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stringlengths 6
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stringlengths 11
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A3PDP9 | MKLKSLLSVFTISIVALTSACSTKNAGPSADPDKLIVALIPDENAATVIQDNQGLKDYLTEAFDKEIELVVTTDYSSMIEAARNDRLDLAYFGPLSYVLAKAVSDIEPFAARIKGGTKTYNSCIIGNTKKGVTSFDDIKGTTFALGDPASTSSRLFPELTLAENGLTKGKDFQGVFLGSHDAVALAVQNGNAQAGGMACPILKSLKKKGVIDPSKVTTIAQSSPIPQYPWTMRSTLSPELKEKIRFTFLDLDSDKVLKPFNADGFASITDSDYDGIRKAGKLLGLDLSKFVK | Function: Probably part of the ABC transporter complex PhnC2D2E2. Binds strongly to methylphosphonate (MPn), ethylphosphonate (EPn) and inorganic phosphite.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31304
Sequence Length: 292
Subcellular Location: Cell membrane
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A0QQ71 | MKIRAHHKIATAAACVALLASACSGSDKPQSTTAEGFPETITLAAIPAENSSDLKASYDPLIKMLEKQTGSKVEFVQASDYAGVVEGMIAGNVDLAFFGPFAYVVAGVNGAKMTPLGAVIKDEGGAPGYQSYGLARADEDNINGLKDFAGKKVCFVDPGSTSGFLYPTAGLIEEGVVKSGSEADISAAMSPIFAGGHDSSALAIANGDCDAGFAFDTMVDKTMIDKGDLKPGQLKTVWKSDMIAGSVFAANDALGPEVIDKLKTMFAQDANVKSFEEEGFCEGDACRITDERAWGVVPVTDADYDGVRHVCDVTGSEKCKG | Function: Part of the ABC transporter complex PhnCDE involved in phosphate import. Responsible for phosphate binding.
Location Topology: Lipid-anchor
Sequence Mass (Da): 33385
Sequence Length: 321
Subcellular Location: Cell membrane
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A0A142C7A2 | MYAFTILGFKRDDMTEDEYHNYISTVHSAHLKALLAQNDIVSYTMQHNTSQTRDDLLNKVYQGQMPAEKVFECDAIIQVVFKTVEDYLRVREDPHFQTVVNPDHVNFAHPTKTRFVMGWHEVHVADGKVVS | Function: Dehydratase; part of the gene cluster that mediates the biosynthesis of phenalenones such as herqueinone, compounds that have been reported to treat tumors, bacterial infections and/or mycoses, and rheumatic diseases . The non-reducing polyketide synthase phnA synthesizes the heptaketide backbone and cyclizes it into the angular, hemiketal-containing naphtho-gamma-pyrone prephenalenone. The product template (PT) domain of phnA catalyzes only the C4-C9 aldol condensation, which is unprecedented among known PT domains . The transformation of prephenalenone to phenalenones requires an FAD-dependent monooxygenase phnB, which catalyzes the C2 aromatic hydroxylation of prephenalenone and ring opening of the gamma-pyrone ring simultaneously . Subsequent intramolecular deprotonation of C3 phenolic oxygen accelerates phenalenone ring closure to yield the tricyclic phenalenone core with a C2 hydroxylation . The prenyltransferase phnF further catalyzes reverse C-prenylation of phenalenone by direct electrophilic substitution at C6, or possibly via first a forward O-prenylation of a neighboring phenol in phenalenone, followed by a Claisen rearrangement . The hydroalkoxylation enzyme phnH catalyzes the 5-exo-trigcyclization via acid catalysis after the spontaneous deprotonation of 7-OH, which leads to the formation of the dihydrobenzofuran atrovenetin . Atrovenetin is further converted to deoxyherqueinone by the O-methyltransferase phnC which can methylate C2-OH to stabilize the northern portion of the phenalenone core . Finally, the oxidoreductase phnG converts deoxyherqueinone to herqueinone via C6 hydroxylation .
Sequence Mass (Da): 15212
Sequence Length: 131
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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P0DP69 | MPDAVQAPYPAYRPEPNMQTITIAPPKRSWFSLLSWAVVLAVLVVSWQGAEMAPLTLIKDGGNMATFAADFFPPDFSQWQDYLTEMAVTLQIAVWGTALAVVLSIPFGLMSAENLVPWWVYQPVRRLMDACRAINEMVFAMLFVVAVGLGPFAGVLACWRCLSTPPACSPSCFPKRWKRLSPARWKAFAPPVPTSSKRSSTACCHR | Function: N-terminal fragment of the PhnE protein, part of a phosphonate usage operon that is cryptic in K12 strains. Growth of K12 strains on phosphonate can be observed when it is used as the sole phosphorus source after a 60 hour lag period, suggesting the operon is activated . An intact PhnE in strain B is (AC A0A140NFA3). Part of the binding-protein-dependent transport system for phosphonates; probably responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22797
Sequence Length: 206
Subcellular Location: Cell inner membrane
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P0DP70 | MLALFIHTTGVLSKLLSEAVEAIEPGPVEGIRATGANKLEEILYGVLPQVMPLLISYSLYRFESNVRSATVVGMVGAGGIGVTLWEAIRGFQFQQTCALMVLIIVTVSLLDFLSQRLRKHFI | Function: C-terminal fragment of the PhnE protein, part of a phosphonate usage operon that is cryptic in K12 strains. Growth of K12 strains on phosphonate can be observed when it is used as the sole phosphorus source after a 60 hour lag period, suggesting the operon is activated . An intact PhnE in strain B is (AC A0A140NFA3). Part of the binding-protein-dependent transport system for phosphonates; probably responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13335
Sequence Length: 122
Subcellular Location: Cell inner membrane
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Q7ZAP3 | MNRIHAVILDWAGTTVDFGSFAPTQIFVEAFRQAFDVEITLAEARVPMGLGKWQHIEALGKLPAVDARWQAKFGRSMSAADIDAIYAAFMPLQIAKVVDFSSPIAGVIDTIAALRAEGIKIGSCSGYPRAVMERLVPAAAGHGYRPDHWVATDDLAAGGRPGPWMALQNVIALGIDAVAHCVKVDDAAPGISEGLNAGMWTVGLAVSGNEFGATWDAYQTMSKEDVAVRREHAASKLYAAGAHYVVDSLADLPGVIAHINARLAQGERP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 28574
Sequence Length: 269
EC: 3.11.1.1
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A0LMC1 | MEIFVRNKPYTGPVKAVVLDWAGTTVDFGCMAPVTAFIEAFALRGVEISASEVRGPMGLMKMDHVRALCGLPSVSERWRELFGRIPNEDDVRLVYGDTVPLMVLSVADHAELIPGLLPAIGYFRGNGIKIGTSTGYTTPMMEVLLPRAEKRGYRPDSVVCSSDVPRGRPFPFMCYRNAIDLEVYPLEAVVKIGDTVSDIREGLNAGMWTIGVSKSGSDLGLTEAELDALPADDLRNRLALVESRFLEAGAHFVVEHIGRCPEIIEEINDLLSQGEVP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 30294
Sequence Length: 277
EC: 3.11.1.1
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Q87JL6 | MSNSPIQAVIFDWAGTIVDFGSFAPTSIFVEAFKQGFDFDIDLEEAREPMGLGKWDHIQAVGRIPAVDKRWNEKFGRSMTNEDIDAIYAAFMPLQKAKVADHAEPILNAVEVVNGLKDKGIKIGSCSGYPREVMDVLIPVAADYGYQPDYVVATDDLPQGGRPAPFMALKNVIELDVTDVKACVKVDDSAPGIFEGHNAGMWTVGLLLSGNEAGLTFEEYQAADEATLEKAREKARAKFIKSAPHYLIDTISDLPEVIVDIEQRLAAGERP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 29649
Sequence Length: 271
EC: 3.11.1.1
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Q6E0X0 | MNRYSRRSRHPNPPVPNQEEPERDPNHIDQDLADLAQPLVLKERHAVMAPTQPSLSDVINEERQAPITFGNPPEVMANARLSALGYDNLTEREKRILAVGVRCGEAAKDYHSLTTTKKWIEDELKSQMVALASSTRTLTEAASLHTTFAMLHSPSIKRKAEAMSHISQGEESIDISKLNKTGMEDIWVAMESESKEDAVDTYLRNILEVDPTQFYAIDGWGLYLDFIPTWHYIAAGKNSAQFKTSYADEIVEQRAAFERVLSKRPRVEI | Function: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA (By similarity).
PTM: Phosphorylated by host kinases.
Sequence Mass (Da): 30420
Sequence Length: 269
Subcellular Location: Virion
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Q5MKM7 | MEKFAPEFVGEDANKKAEEFLKHRSFPSEKPLAGIPNTATHVTKYNMPPILRSSFKLPSPRVAANLTEPSAPPTTPPPTPPQNKEEQPKESDVDIETMHVCKVPDNPEHSKKPCCSDDTDTKKTRKPMVTFVEPEEKFVGLGASLYRETMQTFAADGYDEESNLSFEETNQEPGSSSVEQRLDRIEEKLSYIIGLLNTIMVATAGPTTARDEIRDALIGTREELIEMIKSDILTVNDRIVAMEKLRDEECSRADTDDGSACYLTDRARILDKIVSSNAEEAKEDLDVDDIMGINF | Function: Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins. Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex. Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA. Acts as a chaperone for neo-synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs. Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription.
PTM: Constitutively phosphorylated by host.
Sequence Mass (Da): 32913
Sequence Length: 295
Domain: The N-terminus is important for viral particle assembly. The oligomerization region is central. The C-terminus part contains binding regions for the RNA-directed RNA polymerase L and the nucleoprotein.
Subcellular Location: Virion
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Q9JGU0 | MDKKASGISGENALFGDVPNDVVGTTYEMGLDGIFDDGETDVIESPADAEEHVTTDIVADEGDNLITKVDDMIGYLKRECQDHGIAVRKEWVNVLTRKFHMSKKIYASHLDFFLLGVMGERHVAVEKDFKDTAVRLSDEVNKMSGISKKVADNETRMIKELDAKMKEMGSLIGKFNGVLNEFKGSMAVSSRPASVASWALDQTTETSREKNYNEFLKKLGFQDHHIKSPLMKKCTVMITDEMYDEVMLENTSEDTLGIYKEQIITYGQSIQKKVEKPIKKDPYADF | Function: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA (By similarity).
PTM: Phosphorylated by host kinases.
Sequence Mass (Da): 32174
Sequence Length: 286
Subcellular Location: Virion
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A9CJC9 | MSLKTAPVIVWFRKDLRLSDNLALLAAVEHGGPVIPVYIREKSAGPLGGAQEWWLHHSLAALSSSLEKAGGRLVLASGDAERILRDLISETGADTVVWNRRYDPTGMATDKALKQKLRDDGLTVRSFSGQLLHEPSRLQTKSGGPYRVYTPFWRALEGSDEPHAPADPPKSLTAPKVWPKSEKLSNWKLLPTKPDWAKDFSDIWTPGETGALDKLDDFIDGALKGYEEGRDFPAKPATSLLSPHLAAGEISPAAVWHATKGLSRHIASNDISRFRKEIVWREFCYHLLFHFPELGEKNWNDSFDAFSWRDDEKSFKAWTRGMTGYPIVDAGMRQLWQHGTMHNRVRMIVASFLIKHLLIDWRKGEKWFRDTLVDADPASNAANWQWVAGSGADASPFFRIFNPILQGEKFDGDGDYVRRFVPELEKLERKYIHKPFEAPKDALKKAGVELGKTYPLPIVDHGKARERALAAYAAVKKTT | Cofactor: Binds 1 FAD per subunit.
Function: Photolyase involved in the repair of UV radiation-induced DNA damage. By using blue-light energy, catalyzes the photoreactivation of cyclobutane pyrimidine dimers (CPDs), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. Can repair CPD lesions in ssDNA as well as in dsDNA.
Catalytic Activity: cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).
Sequence Mass (Da): 53885
Sequence Length: 479
EC: 4.1.99.3
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Q00829 | MKSKWMSGLLLVAVGFSFTQVMVHAGETANTEGKTFHIAARNQT | Function: Signaling molecule involved in the regulation of sporulation . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function . Inhibitor of the RapA phosphatase activity . Does not act on RapB .
PTM: Secreted with a propeptide domain, which is cleaved in the cell wall by the secreted serine proteases subtilisin and Vpr to produce a mature signaling peptide . Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably subject to only one processing event, at the N-terminal end of the mature peptide (Probable).
Sequence Mass (Da): 4797
Sequence Length: 44
Subcellular Location: Secreted
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P11394 | MKTPLTEAVAAADSQGRFLSNTEVQAASGRFNRAKASLEAAKALTSKADSLVNGAAQAVYSKFPYTTQMEGSNYSATPEGKAKCSRDVGYYLRMITYCLVAGGTGPMDDYLIAGLDEINRTFELSPSWYVEALKHIKANHGLSGDAATEANSYIDYAINALI | Function: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.
PTM: Contains one covalently linked bilin chromophore.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17335
Sequence Length: 162
Subcellular Location: Cellular thylakoid membrane
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A9CH39 | MSQLVLILGDQLSPSIAALDGVDKKQDTIVLCEVMAEASYVGHHKKKIAFIFSAMRHFAEELRGEGYRVRYTRIDDADNAGSFTGEVKRAIDDLTPSRICVTEPGEWRVRSEMDGFAGAFGIQVDIRSDRRFLSSHGEFRNWAAGRKSLTMEYFYREMRRKTGLLMNGEQPVGGRWNFDAENRQPARPDLLRPKHPVFAPDKITKEVIDTVERLFPDNFGKLENFGFAVTRTDAERALSAFIDDFLCNFGATQDAMLQDDPNLNHSLLSFYINCGLLDALDVCKAAERAYHEGGAPLNAVEGFIRQIIGWREYMRGIYWLAGPDYVDSNFFENDRSLPVFYWTGKTHMNCMAKVITETIENAYAHHIQRLMITGNFALLAGIDPKAVHRWYLEVYADAYEWVELPNVIGMSQFADGGFLGTKPYAASGNYINRMSDYCDTCRYDPKERLGDNACPFNALYWDFLARNREKLKSNHRLAQPYATWARMSEDVRHDLRAKAAAFLRKLD | Cofactor: Binds 1 FAD per subunit.
Function: Photolyase involved in the repair of UV-induced (6-4) lesions in DNA. Catalyzes the photoreactivation of (6-4) pyrimidine-pyrimidone photoproducts by using blue-light energy. Can repair (6-4) photoproducts in ssDNA as well as in dsDNA.
Catalytic Activity: (6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA).
Sequence Mass (Da): 57864
Sequence Length: 507
EC: 4.1.99.13
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P94416 | MKLKSKLFVICLAAAAIFTAAGVSANAEALDFHVTERGMT | Function: Signaling molecule that serves as a cell density signal for both genetic competence development and sporulation . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function . At low concentrations, CSF stimulates expression of the genes controlled by ComA, a transcriptional factor that regulates the development of genetic competence . It includes the srfA operon, which encodes a small protein, ComS, required for competence development, and the surfactin biosynthetic enzymes . Acts by inhibiting RapC, which regulates the activity of ComA . At high concentrations, it inhibits expression of those same ComA-controlled genes, maybe by inhibiting activity of the kinase ComP . In addition, high concentrations of CSF can stimulate sporulation under some conditions . Also inhibits RapB activity, with lower efficiency, but does not act on RapA . Is probably involved in the quorum sensing control of sporulation (Probable). CSF is a species-specific signaling molecule that partially compensates for the lack of ComX-mediated communication between different strains of B.subtilis .
PTM: Secreted with a propeptide domain, which is cleaved in the cell wall by the secreted serine proteases subtilisin, Epr and Vpr to produce a mature signaling peptide . Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably subject to only one processing event, at the N-terminal end of the mature peptide (Probable).
Sequence Mass (Da): 4198
Sequence Length: 40
Subcellular Location: Secreted
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O32025 | MKSKLFISLSAVLIGLAFFGSMYNGEMKEASRNVTLAPTHEFLV | Function: Signaling molecule involved in the regulation of sporulation . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (Probable). Inhibitor of the RapE phosphatase activity . Does not inhibit the phosphatase activity of RapA and RapB . Probably plays a dispensable role in the overall context of sporulation initiation .
PTM: Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably only subject to processing events at the ends of the mature peptide.
Sequence Mass (Da): 4850
Sequence Length: 44
Subcellular Location: Secreted
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P71001 | MKLKSKLLLSCLALSTVFVATTIANAPTHQIEVAQRGMI | Function: Signaling molecule involved in the regulation of genetic competence development . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Stimulates expression of the genes controlled by ComA, a transcriptional factor that regulates the development of genetic competence . Acts by inhibiting RapF, which regulates the activity of ComA .
PTM: Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably subject to only one processing event, at the N-terminal end of the mature peptide.
Sequence Mass (Da): 4199
Sequence Length: 39
Subcellular Location: Secreted
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O32295 | MKRFLIGAGVAAVILSGWFIADHQTHSQEMKVAEKMIG | Function: Signaling molecule involved in the regulation of expression of DegU-controlled genes . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Stimulates the DegU-dependent expression of aprE, an extracellular alkaline protease . Acts by inhibiting RapG activity . At high concentrations, represses the DegS-dependent aprE expression .
PTM: Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably subject to only one processing event, at the N-terminal end of the mature peptide.
Sequence Mass (Da): 4172
Sequence Length: 38
Subcellular Location: Secreted
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Q59HN7 | MPIKKKVMMCLAVTLVFGSMSFPTLTNSGGFKESTDRNTTYIDHSPYKLSDQKKALS | Function: Signaling molecule involved the regulation of both sporulation and competence . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function . Acts by inhibiting RapH activity . Can inhibit both RapH activities, the dephosphorylation of Spo0F and the sequestration of ComA .
PTM: Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably only subject to processing events at the ends of the mature peptide.
Sequence Mass (Da): 6345
Sequence Length: 57
Subcellular Location: Secreted
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Q8MZS4 | MRLLSLLFLLGLATLSFAVRSQWAQQGRATHEALITIRFALTQQNLDVLERTLLDISDTTSKNYGKWKTAEEVTELVAPAREISERVASFLERQGATKVENFRDMVKVTAPVSWIEETLHTNLFFFQHKTRTSKVIIRADGGYKIPAEIAEHVDFVAGLFEFPSIKNARTQVGAGVDGYIVPYVIFDLYGIPTTFPVHPNSSICLVEFQDDQSYNKDDLKKFAKENEITETVVSHTVGPYSGSSADTESTLDVQYGGAIALNTTVWFWTVEDWMYDFATDFLNTKNPPLVVSMSWGWPEPEQCQVGNCTGDETSLEYVVRTNVEFQKIGAIGTTLLAASGDQGAPGDSDPECNSKKKPLSSIFPGASPWVLSVGATMLSNMTTEDADPSAEPPICKSWTCSTSTTELVCTIPQALITTGGGFSDYSLQPSYQNAAVAAYFKSGVPLPPQTDFNASNRGFPDVSALGHNYLIALSGDFEQVDGTSASTPVFAAIIAHLNSYRLNNGKPPLAFAVPLIYQAFASDPTIFNDITTGDNKCTEDCCSKFGYEATKGWDPVTGVGTPVFSKLLAFVQTLP | Cofactor: Binds 1 Ca(2+) ion per subunit.
PTM: Autocatalytically processed.
Catalytic Activity: Milk clotting activity. Preferential cleavage of 8-Gly-|-Ser-9 in B chain of insulin most rapidly, followed by 11-Leu-|-Val-12, 19-Cys(SO(3)H)-|-Gly and 24-Phe-|-Phe-25. No action on Ac-Phe-Tyr(I)2.
Sequence Mass (Da): 62709
Sequence Length: 575
EC: 3.4.21.103
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Q715L4 | MEEDFNMSTPGVKVGVXEEEKKLSYYKYYEQDLAPVPAEKIAILQGGPIAPEKCIPFDERNKFLKGEDDEYANIGFGVAADGTALVCNTTYMPGVTGEMLDWWFPWHSVGSDLRYKIWDPEDHYFARAYPASYVVDPNVPMNQKTWGVDHYIMEDVGPGPEFLKLCFKRPADFGYDESIIGTEKCESLVCAIGESSCAAAMTHKWHPYKDGVLFESRFWIGYRIDEEGNIVKAIPEGVSIPPFVPQGLFAHNIKEFTNLAAILPTLYAEEKDTF | Function: Catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl)propionic acid during flavonoid degradation. Also hydrolyzes other C-acylated phenols.
Catalytic Activity: H2O + phloretin = 1,3,5-trihydroxybenzene + H(+) + phloretate
Sequence Mass (Da): 30923
Sequence Length: 274
Subcellular Location: Cytoplasm
EC: 3.7.1.4
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B1MK49 | MHPITYYPVDTQRLVRSNAERIRHKPYAHYFNPDVAVPEEVFAALKAPLEPEQVLGTSSTELNRLLEPGYLEGETGYCGLPDGAGYTSSLVRFPGATPEMFRWWFWWHSFEPERYSLWHPWCHADIWRTDPETETAPNLTDEQRYVGSTHHINEYIGQDPLDIEITFIDPARWGFDADGFAAAGIGAHACGSVLMKGSHMRLATMVHLARITDDGFELRSRYWIADRAEPRHDPVAGIAQLTTVPGFSGERQAYEQLVHDQTEFNHLATFLPDIYQEFGPR | Function: Catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl)propionic acid. Can also hydrolyze monoacetylphloroglucinol (MAPG) but not 2,4-diacetylphloroglucinol (DAPG).
Catalytic Activity: H2O + phloretin = 1,3,5-trihydroxybenzene + H(+) + phloretate
Sequence Mass (Da): 32091
Sequence Length: 281
EC: 3.7.1.4
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Q9UBF8 | MGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAVSSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGAAVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM | Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity) . May play an important role in the inner ear development.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 91379
Sequence Length: 816
Subcellular Location: Endomembrane system
EC: 2.7.1.67
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B3EX61 | MGDTAVEPAPLKPASEPAPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVRLLHGAVAVSKRGTALELVNGDGVDTEIRCLDDPPAQIREEEDEMGATVTSGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPALNTGLSPSKRTHQRSKSDATASISLSSSLKRTASNPKVENEDEPIRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAAFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTNVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEMHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFRRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMNMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM | Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity). May play an important role in the inner ear development.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89991
Sequence Length: 801
Subcellular Location: Endomembrane system
EC: 2.7.1.67
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A4IID4 | MGDTMVEPVPAKLSDPTLVLRGNGGSPLCVITEGVGEAQMVIDPDVAEKACQDVLDKVKLIRGSSAESLDKIDGSDTGDGGSLANGDAGPRHSESCGPPVSASRITEEEESLIDINSVKSARRRQKNNSAKQSWLLRLFECKLFDVSMAISYLYNSKEPGVQAYIGNRLFCFRYEDVDFYLPQLLNMYIHMDEDVGDAIKPYVVHRCRQSINFSLQCAWLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHKKREIPPLSLAPDTGLSPSKRTHQRSKSDATVSISLSSNLKRTSSNPKVENDDEPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFETSLVPVRIPENRIRSTRSVENLPECGITHEQRASSFTTVPNYDNDDEAWSVDDIGELQVELPELHTNSCDNISQFSVDSITSQESKDPVFIAAGDIRRRLSEQLAHTPTTFRRDPEDPSAVALKEPWQEKVRRIREGSPYGHFPNWRLLSVIVKCGDDLRQELLAYQVLKQLQSIWESERVPLWIRPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSCTTEAFLTAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTSEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDRVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMNMTEEQLQVLVEQMVDGSMRSITTKLYDGFQYLTNGIM | Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May play an important role in the inner ear development.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 90709
Sequence Length: 806
Subcellular Location: Endomembrane system
EC: 2.7.1.67
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Q99755 | MASASSGPSSSVGFSSFDPAVPSCTLSSAASGIKRPMASEVLEARQDSYISLVPYASGMPIKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSIHNIDHAQREPLSSETQYSVDTRRPAPQKALYSTAMESIQGEARRGGTMETDDHMGGIPARNSKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPLKPSPSKKFRSGSSFSRRAGSSGNSCITYQPSVSGEHKAQVTTKAEVEPGVHLGRPDVLPQTPPLEEISEGSPIPDPSFSPLVGETLQMLTTSTTLEKLEVAESEFTH | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility . PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) . PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Can also use phosphatidylinositol (PtdIns) as substrate in vitro . Together with PIP5K1C, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps (By similarity). Promotes particle ingestion by activating the WAS GTPase-binding protein that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup (By similarity). Together with PIP5K1B, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, IP3 and DAG, that will mobilize internal calcium and drive keratinocyte differentiation . Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes (By similarity). Together with PIP5K1C has a role during embryogenesis (By similarity). Independently of its catalytic activity, is required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of the small GTPase RAC1 to the plasma membrane . Also functions in the nucleus where it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+)
Sequence Mass (Da): 62633
Sequence Length: 562
Subcellular Location: Cell membrane
EC: 2.7.1.68
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D3ZSI8 | MASASSGPAAAGFSPLDSGVPAGTAASGIKRGTVSEGPYASLMPVKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMDHAQREPMNSETQYSIDTRRPAPQKALYSTAMESIQGEARRGGTVETEDHMGGIPARNNKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPLKPSPTKKFRSGPSFSRRSGPSGNSCTPSQPTASGEHKAQVTTKAEVEPDIHLGRPDVLPQTPPLEEISEGSPVPGPSFSPAVGQPLQILNLSSTLEKLDVAESELTH | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Can also use phosphatidylinositol (PtdIns) as substrate in vitro (By similarity). Together with PIP5K1C, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps. Promotes particle ingestion by activating the WAS GTPase-binding protein that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, IP3 and DAG, that will mobilize internal calcium and drive keratinocyte differentiation (By similarity). Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes. Together with PIP5K1C has a role during embryogenesis (By similarity). Independently of its catalytic activity, is required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of the small GTPase RAC1 to the plasma membrane. Also functions in the nucleus where it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+)
Sequence Mass (Da): 60605
Sequence Length: 546
Subcellular Location: Cell membrane
EC: 2.7.1.68
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O14986 | MSSAAENGEAAPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETPQNVPDAKRTGMQKVLYSTAMESIQGPGKSGDGIITENPDTMGGIPAKSHRGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQALKASPSKKRCNSIAALKATSQEIVSSISQEWKDEKRDLLTEGQSFSSLDEEALGSRHRPDLVPSTPSLFEAASLATTISSSSLYVNEHYPHDRPTLYSNSKGLPSSSTFTLEEGTIYLTAEPNTLEVQDDNASVLDVYL | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (By similarity). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of phospholipase PLD2. Together with PIP5K1A, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+)
Sequence Mass (Da): 61036
Sequence Length: 540
Subcellular Location: Cytoplasm
EC: 2.7.1.68
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P70181 | MSSTAENGDAVPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRAMRMHLTYDLKGSTYKRRASRKEREKPNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHILDHSLKDKEEEPLQNVPDAKRPGMQKVLYSTAMESIQGPGKSADGIIAENPDTMGGIPAKSHKGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQALKASPSKKRCNSIAALKATSQEIVSSISQEWKDEKRDLLTEGQSFSSLDEEALGSRHRPDLVPSTPSLFEAASLATTISSSSLYVGEHYPHDRTTLYSNSKGLPSSSTFTLEEGTIYLTAEPNTLDLQDDASVLDVYL | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility . PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). Mediates RAC1-dependent reorganization of actin filaments . Contributes to the activation of phospholipase PLD2 . Together with PIP5K1A, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+)
Sequence Mass (Da): 60803
Sequence Length: 539
Subcellular Location: Cytoplasm
EC: 2.7.1.68
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Q9Y2B2 | MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPTVLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGMQWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVLTLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIFSRYMRINSLSFL | Function: Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Catalytic Activity: a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28531
Sequence Length: 252
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.5.1.89
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O35790 | MEVVGLLCVAVAVLTWGFLRVWNSAERMRSPEQAGLPGAGSRALVVIAHPDDEAMFFAPTILGLARLKQQVSLLCFSSGNYYNQGEIRKKELLQSCAVLGIPPSRVMIIDKREFPDDPEVQWDTEHVASTILQHIHANATDLVVTFDAEGVSGHSNHIALYKAVRALHSGGKLPEGCSVLTLQSVNVLRKYVFLLDLPWTLLSPQGVLFVLTSKEVAQAKKAMSCHRSQLLWFRHLYTVFSRYMSVNSLQLL | Function: Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Catalytic Activity: a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27984
Sequence Length: 252
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.5.1.89
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Q500W7 | MSRESENTDDEPSKWMKFRSLLVFSMLLRVFLIVYGEWQDAHMEVRYTDVDYIVFSDAASLMASGESPYKRTTYRYSPLLALLLTPNSFFHRSWGKFLFSASDLLVGWFIHKILKQRKVPEKICTYSVMVWLFNPFTFTIGTRGNCEPIVCAMILWIILCLMQGNLLQAAFWYGLVVHFRVYPIIYALPIILVLDTQVFRSGQKPALLYWNTGQAKTPASNMERKTFLFNLLTTLKSLFSRERIMFALISGGVFLACNAVSFYFYGQEFLHEALLYHLTRTDPRHNFSIYFYHIYLHYERQFSAVEKLISFLPQFTVQFALVFCFSQDLVFCIFLQTVAFVTFNKVITAQYFVWFYCLLPLILPWSHMKLKWEGLLCIIMWIGAQTHWLLWGYMLEFKGVNVFLPLWIASLLFLAANTFVLVRIIQRHRFSPLFRRYESSSSSNNVTKED | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52946
Sequence Length: 450
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.-
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Q5F380 | MAGGRPGLRAALGAGLLARLSLVLYGLYQDAVMRVRYTDVDYRVFTDAARLVTQGRSPYRRATFRYTPLLAWLLTPNVHLGELFGKLLFVAGDLAAAGVAYRALRRRGASPGRACGCCAAAWLLNPLPMAVSSRGNAEALVAVLVLAALHLVEAGSVGRAALCYGLAVHLKIYPLTYALPIALRLQGSGEGAAGAGRDGTAEFTLVGGIWRRVVRVLNRNVLLFGAVAGSVLAALTVLFYHLYGWEFLEHAYLYHLTRRDIRHNFSPYFYMLYLTAESKWSFALGLAAFLPQLLLLLVVSVAFYKDLFFCCFLHTAIFVSFNKVCTSQYFIWYLCLLPIIIPNIKMSWRRGVLLLFLWFAGQGLWLAPAYLLEFKGYNTFVFIWSAGLLFLFINSFILVQIISHYQQETQVARKVKEQ | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46577
Sequence Length: 418
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.-
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Q54IA4 | MTRVKTVMTNENNKYDFIFKGINLTKSIFIVGLVIRLVLIVFAEWQDANMLVKYTDIDYVVYTDASRAVVNGLSPYDRSTYRYTPLLAYLLVPNILIHPAFGKLLFVICDMIIAYLLKGILLERFPKITSRTLLICLASWLLNPFSINVSTRGNAESVIGAMVLASFYFLTKKNLTLASIFYGLSVHFKIYPIIYSIPMYLYIDENFFSRKPSEYTSLNNNFKNIFKNFFNKNRLKFFLISAFTFISLTFIMYLIYGYIFLFETYLYHVIRADNRHNFSVYFYQIYLNTPIVETVGDLVGKVNGSNMIVALASFLPQVILLLAITLVYFNDLEFCLLLETITFVAFNKVCTVQYFIWYYSILPLVIPSSSLGLVQYIILFAVWMGSQGLWFYSAFNLEFLGLQTFWNIWVAGLLFFIANIYILVKLILNHNPIKVNQYLKSK | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51328
Sequence Length: 442
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.-
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Q9H3S5 | MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAARFVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLGRRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMKIYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFALSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLILLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVLLMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERIKYD | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49460
Sequence Length: 423
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.-
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Q4R4E1 | MGSTKHWGEWLLNLKLAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAARFVAEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLARRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIRKRVVACAAVFYGFAVHMKIYPVTYILPITLHLLPDRDNDKSLRQSRYTFQAHLYELLKRLCDRAVLLFVAVAGLTFFALSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQFILLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMTWKRAVVLLMLWFIGQALWLAPAYVLEFQGKNTFLFIWLAGLFFLLINSSILIQIISHYKEEPLTERIKYD | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49451
Sequence Length: 423
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.-
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Q5W259 | MVNDTFEQALQNAINIARLAPSSHNCQPWSVHYDAATRCGEVSIDRQRALKGLPSLEREMLMSCGIFFEYLSTLLKHSGYPLDWQWVGARQNGSSGMLISFAPSAPCVADLVAYQQWVQRISDRHTVRTAYQPTQVNEQQQAQLYALFDRSPVTCDIKYGEATRHDVAFLTANYASLDFADQQAWRETYHYIRFNEQQAAEDGFYLHHLFGPVSCGFRWFFRIAFHPRLSWLAKRLRLPASMAKGLAELVVEGPQYLALSLEHESDENLFIAGMKLGQLWLMLQSWGWSLHPLSVLVQHATARCALADTVRLTGLPVFFARFGQHRQSGIPTPRRAWQRILTTTQHSFSPENGADVKQP | Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the oxidation of the hydroxy group of 4-hydroxy-2,2'-bipyrrole-5-methanol (HBM) to yield 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC).
Sequence Mass (Da): 40860
Sequence Length: 359
Pathway: Antibiotic biosynthesis; prodigiosin biosynthesis.
EC: 1.-.-.-
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Q9BPQ5 | MELQSLIDTVSLQKLLLLGALLRLILIAYAFFHDQWFRVKYTDIDYMIVVDGARHMWNGGSPFDRTTFRYTPLLAALVMPSIWIANPMGKLIFASSDLGAAWYCYGVLKSFAKERSAKWMVSLFILFNPIVLSVSTRGNSDMLVTFMSLMVLSKFARRKCYQAAAVLGFAVHFKIYPIIYALPLTLGVWEQSVAASTNTWRRVVKTAVVVSICALMAAISFAVPTVLCYMKYGQQYLNEAFIYHVYREDHRHNFSPYWLLMYLNMARRHLGQGVDFSPRLVAFAPQAVVLSFVSYKLRRNTAHACCVQTVLFVAFNKVCTVQYFVWFIPFLAFLFCEPKEVEDDESGGSGAFKFFSWVKALGVVLMWAATIPLWVTTAVPLEFHGYSDFAQLWIVSCLFFLAMVVLASMLARIAYRVQCTKCSAKSIKVA | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48849
Sequence Length: 430
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.-
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Q66IJ4 | MMKQAGILKIFLQHQFMFPTAFFLRSALVLFGVYQDQTMLVKYTDVDYHVFTDAAEYLTQGVSPYKRATYRYTPLLAWILTPNIYVTELYGKMLFVCCDLLAAYLIHRILVDRGIKDSASLYCAIWLFNPLPMVVSSRGNAESVLAVLVLSVLYYVQKRRLIKGALIYGLSVHMKIYPITYILPIALFFQKEDFYGSQEGKRVVSNLKYIRIFRNLLQRLLSRDILLFVTVSGVTFALLTLFFYYRYGWEFLENTYLYHLTRRDIRHNFSPYFYMLYLTAENNNSFILGLAAFFPQLVLLFVVSLAYFKDLPFCCFLHTAIFVSFNKVCTSQYFLWYLCLLPLVMPGLKMSMTNGICLIILWFFSQAIWLVPAYFLEFEGQNTFLYIWCAGLLFLLINTVIIVQIISNYQLQSKKTKKT | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49036
Sequence Length: 419
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.-
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O95427 | MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESMFTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSLCKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKPSHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYPLSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSLLLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLSTVLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMSMTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM | Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity). May act as suppressor of replication stress and chromosome missegregation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105810
Sequence Length: 931
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.-.-.-
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Q9R1S3 | MLLFFALGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPAKRLVLFVADGLRADTLYELDEDGNSRAPFIRNVIIHEGSWGVSHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAQREDFGAHDATKLDTWVFDKVKDFFDAARNNQSLFTKVNEEKVVFFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHFYGDDGKTAFIFTSDHGMTDWGSHGAGHPSETLTPFVTWGAGIKFPQNVSAQQYDDEFLKEWRLENWKRRDVNQADIAPLMASLIGVPFPLNSVGILPVGYLNNTGLFKAESMFTNAVQILEQFKVKMTQKKEATLPFLFTPFKLLSDSQQLDILRKARSYIKQEKFDEVVSLCEELIDLALRGLSYYHTYDRLFLGINVAVGFVGWMSYTSLLIIKSHSNIPKGTRKEGKKPHCLLLYSFIATGVLVACFLMIQACPWTYYVYCLLPVPIWYAVLREHEVIQDLVESLLTFPRSHFVAYLLVFTLGIEVLVLSFFYRYMLTAGLIVFAGWPFLTQLWTRAKITFLSWAFFSLLLAVFPLMPVVGRKPNLSLVMGAGFLVLLLSLAVVTTLGKRNIKLVKGELLVLLLQMLSTVLSMYVVYSTHHSLLKKEGLPLMNQIVSWATLASSLVAPLLSSTALSQRLASILLSLMSTYLLLSTGYEALFPLVLSCLMFVWIQVEQETLQQPGVSCKQKLTSIQFTCDTDIAQFRQLCPDDIRRAFFLVFFLLTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAVQITTQLSSKGLFLVVLIISDIMALHFFFLVKDSGSWLDIGTSISHYVIVMSMTIFLVFLNGLAQLLTTKKLQLCGKPKSHLM | Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. May act as suppressor of replication stress and chromosome missegregation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105045
Sequence Length: 931
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.-.-.-
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Q9C999 | MSGFSSGNVNSRVVDILSGVVPLLKLICLTVIGLLLAHPKTQLVPRATFRLLSKLVFALFLPCLIFTELGESITLDNIVQWWFIPVNVLLSAVVGSLIGYLVVLICRPPPEFNRFTIVMTAFGNTGNLLLAIVSSVCHTKTNPFGPNCNSRGVSYVSFAQWVAVILVYTVVYHMMEPPLEYYEVVEEEGVEIEEINVENHDASRPLLVEAEWPGIEDKETEHCKTPFIARVFNSISSFSQTSFPEVDLGGEYGGESSSPRSIQCLAEPRVMRRIRVVAEQTPVKHILQPPTIASLLAIIIGSVPQLKSVVFGYDAPLSFITDSLNIMGSAMVPSVMLVLGGMLSEGPNESTLGLRTTIGISVARLLVLPLVGIGIVMSADKLGLISSADPMFKFVLLLQYSTPSAILLGAIASLRGYAVREASALLFWQHIFALLSLTFYIVIFFKLTVETTVQGMQ | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49880
Sequence Length: 457
Subcellular Location: Endoplasmic reticulum membrane
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Q9C9K5 | MVKLLELFITSSKPVVEILLITSVGFYMALDGVNLLGHDARKYLNNIVFYVFSPSLIGSRLADSVTYESLVKMWFMPVNVLLTFIIGSLLGWIVIVITKPPSHLRGLILGCCAAGNLGNMPLIIIPAVCKEKGGPFGDPESCQKYGMGYVALSMAMGSIYIWTYVYNLMRVLSNSPVETPPSVESNYDSYKVPLISSKEEENNQKAGRWEKVKRRLVSLSQKVNLKTIFAPSTIAAMIALVIGLITPLRKLIIGTEAPLRVLQDSVTLVGDGAVPAMTMIIGGNLLKGLRSSGMKMSSIIGVLVARYVLLPMSGVLIVRGAYKLDLVTSEPLYQFVLLLQYAVPPAMNLGTITQLFGTGESECSVIMLWTYSLASIALTVWPTFFMWLVA | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42632
Sequence Length: 390
Subcellular Location: Endoplasmic reticulum membrane
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Q9C9K4 | MKLLELFIASSKPVVETLLITSVGFYLALDTVNLLGHDARKHLNNIVFYVFSPSLIGSRLADSVTYESLVKMWFMPVNVLLTFMIGSLLGWIVIVITKPPSQLRGLIISCCASGNLGTMPLIIIPAICKEKGGPFGDSESCEKYGMGYVTLSMTAFFISVYKHDTNWYVSGGNGLLMDLYINLMRVLSNSPVETHTHSIESNYDDSCKVQLISSKEEEKEEDNHQVGRWEEVKQRVVSLSKKVNLGSIFAPATIAAIIALVIGLITPLRNLIIGTVAPFRVIQDSLTLLGDGAIPAMTLILGGNLLKGMRRSEVRSSEMKNSCIIGVLVARYILLPVSGVLLVRGAYKLDLVTSEPLYQFVLLLQYAVPPAMNLGTKTQLFGAGESECSVIMLWTYSLAAVSLTVWPTFFMWLVT | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45586
Sequence Length: 415
Subcellular Location: Endoplasmic reticulum membrane
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Q9SHL8 | MGFWSLLEVASMPVIQVLFMSLVGAFMASDRCKLFPVEARNSMNKVVFVLFAPALMFANLAQTVTLEDIISWWFMPVNMGLTFLIGGLLGWLVVKILKPPPYLEGLIVATCSAGNMGNLPIILVPAICDEDKSPFGNRSVCRTVGLSYASFSMALGGFYIWTYTFRLIKGSAMKVQAIEESEKIAIKSSNSDLEADHKTHLLGAPEDKENKVVKEKTGFWRKGVDFLHEILEELLAPPTLGAIIGFIFGAVRWLRNLIIGDDAPLRIVQSTAKLLGDGTIPCMTIILGGNLIQGLRSSAVKPMVVLGIVCVRYIAMPIIGIGIVLTAANLGFLPADPLFQYVLMLQFTLPPAMNIGTMTQLYNVAQDECSVLMLWTYLVAILALTVWSTIFLHLLV | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43394
Sequence Length: 396
Subcellular Location: Endoplasmic reticulum membrane
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Q9LZN2 | MIARILAALADSMEMPVAAGGGSVLGTIKIAVMPIAKVFTMCFLGLLMASKYVNILPPSGRKLLNGLVFSLLLPCLIFSQLGQAVTLQKMLQWWFIPVNVVLGTISGSIIGFIVASIVRPPYPYFKFTIIQIGVGNIGNVPLVLLAALCRDTSNPFGDSEKCSIDGTAYISFGQWVGAIILYTYVYQMFAPPPEGFDAEEENLALKTLPVDAAPEQVPLLTQNFPKDFSPTQDLLPVQSTEPRGRGVSRKGKIAQIFVFLYEKLKLKQIVQPAIVASILAMILGAIPFTKKLIFTNGAPLFFFTDSCMILGDAMIPCILLALGGNLINGPGSSKLGFKTTAAIIIGRLVLVPPVGLGIVTVADKLGFLPADDKMFRFVLLLQHTMPTSVLSGAVANLRGCGRESAAVLFWVHIFAIFSMAGWMVLYINILF | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46465
Sequence Length: 431
Subcellular Location: Endoplasmic reticulum membrane
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Q9FKY4 | MGFLELLEVASMPIVQVLLISVLGAFLATDYCSLLSADTRRSVNKLVFVVFTPCIMFANLAETVTLQDIISWWFMPINVGITFLVGGILGWLVVKLLNPKPQLHGLIIATCASGNMGNLMLILVPAICDEEGSPFGNRSVCRSIGLSYASFSMALGGFYIWTYSYQLVRSSATQFRALEAAGLVKSPNKDIDSDPHALLLKPHQNQDLEIQGKQKVSTRTYIKDLLHQILEELFAPPTIGAILGFVFGATNWLRNLIIGENAPLRVIQDSVKLLGEGTIPCITLILGGNLIQGLRSSAVKKSVIVGVIIVRYILLPVVGVGVVQLAGNLGYLPPDPLFRYVLMLQFALPPAMNISTMAQLFDVAQDECSVIFLWTYLVASLALTVWSTIFLSILS | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43074
Sequence Length: 395
Subcellular Location: Endoplasmic reticulum membrane
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P33639 | MRAERLRLSEEQGQRILRLYHLYRLTIGLVLVLLISSELEDQVLKLVHPELFHVGSWCYLVFNILVALFLPPSRQLLPIFILALTDVLMLCGLFYAGGGVPSGIGSLLVVAVAIANILLRGRIGLVIAAAASLGLLYLTFFLSLSSPDATNHYVQAGGLGTLCFAAALVIQALVRRQEQTETLAEERAETVANLEELNALILQRMRTGILVVDSRQAILLANQAALGLLRQDDVQGASLGRHSPMLMHCMKQWRLNPSLRPPTLKVVPDGPTVQPSFISLNREDDQHVLIFLEDISQIAQQAQQMKLAGLGRLTAGIAHEIRNPLGAISHAAQLLQESEELDAPDRRLTQIIQDQSKRMNLVIENVLQLSRRRQAEPQQLDLKEWLQRFVDEYPGRLRNDSQLHLQLGAGDIQTRMDPHQLNQVLSNLVQNGLRYSAQAHGRGQVWLSLARDPESDLPVLEVIDDGPGVPADKLNNLFEPFFTTESKGTGLGLYLSRELCESNQARIDYRNREEGGGCFRITFAHPRKLS | Function: Member of the two-component regulatory system PilS/PilR that regulates the expression of multiple genes including the type IV pilus (T4P) major subunit PilA . Thereby, plays a major role in the regulation of multiple motility pathways . Functions as a membrane-associated protein kinase that phosphorylates PilR in response to environmental signals leading to activation of specific gene promoters including the pilin gene .
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58985
Sequence Length: 530
Domain: The linker domain is the critical region for polar localization.
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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P24559 | MDITELLAFSAKQGASDLHLSAGLPPMIRVDGDVRRINLPPLEHKQVHALIYDIMNDKQRKDFEEFLETDFSFEVPGVARFRVNAFNQNRGAGAVFRTIPSKVLTMEELGMGEVFKRVSDVPRGLVLVTGPTGSGKSTTLAAMLDYLNNTKYHHILTIEDPIEFVHESKKCLVNQREVHRDTLGFSEALRSALREDPDIILVGEMRDLETIRLALTAAETGHLVFGTLHTTSAAKTIDRVVDVFPAEEKAMVRSMLSESLQSVISQTLIKKIGGGRVAAHEIMIGTPAIRNLIREDKVAQMYSAIQTGGSLGMQTLDMCLKGLVAKGLISRENAREKAKIPENF | Function: ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers . Acts as a molecular motor to provide the energy that is required for T4P retraction while antagonist PilB ATPase activity is required for T4P extension . Promotes also PilU retractation activity through direct interaction .
Sequence Mass (Da): 38021
Sequence Length: 344
Domain: The N-terminal region is responsible for proper localization to the piliated pole.
Subcellular Location: Cytoplasm
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G3XCX3 | MEFEKLLRLMVEKGGSDLFITAGVPPSMKVNGRVMPVTKTPLSPEQTRETVLGVMNEQQRRDFAENHECNFAISARGIGRFRVSAFYQRNLVGMVLRRIETNIPTLEELKLPEILKKLALTKRGLVIFVGATGTGKSTSLAAMIGYRNKNSTGHIISIEDPIEYIHQHQGCIVTQREVGLDTDSFEVALKNTLRQAPDVIMIGEVRSRETMDHAVAFAETGHLCLATLHANNANQALERIIHFFPADRHGQVWMDLSLNLKAIVAQQLVPTPDGKGRRAVIEVLLNTPLAADLIRKGEVHELKPLMKRSTEQGMQTFDQALYQLYTQGEITYEDALAHADSANDLRLMIKLGSESDADHLSSLTQGLSLEITDDDPAGRRFR | Function: ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers . Functions as a PilT-dependent retraction ATPase, providing a functional coupling between PilT and PilU and an optimal mechanism for pilus retraction .
Sequence Mass (Da): 42533
Sequence Length: 382
Domain: The N-terminal region is responsible for proper localization to the piliated pole.
Subcellular Location: Cytoplasm
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P11309 | MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis . Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3) . Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity (By similarity). The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis (By similarity). Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1 (By similarity). Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis . Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C . Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability . Promotes cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels . Phosphorylation of CDKN1B, induces 14-3-3 proteins binding, nuclear export and proteasome-dependent degradation . May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3 . Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity). Acts as a positive regulator of mTORC1 signaling by mediating phosphorylation and inhibition of DEPDC5 component of the GATOR1 complex . Also phosphorylates and activates the ATP-binding cassette transporter ABCG2, allowing resistance to drugs through their excretion from cells . Promotes brown adipocyte differentiation (By similarity).
PTM: Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35686
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P06803 | MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSDFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEDLARGFFWQVLEAVRHCHNCGVLHRDIKDENILIDLSRGEIKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIKGQVFFRQTVSSECQHLIKWCLSLRPSDRPSFEEIRNHPWMQGDLLPQAASEIHLHSLSPGSSK | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis . Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3) (By similarity). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity . The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis . Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1 . Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis (By similarity). Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C (By similarity). Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability (By similarity). Promotes cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels (By similarity). Phosphorylation of CDKN1B, induces 14-3-3 proteins binding, nuclear export and proteasome-dependent degradation (By similarity). May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3 (By similarity). Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis . Acts as a positive regulator of mTORC1 signaling by mediating phosphorylation and inhibition of DEPDC5 component of the GATOR1 complex . Also phosphorylates and activates the ATP-binding cassette transporter ABCG2, allowing resistance to drugs through their excretion from cells (By similarity). Promotes brown adipocyte differentiation .
PTM: Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35451
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P26794 | MLLSKINSLAHLRAAPCNDLHANKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIVKGQVYFRQRVSSECQHLIRWCLSLRPSDRPSFEEIQNHPWMQDVLLPQATAEIHLHSLSPSPSK | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3) (By similarity). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1 (By similarity). Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promotes cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B, induces 14-3-3 proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3 (By similarity). Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity). Acts as a positive regulator of mTORC1 signaling by mediating phosphorylation and inhibition of DEPDC5 component of the GATOR1 complex. Also phosphorylates and activates the ATP-binding cassette transporter ABCG2, allowing resistance to drugs through their excretion from cells (By similarity). Promotes brown adipocyte differentiation (By similarity).
PTM: Autophosphorylated on both serine/threonine and tyrosine residues (By similarity). Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35631
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9YHZ5 | MLDKRIVDVRLDQLEILKAKNGKEHFEKQYTMGNLLGSGGFGSVYSGHRISDGQKVAIKQISRDRIQQWSKMPGEVNPVPNEIALLQSLGGGSGSVPGHRGIIRMLDWFEIPGQEYLIVFEKPQHCQDLFDFITERGALDESLARRFLKQVIEAVQFCHSKGIVHRDIKDENILVDTRTGDIKVIDFGSGATLKDSMYTDFEGTRVYSPPEWILYHKYHALPLTVWSLGVLLYDMVCGDIPFEQDTDIVKAKPSFNKRISNDCRSLICSCLSYNPGDRPSLEQILQHPWMMESSVDNGDLQEESKIKPSL | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35102
Sequence Length: 310
EC: 2.7.11.1
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Q9P1W9 | MLTKPLQGPPAPPGTPTPPPGGKDREAFEAEYRLGPLLGKGGFGTVFAGHRLTDRLQVAIKVIPRNRVLGWSPLSDSVTCPLEVALLWKVGAGGGHPGVIRLLDWFETQEGFMLVLERPLPAQDLFDYITEKGPLGEGPSRCFFGQVVAAIQHCHSRGVVHRDIKDENILIDLRRGCAKLIDFGSGALLHDEPYTDFDGTRVYSPPEWISRHQYHALPATVWSLGILLYDMVCGDIPFERDQEILEAELHFPAHVSPDCCALIRRCLAPKPSSRPSLEEILLDPWMQTPAEDVPLNPSKGGPAPLAWSLLP | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 34190
Sequence Length: 311
EC: 2.7.11.1
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Q07N42 | MPLAPPPEKMMFQLSLRRRGISDQAVLRAMDAVPRDLFVTPDLRDEAWRDTALPIACGQTISQPFVVAYMTEQLQLKPEHRVLEIGTGSGYQAAVLSRLCQQVLTLERFKTLADSARARLESLECHNVEVQLGDGFDVPAKAGLFDRILVTAAMEEVPGALIARLDLDGILIAPVGPHQATQTLVRIRNAKGGIERKELVAVRFVPALPGIAREL | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23611
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q6NCU3 | MVERQIAARGVHDPRVLAAMRKVPREAFLPEPMRDLAYEDAPVPIAAEQTMSQPYIVALMVEALLLQGSDNVLEIGAGSGYAAAVLGEIAGHVTTVERIATLADAAAAKLAELGYGDVDVHRSDGTRGWPAAAPYDAIVVAAGGPQVPESLKAQLKIGGRLVMPVGADQQAQELVRLTRLGEADFKREHLGDVRFVPLLGAEGWQQPEPAGRTAREKG | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23128
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q136H9 | MVSSVAPPPEKMMFQLSLRRRGISDRAVLQAMEAVPRDRFVDPVHRDGAWRDTALPIACGQTISQPFVVAYMTEQLRLEAGHRLLEIGTGSGYHAAVLSRLVRDVVSVERFKTLADRARARLKELNYANVEVLLGDGFAIPEGAGTFDRIIVTAAMTELSQPLLDLLDPGGILIAPIGPANGRQTLIRVERKDDDFIRKALVDVRFVPALTGIAREL | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23880
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q2RTH7 | MSVPSRKIRLIMELRQNGVSATPVLAAIERVPRDAFVSAPFSDQAYENTALPIGCGQTISQPLVVGLMTQALDLNDRHKVLEIGTGSGYQTAVLARLCRRVYTIERHGALLREAEARLTALGLHRTVVTREGDGGRGWPEQAPFERILVTAAALDIPKVLVAQLAIGGVMVLPVGKESGAQEVVRVRRTAEDALVTERLFPVRFVPLVDGLPPRDAPGA | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23627
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q08733 | MEGKEEDVRVGANKFPERQPIGTSAQTDKDYKEPPPAPFFEPGELSSWSFYRAGIAEFIATFLFLYITVLTVMGVKRAPNMCASVGIQGIAWAFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRAVFYIVMQCLGAICGAGVVKGFQPNPYQTLGGGANTVAHGYTKGSGLGAEIIGTFVLVYTVFSATDAKRSARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIIYNKDHAWDDHWIFWVGPFIGAALAALYHQLVIRAIPFKSRS | Function: Water channel required to facilitate the transport of water across cell membrane. Its function is impaired by Hg(2+).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30633
Sequence Length: 286
Domain: The Asn-Pro-Ala (NPA) motifs may contribute to the formation of two hemipores that could generate a narrow channel.
Subcellular Location: Cell membrane
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Q9AR14 | MEGKEEDVRLGANRYSERQPIGTAAQGTEEKDYKEPPPAPLFEAEELTSWSFYRAGIAEFVATFLFLYISILTVMGVSKSSSKCATVGIQGIAWSFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRALFYMVMQCLGAICGAGVVKGFQEGLYMGAGGGANAVNPGYTKGDGLGAEIVGTFVLVYTVFSATDAKRSARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIVYNRSHAWNDHWIFWVGPFIGAALAAIYHVVIIRALPFKSRD | Function: Water channel required to facilitate the transport of water across cell membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30725
Sequence Length: 288
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Cell membrane
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Q1PE40 | MRRVSWSTVLIVVVMVSLFFVEHVVVPAAAGRVLTEKSGDGSATMTVEKMKSTVDSWFQRLASGPSPRGRGH | Function: Endogenous secreted peptide that acts as elicitor of immune response and positive regulator of defense response. Amplifies the immune response triggered by flg22, the active epitope of bacterial flagellin. Acts as negative regulator of root growth.
PTM: Contains 4-hydroxyproline; hydroxylated on Pro-65 and Pro-67.
Sequence Mass (Da): 7831
Sequence Length: 72
Subcellular Location: Secreted
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P43286 | MAKDVEAVPGEGFQTRDYQDPPPAPFIDGAELKKWSFYRAVIAEFVATLLFLYITVLTVIGYKIQSDTDAGGVDCGGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLPRALLYIIAQCLGAICGVGFVKAFQSSYYTRYGGGANSLADGYSTGTGLAAEIIGTFVLVYTVFSATDPKRSARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNKSKPWDDHWIFWVGPFIGAAIAAFYHQFVLRASGSKSLGSFRSAANV | Function: Water channel required to facilitate the transport of water across cell membrane. Probably involved in root water uptake. Its function is impaired by Hg(2+).
PTM: Ubiquitinated by RMA1, leading to proteasomal degradation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30474
Sequence Length: 287
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Cell membrane
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Q6K215 | MAKDIEASAPEGGEFSAKDYTDPPPAPLIDVEELTKWSLYRAVIAEFIATLLFLYITVATVIGYKHQSDATVNTTDAACSGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLIRAVLYIIAQCLGAICGVGLVKGFQSSYYARYGGGANELSDGYSKGTGLGAEIIGTFVLVYTVFSATDPKRNARDSHIPVLAPLPIGFAVFMVHLATIPITGTGINPARSLGTAVIYNKDKAWDDQWIFWVGPLIGAAIAAAYHQYVLRASAAKLGSYRSNA | Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30498
Sequence Length: 288
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Cell membrane
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Q9UG56 | MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer) . Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 46672
Sequence Length: 409
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis.
Subcellular Location: Mitochondrion inner membrane
EC: 4.1.1.65
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Q8BSF4 | MAASGGRACVRSLRGGVLWRSSPCHYESTATRHFLGTLQKLPLQAGVRNFHTAPVRSLFLLRPVPILLATGGGYAGYRQYEKYRERKLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPYWLRRPVYSLYIWTFGVNMTEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHCVTSPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRANTEDLPFPPASSSDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTISHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDRDLHTNSPRYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKIRFGEALGSL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45927
Sequence Length: 406
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis.
Subcellular Location: Mitochondrion inner membrane
EC: 4.1.1.65
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D3ZAW2 | MAVAGGRGCVRSLREGVLWRSSPCHCDYTATRHFLGALQKLPLQAWVRKVHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDQDLHTNSPSYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKILFGEALGSL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45824
Sequence Length: 406
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis.
Subcellular Location: Mitochondrion inner membrane
EC: 4.1.1.65
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Q59RA2 | MPSAKSSDLSPTKTNLESTTKQKVSVQDIFLYIPNLIGYLRIITAIISFLCMANHPVATLIFYGISGFLDAFDGYAARKFNQGTRFGAVLDMVTDRCATSSLIVYLGVLYPQYTVFWQILVSLDLSSHYMHMYAMLSAGSTSHKNVDETQSKLLSLYYNNRLVLFFVCLINELFYMAVYLHYYKFFWLGTVMLVASTPIWLFKQIANIIQLKNASLILARMDAHDHSKRD | Cofactor: Catalytic activity is higher with Mg(2+).
Function: Catalyzes the synthesis of phosphatidylinositol (PtdIns) . Required for proper membrane dynamics and cell wall integrity .
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26212
Sequence Length: 230
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.11
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Q10153 | MGKNEQKDPNVYFFVPNLIGFTRVFLVLISLYFMSWHPNYCTIVYLYSSLLDAFDGWAARKLHQATNFGAILDMVTDRCATSCLLCFLCAAYPKYAIIFQLLVSLDLASHYMHMYSTLHQGASSHKTVTKKHNWMLRLYYGNNKVLFIFCAANEMFFVALYLLSFTPRTPPKLGYLPVPSFIYSTGELPLSYPTLLAVLCGPICLAKQIINVVQLVNAANALVKMDVEQRRAAKKLQ | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+).
Function: Catalyzes the synthesis of phosphatidylinositol (PtdIns).
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26924
Sequence Length: 237
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.11
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P06197 | MSSNSTPEKVTAEHVLWYIPNKIGYVRVITAALSFFVMKNHPTAFTWLYSTSCLLDALDGTMARKYNQVSSLGAVLDMVTDRSSTAGLMCFLCVQYPQWCVFFQLMLGLDITSHYMHMYASLSAGKTSHKSVGEGESRLLHLYYTRRDVLFTICAFNELFYAGLYLQLFSNSATFGKWTTIISFPGYVFKQTANVVQLKRAALILADNDAKNANEKNKTY | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+).
Function: Catalyzes the synthesis of phosphatidylinositol (PtdIns).
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24824
Sequence Length: 220
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.11
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P28069 | MSCQAFTSADTFIPLNSDASATLPLIMHHSAAECLPVSNHATNVMSTATGLHYSVPSCHYGNQPSTYGVMAGSLTPCLYKFPDHTLSHGFPPIHQPLLAEDPTAADFKQELRRKSKLVEEPIDMDSPEIRELEKFANEFKVRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACKLKAILSKWLEEAEQVGALYNEKVGANERKRKRRTTISIAAKDALERHFGEQNKPSSQEIMRMAEELNLEKEVVRVWFCNRRQREKRVKTSLNQSLFSISKEHLECR | Function: Transcription factor involved in the specification of the lactotrope, somatotrope, and thyrotrope phenotypes in the developing anterior pituitary. Specifically binds to the consensus sequence 5'-TAAAT-3'. Activates growth hormone and prolactin genes .
Sequence Mass (Da): 32912
Sequence Length: 291
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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Q05749 | MTCQAFASSDNFVPLNSDSSPSLPLIMHHSAAECLPVSNHATSVVSTVPSVLSLIQTPKCSHLHFAMMTSGNVSAGLHYSVPSCHYGNQTSTYGVMTGIKPATPEMLSASLSQSRILQTCSMPHPNVVNGVSTLQSKSFSFSCSLTPCLYKFPEHALSASSCALGHSFTPMHQTLLSDDPTAADFKQEFRRKSKSVEEPVDMDSPEIRELEKFANEFKLRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENSQLSFKNACKLKSILSKWLEEAEQVGALYNEKVGVNERKRKRRTTISIAAKEALERHFGEQSKPSSQEIMRMAEGLNLEKEVVRVWFCNRRQREKRVKTSLHQNAFSSIIKEHHECR | Function: Transcription factor that activates growth hormone and prolactin genes. Specifically binds to the consensus sequence 5'-TAAAT-3'.
Sequence Mass (Da): 41191
Sequence Length: 370
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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Q9HYF1 | MFESAEVGHSIDKDTYEKAVIELREALLEAQFELKQQARFPVIILINGIEGAGKGETVKLLNEWMDPRLIEVQSFLRPSDEELERPPQWRFWRRLPPKGRTGIFFGNWYSQMLYARVEGHIKEAKLDQAIDAAERFERMLCDEGALLFKFWFHLSKKQLKERLKALEKDPQHSWKLSPLDWKQSEVYDRFVHYGERVLRRTSRDYAPWYVVEGADERYRALTVGRILLEGLQAALATKERAKRQPHAAPLVSSLDNRGLLDSLDLGQYLDKDAYKEQLAAEQARLAGLIRDKRFRQHSLVAVFEGNDAAGKGGAIRRVTDALDPRQYHIVPIAAPTEEERAQPYLWRFWRHIPARRQFTIFDRSWYGRVLVERIEGFCAPADWLRAYGEINDFEEQLSEYGIIVVKFWLAIDKQTQMERFKEREKTPYKRYKITEEDWRNRDKWDQYVDAVGDMVDRTSTEIAPWTLVEANDKRFARVKVLRTINDAIEAAYKKDK | Cofactor: Has low activity with Co(2+) or Ni(2+).
Function: Uses inorganic polyphosphate (polyP) as a donor to convert AMP to ADP. Can also convert GMP to GDP, with lower efficiency. Cannot dephosphorylate ADP in the presence of polyP.
Catalytic Activity: [phosphate](n) + ADP = [phosphate](n+1) + AMP
Sequence Mass (Da): 58331
Sequence Length: 496
Domain: Contains 2 fused PPK2 domains. The N-terminal domain seems to be catalytically inactive and might be responsible for the protein dimerization.
EC: 2.7.4.33
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Q886D9 | MFESAEIGHAIDDDTYEAALPSLREALLEAQIDLHEQAKRQIIVLINGIEGAGKGETVKLLSEWMDPRLIEVRTFDQQTDEELAHPPVWRYWRQLPAKGRMGIFFGNWYSQMLQGRVHGQYKDAVLDQAISGAERLEKMLCDEGALIFKFWFHLSKKQMKLRLKTLKDDPLHSWRISPLDWQQSKTYDKFVRFGERVLRRTSRDYAPWHVIEGVDANYRSLTVGRLLLEGMQAALNKVEPESSALTIGPLAIHNNERTLLDSLDLSLHLSKEDYQHELIAEQARLSGNLRDKRMKSHALVAVFEGNDAAGKGGAIRRVAAALDPRQYAIVPIAAPTQDERAQPYLWRFWRQIPARGKFTIFDRSWYGRVLVERVEGFCSESDWKRAYAEINDFEEQLTEAGVVVVKFWLAIDEQTQLERFQEREKIPFKRYKITEDDWRNRKKWPDYRQAVGDMVDRTSTEIAPWTLIEANDKRWARVKVLRTINEALEKAFARDKKK | Function: Uses inorganic polyphosphate (polyP) as a donor to convert AMP to ADP. Can also convert GMP to GDP, with lower efficiency.
Catalytic Activity: [phosphate](n) + ADP = [phosphate](n+1) + AMP
Sequence Mass (Da): 57955
Sequence Length: 498
EC: 2.7.4.33
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M9XB82 | MKKYRVQPDGRFELKRFDPDDTSAFEGGKQAALEALAVLNRRLEKLQELLYAEGQHKVLVVLQAMDAGGKDGTIRVVFDGVNPSGVRVASFGVPTEQELARDYLWRVHQQVPRKGELVIFNRSHYEDVLVVRVKNLVPQQVWQKRYRHIREFERMLADEGTTILKFFLHISKDEQRQRLQERLDNPEKRWKFRMGDLEDRRLWDRYQEAYEAAIRETSTEYAPWYVIPANKNWYRNWLVSHILVETLEGLAMQYPQPETASEKIVIE | Function: Uses inorganic polyphosphate (polyP) as a donor to convert both AMP to ADP and ADP to ATP. Can also use GMP, CMP, UMP, GDP, CDP and UDP.
Catalytic Activity: [phosphate](n) + ADP = [phosphate](n+1) + AMP
Sequence Mass (Da): 31559
Sequence Length: 267
EC: 2.7.4.-
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Q9P0L9 | MNAVGSPEGQELQKLGSGAWDNPAYSGPPSPHGTLRVCTISSTGPLQPQPKKPEDEPQETAYRTQVSSCCLHICQGIRGLWGTTLTENTAENRELYIKTTLRELLVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDTGVSFQAISSMADFWDFAQGPLLDSLYWTKWYNNQSLGHGSHSFIYYENMLLGVPRLRQLKVRNDSCVVHEDFREDILSCYDVYSPDKEEQLPFGPFNGTAWTYHSQDELGGFSHWGRLTSYSGGGYYLDLPGSRQGSAEALRALQEGLWLDRGTRVVFIDFSVYNANINLFCVLRLVVEFPATGGAIPSWQIRTVKLIRYVSNWDFFIVGCEVIFCVFIFYYVVEEILELHIHRLRYLSSIWNILDLVVILLSIVAVGFHIFRTLEVNRLMGKLLQQPNTYADFEFLAFWQTQYNNMNAVNLFFAWIKIFKYISFNKTMTQLSSTLARCAKDILGFAVMFFIVFFAYAQLGYLLFGTQVENFSTFIKCIFTQFRIILGDFDYNAIDNANRILGPAYFVTYVFFVFFVLLNMFLAIINDTYSEVKEELAGQKDELQLSDLLKQGYNKTLLRLRLRKERVSDVQKVLQGGEQEIQFEDFTNTLRELGHAEHEITELTATFTKFDRDGNRILDEKEQEKMRQDLEEERVALNTEIEKLGRSIVSSPQGKSGPEAARAGGWVSGEEFYMLTRRVLQLETVLEGVVSQIDAVGSKLKMLERKGWLAPSPGVKEQAIWKHPQPAPAVTPDPWGVQGGQESEVPYKREEEALEERRLSRGEIPTLQRS | Function: Pore-forming subunit of a heterotetrameric, non-selective cation channel that is permeable to Ca(2+) . Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, but does not affect cytoplasmic calcium concentration . The channel formed by PKD1L2 and PKD1L1 in primary cilia regulates sonic hedgehog/SHH signaling and GLI2 transcription . Pore-forming subunit of a channel formed by PKD1L2 and PKD1L3 that contributes to sour taste perception in gustatory cells . The heteromeric channel formed by PKD1L2 and PKD1L3 is activated by low pH, but opens only when the extracellular pH rises again . May play a role in the perception of carbonation taste (By similarity). May play a role in the sensory perception of water, via a mechanism that activates the channel in response to dilution of salivary bicarbonate and changes in salivary pH (By similarity).
PTM: Palmitoylation is important for expression at the cell membrane and for channel activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91982
Sequence Length: 805
Domain: The EF-hand domain probably mediates calcium-binding. It is not required for channel activation .
Subcellular Location: Cell projection
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Q9NZM6 | MAEASRWHRGGASKHKLHYRKEVEITTTLQELLLYFIFLINLCILTFGMVNPHMYYLNKVMSSLFLDTSVPGEERTNFKSIRSITDFWKFMEGPLLEGLYWDSWYNNQQLYNLKNSSRIYYENILLGVPRVRQLKVRNNTCKVYSSFQSLMSECYGKYTSANEDLSNFGLQINTEWRYSTSNTNSPWHWGFLGVYRNGGYIFTLSKSKSETKNKFIDLRLNSWITRGTRVIFIDFSLYNANVNLFCIIRLVAEFPATGGILTSWQFYSVKLLRYVSYYDYFIASCEITFCIFLFVFTTQEVKKIKEFKSAYFKSIWNWLELLLLLLCFVAVSFNTYYNVQIFLLLGQLLKSTEKYSDFYFLACWHIYYNNIIAITIFFAWIKIFKFISFNKTMSQLSSTLSRCVKDIVGFAIMFFIIFFAYAQLGFLVFGSQVDDFSTFQNSIFAQFRIVLGDFNFAGIQQANPILGPIYFITFIFFVFFVLLNMFLAIINDTYSEVKADYSIGRRLDFELGKMIKQSYKNVLEKFRLKKAQKDEDKKTKGSGDLAEQARREGFDENEIQNAEQMKKWKERLEKKYYSMEIQDDYQPVTQEEFRELFLYAVELEKELHYINLKLNQVVRKVSAL | Function: May function as a subunit of a cation channel and play a role in fertilization.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73790
Sequence Length: 624
Subcellular Location: Membrane
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G5EFU0 | MNRTFSLRRKVKKSEISTPSNFEHRIHAGFDARSGTYTGLPKQWQALLGPPRSISRPKPMVDPSCITPVDVAELKTVIRGPSSSFRYNSPLPFGMTNSPMPSVARSNSLRISATASPVVNVSSARHSFRPTLPPVSQRGYPFNDPSYAPLPLRNQKPPMSTTFGVEKPHQYQQIITIVAPSRTTTPQLQPKSPSTPQAMRQQPKCTEGVSDEEFRNALKFVVDGTDPRSDLTDYKQIGEGSTGVVEAAYKISTKQIVAVKRMNLRKQQRRELLFNEVSILRQYQHPNIVRFFSSHLVDDELWVVMEFMEGGSLTDIVTATRMTEPQIATISRQVLGALDFLHARKVIHRDIKSDSILLKRDGTVKLTDFGFCGQLSEEVPRRRSLVGTPYWTAAEVIAREPYDTRADIWSFGIMLIEMVEGEPPFFNDQPFQAMKRIRDEHEARFSRHAKVSVELSELLSHCIVKDVNKRWPAKDLLRHPFFAKAQHSSSIAPLLLQLQGNTINGNNPPTHHHSSQITTVIQ | Cofactor: Divalent cations such as magnesium or manganese.
Function: Serine/threonine-protein kinase which plays a redundant role with pak-1 in embryogenesis but, in contrast to pak-1, is not involved in commissural axon guidance of ventral cord motoneurons or in distal tip cell (DTC) migration.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 58837
Sequence Length: 522
EC: 2.7.11.1
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P28178 | MGKGQSKIKNGGSGKPAKAGKPKKGNKNDETTPTSTPTPTPTPTQQNLDNSAQQQQQQQQTTTAAVSLDNKEQQQQQNIPAPATQTPITQTGTPTIEESQKNTDNNNINGASNEASSSPDSPNGSGNGNDDEDEGPEEVIFSKNKQSATKDDFELLNVIGKGSFGKVMQVKKKGEDKIFAMKVLRKDAIIARKQVNHTKSEKTILQCISHPFIVNLHYAFQTKDKLYMVLDFVNGGELFFHLKREGRFSEPRVKIYAAEIVSALDHLHKQDIVYRDLKPENILLDSEGHICITDFGLSKKIETTDGTFTFCGTPEYLAPEVLNGHGHGCAVDWWSLGTLLYEMLTGLPPFYSQNVSTMYQKILNGELKIPTYISPEAKSLLEGLLTREVDKRLGTKGGGEVKQHPWFKNIDWEKLDRKEVEVHFKPKVKSGTDISQIDPVFTQERPMDSLVETSALGDAMGKDTSFEGFTYVADSILKD | Function: Required for morphogenesis during multicellular development. Phosphorylates talB, gefN, gefS, PI4P 5-kinase and gacQ.
PTM: Seems to be myristoylated.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52994
Sequence Length: 479
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P41676 | MKPEQLVYLNPRQHRIYIASPLNEYMLSDYLKQRNLQTFAKTNIKVPADFGFYISKFVDLVSAVKAIHSVNIVHHNINPEDIFMTGPDFDLYVGGMFGSLYKTFIKNNPQNITLYAAPEQIKKVYTPKNDMYSLGIVLFELIMPFKTALERETTLTNFRNNVQQMPASLSQGHPKLTEIVCKLIQHDYSQRPDAEWLLKEMEQLLLEYTTCSKKL | Function: Plays a role in the inhibition of host eIF2alpha/EIF2S1 phosphorylation, thereby increasing viral fitness. In the insect host, targets the endogenous insect heme-regulated inhibitor (HRI)-like eIF2alpha kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 24944
Sequence Length: 215
Subcellular Location: Host cytoplasm
EC: 2.7.11.1
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Q9TXI7 | MIPGMRATPTESFSFVYSCDLQTNVQVKVAEFEGIFRDVLNPVRRLNQLFAEITVYCNNQQIGYPVCTSFHTPPDSSQLARQKLIQKWNEWLTLPIRYSDLSRDAFLHITIWEHEDDEIVNNSTFSRRLVAQSKLSMFSKRGILKSGVIDVQMNVSTTPDPFVKQPETWKYSDAWGDEIDLLFKQVTRQSRGLVEDVPWLDPFASRRIEMIRAKYKYSSPDRHVFLVLEMAAIRLGPTFYKVVYYEDETKNMRVSTSVNGGVGIVSACTRYCVADPELLLESLAEVKHSAMTRRIRDVEDERHRQVKPNKQAKDRLETIVNLPSSQVLTREQRDLVWKFRHYLRQFPKALNKYLRSVNWVHPQEVKTALALMNDWELIEAEDALELLSSAFTHPAVRAYSVSRLLEAASPEQVLLYLPQLVQALKYEQGQQLPEEGNPVPVVSEEEGKIPSVATTPTEELEGRDMTVVTKKEARKAASGDLATFLIDYALASPKVSNYLYWHLKTEIESTKESKEEHSKMYQNIQDRLMEALVKRPDTRAQVDSLHQQQIFVEDLIILMNEAKARGGRLNESKSAEFRTMLSRAKHMLDLKGVHLPLDPSFRLSSVIPDTASFFKSEMMPAKISFKVLQPNGKADRNIPEEYTVIFKTGDDLRQDQLIQQMVRLIDIILKKGQLDLKLTPYLVLSTGVGQGFVQCIKSKPLRAIQEQYKAHKMDCIREAMKELRPGDGPFGIEPNVIDNYVRSLAGYSVIMYILGLGDRHLDNLLLCENGKLFHVDFGFILGRDPKPMPPPMKLTSEMVQVMGGVKSKQFLEFVQHVDSAYRILRRHSNVLLNLFSLMLDAGIPDIAAEPDKAIFKIEQRLRLDLSDEAATKHIFTQIESSLNAKMAMISDIIHAYKQNLM | Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate . Together with bec-1, mediates the production of phosphatidylinositol 3-phosphate on intracellular vesicles and thereby regulates membrane trafficking . Plays a role in endosome-to-Golgi retrograde transport of mig-14 . Involved in clearance of apoptotic cell corpses by phagosomes . Phagosome maturation requires two sequential and non-overlapping pulses of phosphatidylinositol-3-phosphate (PI3P) on the vesicle surface which mediates recruitment of sortins snx-1 and lst-4 and small GTPases rab-5, rab-2 and rab-7, downstream of dynamin dyn-1 . The first pulse is initiated by piki-1, then maintained by vps-34 which also produces the second pulse . Required for embryonic development . Together with bec-1, involved in L3/L4 larval molting stage probably by regulating cuticle shedding . Regulates the expansion of the nucleus outer membrane . Involved in the secretion and localization of lrp-1 at the apical surface of hyp7 syncytium . May regulate endocytosis in hypodermal cells . May play a role in the formation of gut granules (a lysosome-related organelle) . Plays a role in germ stem cell proliferation during larval development .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 103059
Sequence Length: 901
Subcellular Location: Nucleus outer membrane
EC: 2.7.1.137
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Q8NEB9 | MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK | Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis . As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding . Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 . Involved in the transport of lysosomal enzyme precursors to lysosomes (By similarity). Required for transport from early to late endosomes (By similarity).
PTM: Ubiquitinated via 'Lys-29'- and 'Lys-48'-linked ubiquitination by UBE3C, promoting its degradation . Deubiquitination by ZRANB1/TRABID promotes its stabilization, leading to autophagosome maturation .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+)
Sequence Mass (Da): 101549
Sequence Length: 887
Subcellular Location: Midbody
EC: 2.7.1.137
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Q6PF93 | MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGSAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQTSASESLSNSGVSSGDIDSSQIITNPLPPVASPPPASKAKEVSDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSETGPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK | Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for transport from early to late endosomes (By similarity).
PTM: Ubiquitinated via 'Lys-29'- and 'Lys-48'-linked ubiquitination by UBE3C, promoting its degradation. Deubiquitination by ZRANB1/TRABID promotes its stabilization, leading to autophagosome maturation.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+)
Sequence Mass (Da): 101487
Sequence Length: 887
Subcellular Location: Midbody
EC: 2.7.1.137
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O88763 | MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKPFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGRAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQASVSESLSSSGVSSADIDSSQIITNPLPPVASPPPASKSKEVSDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSETGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK | Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Involved in the transport of lysosomal enzyme precursors to lysosomes . Required for transport from early to late endosomes .
PTM: Ubiquitinated via 'Lys-29'- and 'Lys-48'-linked ubiquitination by UBE3C, promoting its degradation. Deubiquitination by ZRANB1/TRABID promotes its stabilization, leading to autophagosome maturation.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+)
Sequence Mass (Da): 101534
Sequence Length: 887
Subcellular Location: Midbody
EC: 2.7.1.137
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Q9P7Y3 | MSYWVELWESIFTPGVTPVLAKSAHVACGALVAVFLGLYIGTKSIHCLILFFLAICLWLSLTWFLVELAHARVNNDLQMSSQSANKNDDNSNNQNPSNNKEMSDKESDSATTTQTFSVPEELLRARTTANNS | Function: Functions together with the other V-type ATPase assembly factors in the endoplasmic reticulum to efficiently assemble the V-type ATPase membrane sector V(0).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14613
Sequence Length: 132
Subcellular Location: Endoplasmic reticulum membrane
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Q03880 | MANFFVRLWESVFEPGTSPQLIIATHVSFVALLLTLIWLIYATNGNIHFYALFCISLLLWITVIWFINELSHVKLKDNDELDKDANKKDDSAIKEDSEDKQESGKSTSTARRTQAQSRSRKA | Function: Functions together with the other V-type ATPase assembly factors in the endoplasmic reticulum to efficiently assemble the V-type ATPase membrane sector V(0).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13962
Sequence Length: 122
Subcellular Location: Endoplasmic reticulum membrane
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Q8NFJ6 | MAAQNGNTSFTPNFNPPQDHASSLSFNFSYGDYDLPMDEDEDMTKTRTFFAAKIVIGIALAGIMLVCGIGNFVFIAALTRYKKLRNLTNLLIANLAISDFLVAIICCPFEMDYYVVRQLSWEHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLKPRMNYQTASFLIALVWMVSILIAIPSAYFATETVLFIVKSQEKIFCGQIWPVDQQLYYKSYFLFIFGVEFVGPVVTMTLCYARISRELWFKAVPGFQTEQIRKRLRCRRKTVLVLMCILTAYVLCWAPFYGFTIVRDFFPTVFVKEKHYLTAFYVVECIAMSNSMINTVCFVTVKNNTMKYFKKMMLLHWRPSQRGSKSSADLDLRTNGVPTTEEVDCIRLK | Function: Receptor for prokineticin 2. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43996
Sequence Length: 384
Subcellular Location: Cell membrane
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Q8K458 | MGPQNRNTSFAPDLNPPQDHVSLNYSYGDYDLPLGEDEDVTKTQTFFAAKIVIGVALAGIMLVCGIGNFVFIAALARYKKLRNLTNLLIANLAISDFLVAIVCCPFEMDYYVVRQLSWAHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLKPRMNYQTASFLIALVWMVSILIAVPSAYFTTETILVIVKNQEKIFCGQIWSVDQQLYYKSYFLFVFGLEFVGPVVTMTLCYARISQELWFKAVPGFQTEQIRKRLRCRRKTVLLLMGILTAYVLCWAPFYGFTIVRDFFPTVVVKEKHYLTAFYVVECIAMSNSMINTICFVTVKNNTMKYFKKMLRLHWRPSHYGSKSSADLDLKTSGVPATEEVDCIRLK | Function: Receptor for prokineticin 2. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43375
Sequence Length: 381
Subcellular Location: Cell membrane
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Q7VEV2 | MSVIAGVFGALPPYRYSQRELTDSFVSIPDFEGYEDIVRQLHASAKVNSRHLVLPLEKYPKLTDFGEANKIFIEKAVDLGVQALAGALDESGLRPEDLDVLITATVTGLAVPSLDARIAGRLGLRADVRRVPLFGLGCVAGAAGVARLHDYLRGAPDGVAALVSVELCSLTYPGYKPTLPGLVGSALFADGAAAVVAAGVKRAQDIGADGPDILDSRSHLYPDSLRTMGYDVGSAGFELVLSRDLAAVVEQYLGNDVTTFLASHGLSTTDVGAWVTHPGGPKIINAITETLDLSPQALELTWRSLGEIGNLSSASVLHVLRDTIAKPPPSGSPGLMIAMGPGFCSELVLLRWH | Function: Could catalyze the elongation of hydroxybenzoyl-CoA as well as elongation of the aliphatic precursor involved in the synthesis of phthiocerol dimycocerosate (DIM).
Sequence Mass (Da): 37146
Sequence Length: 353
Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 2.3.1.-
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Q948R1 | MRFSLSPVRPHSVVVPSLPKQDVVSYISGTTSNRQCRCVLTLPSPSVSTSRPPVLPKPETWESLLLNHDQIPGEFSPTGSSIPVKLGRRWMEYQGLQNWDGLLDPLDDNLRREILRYGQFVESAYQAFDFDPSSPTYGTCRFPRSTLLERSGLPNSGYRLTKNLRATSGINLPRWIEKAPSWMATQSSWIGYVAVCQDKEEISRLGRRDVVISFRGTATCLEWLENLRATLTHLPNGPTGANLNGSNSGPMVESGFLSLYTSGVHSLRDMVREEIARLLQSYGDEPLSVTITGHSLGAAIATLAAYDIKTTFKRAPMVTVISFGGPRVGNRCFRKLLEKQGTKVLRIVNSDDVITKVPGVVLENREQDNVKMTASIMPSWIQRRVEETPWVYAEIGKELRLSSRDSPHLSSINVATCHELKTYLHLVDGFVSSTCPFRETARRVLHR | Function: Sn-1-specific phospholipase that releases free fatty acids from phospholipids. Low activity on galactolipids and triacylglycerols. Catalyzes the initial step of jasmonic acid biosynthesis. Not essential for jasmonate biosynthesis after wounding or upon pathogen infection.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 49960
Sequence Length: 447
Subcellular Location: Plastid
EC: 3.1.1.32
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Q9MA46 | MAAKVFTQNPIYSQSLVRDKTPQQKHNLDHFSISQHTSKRLVVSSSTMSPPISSSPLSLPSSSSSQAIPPSRAPAVTLPLSRVWREIQGSNNWENLIEPLSPILQQEITRYGNLLSASYKGFDLNPNSKRYLSCKYGKKNLLKESGIHDPDGYQVTKYIYATPDINLNPIKNEPNRARWIGYVAVSSDESVKRLGRRDILVTFRGTVTNHEWLANLKSSLTPARLDPHNPRPDVKVESGFLGLYTSGESESKFGLESCREQLLSEISRLMNKHKGEEISITLAGHSMGSSLAQLLAYDIAELGMNQRRDEKPVPVTVFSFAGPRVGNLGFKKRCEELGVKVLRITNVNDPITKLPGFLFNENFRSLGGVYELPWSCSCYTHVGVELTLDFFDVQNISCVHDLETYITLVNRPRCSKLAVNEDNFGGEFLNRTSELMFSKGRRQALHFTNAATNAAYLLCSISNHMLYYNIF | Function: Sn-1-specific phospholipase that releases free fatty acids from phosphatidylcholine. Has a higher galactolipase activity than phospholipase A1 activity when digalactosyldiacylglycerol (DGDG) is used as substrate. Catalyzes the initial step of jasmonic acid biosynthesis. Required for the biosynthesis of basal-level endogenous jasmonate in vegetative tissues. Regulates leaves growth. Not essential for jasmonate biosynthesis after wounding or upon pathogen infection.
Catalytic Activity: a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+)
Sequence Mass (Da): 52800
Sequence Length: 471
Subcellular Location: Plastid
EC: 3.1.1.26
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O23522 | MQTLTPNADIFHAKRRRFTCNTHTSTLIPTKPLSVSPARKTNKEHLRNLENVLRTSSNSIDHIENVTSRQEKTTKNTSTSSLLGGLNLARIWPQMKAAVDEMSPKNLKRLQRLLSKSSEERSPKSKLGSKWRELHGLNNWAGLLDPLDENLRRELVRYGEFVQAAYHAFHSDPEGSPRHVALPDGSFKVTKSLYATSSVRLPKWIDDVAPDLRWMTKQTSWVGYVAVCDDPREIRRMGRREIVIALRGTATLLEWSENFRPNLVSMPEPKPDQSDPTRPKVECGFNSLYTTGDQHAPSLAESLVGEISRLVELYAGEELSISVTGHSLGAAIALLAADDIAERVPHAPPVAVFSFGGPRVGNREFADRLDSKGVKVLRVVNSQDVVTKVPGIFADNDKQGQSRNNGRSPGGIMEMVERNNPWAYSHVGAELRVDMKMSPYLKPNADVACCHDLEAYLHLVDGFLASNCPFRANAKRSLRKLLDEQRSNVKVLYTGKSLRLNRTFHDNGDVLPSPSSS | Function: Acylhydrolase that catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. Has a strong galactolipase activity toward digalactosyldiacylglycerol (DGDG). Hydrolyzes triacylglycerol (TAG), but has a low activity toward phosphatidylcholine (PC) and monogalactosyldiacylglycerol (MGDG).
Sequence Mass (Da): 57640
Sequence Length: 517
Subcellular Location: Plastid
EC: 3.1.1.-
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Q941F1 | MATIPSHNLRPHTTNQRTQYSLSFRPHFSRSTLITFPARSSPARAMSRTDEEASISTRLEQESYGLTTAEDIRRRDGEAKESKRLRDTWRKIQGEDDWAGLMDPMDPVLRSELIRYGEMAQACYDAFDFDPFSRYCGSCRFTRRHLFDSLGIIDSGYEVARYLYATSNINLPNFFSKSRWSKVWSKNANWMGYVAVSDDNEATRCRLGRRDIAIAWRGTVTRLEWIADLKDFLKPVSGNGFRCPDPAVKAESGFLDLYTDKDTSCNFSKFSAREQVLTEVKRLVERYGDEEGEELSITVTGHSLGGALAVLSAYDVAEMGVNRTRKGKVIPVTAFTYGGPRVGNIRFKERIEKLGVKVLRVVNEHDVVAKSPGLFLNERAPQALMKLAGGLPWCYSHVGEMLPLDHQKSPFLKPTVDLSTAHNLEALLHLLDGYHGKGQRFVLSSGRDPALVNKASDFLKDHFMVPPYWRQDANKGMVRNTDGRWIQPDRIRADDQHAPDIHQLLTQLHHPSQLL | Function: Acylhydrolase with a broad specificity. Catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. Moderate activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG). May display dual sn-1/sn-2 substrate specificity. Could be involved in early wound response.
Catalytic Activity: 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate
Sequence Mass (Da): 58445
Sequence Length: 515
Subcellular Location: Plastid
EC: 3.1.1.-
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Q3EBR6 | MAAIPSHNNLLTINHKNSITGSSSLNTNFSEINFPAKFRVATRALSRTDESSLSAVISRLERERRERQGLLIEEAEGAGELWMTAEDIRRRDKKTEEERRLRDTWRKIQGEDDWAGLMDPMDPILRSELIRYGEMAQACYDAFDFDPASKYCGTSRFTRLEFFDSLGMIDSGYEVARYLYATSNINLPNFFSKSRWSKVWSKNANWMGYVAVSDDETSRNRLGRRDIAIAWRGTVTKLEWIADLKDYLKPVTENKIRCPDPAVKVESGFLDLYTDKDTTCKFARFSAREQILTEVKRLVEEHGDDDDSDLSITVTGHSLGGALAILSAYDIAEMRLNRSKKGKVIPVTVLTYGGPRVGNVRFRERMEELGVKVMRVVNVHDVVPKSPGLFLNESRPHALMKIAEGLPWCYSHVGEELALDHQNSPFLKPSVDVSTAHNLEAMLHLLDGYHGKGERFVLSSGRDHALVNKASDFLKEHLQIPPFWRQDANKGMVRNSEGRWIQAERLRFEDHHSPDIHHHLSQLRLDHPC | Function: Acylhydrolase with broad specificity . Catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position . Possesses moderate activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG) .
Catalytic Activity: 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate
Sequence Mass (Da): 60402
Sequence Length: 529
Subcellular Location: Plastid
EC: 3.1.1.-
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Q9C8J6 | MASLSLPITLKNPRFFSSSPQNIFKTQPQTLVLTTKFKTCSIICSSSCTSISSSTTQQKQSNKQTHVSDNKREEKAEEEEEEKEVSLREIWREVQGCNNWEGQLDPMNNHLRREIIRYGEFAQACYDSFDFDPHSKYCGSCKYHPSDFFLNLDLHLHKGYTITRYLYATSNINLPNFFQKSKLSSIWSQHANWMGFVAVATDEEEVSRLGRRDIVIAWRGTVTYLEWIYDLKDILCSANFGDDPSIKIELGFHDLYTKKEDSCKFSSFSAREQVLAEVKRLIEYYGTEEEGHKTSITVTGHSLGASLALVSAYDIAELNLNHVPENNYKIPITVFSFSGPRVGNLRFKERCDELGVKVLRVVNVHDKVPSVPGIFTNEKFQFQKYVEEKTSFPWSYAHVGVELALDHKKSPFLKPTKDLGCAHNLEALLHLVDGYHGKDEEAEKRFCLVTKRDIALVNKSCDFLRGEYHVPPCWRQDENKGMVKNGDGQWVLPDRPLLEPHGPEDIAHHLQQVLGKVNDDNFKPTTT | Function: Acylhydrolase that catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. Moderate activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG).
Catalytic Activity: 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate
Sequence Mass (Da): 60321
Sequence Length: 527
Subcellular Location: Plastid
EC: 3.1.1.-
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O82274 | MVGDIATRWKELSGSSKWKDLLDPLDLDLRRYILHYGDMAEVGYLAFNSDRRSKYVGDSCYTKEELFARTGYLKANPFRYEVTKYIYGTSSIRLPECFIIKSLSREAWNKESNWLGYIAVATDEGKKLLGRRGIVVAWRGTIQLYEWANDFDFPLESAVMVFPGANPNDEPRVANGWLSLYTSTDPRSRFDKTSAQEQVQEELKRLLELYKNEDVTITLTGHSLGAVMSILSAADFLHNEWPKITPSLQHSLCVTVFAFGSPQIGDRSFKRLVESLEHLHILRVTNVPDLIPRYPVFRFTDIGEELQINTLKSEYLKRSLNLGHFHNLEAYLHGVAGTQHNQGEFKLEINRDIALVNKGLDALEDKYLVPGHWWVLENKGMVQSDDGTWKLNGDRSKKKQEEEDEKEENNCKFP | Function: Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
Sequence Mass (Da): 47581
Sequence Length: 414
Subcellular Location: Cytoplasm
EC: 3.1.1.-
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Q6NYZ4 | MAWKWIKAFVYLSVCVTSALGDDEEASASKCADFNNTTWLEYRQATKLQVQYLLLTRKNANCASLFTQDCLNHTQKHTAYFNSSLPTKVIVHGYRALGSKPSWVSGLAQALLREEDVNVLVVDWVYGASFAYNLVVENYKEVAVQISVLINQLTKYGSTLESFHFIGVSLGAHVSGFVGTLFHGKLGRITGLDPAGPMFKSADPFDRLDSSDALFVEAIHTDSDYFGISIPVGHVDFFLNGGMDQAGCARSRFASMYGYVICDHMRALHVYMSALNGSCPLIGFPCSGYEEFLAGKCITCDDPFNGTCPQIGLLKNSGITATPLPNQEKVYLLTTASGPFCAHHILVELNVSRLDKTAEVQLILKSIGHPETELNLKLYTDETRYKTVAAHPEQLCKIDSMQLINTGGRFYRQGDIHFEYICISEIPQTRGMDPLCVKNIHIGRGVPWSHDFVQVC | Function: Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids. Hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1-acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI).
Catalytic Activity: 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine
Sequence Mass (Da): 50476
Sequence Length: 456
Subcellular Location: Secreted
EC: 3.1.1.-
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A0A0R4IY06 | MDNQQRRTDNMASGETDHLQCVEEPQPGDLIEIFRPAYQHWALYLGDGYIINLTPVDEGQATAVSSVKSVFSRKAVVRMQLLKEVVGADSYRINNKYDDDHTPLPVSEIIQRAQMLIGQEVSYDLLGSNCEHFVTLLRYGEGVSEQASRAIGAISLVTAAASAFSVLGLINTRSRNRPF | Function: Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid. Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE) which serves as precursor for N-acylethanolamines (NAEs) (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light . Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19845
Sequence Length: 179
Domain: The C-terminal transmembrane domain is required for the targeting of the protein to damaged organelles.
Subcellular Location: Membrane
EC: 2.3.1.-
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Q9HDD0 | MAFNDCFSLNYPGNPCPGDLIEVFRPGYQHWALYLGDGYVINIAPVDGIPASFTSAKSVFSSKALVKMQLLKDVVGNDTYRINNKYDETYPPLPVEEIIKRSEFVIGQEVAYNLLVNNCEHFVTLLRYGEGVSEQANRAISTVEFVTAAVGVFSFLGLFPKGQRAKYY | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid . Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE) which serves as precursor for N-acylethanolamines (NAEs) .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18750
Sequence Length: 168
Subcellular Location: Membrane
EC: 2.3.1.-
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