGQDGKLKKLKSIKGLAGPVSLDMHPTQPIIITANYGSASASAYSSKDNGELTHLGDFMFKMQGKGKVPDRQDAPHPHQALFDPTGKFVLMPDLGSDLIRILKVDAGQKFSVAPPNKVKPGTGPRHGVLYPASDKPRFYYVVGELSNTVTAMSVEYTVETIKLTEIQTLSTLPDGQRGAAGELILSPSGKHLYASNRLDKVFPGSSSVASYTIDQMTGKLKLLEIFNGGVENIR... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
O34499 | MTKYIGYVGTYTKGGSEGIYSFELDTEKKALSEPKLAAKLGNPTYVATNKNNTILYSIEKADGQGGVAAYQIDKNSGELTFLNHQLIDGPSPCHVSVDDQNQFVLTANYHSGKVHVFPVQEDGSLQSPVSEAAHTGKGPHERQEKPHTHYAGFTPEHNYVVAVDLGIDKLYTYKLKDGVLTESGSHSFAPGAGPRHIAFHPKEKYAYVMTELSNEVIALEYNPTAGEFREIQVVSAIPDDFTDNSQGSAIHVTQDGRFVYVANRGHDSIAVFEVNQYSGELAFVERVSTEGNWPRDFVFDPTEGFLVASNEETGNLVLFE... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
Q7VR81 | MQIFYISSPDNQKIYVWKLDNHQEKLELMQVVSTDGCAQPTVVHPNQNFLYVGIRPDFKIDTYRISQNGLLTKIQSTKICDSPTYLTINIYGTFIYCVSYNFNCINVIKIDKFGLLCNSIQIIKNMLGCHSANINKDRKVLWAPCLQENTIRLFDIDHLYGTLKPHNPHVINTNMQSGPRHMAFHSTDNYAYVINEYNGVIDVIQYNDSITNLAIIQKINILSNHGLDTKKFWSSDIHITPNNRWLYCADRFCNTISLFEILLNTKKLKFINYIYTEDQPRGFLIDSTGNFLIVAGQKSHFITLYRIHANNGNLSVISRH... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
Q492W6 | MIQIIYVASPESQQIHVWKLDSIYGLLELIQVIYTHGQAQPMAVHPNKRFLYVGIRPNFGITTYRIDQIGLLADHGTIGIFSSPTHLISDKKGAFLYCTSYRNNTVSVIPISMSGMLLDSPIQIIEGLLGCHSANIDKFKKLLWVPCLKENAIRLFNINSFGMLTSYDPSIIKINVGSGPRHMIFCDFDCYAYVINELTSTVDVIKYNNFQKIPSIVQTVSIIPKNISINRCWAADIHITPNGRWLYCTDRSINIISCLEISKKTKKLKFVGYQLTEEQPRGFAIDYQGKFLVVAGQKSNCISLYKIDSDNGTLTMLSRY... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
O51240 | MEFLYSDEENYLKDRFFDFFNMNVDKDKYTSIGICGGRSIVNFLSVFLKQNFSFRRSHFFLVDERCVPLNDENSNYNLLNKNFFSKMVDKNLISISKFHAFVYSEIDEATAIHDYNIEFNSRFNIFDFIIVSVGEDGHIASLFPSRKLLFSDVEGYQYEYNSPKFPSKRISLTPKSLFGSKAVVLLFMGVDKKCALENFLASNSSINECPARLLKEHPNLLVLTNIKRDESYAGS | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the glucosamine/galactosamine-6-phosphate isome... |
Q2TBQ8 | MAAPAPRLISVFSSPQELGASLAQLVVQQAACCLADAGARFTLGLSGGSLVSMLARELPAAAAPAGPASLARWTLGFCDERLVPFEHAESTYGLYRTHLLSKLPIFDSQVITINPALPVEEAAEDYAKKLRQAFQGDSIPVFDLLILGVGPDGHTCSLFPDHPLLQEREKIVAPISDSPKPPPQRVTLTLPVLNAARTVIYVATGEGKAAILKRILEDKEENPLPAALVQPSAGKLCWFLDEAAARLLTVPFEKHSTL | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the glucosamine/galactosamine-6-phosphate isome... |
B8D985 | MKQVVYIANSESKNIEVWNLCKSGKMNLIQKIETDGKIQPINIIQKRNLLYAGIFPDNKIITYSINHNGFLEKKNESNIPGKANYISFDKKKEFLFCSSYHSNFISVSPLNKFGIPQNPIQIIYNIEGCHAAKMNYKYNILFVISLKEDCIYLYYLTDFGILKSTEQNILHTQKKSGPRHIIFHPNQDFVYTINELNGTIDVWKIYKKNNVIKVKNIQNIHVLKNRFLKDYWCSDIHITSCGRFLYACDRFFNIISLFHINQNDNKLVFFKSYDTEEQPRSFNINSHNTHLIVAGEKSNTFIIYSISNSTGELKKINVYS... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
P57380 | MKQVVYIANSESKNIEVWNLCKSGKMNLIQKIETDGKIQPINIIQKRNLLYAGIFPDNKIITYSINHNGFLEKKNESNIPGKANYISFDKKKEFLFCSSYHSNFISVSPLNKFGIPQNPIQIIYNIEGCHAAKMNYKYNILFVISLKEDCIYLYYLTDFGILKSTEQNILHTQKKSGPRHIIFHPNQDFIYTINELNGTIDVWKIYKKNNVIKVKNIQNIHVLKNRFLKDYWCSDIHITSCGRFLYACDRFFNIISLFHINQNDNKLVFFKSYDTEEQPRSFNINSHNTHLIVAGEKSNTFIIYSISNSTGELKKINVYS... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
Q8K9N9 | MQQIIYIANAESENIEVWILYNNGDMKLIQTVQTDGQVQPISIIKNTKLLYAGIRPKNRVITYQIDKNGLLKKKKESIVPGTPNYISFDSSEKFLFCSSYHADCISVSPLDKNGIPKDPIQIIHNIEGCHAAKFNSKYNVLFITSLKNDCIYLYYLTHFGILKSTEQKLVFSQKNSGPRHVIFHPNQNFSYTVNELNGSVDVWKISKENKVLEVKNIQNIKLLNDLISKKYWSSDIHLTSCGNFLYVSDRYLNSISLFHVNKNDNTIIFFKQYLTEEQPRAFCIDRNNNYLIVIGQKSNKLSVYKICQKTGELKKINQYQ... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
B8D7I7 | MKQVVYIANSESKNIEVWNLCKSGKMNLIQKIETDGKIQPINIIQKRNLLYAGIFPDNKIITYSINHNGFLEKKNESNIPGKANYISFDKKKEFLFCSSYHSNFISVSPLNKFGIPQNPIQIIYNIEGCHAAKMNYKYNILFVISLKEDCIYLYYLTDFGILKSTEQNILHTQKKSGPRHIIFHPNQDFIYTINELNGTIDVWKIYKKNNVIKVKNIQNIHVLKNRFLKDYWCSDIHITSCGRFLYACDRFFNIISLFHINQNDNKLVFFKSYDTEEQPRSFNINSHNTHLIVAGEKSNTFIIYGISNSTGELKKINVYS... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
Q89AK3 | MKQIIYITLAKNQEIEVWKLHDDFSLNLLQRISTQGEPQPIIISKDKKYLYIGVRPKFKVYSYKIKADGTLTKHACSTLPGSPNHFEIDHTGKYLFSSSYHFNCLSITPLDTLGIPRPVTQTIKNIFGCHASKMNCYNTCLFISALKKDCIYAYNFKKNGKLLKNTRKNFMTNVNFGPRHLDLQKCNNRLYSVNELNGSVDIWSINSFSNELILLKNINIMSKNYCNAAWSSDLHISPCEKFLYVSDRIENTISIIKLEKDVQNIEKIGHIKTELQPRTFSINSTGENLIVVGEKSNSFSVYKISKITGLLELKNTYSTG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
Q2EEL9 | MCLVNEFVSNSNMKPALNVSGDEKELILQLRRYLEEKLTYLLDQNGTVSIGVSGGSMPRVFSKAILSLPQEQLNWKRIRIFMVDERNVDLDSEESNQGEYLRLFPNELRDVFVPMQIFKDPCLTAQHYEISLRKYLLPEQLNNTARFDILFLGVGPDGHTASIFPGKERLEKITELNWVSVITDSPKPPPSRITLTLQTLQHAKNVAFIICGKQKAEIVRGICDRDQKYPAAQARPFNDKLTLFLDEDAATGVPDRDSSDSDSPPPFDG | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Localizes to the nucleus of germ cells. Belongs to the glu... |
Q9A6N1 | MPFTPIKLEAFGSREDLYDAAASVLVGALTTAVARHGRVGFAATGGTTPAPVYDRMATMTAPWDKVTVTLTDERFVPATDASSNEGLVRRHLLVGEAAKASFAPLFFDGVSHDESARKAEAGVNAATPFGVVLLGVGPDGHFASLFPGNPMLDQGLDLATDRSVLAVPPSDPAPDLPRLSLTLAALTRTDLIVLLVTGAAKKALLDGDVDPALPVAAILKQDRAKVRILWAE | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the glucosamine/galactosamine-6-phosphate isome... |
Q9PKK7 | MATLISLNDANRMLIAESQEDFLQIACYDWISTANKAIQKRGAFYVALSGGKTPLQIFQEIVKKRAAISDCSKIFVFWGDERASEDTEAGSNYLKAMDILKWLRIPDTQIFRMDTANPKGDEIYENLIREHVPDTIFDMVMLGVGEDGHTLSLFPGTAALEEKDRLVVFNEVPQLQTRRMTLTFPIVRQARHLVAYIQGTAKQDLCHKLLHPLGRDTFPIERVGTPLNPLQWVLSSDCCRAADLADIPAECKLEMF | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the glucosamine/galactosamine-6-phosphate isome... |
Q9K256 | MATLINFNDTNKLLLTKQPSLFIDLASKDWIASANQAIKQRGAFYVALSGGKTPLEIYKDIVINKDKLIDPSKIFLFWGDERLAPITSSESNYGQAMSILRDLNIPDEQIFRMETENPDGAKKYQELIENKIPDASFDMIMLGLGEDGHTLSLFSNTSALEEENDLVVFNSVPHLETERMTLTFPCVHKGKHVVVYVQGENKKPILKSVFFSEGREEKLYPIERVGRDRSPLFWIISPESYDIADFDNISSIYKMDIL | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the glucosamine/galactosamine-6-phosphate isome... |
O84189 | MATLISLNDANRMLIADSQEEFLQIACYDWISTANKAIHKRGAFYVALSGGKTPLQIFQEIVKKRAAISDCSKIVVFWGDERANEDVEAGSNYLKAMDILKGLRIPEDQIFRMDTADPKGDEAYEALIQKYVPDAIFDMVMLGVGEDGHTLSLFPETHALEEKERFVVFNEVPQLHTRRMTLTFPIVRQARHLVAYVQGENKQDLFHKLVHPLGRDTFPIERVGTPLNPVQWVLSSDSCRKTDLADIPADCKLEMF | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the glucosamine/galactosamine-6-phosphate isome... |
A8AJ27 | MKQTVYTASPESQQIHVWSLNHDGSLKLVQVVDVPGQVQPMVVSPDKRYLYVGVRPEFRVLAYRIAPDDGALTFAAESALPGSPTHISTDHQGRFVFVGSYNAGNVSVTRLDDGLPAGVVDVVEGLEGCHSANISPDNRTLWVPALKQDRICLFTLSDDGKLVAQEPAEVTTVEGAGPRHMAFHPNQQYAYCVNELNSSVDVWELKDPHGNIECVQTLDMMPADFSDTRWAADIHITPDGRHLYACDRTASLITVFSVSEDGSVLTKEGFQPTETQPRGFNVDHSGKYLIAAGQKSHHIAVYAIAGEQGLLTEKGRYAVG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
A7MIZ2 | MKQTVYTASPESQQIHVWRLEPQGTLTLLQVVDAPGQVQPMVISPDKRFLYVGVRPEFRVIAYRIAAHDGTLSEAGEAPLPGSPTHISTDHTGRFLFSGSYNAGSVSVVRLNDGLPGETVTVVEGLEGCHSANISPDNRTLWVPALKQDRICLFTLTDDGHLEPQTPAEVTTVAGAGPRHMVFHPSKPFAYCVNELNSSVDVWALSDPHGNIECVQTLDMMPADFSDTRWAADIHITPDGRHLYACDRTASVITVFTVSEDGSVLAVQGHQPTETQPRGFNIDNSGQYLIAAGQKSHHIAVYGIEGEQGLLAEKGRYAVG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
Q54CJ3 | MTSKLINFITIEKERFEDECVKFIKNVITDSINSRNIATIGLSGGSTPKPIYEMLGNDSSIDWTKVYFFAVDERYIDKSSKDSIYDLISKSVFKNRENLLVDHFITPNTSLPLKECIETYSNDLKKLIEKSNGSPDLVTLGMGEDGHIASIFPNSPKSPLDETDLVYHTTTERFAIFDRITTNINFLASSKNKVFFMSGSSKKKVWDEMESSQINVSRWPAHKIISSGNTNVFYRE | Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the glucosamine/galactosamine-6-phosphate isome... |
Q1C949 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
B2K8S8 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSKDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
Q7CH64 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
C4GWM3 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
A4TNQ8 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
Q66D69 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSKDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
B1JSS6 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSKDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVG... | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
B4FHI9 | MAANGGDHTSARPHVVLLPSAGMGHLVPFARLAVALSEGHGCNVSVAAVQPTVSSAESRLLDALFVAAAPAVRRLDFRLAPFDESEFPGADPFFLRFEATRRSAPLLGPLLDAAEASALVTDIVLASVALPVARERGVPCYVLFTSSAAMLSLCAYFPAYLDAHAAAGSVGVGVGNVDIPGVFRIPKSSVPQALHDPDHLFTQQFVANGRCLVACDGILVNTFDAFEPDAVTALRQGSITVSGGFPPVFTVGPMLPVRFQAEETADYMRWLSAQPPRSVVYVSFGSRKAIPRDQLRELAAGLEASGKRFLWVVKSTIVDR... | Bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids. Converts 2-hydroxynaringenin to isovitexin. Converts eriodictyol to orientin and isoorientin. Converts naringenin and eriodictyol to naringenin 7-O-glucoside and eriodictyol 7-O-glucoside, respectively. Expressed in radicles, hypoc... |
A0A0A1HA03 | MMGDLTTSFPATTLTTNDQPHVVVCSGAGMGHLTPFLNLASALSSAPYNCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSALSPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPEHIFTSFTISNAKYFSLSKGILVNTFDSFEPETLSALNSGDTLSDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELR... | UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin (PubMed:25142187). No activity with flavanones, flavones or flavonols (PubMed:25142187). Exhibits C-glycosylation activity toward 2',4',6'-tr... |
A0A0A1H7N4 | MMGDLTTSFPATTLTTNEQPHVVVCSGAGMGHLIPFLNLASTLSSAPYRCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSTLAPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPDHIFTSFTISNANYLSLSKGIIVNTFDSFEPETLSALNSGDSLPDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELR... | UDP-glucose-dependent glucosyltransferase catalyzing the c-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin. No activity with flavanones, flavones or flavonols. a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-glucose = a 3'-(beta-D-gluco... |
I1L3T1 | MSSSEGVVHVAFLPSAGMGHLNPFLRLAATFIRYGCKVTLITPKPTVSLAESNLISRFCSSFPHQVTQLDLNLVSVDPTTVDTIDPFFLQFETIRRSLHLLPPILSLLSTPLSAFIYDITLITPLLSVIEKLSCPSYLYFTSSARMFSFFARVSVLSASNPGQTPSSFIGDDGVKIPGFTSPIPRSSVPPAILQASSNLFQRIMLEDSANVTKLNNGVFINSFEELEGEALAALNGGKVLEGLPPVYGVGPLMACEYEKGDEEGQKGCMSSIVKWLDEQSKGSVVYVSLGNRTETRREQIKDMALGLIECGYGFLWVVKL... | UDP-glucose-dependent glucosyltransferase catalyzing the c-glucosylation of the A ring of 2-hydroxynaringenin. Also active toward phloretin, but not toward naringenin and apigenin. a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-oxodihydrochalcone + H(+... |
A0A224AM54 | MSDSGGFDSHPHVALIPSAGMGHLTPFLRLAASLVQHHCRVTLITTYPTVSLAETQHVSHFLSAYPQVTEKRFHLLPFDPNSANATDPFFLRWEAIRRSAHLLAPLLSPPLSALITDVTLISAVLPVTINLHLPNYVLFTASARMFSLTASFPAIVASKSTSSGSVEFDDDFIEIPGLPPIPLSSVPPAVMDSKSLFATSFLENGNSFVKSNGVLINSFDALEADTLVALNGRRVVAGLPPVYAVGPLLPCEFEKRDDPSTSLILKWLDDQPEGSVVYVSFGSRLALSMEQTKELGNGLLSSGCRFLWVVKGKTVDKEDE... | UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin and 2-hydroxypinocembrin) and phloretin (PubMed:28370711). No activity with flavanones, flavones or flavonols (PubMed:28370711). Exhibits C-glucosylation activity toward 2-phenyl-2',4',6'-trihydroxyaceto... |
A0A224AKZ9 | MSDSGGFDSHPHVALIPSAGMGHLTPFLRLAASLVQHHCRVTLITTYPTVSLAETQHVSHFLSAYPQVTEKRFHLLPFDPNSANATDPFLLRWEAIRRSAHLLAPLLSPPLSALITDVTLISAVLPVTINLHLPNYVLFTASAKMFSLTASFPAIVASKSTSSGSVEFDDDFIEIPGLPPIPLSSVPPAVMDSKSLFATSFLENGNSFVKSNGVLINSFDALEADTLVALNGRRVVAGLPPVYAVGPLLPCEFEKRDDPSTSLILKWLDDQPEGSVVYVSFGSRLALSMEQTKELGDGLLSSGCRFLWVVKGKIVDKEDE... | UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxylnaringenin and 2-hydroxypinocembrin) and phloretin (PubMed:28370711). No activity with flavanones, flavones or flavonols (PubMed:28370711). Exhibits C-glucosylation activity toward 2-phenyl-2',4',6'-trihydroxyacet... |
K4GKX2 | MVSEITHKSYPLHFVLFPFMAQGHMIPMVDIARLLAQRGVKITIVTTPHNAARFENVLSRAIESGLPISIVQVKLPSQEAGLPEGNETFDSLVSTKLLVPFFKAVNMLEEPVQKLFEEMSPQPSCIISDFCLPYTSKIAKKFNIPKILFHGMCCFCLLCMHVLRKNREILENLKSDKEHFVVPYFPDRVEFTRPQVPLATYVPGEWHEIKEDMVEADKTSYGVIVNTYQELEPAYANGYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLDSKEEGSVLYVCLGSICSLPLSQLKELGLGLEESQRPFI... | Catalyzes the transfer of a glucose (Glc) moiety from UDP-Glc to the C-3 position of the oleanane sapogenins oleanolate and hederagenin, and to the C-28 carboxylic group of the lupane sapogenin betulinate (PubMed:23027665). The monoglucosylated hederagenin 3-O-beta-D-glucoside is a feeding deterrent of the yellow-strip... |
K4GGT4 | MVSEITHKSYPLHFVLFPFMAQGHMIPMVDIARLLAQRGVKITIVTTPHNAARFENVLSRAIESGLPISIVQVKLPSQEAGLPEGNETFDSLVSMELLVPFFKAVNMLEEPVQKLFEEMSPQPSCIISDFCLPYTSKIAKKFNIPKILFHGMCCFCLLCMHVLRKNREILENLKSDKEHFVVPYFPDRVEFTRPQVPMATYVPGEWHEIKEDIVEADKTSYGVIVNTYQELEPAYANDYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLDSKEEGSVLYVCLGSICSLPLSQLKELGLGLEESQRPFI... | Catalyzes the transfer of a glucose (Glc) moiety from UDP-Glc to the C-3 position of the oleanane sapogenins oleanolate and hederagenin, and to the C-28 carboxylic group of the lupane sapogenin betulinate (PubMed:23027665). The monoglucosylated hederagenin 3-O-beta-D-glucoside is a feeding deterrent of the yellow-strip... |
K4GIP0 | MVSEITHKSYPLHFVLFPFMAQGHMIPMVDIARLLAQRGVKITIVTTPHNAARFKNVLSRAIESGLPISIVQVKLPSQEAGLPEGNETLDSLVSMELMIHFLKAVNMLEEPVQKLFEEMSPQPSCIISDFCLPYTSKIAKKFNIPKILFHGMCCFCLLCMHILRKNREIVENLKSDKEHFVVPYFPDRVEFTRPQVPVATYVPGDWHEITEDMVEADKTSYGVIVNTYQELEPAYANDYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLNSKEEGSVLYVCLGSICNLPLSQLKELGLGLEESQRPFI... | Catalyzes the transfer of a glucose (Glc) moiety from UDP-Glc to the C-3 position of the oleanane sapogenins oleanolate and hederagenin, and to the C-28 carboxylic group of the lupane sapogenin betulinate (PubMed:23027665). The monoglucosylated hederagenin 3-O-beta-D-glucoside is a feeding deterrent of the yellow-strip... |
K4GHS2 | MVSEITHKSYPLHFVLFPFMAQGHMIPMVDIARLLAQRGVKITIVTTPHNAARFENVLNRAIESGLPISIVQVKLPSQEAGLPEGNETFDSLVSMELLVPFFKSVNMLEEPVQKLFEEMSPQPSCIISDFCLPYTSKIAKKFNIPKILFHGMCCFCLLCMHVLRKNHEIVENLKSDKEHFVVPYFPDRVEFTRPQVPVATYVPGDWHEITGDMVEADKTSYGVIVNTCQELEPAYANDYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLNSKEEGSVLYVCLGSICNLPLSQLKELGLGLEESQRPFI... | Catalyzes the transfer of a glucose (Glc) moiety from UDP-Glc to the C-3 position of the oleanane sapogenins oleanolate and hederagenin, and to the C-28 carboxylic group of the lupane sapogenin betulinate (PubMed:23027665). The monoglucosylated hederagenin 3-O-beta-D-glucoside is a feeding deterrent of the yellow-strip... |
A0A2R4LMF9 | MASITNHKSDPLHFVLFPFMAQGHMIPMVDIARLLAQRGLTITIVTTPHNASRFKNVLNRAIESGLPINILHVKLPYQEVGLPEGLENIDCFDSMEHMIPFFKGVNMVEESVQKLFEEMSPRPSCIISDFCLPYTSKVAKKFNIPKILFHGMCCLCLLCMHVLRKNPKILENLKSDKEHFVVPYFPDKIELTRPQVPMDTYVPGELKEFMEDLVEADKTSYGVIVNTFQELEPAYVKDYKETRSGKAWSVGPVALCNKARIDKAERGNKSDIDQDECLKWLDSKEERSVLYVCLGSICNLPLAQLKELGLGLEESTRPFI... | Catalyzes the transfer of a glucose (Glc) moiety from UDP-Glc to the C-28 carboxylic group of oleanolate 3-O-beta-D-glucoside to form oleanolate 3,28-O-beta-D-diglucoside. Belongs to the UDP-glycosyltransferase family. |
K4GMD6 | MVSEITHQSYPLHFVLFPYMAQGHMIPMVDIARLLAQRGVKITIVTTPQNAARFENVLSRAIESGLPISIVQVKLPSQEAGLPEGIETFESLVSMELLVPFFKAVNMLEEPVQKLFEEMSPQPSCIISDFCLHYTSKIAKKFNIPKILFHGMCCFCLLCMHVLRKNCEILENLKSDKEHFVVPYFPDRVEFTRPQVPMATYAPGDWQEIREDIVEADKTSYGVIVNTYQELEPAYANDYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLDSKEEGSVLYVCLGSNCSVPLSQLKELGLGLEESQRPFI... | Possesses very weak glucosyltransferase activity toward 2,4,5-trichlorophenol (TCP), when assayed with high concentrations of TCP. Belongs to the UDP-glycosyltransferase family. |
K7NBW3 | MEKGDTHILVFPFPSQGHINPLLQLSKRLIAKGIKVSLVTTLHVSNHLQLQGAYSNSVKIEVISDGSEDRLETDTMRQTLDRFRQKMTKNLEDFLQKAMVSSNPPKFILYDSTMPWVLEVAKEFGLDRAPFYTQSCALNSINYHVLHGQLKLPPETPTISLPSMPLLRPSDLPAYDFDPASTDTIIDLLTSQYSNIQDANLLFCNTFDKLEGEIIQWMETLGRPVKTVGPTVPSAYLDKRVENDKHYGLSLFKPNEDVCLKWLDSKPSGSVLYVSYGSLVEMGEEQLKELALGIKETGKFFLWVVRDTEAEKLPPNFVES... | Catalyzes the transfer of a glucose moiety to the C-3 hydroxyl of mogrol to form mogroside IE (PubMed:25759326, Ref.3). Besides mogrol, UGT74AC1 also shows activity in vitro with quercetin and naringenin as substrate (PubMed:25759326). mogrol + UDP-alpha-D-glucose = H(+) + mogroside IE + UDP Mogrosides, the major activ... |
C0JAW3 | MGHMVNAIAQIDEFVNLGANSIETDVSFDSSANPEYTYHGVPCDCRRWCKKWEYFNNFLKALRKATTPGDSKYHEKLVLVVFDLKTGSLYDNQASDAGKKLAKSLLQNYWNNGNNGGRAYIVLSIPNLAHYKLIAGFKEALTSEGHPELMDKVGYDFSGNDDIGDVANAYKEAGVTGHVWQSDGITNCLLRGLDRVRKAVANRDSSNGYVNKVYYWTVDKRQSTRDALDAGVDGIMTNYPDVIADVLNESAYKAKFRIASYDDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
Q5YD75 | ANKRPAWIMGHMVNAVAQIDEFVNLGANSIETDVSFDKNANPEYTYHGIPCDCGRTCTKWENFNDFLKGLRKATTPGDSKYHEKLVLVVFDLKTGSLYDNQAYDAGKKLAKNILQHYWNNGNNGGRAYIVLSIPNLAHYKLITGFKETLTSEGHPELMEKVGYDFSGNDDIDKVGNAYKNAGVTGHVWQSDGITNCLLRGLSRVKEAVKNRDSSNGFINKVYFWTVDKRASTRDALDAGVDGIMTNYPDVIADVLSESAYKANFRIATYDDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with high activity (18.3 U/mg) (PubMed:16759681). ... |
C0JAU7 | WIMGHMVNAIYQIDEFVNLGANSIETDVSFDDSANPEYTYHGVPCDCRRWCKKWEYFNNFLKALREATTPGDSKYHEKLVLVVFDLKTNSLYDHQAYDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPNLSHYKLITGFKETLKNEGHPELMEKVGFDFSGNDNIDQVAKAYKKAGVTGHVWQSDGITNCIASFIRGLDRAKEAVANRDSSNGFINKVYYWTVDKRATTREALDAEVDGIMTNDPDVIADVLNESAYKAKFRIATYDDNPWETFKK | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAU8 | WIMGHMVNAIYQIDEFVNLGANSIETDVSFDDSANPEYTYHGVPCDCRRWCKKWEYFNNFLKALRKATTPGDSKYHEKLVLVVFDLKTNSLYDHQAYDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPNLSHYKLITGFKETPKNEGHPELKEKVGFDFSGNDNIDQVAKAYKKAGVTGHVWQSDGITNCIASFIRGLDRAKEAVANRDSSNGFINKVYYWTVDKRATTREALDAEVDGIMTNDPDVIADVLNESAYKAKFRIATYDDNPWETFKK | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAU9 | WIMGHMVNAIYQIDEFVNLGANSIETDVSFDDSANPEYTYHGVPCDCRRWCKKWEYFNNFLKALRKATTPGDSKYHEKLVLVVFDLKTNSLYDHQAYDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPNLSHYKLITGFKETLKNEGHPELMEKVGFDFSGNDNIDQVAKAYKKAGVTGRVWQSDGITNCIASFIRGLDRAKEAVANRDSSNGFINKVYYWTVDKRATTREALDAEVDGIMTNDPDVIADVLNESAYKAKFRIATYDDNPWETFKK | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
Q7Z1N2 | MSHSSTALLHPYVAARATEKFAPIYFFCHPLQSAETDVAERANKRPIWIMGHMVNANYQIDEFVNLGANSIETDVSFDSSANPEYTYHGVPCDCRGWCKKWEYFNNFLKALRKATTPGDSKYHEKLVLVVFDLKTGSLYDNQAYDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFSGNDNIDQVANAYKKAGVTGHVWQSDGITNCLLRGLDRVRKAVANRDSSNGYINKVYYWTVDKRQSTKNALDAGVDGIMPNYPDVIADVPNESAYKAKFRIASYDDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
Q4ZFU2 | VRATEKFAPIYFFCHPLQSAETDVAERANKRPIWIMGHMVNANYQIDEFVNLGANSIETDVSFDSSANPEYTYHGVPCDCRRWCKKWEYFNNFLKALRKATTPGDSKYHEKLVLVVFDLKTGSLYDNQAYDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFSGNDNIDQVANAYKKAGVTGHVWQSDGITNCVASFIRGLDRAKKAVKNRDSSNGYINKVYYWTVDKYATTREAFDIGVDGIMTNYPDVIANVLNESAYKGKFRLATYDDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (PubMed:24009677, PubMed:25752604). This toxin acts on sphingomyelin (SM) with high activity and on lysop... |
C0JAU4 | MGHMVNANYQIDEFVNLGANSIETDVSFDSSANPEYTYHGVPCDCRRWCKKWEYFNNFLKALRKATTPGDSKYHEKLVLVVFDLKAGSLYDNQAYDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFSGNDSIDQVANAYKKAGVTGRVWQSDGITNCVASFIRGLDRAKKAVKNRDSSNGYINKVYYWTVDKYATTREALDIGVDGIMTNYPDVIANVLNESAYKEKFRLATYDDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAU6 | WIMGHMVNAIYQIDEFVDLGANSIEVDVSFDDNAKPEYTYHGIPCDCRRWCTKWEYFNDFLKALRKATTPGDSKYHEKLVLVVFDLKTNSLYNYQAYDAGKKLAENLLQHYWNNGNNGGRAYIVLSIPNLAHYQLITGFKETLKNKGHPELMDKVGHDFSGNDNIDQVEKAYKKAGVTGHVWQSDGITNCIASFIRGLDRAKKAVKNRDSSNGYINKVYYWTVDKYATTREALDIGVDGIMTNYPDVIANVLNESAYKEKFRLATYDDNPWEAFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAU3 | WIMGHMVNANYQIDEFVNLGANSIETDVSFDSSANPEYTYHGVPCDCRRWCKKWEYFNNFLKALRKATTPGDSKYHEKLVLVVFDLKTGSLYDNQAYDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFSGNDDIGDVANAYKKAGVTGHVWQSDGITNCLLRGLDRVRKAVANRDSSNGYINKVYYWTVDKRQSTRDALDAGVDGIMTNYPDVIADVLNESAYKAKFRIASYDDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAU5 | LIMGHMVNAIYQIDEFVNLGANSIEIDVSFDDSANPEYTYHGIPCDCRRWCTKWEYFNGFLKALRKATTPGDSKYHEKLVLVVFDLKTNSLYNYQAYDAGKKLAENLLQHYWNNGNNGGRAYIVLSIPNLAHYKLITGFKETLKNKGHPELMEKVGHDFSGNDNLDQVAKAYKKAGVTGHVWQSDGITNCIASFIRGIDRAKKAVANRDSSNGFINKVYYWTVDKYSTTREALDAGVDGIMTNYPDVIANVLNESAYKTKFRLATYADNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAX3 | WIMGHMVNAIAQIDEFVNLGANSIETDVSFDKNANPEYTYHGIPCDCGRTCTKSEKFNVFLQGLQKATTPGDSKYQEKLVLVVFDLKSSSLYDNQASDAGKKLAKSLLQNYWKNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFSGNDDIDQVAKAYKKAGVTGHVWQSDGITNCLPRGLDRVRQAVANRDSSNGFINKVYYWTVDKRSTTRGALDAGVDGIMTNYPDVIAVVLSESAYKSKFRIATYEDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAX4 | WIMGHMVNAIAQIDEFVNLGANSIETDVSFDKNANPEYTYHGIPCDCGRTCTKSEKFNVFLQGLQKATTPGDSKYQEKLVLVVFDLKSSSLYDNQASDAGKKLAKSLLQNYWKNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFSGNDDIDQVAKAYKKAGVTGHVWQSDGITNCLPRGLDRVKQAVANRDSSNGFINKVYYWTVDKRSTTRGALDAGVDGIMTNYPDVIADVLSESAYKSKFRIATYEDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAX5 | WIMGHMVNAIAQIDEFVNLGANSIETDVSFDKNANPEYTYHGIPCDCGRTCTKSEKFNVFLQGLQKATTPGDSKYQEKLVLVVFDLKSSSLYDNQASDAGKKLAKSLLQNYWKNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFSGNDDIDQVAKAYKKAGVTGHVWQSDGITNCLPRGLDRVKQAVANRDSSNGFINKVYYWTVDKRSTTRGALDAGVDGIMANYPDVIADVLSESAYKSKFRIATYEDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAX7 | WIMGHMVNAIAQIDEFVNLGANSIETDVSFDKNANPEYTYHGIPCGCGRTCTKSEKFNVFLQGLQKATTPGDSKYQEKLVLVVFDLKSSSLYDNQASDAGKKLAKSLLQNYWKNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFFGNDDIDQVAKAYKKAGVTGHVWQSDGITNCLPRGLDRVKQAVANRDSSNGFINKVYYWTVDKRSTTRGALDAGVDGIMTNYPDVIADVLSESAYKSKFRIATYEDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAX9 | WIMGHMVNAIAQIDELVNLGANSIETDVSFDKNANPEYTYHGIPCDCGRTCTKSEKFNVFLQGLQKATTPGDSKYQEKLVLVVFDLKSSSLYDNQASDAGKKLAKSLLQNYWKNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFSGNDDIDQVAKAYKKAGVTGHVWQSDGITNCLPRGLDRVKQAVANRDSSNGFINKVYYWTVDKRSTTRGALDAGVDGIMTNYPDVIADVLSESAYKSKFRIATYEDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAY0 | WIMGHMVNAIAQIDEFVNLGANSIETDVSFDKNANPEYTYHGIPCDCGRTCTKSEKFNVFLQGLQKATTPGDSKYQVKLVLVVFDLKSSSLYDNQASDAGKKLAKSLLQNYWKNGNNGGRAYIVLSIPNLTHYKLITGFKETPKTEGHPELMEKVGYDFSGNDDIDQVAKAYKKAGVTGHVWQSDGITNCLPRGLDRVKQAVANRDSSNGFINKVYYWTVGKRSTTRGALDAGVDGIMTNYPDVIADVLSESAYKSKFRIATYEDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
C0JAX2 | WIMGHMVNAIAQIDEFVNLGANSIETDVSFDKNANPEYTYHGIPCDCGRTCTKSEKFNDFLQGLQKATTPGDSKYQEKLVLVVFDLKSSSLYDNQASDAGKKLAKSLLQNYWKNGNNGGRAYIVLSIPNLAHYKLITGFKETLKTEGHPELMEKVGYDFSGNDDIDQVAKAYKKAGVTGHVWQSDGITNCLPRGLDRVKQAVANRDSSNGFINKVYYWTVDKRSTTRGALDAGVDGVMTNYPDVIADVLSESAYKSKFRIATYEDNPWETFKN | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
Q63332 | MRRNQLPIPVFLLLLLLLPRDATAATGKPRYVVLVPSELYAGVPEKVCVHLNHLNETVTLNVTLEYGVQYSNLLIDQAVDKDSSYCSSFTISRPLSPSALIAVEIKGPTHHFIKKKSMWITKAESPVFVQTDKPIYKPGQTVKFRVVSVDISFRPVNETFPVVYIENPKRNRIFQWQNVDLPGGLHQLSFPLSVEPALGIYKVVVQKDSGKKIEHSFEVKEYVLPKFEVQVKMPKTMAFLEEELVVTACGLYTYGKPVPGLVTMKVCRKYTQSYSNCHGQHSKSICEEFSKQADEKGCFRQVVKTKVFQPRQKGYDMKIE... | Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the... |
C0JAZ1 | WIMGHMVNSLAQMDEFVGLGSNSIETDVSFDKQANPEYTYHGVPCDCGRSCGHSTKFNDFLKGLRKATTPGDSKYHEKLILVVFDLKTGSLYDNQAYDAGTKLAKNLLQHYWNNGNNGGRAYIILSIPKLNHYKLITGFKETLKNEGHEDLLEKVGHDFSGNDDISEVQKTYNKAGVTGHVWQSDGITNCLLRGLSRVKAAVANRDSGRGIINKVYYWTVDKRSTTRDSLDAKVDGIMTNYPDITVEILNEDAYKTKFRIATYEDNPWETFKE | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosp... |
Q9UQ58 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFF... | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912). Involved in cell mobility and transcription regulation thr... |
Q95KN7 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFF... | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
P29216 | EVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSVMSQSLRKTTREPLTRDPVKL | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
Q99K32 | MLPSLALLLLAAWTVRALEVPTDGNAGLLAEPQIAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDSVDSADAEEDDSDVWWGGADTDYADGGEDKVVEVAEEEEVADVEEEEADDDEDVEDGDEVEEEAEEPYEEATERTTSTATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCVPFF... | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
Q5IS80 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFF... | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
Q9TUI0 | MLPGLALVLLAAWTARALEVPTDGNAGLLAEPQVAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRSRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNIDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVADVEEEEAEDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFF... | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
Q28748 | SEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLK | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
Q547B7 | MLPSLALLLLAAWTVRALEVPTDGNAGLLAEPQIAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDSIDSADAEEDDSDVWWGGADTDYADGGEDKVVEVAEEEEVADVEEEEAEDDEDVEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFF... | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
Q95241 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRDRKQCKTHPHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDHVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFF... | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
Q28757 | SEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLK | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
O93279 | MGETTAFVLLLVATLTRSSEIPADDTVGLLTEPQVAMFCGKLNMHINVQNGKWESDPSGTKSCLNTKEGILQYCQEVYPELQITNVVEANQPVSIQNWCKKGRKQCRSHTHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMNQCESHLHWHTVAKESCGDRSMNLHDYGMLLPCGIDRFRGVKFVCCPAETEQETDSSEVEGEESDVWWGGADPEYSENSPPTPSRATYVAGDAFERDENGDGDEDEEDDEDVDPTDEQESDERTANVAMTTTTTTTTESVEEVVRAVCWAQAESGPCRAMLERWYFNPKKRRCVPFLF... | Functional neuronal receptor which couples to intracellular signaling pathway through the GTP-binding protein G(O). Belongs to the APP family. |
O73683 | MGHSVAWLLLVAAASTLAAEVPTDVSMGLLAEPQVAMFCGKINMHINVQSGKWEPDPSGTKSCIGTKEGILQYCQEVYPELQITNVVEANQPVSIQNWCKKGRKQCRSHMHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMNQCESHLHWHTVAKESCGDRAMNLHDYGMLLPCGIDRFRGVEFVCCPAEAERDMDSTEKDADDSDVWWGGADNDYSDNSMVREPEPAEQQEETRPSVVEEEEEGEVAQEDDEEEEEVLDTDQDGDGEEDHEAADDEEEEEDVDEIDAFGESDDVDADEPTTNVAMTTTTTTTTTESVE... | Functional neuronal receptor which couples to intracellular signaling pathway through the GTP-binding protein G(O). Belongs to the APP family. |
Q29149 | SEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVML | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-prote... |
P20983 | MDFFNKFSQGLAESSTPKSSIYYSEEKDPDTKKDEAIEIGLKSQESYYQRQLREQLARDNMMAASRQPIQPLQPTIHITPQPVPTATPAPILLPSSTAPTPKPRQQTNTSSDMSNLFDWLSEDTDAPASSLLPALTPSNAVQDIISKFNKDQKTTTPPSTQPSQTLPTTTCTQQSDGNISCTTPTVTPPQPPIVATVCTPTPTGGTVCTTAQQNPNPGAASQQNLDDMALKDLMSSVEKDMHQLQAETNDLVTNVYDAREYTRRAIDQILQLVKGFERFQK | Component of the virion core. Interacts with P4A/A10 and its cleaved form 4A. Localizes between the core and the membrane; might surround the outer core wall like a palisade (spikes). Expressed in the late phase of the viral replicative cycle. Its phosphorylation state is regulated by the F10 kinase and the H1 phosphat... |
Q76ZQ9 | MDFFNKFSQGLAESSTPKSSIYYSEEKDPDTKKDEAIEIGLKSQESYYQRQLREQLARDNMTVASRQPIQPLQPTIHITPQPVPTATPAPILLPSSTVPTPKPRQQTNTSSDMSNLFDWLSEDTDAPASSLLPALTPSNAVQDIISKFNKDQKTTTPPSTQPSQTLPTTTCTQQSDGNISCTTPTVTPPQPPIVATVCTPTPTGGTVCTTAQQNPNPGAASQQNLDDMALKDLMSNVERDMHQLQAETNDLVTNVYDAREYTRRAIDQILQLVKGFERFQK | Component of the virion core. Interacts with P4A/A10 and its cleaved form 4A. Localizes between the core and the membrane; might surround the outer core wall like a palisade (spikes). Expressed in the late phase of the viral replicative cycle. Its phosphorylation state is regulated by the F10 kinase and the H1 phosphat... |
P33832 | MDFFNKFSQGLAESSTPKSSIYYSEEKDLDIKKDEAIEIGLKSQESYYQRQLREQLARDNMMAASRQPIQPLQPTIHITPLQVPTPAPTPKPRQQQTNTSSDMSNLFDWLSADDNTQPSSLLPALTPINAVQDIISKFNKDQKTTTTPSTQPSQTLPTTTCTQQSDGSISCTTPTVTPPQPPIVATVCTPTPTGGTVCTTAQQNPNPGATSQQNLDNMALKDLMSSVEKDMRQLQAETNDLVTNVYDAREYTRRAIDQILQLVKGFERFQK | Component of the virion core. Interacts with P4A/A10 and its cleaved form 4A. Localizes between the core and the membrane; might surround the outer core wall like a palisade (spikes). Expressed in the late phase of the viral replicative cycle. Its phosphorylation state is regulated by the F10 kinase and the H1 phosphat... |
A4USB4 | MLCFFVLFFCCGTVLLEGADIDEIEHADKRRPIWNMGHMVNAVYQIDEFVDLGANAIETDVTFTKSANAEYTYHGVPCDCHRWCKKWEYVNDFLKALRRATTPGDAKYRSQLILVVFDLKTDYLTASTAYDAGKDFAKRLLQHYWNGGSNGGRAYIILSIPDLAHYKFINGFKEQLKTQGHEDLLAKVGYDFWGNEDLSSTRAAFQKAGVQDKEHIWQSDGITNCWLRTLKRVREAVANRDSSNGYINKVYYWTVDKYASVRDAINAGADGIMTNYPNVIVDVLKENDFKGKFRMATYNDNPWETFK | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with high activity (PubMed:18082635). It may also ... |
Q89181 | MDGVIVYCLNALVKHGEEINHIKNDFMIKPCCEKVKNVHIGGQSKNNTVIADLPYMDNAVSDVCNSLYKKNVSRISRFANLIKIDDDDKTPTGVYNYFKPKDAIPVIISIGKDRDVCELLISSDKACACIELNSYKVAILPMDVSFFTKGNASLIILLFDFSIDAAPLLRSVTDNNVIISRHQRLHDELPSSNWFKFYISIKSDYCSILYMVVDGSVMHAIADNRTYANISKNILDNTTINDECRCCYFEPQIRILDRDEMLNGSSCDMNRHCIMMNLPDVGEFGSSMLGKYEPDMIKIALSVAGIWKVL | Belongs to the poxviridae A51 protein family. |
B4TUM9 | MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKKLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
Q7C7F5 | MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLIAPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
Q8ZMA4 | MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
B2TYQ5 | MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDASRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
Q0T128 | MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
Q7C061 | MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
Q3YY21 | MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
A1JPF0 | MAYRLLRALFRGLFRVTIDGITDQFSHQKLIITPNHVSFLDGALLALFLPIKPVFAVYSNITESWYMRWLKPYVDFVALDPTKPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLEGPEFTRFGRLGDVLKVRWFPKISIHVLPATTLPMPQAPRARDRRVLAGERLHAIMMAARMAIVPRETLFEALLSAQTRYGRFKPCIEDISFKEDSYQTLLKKILGVSRILQRFTAQGEHVGMLLPNATITAAAIFGATLRGRIPALLNYTSGAKGLKSAITAASLKTIITSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
A7FFD1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
Q1CAS8 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
B2JZ75 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
Q8ZHU1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
A9R2S1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
A4TLD3 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
Q667F1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
B1JQC1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... |
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