UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
|---|---|---|
Q9P1Y1 | MNITNCTTEASMAIRPKTITEKMLICMTLVVITTLTTLLNLAVIMAIGTTKKLHQPANYLICSLAVTDLLVAVLVMPLSIIYIVMDRWKLGYFLCEVWLSVDMTCCTCSILHLCVIALDRYWAITNAIEYARKRTAKRAALMILTVWTISIFISMPPLFWRSHRRLSPPPSQCTIQHDHVIYTIYSTLGAFYIPLTLILILYYRIYHAAKSLYQKRGSSRHLSNRSTDSQNSFASCKLTQTFCVSDFSTSDPTTEFEKFHASIRIPPFDNDLDHPGERQQISSTRERKAARILGLILGAFILSWLPFFIKELIVGLSIYTVSSEVADFLTWLGYVNSLINPLLYTSFNEDFKLAFKKLIRCREHT | 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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Detected in brain. Belongs to the G-protein coupled receptor 1 family. |
Q9N2B6 | MNITNCTTEASMAIRPKTITEKMLICMTLVVITTLTTLLNLAVIMAIGTTKKLHQPANYLICSLAVTDLLVAVLVMPLSIIYIVMDRWKLGYFLCEVWLSVDMTCCTCSILHLCVIALDRYWAITNAIEYARKRTAKRAALMILTVWTISIFISMPPLFWRSHRRLSPPPSQCTIQHDHVIYTIYSTLGAFYIPLTLILILYYRIYHAAKSLYQKRGSSRHLSNRSTDSQNSFASCKLTQTFCVSDFSTSDPTTEFEKFHASIRIPPFDNDLDHPGERQQISSTRERKAARILGLILGAFILSWLPFFIKELIVGLSIYTVSSEVADFLTWLGYVNSLINPLLYTSFNEDFKLAFKKLIRCRE | 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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity (By similarity). Belongs to the G-protein coupled receptor 1 family. |
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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity (By similarity). Belongs to the G-protein coupled receptor 1 family. |
O08890 | MDFLNSSDQNLTSEELLHRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVLCDIWLSVDIICCTCSILHLSAIALDRYRAITDAVEYARKRTPKQAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLVLILILYYKIYKAAKTLYHKRQASRIAKEELNGQVLLESGEKSIKMVSTTYVPEKSLSDPSTDFDKIHNTVKSPRCKLRHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCEKCKISEEMANFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCQY | 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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Belongs to the G-protein coupled receptor 1 family. |
P30939 | MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC | 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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Belongs to the G-protein coupled receptor 1 family. |
Q02284 | MDFLNASDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVLCDIWLSVDIICCTCSILHLSAIALDRYRAITDAVEYARKRTPRHAGIMITIVWVISVFISMPPLFWRHQGTSRDDECVIKHDHIVSTIYSTFGAFYIPLVLILILYYKIYRAARTLYHKRQASRMIKEELNGQVFLESGEKSIKLVSTSYMLEKSLSDPSTDFDRIHSTVKSPRSELKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCEKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRY | 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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Detected in hippocampus. Belongs to the G-protein coupled receptor 1 family. |
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 isomerase family. 6-phosphogluconolactonase subfamily. |
D4B0N9 | MKTVPFLSLLQAGILTSGIVAQNIAFVGSNANAIATVSFDTKTGTFKVTGNNTDSSTPSWQEVSRDGKLLYSIEETSTEHALTSYSIGQDGKLKKLKSIKGLAGPVSLDMHPTQPIIITANYGSASASAYSSKDNGELTHLGDFMFKMQGKGKVPDRQDAPHPHQALFDPTGKFVLMPDLGSDLIRILKVDAGQKFSVAPPNKVKPGTGPRHGVLYPASDKPRFYYVVGELSNTVTAMSVEYTVETIKLTEIQTLSTLPDGQRGAAGELILSPSGKHLYASNRLDKVFPGSSSVASYTIDQMTGKLKLLEIFNGGVENIRHMSIHPSGKWFVTEGQNSNDIKVFALDPETGKVTPEAKSTLEIEKPVCLQWWHNGAQESEAPEAGTETECEFDD | 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 | MTKYIGYVGTYTKGGSEGIYSFELDTEKKALSEPKLAAKLGNPTYVATNKNNTILYSIEKADGQGGVAAYQIDKNSGELTFLNHQLIDGPSPCHVSVDDQNQFVLTANYHSGKVHVFPVQEDGSLQSPVSEAAHTGKGPHERQEKPHTHYAGFTPEHNYVVAVDLGIDKLYTYKLKDGVLTESGSHSFAPGAGPRHIAFHPKEKYAYVMTELSNEVIALEYNPTAGEFREIQVVSAIPDDFTDNSQGSAIHVTQDGRFVYVANRGHDSIAVFEVNQYSGELAFVERVSTEGNWPRDFVFDPTEGFLVASNEETGNLVLFERDKETGRLTLLPSTVSVPYPVCVKFLHQV | 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 | MQIFYISSPDNQKIYVWKLDNHQEKLELMQVVSTDGCAQPTVVHPNQNFLYVGIRPDFKIDTYRISQNGLLTKIQSTKICDSPTYLTINIYGTFIYCVSYNFNCINVIKIDKFGLLCNSIQIIKNMLGCHSANINKDRKVLWAPCLQENTIRLFDIDHLYGTLKPHNPHVINTNMQSGPRHMAFHSTDNYAYVINEYNGVIDVIQYNDSITNLAIIQKINILSNHGLDTKKFWSSDIHITPNNRWLYCADRFCNTISLFEILLNTKKLKFINYIYTEDQPRGFLIDSTGNFLIVAGQKSHFITLYRIHANNGNLSVISRHASGMGPMWISILSKNTIH | 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 | MIQIIYVASPESQQIHVWKLDSIYGLLELIQVIYTHGQAQPMAVHPNKRFLYVGIRPNFGITTYRIDQIGLLADHGTIGIFSSPTHLISDKKGAFLYCTSYRNNTVSVIPISMSGMLLDSPIQIIEGLLGCHSANIDKFKKLLWVPCLKENAIRLFNINSFGMLTSYDPSIIKINVGSGPRHMIFCDFDCYAYVINELTSTVDVIKYNNFQKIPSIVQTVSIIPKNISINRCWAADIHITPNGRWLYCTDRSINIISCLEISKKTKKLKFVGYQLTEEQPRGFAIDYQGKFLVVAGQKSNCISLYKIDSDNGTLTMLSRYSSGKGPMWVSIITLNCK | 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 isomerase family. 6-phosphogluconolactonase subfamily. |
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 isomerase family. 6-phosphogluconolactonase subfamily. |
B8D985 | MKQVVYIANSESKNIEVWNLCKSGKMNLIQKIETDGKIQPINIIQKRNLLYAGIFPDNKIITYSINHNGFLEKKNESNIPGKANYISFDKKKEFLFCSSYHSNFISVSPLNKFGIPQNPIQIIYNIEGCHAAKMNYKYNILFVISLKEDCIYLYYLTDFGILKSTEQNILHTQKKSGPRHIIFHPNQDFVYTINELNGTIDVWKIYKKNNVIKVKNIQNIHVLKNRFLKDYWCSDIHITSCGRFLYACDRFFNIISLFHINQNDNKLVFFKSYDTEEQPRSFNINSHNTHLIVAGEKSNTFIIYSISNSTGELKKINVYSTGQRPVWILIHALC | 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 | MKQVVYIANSESKNIEVWNLCKSGKMNLIQKIETDGKIQPINIIQKRNLLYAGIFPDNKIITYSINHNGFLEKKNESNIPGKANYISFDKKKEFLFCSSYHSNFISVSPLNKFGIPQNPIQIIYNIEGCHAAKMNYKYNILFVISLKEDCIYLYYLTDFGILKSTEQNILHTQKKSGPRHIIFHPNQDFIYTINELNGTIDVWKIYKKNNVIKVKNIQNIHVLKNRFLKDYWCSDIHITSCGRFLYACDRFFNIISLFHINQNDNKLVFFKSYDTEEQPRSFNINSHNTHLIVAGEKSNTFIIYSISNSTGELKKINVYSTGQRPVWILIHALC | 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 | MQQIIYIANAESENIEVWILYNNGDMKLIQTVQTDGQVQPISIIKNTKLLYAGIRPKNRVITYQIDKNGLLKKKKESIVPGTPNYISFDSSEKFLFCSSYHADCISVSPLDKNGIPKDPIQIIHNIEGCHAAKFNSKYNVLFITSLKNDCIYLYYLTHFGILKSTEQKLVFSQKNSGPRHVIFHPNQNFSYTVNELNGSVDVWKISKENKVLEVKNIQNIKLLNDLISKKYWSSDIHLTSCGNFLYVSDRYLNSISLFHVNKNDNTIIFFKQYLTEEQPRAFCIDRNNNYLIVIGQKSNKLSVYKICQKTGELKKINQYQTGNGPLWITSFLI | 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 | MKQVVYIANSESKNIEVWNLCKSGKMNLIQKIETDGKIQPINIIQKRNLLYAGIFPDNKIITYSINHNGFLEKKNESNIPGKANYISFDKKKEFLFCSSYHSNFISVSPLNKFGIPQNPIQIIYNIEGCHAAKMNYKYNILFVISLKEDCIYLYYLTDFGILKSTEQNILHTQKKSGPRHIIFHPNQDFIYTINELNGTIDVWKIYKKNNVIKVKNIQNIHVLKNRFLKDYWCSDIHITSCGRFLYACDRFFNIISLFHINQNDNKLVFFKSYDTEEQPRSFNINSHNTHLIVAGEKSNTFIIYGISNSTGELKKINVYSTGQRPVWILIHALC | 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 | MKQIIYITLAKNQEIEVWKLHDDFSLNLLQRISTQGEPQPIIISKDKKYLYIGVRPKFKVYSYKIKADGTLTKHACSTLPGSPNHFEIDHTGKYLFSSSYHFNCLSITPLDTLGIPRPVTQTIKNIFGCHASKMNCYNTCLFISALKKDCIYAYNFKKNGKLLKNTRKNFMTNVNFGPRHLDLQKCNNRLYSVNELNGSVDIWSINSFSNELILLKNINIMSKNYCNAAWSSDLHISPCEKFLYVSDRIENTISIIKLEKDVQNIEKIGHIKTELQPRTFSINSTGENLIVVGEKSNSFSVYKISKITGLLELKNTYSTGNRPVWISSLML | 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 glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily. |
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 isomerase family. 6-phosphogluconolactonase subfamily. |
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 isomerase family. 6-phosphogluconolactonase subfamily. |
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 isomerase family. 6-phosphogluconolactonase subfamily. Extended N-terminus. Extended N-terminus. Truncated C-terminus. |
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 isomerase family. 6-phosphogluconolactonase subfamily. |
A8AJ27 | MKQTVYTASPESQQIHVWSLNHDGSLKLVQVVDVPGQVQPMVVSPDKRYLYVGVRPEFRVLAYRIAPDDGALTFAAESALPGSPTHISTDHQGRFVFVGSYNAGNVSVTRLDDGLPAGVVDVVEGLEGCHSANISPDNRTLWVPALKQDRICLFTLSDDGKLVAQEPAEVTTVEGAGPRHMAFHPNQQYAYCVNELNSSVDVWELKDPHGNIECVQTLDMMPADFSDTRWAADIHITPDGRHLYACDRTASLITVFSVSEDGSVLTKEGFQPTETQPRGFNVDHSGKYLIAAGQKSHHIAVYAIAGEQGLLTEKGRYAVGQGPMWVVVNAY | 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 | MKQTVYTASPESQQIHVWRLEPQGTLTLLQVVDAPGQVQPMVISPDKRFLYVGVRPEFRVIAYRIAAHDGTLSEAGEAPLPGSPTHISTDHTGRFLFSGSYNAGSVSVVRLNDGLPGETVTVVEGLEGCHSANISPDNRTLWVPALKQDRICLFTLTDDGHLEPQTPAEVTTVAGAGPRHMVFHPSKPFAYCVNELNSSVDVWALSDPHGNIECVQTLDMMPADFSDTRWAADIHITPDGRHLYACDRTASVITVFTVSEDGSVLAVQGHQPTETQPRGFNIDNSGQYLIAAGQKSHHIAVYGIEGEQGLLAEKGRYAVGQGPMWVVINAFDA | 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 isomerase family. 6-phosphogluconolactonase subfamily. |
Q1C949 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVGKGPMWVSIRGAQNS | 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 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSKDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVGKGPMWVSIRGAQNS | 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 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVGKGPMWVSIRGAQNS | 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 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVGKGPMWVSIRGAQNS | 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 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVGKGPMWVSIRGAQNS | 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 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSKDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVGKGPMWVSIRGAQNS | 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 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSKDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVGKGPMWVSIRGAQNS | 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 | MAANGGDHTSARPHVVLLPSAGMGHLVPFARLAVALSEGHGCNVSVAAVQPTVSSAESRLLDALFVAAAPAVRRLDFRLAPFDESEFPGADPFFLRFEATRRSAPLLGPLLDAAEASALVTDIVLASVALPVARERGVPCYVLFTSSAAMLSLCAYFPAYLDAHAAAGSVGVGVGNVDIPGVFRIPKSSVPQALHDPDHLFTQQFVANGRCLVACDGILVNTFDAFEPDAVTALRQGSITVSGGFPPVFTVGPMLPVRFQAEETADYMRWLSAQPPRSVVYVSFGSRKAIPRDQLRELAAGLEASGKRFLWVVKSTIVDRDDTADLGGLLGDGFLERVQGRAFVTMGWVEQEEILQHGSVGLFISHCGWNSLTEAAAFGVPVLAWPRFGDQRVNAALVARSGLGAWEEGWTWDGEEGLTTRKEVAKKIKGMMGYDAVAEKAAKVGDAAAAAIAKCGTSYQSLEEFVQRCRDAERK | 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, hypocotyls and juvenile leaves. Expressed at low levels in roots. Belongs to the UDP-glycosyltransferase family. |
A0A0A1HA03 | MMGDLTTSFPATTLTTNDQPHVVVCSGAGMGHLTPFLNLASALSSAPYNCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSALSPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPEHIFTSFTISNAKYFSLSKGILVNTFDSFEPETLSALNSGDTLSDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELRKLFGEELYLKLSEKGKLVKWVNQTEILGHTAVGGFLSHCGWNSVMEAARRGVPILAWPQHGDQRENAWVVEKAGLGVWEREWASGIQAAIVEKVKMIMGNNDLRKSAMKVGEEAKRACDVGGSSATALMNIIGSLKR | 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'-trihydroxyacetophenone and phloretin using UDP-glucose as sugar donor (PubMed:32699169). Can use UDP-galactose as sugar donor, but catalytic efficiency is 14-fold lower toward UDP-galactose than toward UDP-glucose (PubMed:32699169). a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-oxodihydrochalcone + H(+) + UDP Optimum pH is 6.5-7.0. Optimum temperature is 45-50 degrees Celsius. Expressed in cotyledons. Not detected in flowers, leaves, roots and hypocotyls. Expressed in germinating seeds and during cotyledon development. Belongs to the UDP-glycosyltransferase family. |
A0A0A1H7N4 | MMGDLTTSFPATTLTTNEQPHVVVCSGAGMGHLIPFLNLASTLSSAPYRCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSTLAPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPDHIFTSFTISNANYLSLSKGIIVNTFDSFEPETLSALNSGDSLPDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELRKLFGEELYVKLSEKGKLVKWVNQTEILGHTAVGGFLSHCGWNSVMEAARRGVPILAWPQHGDQRENAWVVEKAGLGVWEREWSSGIQVAIVEKVKMIMGNNDLRNSAVRVGEEAKRACDVGGSSATALMNIIGSLKR | 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-glucopyranosyl)-2'-hydroxy-beta-oxodihydrochalcone + H(+) + UDP Optimum pH is 6.5-7.0. Optimum temperature is 50-55 degrees Celsius. Expressed in cotyledons. Not detected in flowers, leaves, roots and hypocotyls. Expressed in germinating seeds and during cotyledon development. Belongs to the UDP-glycosyltransferase family. |
I1L3T1 | MSSSEGVVHVAFLPSAGMGHLNPFLRLAATFIRYGCKVTLITPKPTVSLAESNLISRFCSSFPHQVTQLDLNLVSVDPTTVDTIDPFFLQFETIRRSLHLLPPILSLLSTPLSAFIYDITLITPLLSVIEKLSCPSYLYFTSSARMFSFFARVSVLSASNPGQTPSSFIGDDGVKIPGFTSPIPRSSVPPAILQASSNLFQRIMLEDSANVTKLNNGVFINSFEELEGEALAALNGGKVLEGLPPVYGVGPLMACEYEKGDEEGQKGCMSSIVKWLDEQSKGSVVYVSLGNRTETRREQIKDMALGLIECGYGFLWVVKLKRVDKEDEEGLEEVLGSELSSKVKEKGVVVKEFVDQVEILGHPSVGGFLSHGGWNSVTETVWKGVPCLSWPQHSDQKMSAEVIRMSGMGIWPEEWGWGTQDVVKGDEIAKRIKEMMSNESLRVKAGELKEAALKAAGVGGSCEVTIKRQIEEWKRNAQAN | 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(+) + UDP Belongs to the UDP-glycosyltransferase family. |
A0A224AM54 | MSDSGGFDSHPHVALIPSAGMGHLTPFLRLAASLVQHHCRVTLITTYPTVSLAETQHVSHFLSAYPQVTEKRFHLLPFDPNSANATDPFFLRWEAIRRSAHLLAPLLSPPLSALITDVTLISAVLPVTINLHLPNYVLFTASARMFSLTASFPAIVASKSTSSGSVEFDDDFIEIPGLPPIPLSSVPPAVMDSKSLFATSFLENGNSFVKSNGVLINSFDALEADTLVALNGRRVVAGLPPVYAVGPLLPCEFEKRDDPSTSLILKWLDDQPEGSVVYVSFGSRLALSMEQTKELGNGLLSSGCRFLWVVKGKTVDKEDEESLKNVLGHELMEKIKDQGLVVKNWVDQDKVLSHRAVGGFVSHGGWNSLVEAARHGVPVLVWPQFGDQKINAEAVESAGLGMWVRSWGWGTELRAKGDEIGLKIKDLMANDFLREQAKRIEEEARKAIGVGGSSERTFKELIDKWKCNNNTH | 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'-trihydroxyacetophenone (PubMed:28370711). Can use UDP-xylose as sugar donor, but catalytic efficiency is much lower toward UDP-xylose than toward UDP-glucose (PubMed:28370711). a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-oxodihydrochalcone + H(+) + UDP Optimum pH is 8.0-11.0. Optimum temperature is 50 degrees Celsius. Expressed in leaves and flowers, and at lower levels in immature fruits. Belongs to the UDP-glycosyltransferase family. |
A0A224AKZ9 | MSDSGGFDSHPHVALIPSAGMGHLTPFLRLAASLVQHHCRVTLITTYPTVSLAETQHVSHFLSAYPQVTEKRFHLLPFDPNSANATDPFLLRWEAIRRSAHLLAPLLSPPLSALITDVTLISAVLPVTINLHLPNYVLFTASAKMFSLTASFPAIVASKSTSSGSVEFDDDFIEIPGLPPIPLSSVPPAVMDSKSLFATSFLENGNSFVKSNGVLINSFDALEADTLVALNGRRVVAGLPPVYAVGPLLPCEFEKRDDPSTSLILKWLDDQPEGSVVYVSFGSRLALSMEQTKELGDGLLSSGCRFLWVVKGKIVDKEDEESLKNVLGHELTEKIKDQGLVVKNWVDQDKVLSHRAVGGFVSHGGWNSLVEAARHGVPLLVWPHFGDQKINAEAVERAGLGMWVRSWGWGTELRAKGDEIGLKIKDLMANDFLREQAKRIEEEARKAIGVGGSSERTFKELIDKWKCNNNTH | 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'-trihydroxyacetophenone (PubMed:28370711). Can use UDP-xylose as sugar donor, but catalytic efficiency is much lower toward UDP-xylose than toward UDP-glucose (PubMed:28370711). a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-oxodihydrochalcone + H(+) + UDP Optimum pH is 8.0-11.0. Optimum temperature is 45 degrees Celsius. Expressed at low levels in leaves, flowers and immature leaves. Belongs to the UDP-glycosyltransferase family. |
K4GKX2 | MVSEITHKSYPLHFVLFPFMAQGHMIPMVDIARLLAQRGVKITIVTTPHNAARFENVLSRAIESGLPISIVQVKLPSQEAGLPEGNETFDSLVSTKLLVPFFKAVNMLEEPVQKLFEEMSPQPSCIISDFCLPYTSKIAKKFNIPKILFHGMCCFCLLCMHVLRKNREILENLKSDKEHFVVPYFPDRVEFTRPQVPLATYVPGEWHEIKEDMVEADKTSYGVIVNTYQELEPAYANGYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLDSKEEGSVLYVCLGSICSLPLSQLKELGLGLEESQRPFIWVVRGWEKNKELLEWFSESGFEERVKDRGLLIKGWSPQMLILAHHSVGGFLTHCGWNSTLEGITSGVPLLTWPLFGDQFCNQKLVVQVLKVGVSAGVEEVTNWGEEEKIGVLVDKEGVKKAVEELMGESDDAKEIRKRVKELGQLAHKAVEEGGSSHSNITSLLEDIMQLAQPNN | 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-striped flea beetle (Phyllotreta nemorum) (PubMed:23027665). oleanolate + UDP-alpha-D-glucose = H(+) + oleanolate 3-O-beta-D-glucoside + UDP Belongs to the UDP-glycosyltransferase family. |
K4GGT4 | MVSEITHKSYPLHFVLFPFMAQGHMIPMVDIARLLAQRGVKITIVTTPHNAARFENVLSRAIESGLPISIVQVKLPSQEAGLPEGNETFDSLVSMELLVPFFKAVNMLEEPVQKLFEEMSPQPSCIISDFCLPYTSKIAKKFNIPKILFHGMCCFCLLCMHVLRKNREILENLKSDKEHFVVPYFPDRVEFTRPQVPMATYVPGEWHEIKEDIVEADKTSYGVIVNTYQELEPAYANDYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLDSKEEGSVLYVCLGSICSLPLSQLKELGLGLEESQRPFIWVVRGWEKNKELLEWFSESGFEERVKDRGLLIKGWSPQMLILAHHSVGGFLTHCGWNSTLEGITSGIPLLTWPLFGDQFCNQKLVVQVLKVGVSAGVEEVTNWGEEEKIGVLVDKEGVKKAVEELMGESDDAKERRKRVKELGQLAQKAVEEGGSSHSNITSLLEDIMQLAQSNN | 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-striped flea beetle (Phyllotreta nemorum) (PubMed:23027665). oleanolate + UDP-alpha-D-glucose = H(+) + oleanolate 3-O-beta-D-glucoside + UDP kcat is 0.023 sec(-1) with oleanolate as substrate (PubMed:23027665). kcat is 0.006 sec(-1) with hederagenin as substrate (PubMed:23027665). Optimum pH is 8.6. Belongs to the UDP-glycosyltransferase family. |
K4GIP0 | MVSEITHKSYPLHFVLFPFMAQGHMIPMVDIARLLAQRGVKITIVTTPHNAARFKNVLSRAIESGLPISIVQVKLPSQEAGLPEGNETLDSLVSMELMIHFLKAVNMLEEPVQKLFEEMSPQPSCIISDFCLPYTSKIAKKFNIPKILFHGMCCFCLLCMHILRKNREIVENLKSDKEHFVVPYFPDRVEFTRPQVPVATYVPGDWHEITEDMVEADKTSYGVIVNTYQELEPAYANDYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLNSKEEGSVLYVCLGSICNLPLSQLKELGLGLEESQRPFIWVIRGWEKNKELHEWFSESGFEERIKDRGLLIKGWAPQMLILSHHSVGGFLTHCGWNSTLEGLTAGLPLLTWPLFADQFCNEKLAVQVLKAGVSAGVDQPMKWGEEEKIGVLVDKEGVKKAVEELMGESDDAKEIRRRAKELGELAHKAVEEGGSSHSNITSLLEDIMQLAQSNN | 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-striped flea beetle (Phyllotreta nemorum) (PubMed:23027665). oleanolate + UDP-alpha-D-glucose = H(+) + oleanolate 3-O-beta-D-glucoside + UDP Belongs to the UDP-glycosyltransferase family. |
K4GHS2 | MVSEITHKSYPLHFVLFPFMAQGHMIPMVDIARLLAQRGVKITIVTTPHNAARFENVLNRAIESGLPISIVQVKLPSQEAGLPEGNETFDSLVSMELLVPFFKSVNMLEEPVQKLFEEMSPQPSCIISDFCLPYTSKIAKKFNIPKILFHGMCCFCLLCMHVLRKNHEIVENLKSDKEHFVVPYFPDRVEFTRPQVPVATYVPGDWHEITGDMVEADKTSYGVIVNTCQELEPAYANDYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLNSKEEGSVLYVCLGSICNLPLSQLKELGLGLEESQRPFIWVIRGWEKNKELLEWFSESGFEERIKDRGLLIKGWAPQMLILSHHSVGGFLTHCGWNSTLEGLTAGLPLLTWPLFADQFCNEKLAVQVLKAGVSAGVDQPMKWGEEEKIGVLVDKEGVKKAVEELMGESDDAKEIRRRAKELGELAHKAVEEGGSSHSNITSLLEDIMQLAQSNN | 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-striped flea beetle (Phyllotreta nemorum) (PubMed:23027665). oleanolate + UDP-alpha-D-glucose = H(+) + oleanolate 3-O-beta-D-glucoside + UDP kcat is 0.816 sec(-1) with oleanolate as substrate (PubMed:23027665). kcat is 0.389 sec(-1) with hederagenin as substrate (PubMed:23027665). Optimum pH is 7.9. Belongs to the UDP-glycosyltransferase family. |
A0A2R4LMF9 | MASITNHKSDPLHFVLFPFMAQGHMIPMVDIARLLAQRGLTITIVTTPHNASRFKNVLNRAIESGLPINILHVKLPYQEVGLPEGLENIDCFDSMEHMIPFFKGVNMVEESVQKLFEEMSPRPSCIISDFCLPYTSKVAKKFNIPKILFHGMCCLCLLCMHVLRKNPKILENLKSDKEHFVVPYFPDKIELTRPQVPMDTYVPGELKEFMEDLVEADKTSYGVIVNTFQELEPAYVKDYKETRSGKAWSVGPVALCNKARIDKAERGNKSDIDQDECLKWLDSKEERSVLYVCLGSICNLPLAQLKELGLGLEESTRPFIWVIRGWDKNKQLVEWFSESGFEERIKDRGLLIKGWSPQMLILSHQSVGGFLTHCGWNSTLEGITAGLPLLTWPLFADQFCNEKLVVQVLNSGVRAGVEQPMKWGEEEKIGVLVDKEGVKKAVEELMGESDEANERRRRAKELGELAHKAVEEGGSSHSNITFLLQDIMQLAQSNN | 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 | MVSEITHQSYPLHFVLFPYMAQGHMIPMVDIARLLAQRGVKITIVTTPQNAARFENVLSRAIESGLPISIVQVKLPSQEAGLPEGIETFESLVSMELLVPFFKAVNMLEEPVQKLFEEMSPQPSCIISDFCLHYTSKIAKKFNIPKILFHGMCCFCLLCMHVLRKNCEILENLKSDKEHFVVPYFPDRVEFTRPQVPMATYAPGDWQEIREDIVEADKTSYGVIVNTYQELEPAYANDYKEARSGKAWTIGPVSLCNKVGADKAERGNKADIDQDECLKWLDSKEEGSVLYVCLGSNCSVPLSQLKELGLGLEESQRPFIWVVRGWEKNKELLEWFSESGFEERVKDRGLLIKGWSPQMLILAHHSVGGFLTHCGWNSTLEGITSGIPLLTWPLIVDQFCNQKLVVQVLKVGVSAGVEEVTNWGEEEKIGVLVDKEGVKKAVEELMGESDDAKERRKRVKALGQLAHKAVEEGGSSHSNITSLLEDIMQLAQSNN | 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 | MEKGDTHILVFPFPSQGHINPLLQLSKRLIAKGIKVSLVTTLHVSNHLQLQGAYSNSVKIEVISDGSEDRLETDTMRQTLDRFRQKMTKNLEDFLQKAMVSSNPPKFILYDSTMPWVLEVAKEFGLDRAPFYTQSCALNSINYHVLHGQLKLPPETPTISLPSMPLLRPSDLPAYDFDPASTDTIIDLLTSQYSNIQDANLLFCNTFDKLEGEIIQWMETLGRPVKTVGPTVPSAYLDKRVENDKHYGLSLFKPNEDVCLKWLDSKPSGSVLYVSYGSLVEMGEEQLKELALGIKETGKFFLWVVRDTEAEKLPPNFVESVAEKGLVVSWCSQLEVLAHPSVGCFFTHCGWNSTLEALCLGVPVVAFPQWADQVTNAKFLEDVWKVGKRVKRNEQRLASKEEVRSCIWEVMEGERASEFKSNSMEWKKWAKEAVDEGGSSDKNIEEFVAMLKQT | 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 active constituents of S.grosvenorii fruits, are a mixture of cucurbitane-type triterpenoid glycosides that have been proven to be powerful and zero-caloric sweeteners and can hence be used as a sucrose substitute for diabetic and obese patients. Belongs to the UDP-glycosyltransferase family. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). Is lethal to mice (PubMed:16759681). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. LD(50) is 175 ug/kg by intraperitoneal injection into mice. Belongs to the arthropod phospholipase D family. Class II subfamily. Class IIa sub-subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 lysophosphatidylcholine (LPC) and ceramide phosphoethanolamine (CPE) with low activity (PubMed:24009677, PubMed:25752604). In vivo, shows potent insecticidal activities (PubMed:22561243). On mammals, induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline N-hexanoyl-sphing-4-enine-1-phosphocholine = choline + N-(hexanoyl)-sphing-4-enine-1,3-cyclic phosphate N-(dodecanoyl)-sphing-4-enine-1-phosphocholine = choline + N-dodecanoyl-sphing-4-enine-1,3-cyclic phosphate a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline 1-tetradecanoyl-sn-glycero-3-phosphocholine = 1-tetradecanoyl-sn-glycero-2,3-cyclic phosphate + choline 1-octanoyl-sn-glycero-3-phosphocholine = 1-octanoyl-sn-glycero-2,3-cyclic phosphate + choline 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-sn-glycero-2,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine N-dodecanoyl-heptadecasphing-4-enine-1-phosphoethanolamine = ethanolamine + N-dodecanoyl-heptadecasphing-4-enine-1,3-cyclic phosphate Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. PD(50) is 2.27 +-0.43 ug/g when injected into cricket (Acheta domestica) (observed at 60 minutes). LD(50) is 2.27 +-0.43 ug/g when injected into cricket (Acheta domestica) (observed at 24 hours). Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects catalytic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
Q63332 | MRRNQLPIPVFLLLLLLLPRDATAATGKPRYVVLVPSELYAGVPEKVCVHLNHLNETVTLNVTLEYGVQYSNLLIDQAVDKDSSYCSSFTISRPLSPSALIAVEIKGPTHHFIKKKSMWITKAESPVFVQTDKPIYKPGQTVKFRVVSVDISFRPVNETFPVVYIENPKRNRIFQWQNVDLPGGLHQLSFPLSVEPALGIYKVVVQKDSGKKIEHSFEVKEYVLPKFEVQVKMPKTMAFLEEELVVTACGLYTYGKPVPGLVTMKVCRKYTQSYSNCHGQHSKSICEEFSKQADEKGCFRQVVKTKVFQPRQKGYDMKIEVEAKIKEDGTGIELTGTGSCEIANTLSKLKFTKANTFYRPGLPFFGQVLLVDEKGQPIPNKNLTVQVNSVRSQFTFTTDEHGLANILIDTTNFTFSFMGIRVIYKQNNICFDNWWVDEYHTQADHSAARIFSPSRSYIQLELVLGTLACGQTQEIRIHFLLNEDALKDAKDLTFYYLIKARGSIFNSGSHVLPLEQGKVKGVVSFPIRVEPGMAPVAKLIVYTILPNEELIADVQKFDIEKCFANTVNLSFPSAQSLPASDTHLTVKATPLSLCALTAVDQSVLLLKPEAKLSPQSIYNLLPQKAEQGAYLGPLPYKGGENCIKAEDITHNGIVYTPKQDLNDNDAYSVFQSIGLKIFTNTRVHKPRYCPMYQAYPPLPYVGEPQALAMSAIPGAGYRSSNIRTSSMMMMGASEVAQEVEVRETVRKYFPETWIWDMVPLDLSGDGELPVKVPDTITEWKASAFCLSGTTGLGLSSTISHKVFQPFFLELTLPYSVVRGEAFILKATVLNYMPHCIRIHVSLEMSPDFLAVPVGSHEDSHCICGNERKTVSWAVTPKSLGEVNFTATAEALQSPELCGNKVAEVPALVQKDTVVKPVIVEPEGIEKEQTYNTLLCPQDAELQENWTLDLPANVVEGSARATQSVLGDILGSAMQNLQNLLQMPYGCGEQNMVLFVPNIYVLEYLNETQQLTEAIKSKAISYLISGYQRQLNYQHSDGSYSTFGDRGMRHSQGNTWLTAFVLKAFAQAQSYIYIEKTHITNAFNWLSMKQRENGCFQQSGSLLNNAMKGGVDDEVTLSAYITIALLEMPLPVTHSVVRNALFCLETAWASISNSQESHVYTKALLAYAFALAGNRAKRSEVLESLNKDAVNEEESVHWQRPKNVEENVREMRSFSYKPRAPSAEVEMTAYVLLAYLTSASSRPTRDLSSSDLTTASKIVKWISKQQNSHGGFSSTQDTVVALQALSKYGAATFTKSNKEVSVTIESSGTVSGTLHVNNGNRLLLQEVRLADLPGNYITKVSGSGCVYLQTSLKYNILPEAEGEAPFTLKVNTLPLNFDKAEHHRKFQIHINVSYIGERPNSNMVIVDVKMVSGFIPVKPSVKKLQDQSNIQRTEVNTNHVLIYIEKLTNQTMGFSFAVEQDIPVKNLKPAPVKVYDYYETDEFAIEEYSAPFSSDSEQGNA | 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 proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). Homotetramer; disulfide-linked. Widely expressed. Highest level in ovary, testis, uterus and prostate. Protein found in plasma. Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. |
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 phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
Q9UQ58 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | 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 through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (PubMed:17062754, PubMed:23011729). Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Amyloid-beta protein 42 is a more effective reductant than amyloid-beta protein 40. Amyloid-beta peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. APP42-beta may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity. Also binds GPC1 in lipid rafts. Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and, NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons. Amyloid-beta associates with HADH2. Soluble APP binds, via its N-terminal head, to FBLN1. Interacts with CPEB1 and AGER (By similarity). Interacts with ANKS1B and TNFRSF21. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions (PubMed:25122912). Can form homodimers; this is promoted by heparin binding. Amyloid-beta protein 40 interacts with S100A9. CTF-alpha product of APP interacts with GSAP. Isoform APP695 interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (PubMed:16174740, PubMed:16407538, PubMed:17855360, PubMed:24523320). The C99 fragment also interacts with SORL1 (PubMed:16407538). Isoform APP751 interacts with SORL1 (PubMed:16174740). Isoform APP770 interacts with SORL1 (PubMed:16174740). Interacts with PLD3. Interacts with VDAC1 (PubMed:25168729). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (PubMed:11689470). Interacts with SYT7 (By similarity). Interacts (via transmembrane region) with PSEN1; the interaction is direct (PubMed:30630874). Interacts with LRRK2 (PubMed:28720718). Interacts (via cytoplasmic domain) with KIF5B (PubMed:23011729). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (PubMed:14527950, PubMed:8855266). Interacts (via intracellular domain) with APBB3 (PubMed:10081969). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles (PubMed:20580937). During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body (PubMed:10341243). Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions. Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65) (PubMed:11544248). In dopaminergic neurons, the phosphorylated Thr-743 form is localized to the nucleus (By similarity). Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms. Expressed in the brain and in cerebrospinal fluid (at protein level) (PubMed:2649245). Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex-opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra-striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes. Increased levels during neuronal differentiation. The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1. The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells. The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization. The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis. The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers. The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2. Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro) (PubMed:30630874). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE (PubMed:11604391, PubMed:16154999). Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase and all terminating at Gln-686. Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either CASP6, CASP8 or CASP9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides. N-glycosylated (PubMed:2900137). N- and O-glycosylated (PubMed:2649245). O-glycosylation on Ser and Thr residues with core 1 or possibly core 8 glycans. Partial tyrosine glycosylation (Tyr-681) is found on some minor, short amyloid-beta peptides (amyloid-beta 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but not found on amyloid-beta protein 38, amyloid-beta protein 40 nor on amyloid-beta protein 42. Modification on a tyrosine is unusual and is more prevelant in AD patients. Glycans had Neu5AcHex(Neu5Ac)HexNAc-O-Tyr, Neu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr and O-AcNeu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr structures, where O-Ac is O-acetylation of Neu5Ac. Neu5AcNeu5Ac is most likely Neu5Ac 2,8Neu5Ac linked. O-glycosylations in the vicinity of the cleavage sites may influence the proteolytic processing. Appicans are L-APP isoforms with O-linked chondroitin sulfate. Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific (PubMed:10341243). Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins (PubMed:10341243). Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta (PubMed:8131745, PubMed:11146006). The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members (PubMed:11517218). In dopaminergic (DA) neurons, phosphorylation on Thr-743 by LRKK2 promotes the production and the nuclear translocation of the APP intracellular domain (AICD) which induces DA neuron apoptosis (PubMed:28720718). Phosphorylation on Tyr-757 is required for SHC binding (PubMed:11877420). Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin (PubMed:8999878). Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. In vitro, the APP-Cu(+) complex in the presence of hydrogen peroxide results in an increased production of amyloid-beta-containing peptides. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). Amyloid-beta peptides are degraded by IDE. Sulfated on tyrosine residues. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between amyloid-beta molecules resulting in amyloid-beta-metal aggregates. The affinity for copper is much higher than for other transient metals and is increased under acidic conditions. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding. A major isoform. The L-isoforms are referred to as appicans. A major isoform. The L-isoforms are referred to as appicans. The L-isoforms are referred to as appicans. A major isoform. Belongs to the APP family. Contamination by an Alu repeat. APP mutations Amyloid beta entry |
Q95KN7 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSVMSQSLRKTTREPLTRDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | 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-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron (By similarity). The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons (By similarity). Amyloid-beta associates with HADH2 (By similarity). Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Amyloid-beta protein 40 interacts with S100A9 (By similarity). CTF-alpha product of APP interacts with GSAP (By similarity). Isoform APP695 interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). Isoform APP770 interacts with SORL1 (By similarity). The C99 fragment also interacts with SORL1 (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity). Interacts with LRRK2 (By similarity). Interacts (via cytoplasmic domain) with KIF5B (By similarity). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (By similarity). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions. Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated Thr-743 form is localized to the nucleus (By similarity). Additional isoforms seem to exist. The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1. The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells. The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization. The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis. The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers. The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2. Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase. Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides. N- and O-glycosylated. Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. In dopaminergic (DA) neurons, phosphorylation on Thr-743 by LRKK2 promotes the production and the nuclear translocation of the APP intracellular domain (AICD) which induces DA neuron apoptosis. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). Amyloid-beta peptides are degraded by IDE. Sulfated on tyrosine residues. Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between amyloid-beta molecules resulting in amyloid-beta-metal aggregates. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding. Belongs to the APP family. |
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-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Interacts with LRRK2 (By similarity). Interacts (via cytoplasmic domain) with KIF5B (By similarity). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (By similarity). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Experimental confirmation may be lacking for some isoforms. The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2. Belongs to the APP family. |
Q99K32 | MLPSLALLLLAAWTVRALEVPTDGNAGLLAEPQIAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDSVDSADAEEDDSDVWWGGADTDYADGGEDKVVEVAEEEEVADVEEEEADDDEDVEDGDEVEEEAEEPYEEATERTTSTATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCVPFFYGGCGGNRNNFDTEEYCMAVCGSVSTQSLLKTTSEPLPQDPDKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPHHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHPFGVDSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFGHDSGFEVRHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | 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-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons (By similarity). Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse amyloid-beta peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Amyloid-beta protein 42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also binds GPC1 in lipid rafts (By similarity). The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1, NUMB and DAB1. Binding to DAB1 inhibits its serine phosphorylation. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1 (By similarity). In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1 (By similarity). Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons (By similarity). Amyloid-beta associates with HADH2 (By similarity). Interacts with ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with CPEB1. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Amyloid-beta protein 40 interacts with S100A9 (By similarity). CTF-alpha product of APP interacts with GSAP (By similarity). Isoform APP695 interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (PubMed:16174740, PubMed:16407538). The C99 fragment also interacts with SORL1 (PubMed:16407538). Isoform APP751 interacts with SORL1 (PubMed:16174740). Isoform APP770 interacts with SORL1 (PubMed:16174740). Interacts with PLD3 (By similarity). Interacts with VDAC1 (PubMed:25168729). Interacts with NSG1; could regulate APP processing (PubMed:21084623). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts with SYT7 (PubMed:30429473). Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity). Interacts with LRRK2 (PubMed:28720718). Interacts (via cytoplasmic domain) with KIF5B (By similarity). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (PubMed:18650440). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment (By similarity). Associates with GPC1 in perinuclear compartments (PubMed:15677459). Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions (By similarity). Upon neuronal activation, routed into BACE1-positive recycling endosomes via a clathrin -dependent mechanism (PubMed:23931995). Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65) (By similarity). In dopaminergic neurons, the phosphorylated Thr-743 form is localized to the nucleus (PubMed:28720718). Additional isoforms seem to exist. Expressed in the brain with expression in cortex, cerebellum, hippocampus, olfactory bulb, neurons, astrocytes and microglia (at protein level) (PubMed:25757569, PubMed:26260791, PubMed:28720718). Expressed in the retinal lens (PubMed:25757569). Expressed at a low level in muscle cells (at protein level) (PubMed:25757569). Expressed in kidney. Widely expressed (PubMed:8510506). Expressed in several different brain regions including hippocampus, substantia nigra pars compacta and cerebellum (PubMed:8510506). Within the cerebellum, abundantly expressed in Purkinje cells (PubMed:8510506). Expressed in the brain, kidney and liver (PubMed:8510506). Expressed in several different brain regions including hippocampus, substantia nigra pars compacta and cerebellum (PubMed:8510506). Within the cerebellum, abundantly expressed in Purkinje cells (PubMed:8510506). Expressed in several different brain regions including hippocampus, substantia nigra pars compacta and cerebellum (PubMed:8510506). Within the cerebellum, abundantly expressed in Purkinje cells (PubMed:8510506). Expressed in 4 to 24 week old mice. Up-regulated in animals on a high-fat diet compared to a regular diet. The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1. The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells. The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization. The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis. The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers. The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2. Proteolytically processed under normal cellular conditions (PubMed:11553691, PubMed:23931995). Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99 (PubMed:11553691, PubMed:23931995). Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase (By similarity). Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either CASP6, CASP8 or CASP9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides. N- and O-glycosylated. Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific (By similarity). Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins (By similarity). Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta (By similarity). The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members (By similarity). In dopaminergic (DA) neurons, phosphorylation on Thr-743 by LRKK2 promotes the production and the nuclear translocation of the APP intracellular domain (AICD) which induces DA neuron apoptosis (PubMed:28720718). Phosphorylation on Tyr-757 is required for SHC binding (By similarity). Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP (By similarity). This phosphorylation is inhibited by heparin (By similarity). Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). Amyloid-beta peptides are degraded by IDE. Sulfated on tyrosine residues. Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between amyloid-beta molecules resulting in amyloid-beta-metal aggregates. Rat and mouse amyloid-beta peptides have an arginine residue substituted for the bridging histidine residue and are thus less capable of forming amyloid aggregates. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding (By similarity). Belongs to the APP family. |
Q5IS80 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSVMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | 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-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron (By similarity). The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons (By similarity). Amyloid-beta associates with HADH2 (By similarity). Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Amyloid-beta protein 40 interacts with S100A9 (By similarity). CTF-alpha product of APP interacts with GSAP (By similarity). Interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). The C99 fragment also interacts with SORL1 (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity). Interacts with LRRK2 (By similarity). Interacts (via cytoplasmic domain) with KIF5B (By similarity). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (By similarity). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions. Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated Thr-743 form is localized to the nucleus (By similarity). The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1. The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells. The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization. The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis. The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers. The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2. Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase. Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides. N- and O-glycosylated. Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. In dopaminergic (DA) neurons, phosphorylation on Thr-743 by LRKK2 promotes the production and the nuclear translocation of the APP intracellular domain (AICD) which induces DA neuron apoptosis. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). Amyloid-beta peptides are degraded by IDE. Sulfated on tyrosine residues. Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between amyloid-beta molecules resulting in amyloid-beta-metal aggregates. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding. Belongs to the APP family. |
Q9TUI0 | MLPGLALVLLAAWTARALEVPTDGNAGLLAEPQVAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRSRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNIDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVADVEEEEAEDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSVMSQSLLKTTQEHLPQDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHPFGVDSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | 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-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron (By similarity). The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons (By similarity). Amyloid-beta associates with HADH2 (By similarity). Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Amyloid-beta protein 40 interacts with S100A9 (By similarity). CTF-alpha product of APP interacts with GSAP (By similarity). Interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). The C99 fragment also interacts with SORL1 (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity). Interacts with LRRK2 (By similarity). Interacts (via cytoplasmic domain) with KIF5B (By similarity). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (By similarity). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions. Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated Thr-743 form is localized to the nucleus (By similarity). The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1. The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells. The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization. The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis. The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers. The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2. Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase. Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides. N- and O-glycosylated. Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. In dopaminergic (DA) neurons, phosphorylation on Thr-743 by LRKK2 promotes the production and the nuclear translocation of the APP intracellular domain (AICD) which induces DA neuron apoptosis. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin. Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). Amyloid-beta peptides are degraded by IDE. Sulfated on tyrosine residues. Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between amyloid-beta molecules resulting in amyloid-beta-metal aggregates. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding. Belongs to the APP family. |
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-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts with LRRK2 (By similarity). Interacts (via cytoplasmic domain) with KIF5B (By similarity). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (By similarity). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated form is localized to the nucleus (By similarity). Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase. Belongs to the APP family. |
Q547B7 | MLPSLALLLLAAWTVRALEVPTDGNAGLLAEPQIAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDSIDSADAEEDDSDVWWGGADTDYADGGEDKVVEVAEEEEVADVEEEEAEDDEDVEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSVSSQSLLKTTSEPLPQDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPHHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHPFGVDSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFGHDSGFEVRHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | 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-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o)-alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse amyloid-beta peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Amyloid-beta protein 42 may activate mononuclear phagocytes in the brain and elicits inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also binds GPC1 in lipid rafts (By similarity). Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons (By similarity). Amyloid-beta associates with HADH2 (By similarity). Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Amyloid-beta protein 40 interacts with S100A9 (By similarity). CTF-alpha product of APP interacts with GSAP (By similarity). Isoform APP695 interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). The C99 fragment also interacts with SORL1 (By similarity). Isoform APP751 interacts with SORL1 (By similarity). Isoform APP770 interacts with SORL1 (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts with SYT7 (By similarity). Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity). Interacts with LRRK2 (By similarity). Interacts (via cytoplasmic domain) with KIF5B (PubMed:23011729). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (By similarity). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. APP sorts to the basolateral surface in epithelial cells (By similarity). During neuronal differentiation, the Thr-742 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body (PubMed:10341243). Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions (By similarity). Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65) (By similarity). In dopaminergic neurons, the phosphorylated Thr-743 form is localized to the nucleus (By similarity). Expressed in the brain (PubMed:23011729). In the brain, non-L-APP isoforms are expressed in neurons, isoform APP695 being the predominant form. In astrocytes and microglial cells, almost 50% is L-isoform (appican). From 6 days to 7 months, levels of KPI-containing isoforms increase in the brain cortex and hippocampus. Levels of L-APP increase in all brain regions during the same period, but levels are low compared to non-L-APP isoforms. Phosphorylation of mature, glycosylated APP occurs 48-72 hours after treatment of neuronal cells with nerve growth factor which correlates with the timing of neurite outgrowth. The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1. The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells. The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization. The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis. The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers. The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2. Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase. Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides. N-glycosylated. O-glycosylated. O-linkage of chondroitin sulfate to the L-APP isoforms produces the APP proteoglycan core proteins, the appicans. The chondroitin sulfate chain of appicans contains 4-O-sulfated galactose in the linkage region and chondroitin sulfate E in the repeated disaccharide region. Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific (PubMed:9085254, PubMed:10329382, PubMed:10341243). Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins (PubMed:10341243). Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta (PubMed:10936190). The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members (By similarity). In dopaminergic (DA) neurons, phosphorylation on Thr-743 by LRKK2 promotes the production and the nuclear translocation of the APP intracellular domain (AICD) which induces DA neuron apoptosis (By similarity). Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP (By similarity). This phosphorylation is inhibited by heparin (By similarity). Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). Amyloid-beta peptides are degraded by IDE. Sulfated on tyrosine residues. Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between amyloid-beta molecules resulting in amyloid-beta-metal aggregates. Rat and mouse amyloid-beta peptides have an arginine residue substituted for the bridging histidine residue and are thus less capable of forming amyloid aggregates. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding (By similarity). L-isoforms are referred to as appicans. L-isoforms are referred to as appicans. L-isoforms are referred to as appicans. L-isoforms are referred to as appicans. Belongs to the APP family. |
Q95241 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRDRKQCKTHPHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDHVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSVIPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | 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-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron (By similarity). The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons (By similarity). Amyloid-beta associates with HADH2 (By similarity). Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Amyloid-beta protein 40 interacts with S100A9 (By similarity). CTF-alpha product of APP interacts with GSAP (By similarity). Isoform APP695 interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). Isoform APP770 interacts with SORL1 (By similarity). The C99 fragment also interacts with SORL1 (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity). Interacts with LRRK2 (By similarity). Interacts (via cytoplasmic domain) with KIF5B (By similarity). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (By similarity). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions. Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated Thr-724 form is localized to the nucleus (By similarity). Additional isoforms seem to exist. The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1. The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells. The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization. The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis. The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers. The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2. Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase. Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-720 by either caspase-3, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides. N- and O-glycosylated. Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-724 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-724 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. In dopaminergic (DA) neurons, phosphorylation on Thr-724 by LRKK2 promotes the production and the nuclear translocation of the APP intracellular domain (AICD) which induces DA neuron apoptosis. Phosphorylation on Tyr-738 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). Amyloid-beta peptides are degraded by IDE. Sulfated on tyrosine residues. Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between amyloid-beta molecules resulting in amyloid-beta-metal aggregates. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding. Belongs to the APP family. |
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-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts with LRRK2 (By similarity). Interacts (via cytoplasmic domain) with KIF5B (By similarity). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (By similarity). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated form is localized to the nucleus (By similarity). Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase. Belongs to the APP family. |
O93279 | MGETTAFVLLLVATLTRSSEIPADDTVGLLTEPQVAMFCGKLNMHINVQNGKWESDPSGTKSCLNTKEGILQYCQEVYPELQITNVVEANQPVSIQNWCKKGRKQCRSHTHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMNQCESHLHWHTVAKESCGDRSMNLHDYGMLLPCGIDRFRGVKFVCCPAETEQETDSSEVEGEESDVWWGGADPEYSENSPPTPSRATYVAGDAFERDENGDGDEDEEDDEDVDPTDEQESDERTANVAMTTTTTTTTESVEEVVRAVCWAQAESGPCRAMLERWYFNPKKRRCVPFLFGGCGGNRNNFESEEYCLAVCSSSLPTVAPSPPDAVDQYFEAPGDDNEHADFRKAKESLEAKHRERMSQVMREWEEAERQAKNLPRADKKAVIQHFQEKVEALEQEAAGERQQLVETHMARVEALLNSRRRLTLENYLGALQANPPRARQVLSLLKKYVRAEQKDRQHTLKHYEHVRTVDPKKAAQIRPQVLTHLRVIDERMNQSLALLYKVPSVASEIQNQIYPAAGSDCKDPVEHCVCPQVDGLVSYGNDALMPDQAYSSAPMDMGVDGLGSIDQSFNQANTENHVEPVDARPIPDRGLPTRPVSSLKLEEMPEVRTETDKRQSAGYEVYHQKLVFFADDVGSNKGAIIGLMVGGVVIATVIVITLVMLRKKQYTSIHHGVIEVDAAVTPEERHLARMQQNGYENPTYKFFEQMQN | Functional neuronal receptor which couples to intracellular signaling pathway through the GTP-binding protein G(O). Belongs to the APP family. |
O73683 | MGHSVAWLLLVAAASTLAAEVPTDVSMGLLAEPQVAMFCGKINMHINVQSGKWEPDPSGTKSCIGTKEGILQYCQEVYPELQITNVVEANQPVSIQNWCKKGRKQCRSHMHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMNQCESHLHWHTVAKESCGDRAMNLHDYGMLLPCGIDRFRGVEFVCCPAEAERDMDSTEKDADDSDVWWGGADNDYSDNSMVREPEPAEQQEETRPSVVEEEEEGEVAQEDDEEEEEVLDTDQDGDGEEDHEAADDEEEEEDVDEIDAFGESDDVDADEPTTNVAMTTTTTTTTTESVEEVVRMFCWAHADTGPCTASMPSWYFDAVDGRTMYELMYGGCGGNMNNFESEEYCLSVCSSVVPTDMPSSPDAVDHYLETPADENEHAHFQKAKESLEAKHRERMSQVMREWEEAERQAKNLPRADKKIVIQRFQEKVEALEQEAASERQQLVETHMARVEALLNDRRRLALENYLTALQQDPPRPRHVFSLLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRPQVLTHLRVIEERMNQSLGLLYKVPGVADDIQDQVELLQREQAEMAQQLANLQTDVRVSYGNDALMPDQELGDGQADLLPQEDTLGGVGFVHPESFNQLNTENQVEPVDSRPTFERGVPTRPVTGKSMEAVPELRMETEDRQSTEYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLRKKQYTSIHHGIIEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | 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-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts with LRRK2 (By similarity). Interacts (via cytoplasmic domain) with KIF5B (By similarity). Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus) (By similarity). Interacts (via intracellular domain) with APBB3 (By similarity). Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Associates with FPR2 at the cell surface and the complex is then rapidly internalized. Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated form is localized to the nucleus (By similarity). Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase. Belongs to the APP family. |
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 phosphatase. Belongs to the chordopoxvirinae A4 family. |
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 phosphatase. Belongs to the chordopoxvirinae A4 family. |
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 phosphatase. Belongs to the chordopoxvirinae A4 family. |
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 act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, massive inflammatory response, platelet aggregation, increased vascular permeability, and causes edema and death in mice (PubMed:18082635). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. Class IIa sub-subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation. |
Q89181 | MDGVIVYCLNALVKHGEEINHIKNDFMIKPCCEKVKNVHIGGQSKNNTVIADLPYMDNAVSDVCNSLYKKNVSRISRFANLIKIDDDDKTPTGVYNYFKPKDAIPVIISIGKDRDVCELLISSDKACACIELNSYKVAILPMDVSFFTKGNASLIILLFDFSIDAAPLLRSVTDNNVIISRHQRLHDELPSSNWFKFYISIKSDYCSILYMVVDGSVMHAIADNRTYANISKNILDNTTINDECRCCYFEPQIRILDRDEMLNGSSCDMNRHCIMMNLPDVGEFGSSMLGKYEPDMIKIALSVAGIWKVL | Belongs to the poxviridae A51 protein family. |
B4TUM9 | MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKKLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
Q7C7F5 | MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLIAPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSAEKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
Q8ZMA4 | MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENSRGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
B2TYQ5 | MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDASRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWIDEAEQHDE | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
Q0T128 | MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPDLVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
Q7C061 | MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPDLVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
Q3YY21 | MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
A1JPF0 | MAYRLLRALFRGLFRVTIDGITDQFSHQKLIITPNHVSFLDGALLALFLPIKPVFAVYSNITESWYMRWLKPYVDFVALDPTKPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLEGPEFTRFGRLGDVLKVRWFPKISIHVLPATTLPMPQAPRARDRRVLAGERLHAIMMAARMAIVPRETLFEALLSAQTRYGRFKPCIEDISFKEDSYQTLLKKILGVSRILQRFTAQGEHVGMLLPNATITAAAIFGATLRGRIPALLNYTSGAKGLKSAITAASLKTIITSRQFLEKGKLTHLPEQVTEANWVYLEDLKDTVTLADKLWILFHLCCPRRAMVPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARLRYVVAGAEKLADSTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMESRVIPVPGIEQGGRLQLRGPNIMRGYLRVEKPGVLEQPSAENTQGEQEAGWYDTGDIVAIDEQGFCTIRGRMKRFAKLAGEMVSLESVEQLVLRISPEGQHAAATKTDSAKGEALVLFTTDSEITREKLVKAARESGVPELAVPRDIRVVKALPLLGSGKPDFVTLSKMAEDPEMSA | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
A7FFD1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKAARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
Q1CAS8 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
B2JZ75 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKAARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
Q8ZHU1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
A9R2S1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
A4TLD3 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
Q667F1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKAARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |
B1JQC1 | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKAARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV | 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 reactions or degradation by phospholipase A1. a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP] a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. |