ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q09905 | MIYAVFIFNNKGKPRLTKFYTPIDESIQQKLIGDIYAAVSTRPPTACNFLESNLIAGKNRIIYRQYATLYFVFVVDEGESELGILDLIQVFVEALDRCFNNVCELDLVFKFQEIHAILAEVVSGGLVLETNLNEIVLAAQNQMPKTKRSNAMPFSNTLSSFATRF | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18643
Sequence Length: 165
Subcellular Location: Golgi apparatus
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P47064 | MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSDFQSSFLVTPPSLLLSNENNNDEVNNEDIQIIYKNYATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELNKAAESTDSKIGRLTSTGFGSALQAFAQGGFAQWATGQ | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. Required for the transport via the ALP pathway, which directs the transport of the cargo proteins PHO8 and VAM3 to the vacuole.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21938
Sequence Length: 194
Subcellular Location: Golgi apparatus
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P9WEP1 | MDIYVVGPFGHAMDLLPNPTRPFSGRLHELSALALQRPQLVITTLGALLLAAFYLLPSKDPYNLKRIPMVSRSRVLDAYRSGVWWRFILPRFYPYIHEGYLKYSTKDRPFRVWLAQFQIWVYILPLKYLPLVKNQGITELSLRDFIDKATSAQLSSGSFDTFEVQVGSKLLNGNLIDIKPIVQTRTEQILERVIGRPREWRRFNIRALSVQVVKHVSARIAFGEALADNPGFLDAMERYSLNVIPYTLVFRYFNLGPLRYPLLYLIHLRQRQTLAVATRYVTDLIAERQRKEKEHRLDGDERPVDCIQWSMDQDIPDEQKAPEAVAHRLLHISAALIDAPITSMMNVLADIISYARDEVLDDLRAEIVECLAEFDGAWTEASMAKMKKLDSFFQESFRMTSGLIPLTGWRLIKADCFRFDNDLVLPRGSTIVFPTQCIQLDPNIYPNPDKFDYLRFYRMKEHTQSTDARTGKEVPRHEWLSFGHGRQACPGRFYSIRLLKTILGEMMLRYDIRYAGGDRPRPPMIDLEPILAPDTSVELEFRVRQNVT | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspergiltriene A, aspergildienes A-D and aspergilols A-D . The bifunctional terpene synthase AuAS converts DMAPP and IPP into sesterterpenes . The C-terminal prenyltransferase (PT) domain of AuAS catalyzes formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP into 5 distinct sesterterpenes: aspergiltriene A, aspergildiene A, aspergildiene B, aspergildiene C and aspergildiene D . The cytochrome P450 monooxygenase AP450 then hydroxylates the aspergildienes A, B, C and D to yield the corresponding sesterterpene alcohols, aspergilols A-D .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 63447
Sequence Length: 548
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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P54456 | MNREEALACVKQQLTEHRYIHTVGVMNTAIELAERFGADSKKAEIAAIFHDYAKFRPKEEMKQIIAREKMPAHLLDHNPELWHAPVGAYLVQREAGVQDEDILDAIRYHTSGRPGMTLLEKVIYVADYIEPNRAFPGVDEVRKLAETDLNQALIQSIKNTMVFLMKKNQPVFPDTFLTYNWLVSGS | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 21282
Sequence Length: 186
EC: 3.6.1.41
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Q88A48 | MAVYAVGDLQGCLEPLQCLLEHVRFDPVQDRLWLVGDLVNRGPQSLQTLRYLYSIRESLVCVLGNHDLHLLAVARKNELLKKGDTLREILEAPDRDELLRWVRQQKLMHYDAERNIAMVHAGIAPQWSVKKALKQAAEVEHALQDDQLYGAFLDGMYGNEPAKWNNDLQGVTRLRVITNYFTRMRFCTSDGKLDLKSKEGVGTAIPGYAPWFSHQNRKTRDVKIIFGHWAALEGRCDEPGVFALDSGCVWGGAMTLLNVDTLERHQCNCDAVGNAATGIIASAQPGNAHIQQIPAQEPKQ | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 33622
Sequence Length: 300
EC: 3.6.1.41
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A1STS0 | MATYIVGDVHGCFDELQALLELAQFKKNKDQLWITGDLVGRGPKSLETLRFVKSLGDSAKIVLGNHDLHLLAIHQGIHSDKESDKLSALLNAPDCDELLTWLRFQPLFRRHPEFNFVMVHAGISPQWTIQQAQGYAQEVQNILQGNEFKKLLKNMYGNHPASWNDSSQGIKRLRFIINALTRMRYCLLDGSLEFYSKLAPEQTDSTIIKPWFEINTLDQSSDIIFGHWAALLGTGTKQGIYALDTGCVWGNSLSMLRWQDKKMFSFACQRQRVHSK | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 31453
Sequence Length: 276
EC: 3.6.1.41
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Q8Y1K9 | MTVASIPPHAIGDLQGCCSPLQTLLTALPANAPLRFVGDLVNRGPDSLGTLRRVIMLCEGGRARAVLGNHDIHLLAVAAGVRKLGKRDTLDDILGAPDCDALIHWLRHQPLAIFENGFLMVHAGVLPQWTTGDVLELAGAVERELRSPHWKTFLTDAFGNQPAKWSSDLIGIDRLRLTINALTRLRFCTPDGAMEFETTDADGAPDGHVPWFDVPGRRTRGTPIAFGHWSTRGLVMRDDLLGLDTGCVWGGKLTAARMTLAPAGREVIQVACEQAQDPLAHKK | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 30660
Sequence Length: 283
EC: 3.6.1.41
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Q21MT2 | MATYAVGDIQGCYRALKLLLKKVKFNADNDHLWVAGDLVNRGPESLKSLRYIKKLGPSATLVLGNHDLHLLAHAYGVRTLNPKDTLAPILTAKDSDELLEWLQAQPLLHYDAEFDAVLVHAGIPPIWSIENALNYALEVEQALSTTQTAAAFFVDMYGNQPDVWQPSLEGTARLRLITNYLTRMRFCSPTGKLELQTKNAPSLPPTGFAPWYTHKHNKWGNTKILFGHWAALMGETRSKQFIGLDTGCVWGGALTMMRLEDGQFFAVDCPC | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 30183
Sequence Length: 271
EC: 3.6.1.41
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Q28IW8 | MDSEVLRDGRILDLIDDAWREDKLPYEDVTIPLNELPEPEQDNGGATESVKEQEMKWADLALQYLHENISSSGS | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
Sequence Mass (Da): 8417
Sequence Length: 74
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q58DR0 | MAASSSSSSAGGVSGSSVAGSGFSVSDLAPPRKALFTYPKGAGEMLEDGSERFLCESVFSYQVASTLKQVKHDQQVARMEKLAGLVEELEADEWRFKPIEQLLGFTPSSG | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
Sequence Mass (Da): 11637
Sequence Length: 110
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q96DE5 | MAASSSSSSAGGVSGSSVTGSGFSVSDLAPPRKALFTYPKGAGEMLEDGSERFLCESVFSYQVASTLKQVKHDQQVARMEKLAGLVEELEADEWRFKPIEQLLGFTPSSG | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Sequence Mass (Da): 11667
Sequence Length: 110
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q6DJQ9 | MAASSSSSSAGGVSGSSVTGSGFSVSDLAPPRKALFTCPKAAGEMLEADGSERFLCESVFSYQVASTLKQVKHDQQVSRMEKLAGLVEELEADEWRYTPIEQLLGFTPSSGGK | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
Sequence Mass (Da): 11882
Sequence Length: 113
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q5ATG7 | MSSVRESSKDESIVHPPKAPESEPFPDGGARAWMVALGAGGVLFCTFGYVNAFGVYQDYYITHQLSNYSASDIAWIGSVQTFFLFGSGLVGGPLFDRYGAKVIWAPAVLVIFSVMMTSLCTKFYQFFLAQGILGGMSMGLSLAPALSSTAQYFQKKRAAAMGITIAGSSLGGVIFPIALEQMLYSSLGFAWAVRIVGFIILGVMSFAVLGIRARLPPKRQRFLKLEAFKKTHYVATLTAVFFLNVGIFTPFFYLPLYGQSHGMSTGLAFYLIAIQNASSFFGRLVPGVIADKIGPYNMLSTVSIITAIITFCWIRMTTNASIIVFSVLYGFFSGGIIGITPAAIANCAGHPQEIGTYIGMGMAVMSVATLIGPPINGALLNEYGGFLQVQIFSAAVMMFGGVLAFGAKMISFSGEGKGMRKFDHAVAGLAYYVREGGSRMEHIYFGSVAIVAGHLHGPVCAQNKRQMLVTGIGAEMVYVLEYFVEAG | Function: Efflux pump that may be involved in the secretion of aspyridones .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52253
Sequence Length: 487
Subcellular Location: Cell membrane
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Q5ATG5 | MAEISSVPFAEPPYLRGLPSPYYNESHRRFQKACRAFLYENLLKHAMEWEKAGTVPEHVFSDFCKANMLLPNLPAPLPVAWLKRLGIHDILGVKVEEWDYLHTGIYSDEMARSGLSGPSGSLTAGFAFGTPPIIKYGSKELQEKFLPDLLTGKKRNCIAITEPDAGSDVAGITTTATKSADGKYYIVNGNKKWITNGIWSDYSTMAVRTGGPGAGGLSLLVVPLKNYPGVTMQRLKVSGQITGGTTYIELDEVKVPVENLIGLEGDGMKMIMNNFNHERLTIAVGVTRQARVALSTAFSYCLKREAFGKTLMDQPVVRHRLAKAGAELETMWAFVEQLLYQLTNLPKEEADRQLGGITAMAKAKGAMVLNECAQTAVLLFGGAGFTKQGQGELAEAILRDVPGARIPGGSEDVLLDLSIRQLVKLFKAEEKKLGKARI | Function: Acyl-CoA dehydrogenase; part of the gene cluster that mediates the biosynthesis of aspyridones . The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA . The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to yield the acetyl starter unit . The growing polyketide chain then elongates into a tetraketide . The adpA PKS module catalyzes three Claisen condensations, as well as beta-keto processing and methylation . Alpha-methylation step during polyketide synthesis is a prerequisite and a key checkpoint for chain transfer between PKS and NRPS modules . The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the incorporation of tyrosine via the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide . The bimodular assembly line is terminated with a reductase (R) domain that facilitates formation and release of the tetramic acid product . Because apdA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase apdC (PubMed:17369821, PubMed:20828130, Ref.5). ApdC appears to operate with different stereoselectivity in different PKS cycle (Ref.5). Combined with apdC, apdA is proposed to synthesize preaspyridone A via about 20 enzymatic steps . A number of oxidative steps performed successively by the cytochrome P450 monooxygenases apdE and apdB are required for the conversion of preaspyridone A to aspyridone A . The cytochrome P450 monooxygenase apdE is responsible for the oxidative dephenylation of preaspyridone A (Ref.5). Finally, the predicted FAD-dependent monooxygenase apdD and the acyl-CoA dehydrogenase apdG may be involved in the transformation of aspyridone A into aspyridone B (Probable).
Sequence Mass (Da): 47824
Sequence Length: 438
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q5XF07 | MKRFFKPIEKENSPAAKKPCLSPEKRDGDGDGVEEEKNQNEPSKFMTWNANSFLLRVKNDWSQFSKFVSDFDPDVIAIQEVRMPAAGGKGKPKNHEELSDDTKVLREEKQILTRALSSPPFGNYGVWWSLADSKYAGTALLVKKCFKPRKVYFNLDKLASKHEPDGRVILAEFETFRLLNTYSPNNGWKDEENAFQRRRKWDKRIVEFLNKTSDKPLIWCGDLNVSHEEIDVSHPEFFATAKLNGYVPPNKEDCGQPGFTPSERGRFGATIKEGRLVDAYRYLHKEQEMESGFSWSGNPIGKYRGKRMRIDYFLVSEQLKDRIVSCKMHGRGIELEGFHGSDHCPVTLELSKPSSEMEQNQVSN | Cofactor: Probably binds two magnesium ions per subunit.
Function: Apurinic/apyrimidinic (AP) endonuclease involved in active DNA demethylation and gene imprinting . According to a report, also displays an in vitro 3'-phosphatase activity . According to another report, has no in vitro 3'-phosphatase activity . Catalyzes the conversion of the 3'-blocking groups 3'-phosphor-alpha,beta-unsaturated aldehyde (3'-PUA) generated by ROS1 to 3'-OH . Has a strong non-specific affinity to DNA . Redundant with APE2 and at least one functional allele is required for seed viability .
Sequence Mass (Da): 41783
Sequence Length: 364
Subcellular Location: Nucleus
EC: 3.1.-.-
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O73942 | MDGYALFYLVGALRDGSVYRYSRNYYVIWYSSNKDYLERVIVSKLRILGFHNVRVYQYKRGAYRVRISSKQLFHILVNQFEHPLSTSSRKTPWPTPQRVKDGPLALQIEYVKGFVDAEGSVIKSSKGVQVDVSQQIMEPLKFLAQVLEKVGVKVTGIYLGSDGVWRLRIASLASLRRFAHYIGFRHPCKSKKLNELLGRPLPGPSKLKGIGGGAPQGVEPAA | Cofactor: 1-5 mM manganese gives higher cleavage activity than the same concentration of magnesium.
Function: Endonuclease involved in 16S rRNA intron I-alpha homing. Recognizes the minimal target 5'-GCAAGGCTGAAACTTAAAGG-3'; generates 4 base 3' protruding ends 5'-AAAC-3' and 5'-GTTT-3'.
Sequence Mass (Da): 25031
Sequence Length: 222
EC: 3.1.-.-
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Q97VF1 | MPNIEKYEIFLDFNGNEYEGVEKIYLNSEEEKLELDSVNLEIRSVKSDGKDTKFELKGEKLVIYGKIERELEIKFKGKASRDSILGIYVAPYDGKGMITTQFEAVYARRFIPCFDHPAMKARFKLSVRVQKGLKVISNMPVERIEEDVDGKVIYRFQETPKMSTYLLYLGIDEFEEISDNSKQPTVILATVPGKSKRGLFAINVARKVIEFYEKYFEIPYQLPKVHLIQVPEFAAGAMENWGAITFRETALLADDSSSISQKFRVAEVVAHELAHQWFGNLVTLKWWDDLWLNESFATFMSYKSIKHLFPQWDSEGHLIYDESIGALEDDSLSTTHPIEAHVKDPHEIEQMFDNISYGKGASILKMIEAYVGEENFRRGVVNYLNSFKFGNAEGKDLWNSISNAAGQSIGEIMADWITKPGYPVIFVNAYGNSIRFSQKRFTLLDSGLNEVYKVPITYEINDKFGTLLLDKESAEIRLDEGLKSIKVNINRTGFYRVLYDSLNLAFSSKLNAYEELGLVNDYWNFLLADLIDAKTYFGVIGRFVYTSNSFVSREITSQLLTLYYLFKKNYGKDFLVNQVKIFRKANDDLGKLAYSTVISALARMDEEFALGLSTLFDQYENIDSNIKEAVAIAYAVTNNDFNTLLEKYKRYTIDEEKNRILSAISSLRDPSIVVKVFSLIFERNIKAQDTRFVISSLLHNPHIREEVCSYLMNNFEEVKKFVNTVYGGPWGLGSIVRSMSFCGVDKPKDIIDFLEKVKFKEIERPIKESEERIKVYSRLKQNLP | Cofactor: Binds 1 zinc ion per subunit.
Sequence Mass (Da): 90143
Sequence Length: 784
Subcellular Location: Cytoplasm
EC: 3.4.11.-
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F4JNY0 | MKIVTYNVNGLRQRVSQFDSLLKLLDSFDADIICFQETKLRRQELTADLAIADGYESFFSCTRTSEKGRTGYSGVATFCRVKSASSSCETALPVTAEEGITGLVNSNSRGGKSETSTVAEGLEEYEKEELLMIDQEGRCVITDHGHFVVFNVYGPRAVADDADRIEFKHRFYGVLERRWECLLRQGRRVFVVGDLNIAPFAMDRCEAGPDFEKNEFRKWFRSLLVERGGSFSDVFRSKHPERKDAFTCWSSSSGAEQFNYGSRIDHILVAGSCLHQDEDKQGHSFLACHVKECDILTEYKRFKNENMPTRWKGGLVTKFKGSDHVPVFISFDDLPDIPEHSTPPLASRYLPMIYGFQQTLVSVFKKRRANEEAKAIEVSCSSSTQSNTSSICGDISTGPLRNCGSMGISLEKSCSFENKSTSGVTEAETVAATGSIDNLSDGIRASSVRALNISRDGDRKKARKIQSSQLSLKSFFTTNSKVNNVEDSSSSYVSSSPSSQVESITEPNVSGKEDSEPTTSTQEQDQTGSSAKQKNDAALMEWQRIQNLMQNSIPLCKGHKEACVARVVKKPGPTFGRRFYVCSRAEKQTVVISNGLHQNSETSKRVMRSK | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Function: Exhibits apurinic/apyrimidinic (AP) endonuclease activity in vitro . By contrast, another report show that APE2 has no biochemical activity . Unable to catalyze the conversion of 3'-phosphor-alpha,beta-unsaturated aldehyde (3'-PUA) to 3'-OH . Has no in vitro 3'-phosphatase activity . Redundant with APE1L and at least one functional allele is required for seed viability . Has a strong non-specific affinity to DNA .
Sequence Mass (Da): 67825
Sequence Length: 610
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q59KZ1 | MASNNTSQRSGFSSFFCRLKTYFCNHFLCLFVLSFFPLSFRRLCLLCHLCEKSNLWLSSDNSASVVKQEREVLPTNVKPLHYDLTIEPIFDNFTFKGEETIDFQVNEKTNFITLNSLEIEVQEAKIDGKSVTDISFDAGKQTVTFKFDDDLSTGSIAKLYIKFTGELNDKMAGFYRASYQEDGKTKYMATTQMEPTDCRRAFPSYDEPAAKSKFTISLIADKELVCLSNSSEKETVSLDGNKKKVTFQTTPLMSTYLVAFIVGDLRYISNDNYRVPIRVYSTPGTEHLGEYSANIAAQTLKFFDQQFGIDYPYDKLDMVAVPSFSAGAMENCGLVTFRTVDLLIDADNANVNTKQRVTEVVMHELAHQWFGDLVTMEFWDGLWLNEGFATWMSWYACNSLYPDWKVWESYVSDSLQHALTLDALRASHPIEVPVKRADEINQIFDAISYSKGSSLLRMISKWLGEDVFVKGVSNYLKKHKWGNTKTSDLWEALSEASGEDVVKVMDIWTKNIGFPIVKVEEIGNGEIKVTQNRFLATGDVKESEDKTLYPVFLGLKTSEGVDESSVLETRSKTIKLPTSDDFFKINGDQSGIYRTAYEPARWTKLGKAGVEGKLSVEDRVGLVADAGSLASSGFIKTSSLLDLVKSWSKESNYVVWNEILTRIGSIKAALMFEDEATKKALEIFTRDLISEKLKETGWEFSADDSFADQQLKSSLFASAANAEDPEAVAFAKEAFAKFIAGDKKAIHPNLRASIFNTNAKYGDEKTFDELYNIYRNPSSVEEKIAALRSFGRFTKPEILDKVTGLLLQTDIVKQQDIYIPMQGLRAHKLGVEKLWTWLSENWDQIYILLPPGLSMLGSVVTLGTSGFTKEEQKKKVEEFFAQKDNKGYDQSLAQSLDIITAKSKWTDRDAKSIYEWLEANEYTK | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease that specifically hydrolyzes peptides with N-terminal alanine, arginine and leucine residues.
Sequence Mass (Da): 104382
Sequence Length: 924
Subcellular Location: Secreted
EC: 3.4.11.-
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P95928 | MIKVNRYEIFLDFSFQTGDYKGYEKIEMESDEETVVLDAVGLKIVKAKVNGKEIEFSQDESRVNVKSGSFSGILEVEFEGKVTERKLVGIYKASYKDGYVISTQFEATHARDFIPCFDHPAMKARFKLTVRVDKGLKVISNMPVVREKEENGKVVYEFDETPKMSTYLLYLGIGNFEEIRDEGKIPTIIVATIPGKVQKGRFSMQISRNSIEFYEKYFEIPYQLPKVHLIAIPEFAYGAMENWGAITFRETALLADDSSSVYQKFRVAEVVAHELAHQWFGNLVTLKWWDDLWLNESFATFMSHKAISQLFPSWNFWDYFVLNQTSRALEKDSVSTTHPIEAHVRDPNEVEQMFDDISYGKGASILRMIEAYVGEENFRRGVVNYLKKFSYSNAQGSDLWNSISEVYGSDISPIMADWITKPGYPMVRVSVSGKRVSLEQERFSLIGNVENLLYKIPLTMEVNGKVVTHLLDKERDTMVFEEDVKSLKVNVNRTGFYRVFYYNNSDLVFNSNLSELDKWGIINDYWAFLLAGKIGFKEYERVISKFFNDKDFLPVNELSNELFTLHAINPDKYQGIAKEFHRIQLKNWRNSKDELGRLTYSNILYRLAAIDDEFSLGLSELFRFYGSLDSDTRQGVAVAYAITYEDNSVDELLERFRKETFDEEKLRYLTAMLFFRKPYLVGNTLSLILSGEIKKQDIPLTLSTAAYNPYAKSAVLNWIKMHINFMREAYKGTGILGRRLAEVIPLIGIGAERETEQFFSNLNMPEAERGIGTGLELLKAYSRLK | Cofactor: Binds 1 zinc ion per subunit.
Function: Preferentially acts as a leucyl-aminopeptidase, although it also has activity against other substrates.
PTM: Can be phosphorylated by cell extracts.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Sequence Mass (Da): 90515
Sequence Length: 785
Subcellular Location: Cytoplasm
EC: 3.4.11.1
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P37302 | MHFSLKQLAVAAFYATNLGSAYVIPQFFQEAFQQEEPIENYLPQLNDDDSSAVAANIPKPHIPYFMKPHVESEKLQDKIKVDDLNATAWDLYRLANYSTPDYGHPTRVIGSKGHNKTMEYILNVFDDMQDYYDVSLQEFEALSGKIISFNLSDAETGKSFANTTAFALSPPVDGFVGKLVEIPNLGCEEKDYASVVPPRHNEKQIALIERGKCPFGDKSNLAGKFGFTAVVIYDNEPKSKEGLHGTLGEPTKHTVATVGVPYKVGKKLIANIALNIDYSLYFAMDSYVEFIKTQNIIADTKHGDPDNIVALGAHSDSVEEGPGINDDGSGTISLLNVAKQLTHFKINNKVRFAWWAAEEEGLLGSNFYAYNLTKEENSKIRVFMDYDMMASPNYEYEIYDANNKENPKGSEELKNLYVDYYKAHHLNYTLVPFDGRSDYVGFINNGIPAGGIATGAEKNNVNNGKVLDRCYHQLCDDVSNLSWDAFITNTKLIAHSVATYADSFEGFPKRETQKHKEVDILNAQQPQFKYRADFLII | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: Preferentially, release of N-terminal lysine.
Sequence Mass (Da): 60137
Sequence Length: 537
Subcellular Location: Vacuole
EC: 3.4.11.15
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Q7SZP9 | MEPTSEYTETYDYYDTGYNDSGCDYSEWEPSYSLIPVLYMLIFILGLSGNGVVIFTVWRAKSKRRAADVYIGNLALADLTFVITLPLWAVYTALGYHWPFGVALCKISSYVVLVNMYASVFCLTCLSFDRYLAIVHSLSSGRLRSRATMLASLGAIWFLSCLLAVPTLLFRTTVDDTGSNRTTCAMDFSLVTLNQDHESLWIAGLSLSSSALGFLLPFLAMTVCYCFIGCTVTRHFSHLRKEDQKKRRLLKIITTLVVVFAFCWTPFHVLKSMDALSYLDLAPNSCGFLHFLLLAHPYATCLAYVNSCLNPFLYAFFDLRFRSQCLCLLNLKKAMHGHMSSMSSTLSAQTQKSEVQSLATKV | Function: Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity . Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoting endoderm and mesendoderm cell migration and regulating the migration of cells fated to become myocardial progenitors, respectively . Positively regulates angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis . May promote sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Required for cardiovascular development, particularly for intersomitic vein angiogenesis by acting as a receptor for apln hormone (By similarity). Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility, and heart failure (By similarity). Acts redundantly with agtrl1b in heart development .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40649
Sequence Length: 362
Subcellular Location: Cell membrane
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P79960 | METEGLSPMLYEDDYYYGNETGLQPCDETDWDFSYSLLPVFYMIVFVLGLSGNGVVIFTVWKSKPKRRSADTYIGNLALADLAFVVTLPLWATYTALGFHWPFGSALCKLSSYLVLLNMFASVFCLTCLSFDRYLAIVHSLSSAKLRSRSSIIVSLAVIWLFSGLLALPSLILRDTRVEGNNTICDLDFSGVSSKENENFWIGGLSILTTVPGFLLPLLLMTIFYCFIGGKVTMHFQNLKKEEQKKKRLLKIIITLVVVFAICWLPFHILKTIHFLDLMGFLELSCSTQNIIVSLHPYATCLAYVNSCLNPFLYAFFDLRFRSQCFFFFGFKKVLQGHLSNTSSSLSAQTQKSEIHSLATKV | Function: Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity . Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoting endoderm and mesendoderm cell migration and regulating the migration of cells fated to become myocardial progenitors, respectively (By similarity). Promotes angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). May promote sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Required for cardiovascular development, particularly for intersomitic vein angiogenesis by acting as a receptor for apln hormone . Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility, and heart failure (By similarity). Acts upstream of the i/o type of G-alpha proteins in the differentiation of endothelium, erythroid cells, myeloid cells and cardiomyocytes .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40858
Sequence Length: 362
Subcellular Location: Cell membrane
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A0T2N3 | MNAMDNMTADYSPDYFDDAVNSSMCEYDEWEPSYSLIPVLYMLIFILGLTGNGVVIFTVWRAQSKRRAADVYIGNLALADLTFVVTLPLWAVYTALGYHWPFGVALCKISSYVVLLNMYASVFCLTCLSLDRYMAIVHSLTSTQLRTRGHMRASLTAIWLLSGVLAAPTLLFRTTVYDVETNRTSCAMDFNLVVSQPGQETYWIAGLSISSTALGFLIPLLAMMVCYGFIGCTVTRHFNSLRKEDQRKRRLLKIITTLVVVFAACWMPFHVVKTMDALSYLNLAPDSCTFLNLLLLAHPYATCLAYVNSCLNPLLYAFFDLRFRSQCLCLLNLKKALHASPASSLSSQKTEAQSLATKV | Function: Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity . Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoting endoderm and mesendoderm cell migration and regulating the migration of cells fated to become myocardial progenitors, respectively . Positively regulates angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis . May promote sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Required for cardiovascular development, particularly for intersomitic vein angiogenesis by acting as a receptor for apln hormone (By similarity). Plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure (By similarity). Acts redundantly with agtrl1a in heart development .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40147
Sequence Length: 359
Subcellular Location: Cell membrane
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Q9WV08 | MEDDGYNYYGADNQSECDYADWKPSGALIPAIYMLVFLLGTTGNGLVLWTVFRTSREKRRSADIFIASLAVADLTFVVTLPLWATYTYREFDWPFGTFSCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAVPVMVFRSTDASENGTKIQCYMDYSMVATSNSEWAWEVGLGVSSTAVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDIFLMNVFPYCTCISYVNSCLNPFLYAFFDPRFRQACTSMLCCDQSGCKGTPHSSSAEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVD | Function: Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone . May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development . Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42266
Sequence Length: 377
Subcellular Location: Cell membrane
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Q43295 | MIAAGAKSLLGLSMASPKGIFDSNSMSNSRSVVVVRACVSMDGSQTLSHNKNGSIPEVKSINGHTGQKQGPLSTVGNSTNIKWHECSVEKVDRQRLLDQKGCVIWVTGLSGSGKSTLACALNQMLYQKGKLCYILDGDNVRHGLNRDLSFKAEDRAENIRRVGEVAKLFADAGIICIASLISPYRTDRDACRSLLPEGDFVEVFMDVPLSVCEARDPKGLYKLARAGKIKGFTGIDDPYEPPLNCEISLGREGGTSPIEMAEKVVGYLDNKGYLQA | Function: Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 29787
Sequence Length: 276
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Subcellular Location: Plastid
EC: 2.7.1.25
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O49196 | MEGLAIRASRPSVFCSIPGLGGDSHRKPPSDGFLKLPASSIPADSRKLVANSTSFHPISAVNVSAQASLTADFPALSETILKEGRNNGKEKAENIVWHESSICRCDRQQLLQQKGCVVWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEHRTENIRRIGEVAKLFADVGVICIASLISPYRRDRDACRSLLPDGDFVEVFMDVPLHVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPVNCEVVLKHTGDDESCSPRQMAENIISYLQNKGYLEG | Function: Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 31977
Sequence Length: 293
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Subcellular Location: Plastid
EC: 2.7.1.25
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Q9SRW7 | MSTVGNSTNIFWQESPIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEVAKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNCEIELKEKEGECPSPVAMAEEVISYLEDKGFLQNE | Function: Catalyzes the synthesis of activated sulfate for the sulfation of secondary metabolites, including the glucosinolates . Essential for plant reproduction and viability .
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 23146
Sequence Length: 208
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.25
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Q84JF0 | MDVAAMARCVGRCYVSPAFGESESHRLSERRFLKLSSSTNSDPAGSKSLKLRGKIHRRMSYFRPIMAKDESISSRSGETKQINGKQKNIVWHDCPVTKSDRQELIKQKGCVIWITGLSGSGKSSLACALSRALHNRGKLSYILDGDNVRHGLNSDLSFEADDRAENIRRVGEVAKLFADSGIICIASLISPYRIERAACRALLPQGDFIEVFMDVPLHVCEARDPKGLYKRARAGKIKGFTGVDDPYEAPLDCEIVIQNSRDKGLSSSSSSSSSPSSSSSSLCEMADIVVSYLDQNGYLKKHSTKSRNCM | Function: Catalyzes the phosphorylation of adenosine 5'-phosphosulfate to 3'-phosphoadenylyl sulfate, which is the activated sulfate form for sulfation reactions. Essential for plant reproduction and viability.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 34065
Sequence Length: 310
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Subcellular Location: Plastid
EC: 2.7.1.25
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A1Z9X0 | MQKMPSQILNDGSSVSLNSASMNMANTPNSITVKTAYNGQIIITTINKNISYEELCYEIRNICRFPLDQPFTIKWVDEENDPCTISTKMELDEAIRLYEMNFDSQLVIHVFPNVPQAPGLSCDGEDRSIYRRGARRWRKLYRVNGHIFQAKRFNRRAFCAYCQDRIWGLGRQGFKCIQCKLLVHKKCHKLVQKHCTDQPEPLVKERAEESSDPIPVPLPPLPYEAMSGGAEACETHDHAHIVAPPPPEDPLEPGTQRQYSLNDFELIRVIGRGSYAKVLMVELRRTRRIYAMKVIKKALVTDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTPSRLFFVIEFVRGGDLMYHMQRQRRLPEEHARFYAAEISLALNFLHEKGIIYRDLKLDNVLLDHEGHIKLTDYGMCKEGIRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLLYEMLAGRSPFDLAGASENPDQNTEDYLFQVILEKTIRIPRSLSVRAASVLKGFLNKNPADRLGCHRESAFMDIVSHPFFKNMDWELLERKQVTPPFKPRLDSDRDLANFPPEFTGEAVQLTPDDDHVIDNIDQSEFEGFEYVNPLLMSLEDCV | Function: Serine/threonine protein kinase which is required for apico-basal cell polarity in the germ line as well as in epithelial and neural precursor cells, for epithelial planar cell polarity and for cell proliferation. During oocyte development, required for the posterior translocation of oocyte specification factors and for the posterior establishment of the microtubule organizing center within the presumptive oocyte. Phosphorylates l(2)gl which restricts l(2)gl activity to the oocyte posterior and regulates posterior enrichment of par-1, leading to establishment of correct oocyte polarity. Essential for apical localization of l(2)gl and par-6 in neuroblasts and for exclusion of mira from the apical cortex. Phosphorylates baz which is required for targeting of baz to the postsynaptic region where it is involved in actin organization, and for apical exclusion of baz which is necessary for establishment of the apical/lateral border in epithelial cells. Phosphorylates yrt which prevents its premature apical localization and is necessary for correct epithelial cell polarization. Required for the establishment of mitotic spindle orientation during symmetric division of epithelial cells and for apical exclusion of raps/Pins. Involved in symmetric adherens junction positioning during embryogenesis. Required for polarization of the spermatid cyst which is necessary for sperm differentiation. Required for stimulation of the Toll signaling pathway which activates Dif and dl and plays a role in innate immunity. Plays a role in memory enhancement.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69556
Sequence Length: 606
Subcellular Location: Cytoplasm
EC: 2.7.11.13
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P02656 | MQPRVLLVVALLALLASARASEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQARGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVAA | Function: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma . Plays a multifaceted role in triglyceride homeostasis . Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs) . Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors . Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners .
PTM: The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-94 with a core 1 or possibly core 8 glycan.
Sequence Mass (Da): 10852
Sequence Length: 99
Subcellular Location: Secreted
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P33622 | MQPRTLLTVALLALLASARAEEVEGSLLLGSVQGYMEQASKTVQDALSSVQESDIAVVARGWMDNHFRFLKGYWSKFTDKFTGFWDSNPEDQPTPAIES | Function: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners.
PTM: The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-94 with a core 1 or possibly core 8 glycan.
Sequence Mass (Da): 10982
Sequence Length: 99
Subcellular Location: Secreted
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P53933 | MNSQGYDESSSSTAATSGPTSGDPRMGKKQRFMNLIRTTKDVYIPNLTSSISQKTMDGIRSTTNSFEGYNDLPMELPHNTTITYFPTYTTTNLVDPDGLSAPRKDFETTVRCAVSYPGNPTSRRNRWLLSLCKQYLRTGTAEADVAPVVPPHLEEDSGDLNDSQSSIESSLSSKSENRYSHMGIQEEDVLNERIQGFLSKKVPNTPVVVDLLPKDKLRGDTASFFGTTDSYGNLLIKAETDFLPSKINITLDTPIEGHADPISETFPANYVSPYGIGLISDIDDTIKHTGVTGDRRSMFRNVFIHDVQSWVIDGVPLWYKTLHDVADVDFFYVSNSPIQTFTLLKQYICANFPPGPIFLKQYSGNFFSTIMTSSANRKIQPIANILKDFPKKKFILVGDSGEHDLEAYTTTALQFPNQILAIYIRCCSNSMSDVPSHDEEVMNEVNNIIELQQRPMQMTKSTVRTRRRPPPPPIPSTQKPSLTEEQTESIRMSRRNKDENNAKRVAPPPLPNRQLPNLDANTYYVPSSQNDYGMYGAFMDKKADEWKRRVMDSIQKLSNQDTTLMFFSDPALSLEDSIRRIREKYSN | Function: Mg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. May play a role in vesicular trafficking through its PAP activity at cortical actin patches . Can also utilize diacylglycerol pyrophosphate and lyso-PA as substrates with specificity constants 4- and 7-fold lower, respectively, when compared with PA .
PTM: N-glycosylated.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Sequence Mass (Da): 66134
Sequence Length: 587
Domain: Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity.
Subcellular Location: Cytoplasm
EC: 3.1.3.4
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P42061 | MKRRKTALMMLSVLMVLAIFLSACSGSKSSNSSAKKSAGKPQQGGDLVVGSIGEPTLFNSLYSTDDASTDIENMLYSFLTKTDEKLNVKLSLAESIKELDGGLAYDVKIKKGVKFHDGKELTADDVVFTYSVPLSKDYKGERGSTYEMLKSVEKKGDYEVLFKLKYKDGNFYNNALDSTAILPKHILGNVPIADLEENEFNRKKPIGSGPFKFKEWKQGQYIKLEANDDYFEGRPYLDTVTYKVIPDANAAVAQLQAGDINFFNVPATDYKTAEKFNNLKIVTDLALSYVYIGWNEKNELFKDKKVRQALTTALDRESIVSQVLDGDGEVAYIPESPLSWNYPKDIDVPKFEYNEKKAKQMLAEAGWKDTNGDGILDKDGKKFSFTLKTNQGNKVREDIAVVVQEQLKKIGIEVKTQIVEWSALVEQMNPPNWDFDAMVMGWSLSTFPDQYDIFHSSQIKKGLNYVWYKNAEADKLMKDAKSISDRKQYSKEYEQIYQKIAEDQPYTFLYYPNNHMAMPENLEGYKYHPKRDLYNIEKWWLAK | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence. AppA can bind and transport tetra- and pentapeptides but not tripeptides.
Location Topology: Lipid-anchor
Sequence Mass (Da): 61917
Sequence Length: 543
Subcellular Location: Cell membrane
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P42062 | MAAYIIRRTLMSIPILLGITILSFVIMKAAPGDPMTLMMDPKISQADREQFIEKYGLNDPQYVQYLKWLGNMVQGDFGTSIVRKGTPVSELIMARLPNTLLLMLVSTILALMISIPFGVLSAKRPYSKIDYGITFTSFIGLAIPNFWFGLILIMVLSVNLGWFPTGGVETLNTEFNIFDRIHHLILPAFVLATADMAGLTRYTRSNMLDVLNQDYIRTARAKGFKENRVLFKHGLRNALLPVITIFGLMIPSFIGGSVVVEQIFTWPGLGKLFVDSAFQRDYPVIMAMTVISAVLVVVGNLIADILYAIVDPRIEY | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35278
Sequence Length: 316
Subcellular Location: Cell membrane
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P26458 | MFDYETLRFIWWLLIGVILVVFMISDGFDMGIGCLLPLVARNDDERRIVINSVGAHWEGNQVWLILAGGALFAAWPRVYAAAFSGFYVAMILVLCSLFFRPLAFDYRGKIADARWRKMWDAGLVIGSLVPPVVFGIAFGNLLLGVPFAFTPQLRVEYLGSFWQLLTPFPLLCGLLSLGMVILQGGVWLQLKTVGVIHLRSQLATKRAALLVMLCFLLAGYWLWVGIDGFVLLAQDANGPSNPLMKLVAVLPGAWMNNFVESPVLWIFPLLGFFCPLLTVMAIYRGRPGWGFLMASLMQFGVIFTAGITLFPFVMPSSVSPISSLTLWDSTSSQLTLSIMLVIVLIFLPIVLLYTLWSYYKMWGRMTTETLRRNENELY | Cofactor: May bind up to 3 heme groups per complex.
Function: A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested . Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.
Catalytic Activity: 2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42424
Sequence Length: 378
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Cell inner membrane
EC: 7.1.1.3
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P42063 | MSELQTTPSPEIRLKENISKKPETMTKIFWEKFSKNKLAILGAVILFIIIMSAVFAPLIAPYPQEQQSLLDKYKAPGLEHLMGTDKFGRDIFSRILYGARVSLLVGFASVVGSILIGTVLGALAGYFRGIVDAVIMRVVDIVLSIPDIFLLITLVTIFKPGVDKLILIFCLTGWTTTARLVRGEFLSLRSREYVLAAKTIGTKTHKIIFSHILPNALGPIIVSATLKVGSVILAESALSYLGFGIQPPIASWGNMLQDAQNFTVMIQAWWYPLFPGLFILMTVLCFNFVGDGLRDALDPKNIK | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33420
Sequence Length: 303
Subcellular Location: Cell membrane
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P26459 | MWDVIDLSRWQFALTALYHFLFVPLTLGLIFLLAIMETIYVVTGKTIYRDMTRFWGKLFGINFALGVATGLTMEFQFGTNWSFYSNYVGDIFGAPLAMEALMAFFLESTFVGLFFFGWQRLNKYQHLLVTWLVAFGSNLSALWILNANGWMQYPTGAHFDIDTLRMEMTSFSELVFNPVSQVKFVHTVMAGYVTGAMFIMAISAWYLLRGRERNVALRSFAIGSVFGTLAIIGTLQLGDSSAYEVAQVQPVKLAAMEGEWQTEPAPAPFHVVAWPEQDQERNAFALKIPALLGILATHSLDKPVPGLKNLMAETYPRLQRGRMAWLLMQEISQGNREPHVLQAFRGLEGDLGYGMLLSRYAPDMNHVTAAQYQAAMRGAIPQVAPVFWSFRIMVGCGSLLLLVMLIALVQTLRGKIDQHRWVLKMALWSLPLPWIAIEAGWFMTEFGRQPWAIQDILPTYSAHSALTTGQLAFSLIMIVGLYTLFLIAEVYLMQKYARLGPSAMQSEQPTQQQG | Cofactor: May bind up to 3 heme groups per complex.
Function: A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested . Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.
Catalytic Activity: 2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out) + 2 H2O
PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57920
Sequence Length: 514
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Cell inner membrane
EC: 7.1.1.3
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P42064 | MSTLLEVNNLKTYFFRKKEPIPAVDGVDFHISKGETVALVGESGSGKSITSLSIMGLVQSSGGKIMDGSIKLEDKDLTSFTENDYCKIRGNEVSMIFQEPMTSLNPVLTIGEQITEVLIYHKNMKKKEARQRAVELLQMVGFSRAEQIMKEYPHRLSGGMRQRVMIAIALSCNPKLLIADEPTTALDVTIQAQVLELMKDLCQKFNTSILLITHDLGVVSEAADRVIVMYCGQVVENATVDDLFLEPLHPYTEGLLTSIPVIDGEIDKLNAIKGSVPTPDNLPPGCRFAPRCPKAMDKCWTNQPSLLTHKSGRTVRCFLYEEEGAEQS | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36311
Sequence Length: 328
Subcellular Location: Cell membrane
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P42065 | MTAANQETILELRDVKKYFPIRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKHELYDNPLHPYTQALLSSVPVTRKRGSVKRERIVLKGELPSPANPPKGCVFHTRCPVAKPICKEQIPEFKEAAPSHFVACHLYS | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37086
Sequence Length: 329
Subcellular Location: Cell membrane
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P24244 | MWYLLWFVGILLMCSLSTLVLVWLDPRLKS | Function: Might be part of cytochrome bd-II oxidase (appB and appC). Able to restore reductant resistance to a cydX deletion mutant upon overexpression. CydX and this protein may have some functional overlap.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3597
Sequence Length: 30
Subcellular Location: Cell inner membrane
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A2VEY9 | MNLLCCCCCSNMAPNQRVTRKWELFAGRNKFYCDGLLMSAPHTGVFYLTCILITGTSALFFAFDCPFLADSINPAIPIVGAVLYFFTMSSLLRTTFTDPGVIPRASNDEAAYIEKQIEVPNSLNSPTYRPPPRTKEVLVKGQTVKLKYCFTCKIFRPPRASHCSLCDNCVDRFDHHCPWVGNCVGKRNYRFFYLFLVSLAFLAVFIFSCSVTHLVLLMKKEHEVFNVIKAAPFTVIVVFICFFSIWSVIGLAGFHTYLTTSDQTTNEDLKGSFSSKGGPRTQNPYSRGNICLNCCHILCGPMTPSLIDRRGIATDEFIQQMQHQSSPRHALSDVLSASHMVTTSQPMMGGLGGGGIGGAGGGISIGGAELKPRFYDESNPSSSTLEGNGGAINGHGNGHGNGFDHPPPSYDLVQNGNSNSLAQLVDNEIPLVQMDIPAYTHQTATQARQYRHRHHKQRQICNGGTVSYENQLANASSEDELDDPDVVVVGSPEVVAAVAAIASNKAREMRNRSGSYSNLFDADFEAALVNSSLADNHVRGEGASSSGKPSAGAALLAAAISGKTENMYSNVLPVDNDTDPADSTLHVYSNIIDERKQQEQANNVLSSTLLCDDLDLDDPVSASCHVKRKSLGDGAEQVKSAERLRMLHDNTMIDTALDLDSLDGSSMGNNSQSCLVKSGKPNATSVTTNVAIV | Function: Palmitoylates Dlish which is required for the apical cell cortex localization, total cellular level and full activity of dachs.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75008
Sequence Length: 693
Domain: The DHHC domain is required for palmitoyltransferase activity.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.225
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O94353 | MSLTSVLWNFVAKLAVDHGLNTNPDQVFQTVENVGKSFEKYETSFLKSLFNGNLGLSLPSAINILTLIIVLYFSLVIVNKTTSIALALFKTLAVISFFLLIGCLFAYWFINNGSF | Function: Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12762
Sequence Length: 115
Subcellular Location: Nucleus membrane
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P40532 | MDATQPQYELSVVTQCLKSAIDVIQWLIPTITKFSQSHPLVFQLLFIFFTFYVFYKLLMNFITLVKRFLYLTLVVTCIGIYMRGSQQFLTVDLLNFYNFVMSNRYYAFKIYTLFINALEREINTVYHLAQMKMEQLLK | Function: Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16508
Sequence Length: 138
Subcellular Location: Nucleus membrane
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P92979 | MAMSVNVSSSSSSGIINSRFGVSLEPKVSQIGSLRLLDRVHVAPVSLNLSGKRSSSVKPLNAEPKTKDSMIPLAATMVAEIAEEVEVVEIEDFEELAKKLENASPLEIMDKALEKYGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKHYGIRIEYMFPDSVEVQGLVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYISIGCEPCTKAVLPGQHEREGRWWWEDAKAKECGLHKGNVKENSDDAKVNGESKSAVADIFKSENLVTLSRQGIENLMKLENRKEPWIVVLYAPWCPFCQAMEASYDELADKLAGSGIKVAKFRADGDQKEFAKQELQLGSFPTILVFPKNSSRPIKYPSEKRDVESLTSFLNLVR | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons.
Catalytic Activity: AMP + glutathione disulfide + 2 H(+) + sulfite = adenosine 5'-phosphosulfate + 2 glutathione
Sequence Mass (Da): 51714
Sequence Length: 465
Domain: The C-terminal domain may function as glutaredoxin and mediates the interaction of the enzyme with glutathione (GSH). Active in GSH-dependent reduction of hydroxyethyldisulfide, cystine, dehydroascorbate, insulin disulfides and ribonucleotide reductase.
Subcellular Location: Plastid
EC: 1.8.4.9
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Q2KUE4 | MQTDYAEVVRRTIRSVPDWPVPGVTFRDITPVLQDPRTFRALVDLFVYRYMRQRLDLVAGVDARGFILGSVLAYELNLGFVPVRKKGKLPYRTVAEEYSLEYGNATVEIHTDAVRTGQRVLLVDDLIATGGTMVAAIKLLQRLGANVVEAAAIIDLPYIGGSQHIAETGTPLYTVCQFSATD | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20131
Sequence Length: 182
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.4.2.7
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O51718 | MKNKTEYYDQFISKIPNFPKKGVLFYDITSVLLKPEVYSSLINEVYSFYNFKKIDCIAVVESRGYLIGAPLSLKMQLPLVLIRKEGKLPREVFSEEYELEYGFGRIEVHKDDVRTYSNILLIDDILATGGTLKSSAILLERAGGKVKDIFCFIELCAINGRQSLESYEVNSLVRYN | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20173
Sequence Length: 176
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.4.2.7
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Q56JW4 | MADPELQLVARRIRSFPNFPIPGVLFRDISPVLKDPTSFRASINLLANHLKKAHGGRIDYIAGLDSRGFLFGPSLAQELGLGCILIRKRGKLPGPTVCASYALEYGKGELEIQRDALEPGQKVVVVDDLLATGGTMCAACELLGQLRAEVLECVSLVELTSLKGREKLGAVPFFSLLQYE | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19537
Sequence Length: 180
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.4.2.7
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Q89SB5 | MTFDHDLKASVRTIPDYPKPGIMFRDITTLLADARAFRRAVDELVNPWAGNKIDKVAGMEARGFIIGGAVAHQLSAGFVPIRKKGKLPHTTVRIAYSLEYGIDEMEMHVDAIQPGERVILVDDLIATGGTAEGAVKLLRQIGANVVAACFIIDLPELGGAAKLRAMDVPVRTLMTFEGH | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19406
Sequence Length: 179
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.4.2.7
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C0QVL4 | MELKDYIRNIQDYPKKGILFRDITTLLQNKDAFKYAIDKMAEQISSEKIDYIVGAESRGFLIGSALAYKLNCGFIPVRKKGKLPYKTISEEYALEYGTDTLYMHEDAIKKGERVLIVDDLIATGGTALAMIKMVEKLEGIVVGSSFLIELKELNGRKEIEKYPVNVLIEY | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19298
Sequence Length: 170
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.4.2.7
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Q038P1 | MTINFKDYIASVQDYPEPGIIFRDISPLMADGKAYAAATDEIAAYAQDKGVEMIVGPEARGFIVGCPVAYKLGIGFAPARKKGKLPRPTVKASYDLEYGEATLYLHKDAIKPGQRVLVCDDLLATGGTIAATIRLVEQLGGIVVGTAFLIELSDLHGRDKIKDYDMFTLMSYTGA | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18897
Sequence Length: 175
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.4.2.7
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A3QF54 | MNTDKLALIKQSIKTIPDYPKPGIMFRDVTSLMEDPAAYQATIALFVERYKDLGVTKVVGTEARGFLFGAPLALELGVGFVPVRKPGKLPRETISESYELEYGHDMLEIHTDAIKPGDKVLVVDDLLATGGTIEATVKLIRQLGGEVEHAAFVISLPELGGEHRLAEMGLSLMTLCEFEGE | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19744
Sequence Length: 181
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.4.2.7
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Q8EFG1 | MAMNTETLSLIKQSIKTIPNYPKEGILFRDVTSLLENATAYKATIDLLVEHYRSKGFTKIVGTEARGFLFGAPLALGLGIGFVPVRKPGKLPRATISQSYELEYGHDSLEIHTDAITANDKVLVVDDLLATGGTIEATVKLIRQLGGEVQDAAFVISLPDLGGEARLTALGLELVKLCEFEGE | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19746
Sequence Length: 183
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.4.2.7
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P50635 | MAGRPGYSEVIFLYVVSVAVIARATDNMPVNKDVSKLFPLTLIHINDLHARFEETNMKSNVCTQKDQCIAGIARVYQKIKDLLKEYESKNPIYLNAGDNFQGTLWYNLLRWNVTADFIKKLKPAAMTLGNHEFDHTPKGLAPYLAELNKEGIPTIVANLVMNNDPDLKSSKIPKSIKLTVGKRKIGIIGVLYDKTHEIAQTGKVTLSNAVEAVRREAAALKKDNIDIIVVLSHCSYEEDKKIAAEAGDDIDVIVGAHSHSFLYSPDSKQPHDPKDKVEGPYPTLVESKNKRKIPIVQAKSFGKYVGRLTLYFDEEGEVKNWEGYPVFIDHKVQQDPQILKDLVPWRAKVEAIGSTVVGETMIELDRDSCRDQECTLGVLYADGFADQYTNDTFRPFAIIQAGNFRNPIKVGKITNGDIIEAAPFGSTADLIRLKGADIWDVAEHSFALDDEGRTNCLQVSGLRIVIDISKPVRSRVKKIEVMDYTNPKSDKLKPLDKEAEYYIVVPSYLADGKDGFSAMKRATARRTGPLDSDVFKNYVEKIKKVDNLKLGRVIVCKGSKCT | Function: Facilitates hematophagy by preventing ADP-dependent platelet aggregation in the host. May reduce probing time by facilitating the speed of locating blood.
PTM: The N-terminus is blocked.
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate
Sequence Mass (Da): 62754
Sequence Length: 562
Subcellular Location: Secreted
EC: 3.6.1.5
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O96559 | MRSSYRVGNPIRFQPTNVVGLLLLSLVLSFMLVQSYELGHASGETNANSKYPLTTPVEENLKVRFKIGVISDDDKNAVSKDESNTWVSTYLTGTLEWEKSTDKITVQWDKGNEKKVKSKYSYGGRGMELSELVTFNGNLLTFDDRTGLVYILKDDKVYPWVVLADGDGKNSKGFKSEWATEKAGNLYVGSSGKEWTTKEGTIENYNPMWVKMINKNGEVTSLNWQTNYEKIRSSMNITFPGYMWHEAACWSDKYNKWFFLPRALSQEAYDSKKFETQGANVIISCDDKFEKCEPTQIQGKTEDKRGFSNFKFVPTSEDKIIVGLKTVEADDTTETYFTAFDLEGKVLLEETKIDDHKYEGVDFV | Function: Inhibits platelet aggregation by the calcium-dependent hydrolysis of ATP and ADP.
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate
Sequence Mass (Da): 41474
Sequence Length: 364
EC: 3.6.1.5
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P80595 | MLNQNSHFIFIILAIFLVLPLSLLSKNVNAQIPLRRHLLSHESEHYAVIFDAGSTGSRVHVFRFDEKLGLLPIGNNIEYFMATEPGLSSYAEDPKAAANSLEPLLDGAEGVVPQELQSETPLELGATAGLRMLKGDAAEKILQAVRNLVKNQSTFHSKDQWVTILDGTQEGSYMWAAINYLLGNLGKDYKSTTATIDLGGGSVQMAYAISNEQFAKAPQNEDGEPYVQQKHLMSKDYNLYVHSYLNYGQLAGRAEIFKASRNESNPCALEGCDGYYSYGGVDYKVKAPKKGSSWKRCRRLTRHALKINAKCNIEECTFNGVWNGGGGDGQKNIHASSFFYDIGAQVGIVDTKFPSALAKPIQYLNAAKVACQTNVADIKSIFPKTQDRNIPYLCMDLIYEYTLLVDGFGLNPHKEITVIHDVQYKNYLVGAAWPLGCAIDLVSSTTNKIRVASS | Function: Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates.
PTM: The N-terminus is blocked.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate
Sequence Mass (Da): 50041
Sequence Length: 454
Subcellular Location: Membrane
EC: 3.6.1.5
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B3A0N5 | MFKITVFIYVLQLILPSKVHSSPVPDSDNGLREFPLSIVHINDFHARFEQTDELGGQCKPTAKCVGGYARLVTTVKKLKEEGQNTIFLNAADNYQGTLWYNLGKWNVTAYFMNLLPADAMTLGNHEFDDKIEGIVPFLEVIKTPIVVANIDDSLEPTFKGKYTKSVVLERGGRKIGIVGVIAQNTDNISSPGKLRFLDEIQSVKNESKRLREEEKVDIVIVLSHIGLDHDYDLAEQAGDYIDAIIGGHSHSFLWTGDNPPGKEKVVDAYPVEIVQTSGKKVLIVQASAFARYVGNITLYFGENNNLIRYAGAPVYLDSDVPEVPQIVEEMKAWEEFVHEKGNEIIAESRVVLSRENCRVSDCNIGNFFTDAYVHEYVTSHTGPYWTPVSVGLMNVGGIRASVDRGNITFSQLITMAPFENTVDTFDLSGKHLLEAFEHAVTVPNRLGFNGQNMLQVSGVKLVYDVTKCEGQRVVSAKIRCQKCDIPKYEPLDPEETYRIVTASFLANGGDGFTMIRDNKKNYKVGRKDYDVLINYAKYSSPITIGEEGRIRIIQ | Function: Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. Shows potential for antithrombotic activity. May reduce probing time by facilitating the speed of locating blood.
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate
Sequence Mass (Da): 61880
Sequence Length: 554
Subcellular Location: Secreted
EC: 3.6.1.5
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A6NM10 | MAGLNVSLSFFFATFTLCEAARRASKALLPVGAYEVFAREAMRTLVELGPWAGDFGPDLLLTLLFLLFLAHGVTLDGASANPTVSLQEFLMAEESLPGTLLKLAAQGLGMQAACTLTRLCWAWELSDLHLLQSLMAQSCSSALRTSVPHGALVEAACAFCFHLTLLHLRHSPPAYSGPAVALLVTVTAYTAGPFTSAFFNPALAASVTFACSGHTLLEYVQVYWLGPLTGMVLAVLLHQGRLPHLFQRNLFYGQKNKYRAPRGKPAPASGDTQTPAKGSSVREPGRSGVEGPHSS | Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31475
Sequence Length: 295
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: Membrane
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A0A0G3FWY4 | MTANGDVRQPDARTYFTHQHPADYHADWKGYYERALVSRARSMERFAHELDIRYGTDPHQILNVFRAADTRSAPVIIYFHGGRWREGHPAFYDHLADTWAADGAVFVSAGYRLTPEHSIADSVADAWAVTDWVVRNIAAYGGDPSRITVAGHSSGGHLASMVALTDNCAVSIVGLVCMSAPVDLRTLGFWDDDTLSPHLQISRVPRRVVVSFGDPEPNRKGDDALRLTREGQMLADSLVAYGASLRTVVLPNADHVRTATAFADRQSPLFGAAHSVIFGDSTEDRSAPRSPHFQEEKQSCPE | Function: Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Probably catalyzes the hydrolysis of N-octanoylanthranilic acid to anthranilic acid.
Catalytic Activity: H2O + N-octanoylanthranilate = anthranilate + H(+) + octanoate
Sequence Mass (Da): 33270
Sequence Length: 302
EC: 3.5.1.-
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A0A0E4AET8 | MFQTVTAPTGVWRGRVTGDVTVFHGIQYARADRFAPPQRCEPQLQHLVEVPEPGPIAPQSPSRLEGVMGAPSSLKQSEACLTVTVTTPHLAQPGSLPVLVWLHGGAFLSGSGAWEQYGAEQLVRETGIVVVSVNYRLGVLGYLCAPGISSGNLGLLDQITALEWVRDNIEAFGGDNGRVTLDGQSAGAHSIVAMLGIDRARSLFSRAIIQSAPLGLGFHSVEQARRAAEIFEEELGSDPRRAVVTDILAAQARTAHRLAGRGAMNSAPPFLPVHGMAPLPFVGEWNGKVAANAARRKILIGNTRDEMAAFFGPHPVFSAMRRVPLAGPQLAGAIQRRVQKVVFDNPVQEFADRFASAGASVWRYGIGPLHPDNPFGACHCIDIPLLFGDGDTWRDAPMLRPLSPKEIGESGTRTRRYWGEFVHTGRISDPAWPMHRPKSRYAHLLTDETIGGSA | Function: Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Probably catalyzes the hydrolysis of N-octanoylanthranilic acid to anthranilic acid.
Catalytic Activity: H2O + N-octanoylanthranilate = anthranilate + H(+) + octanoate
Sequence Mass (Da): 48937
Sequence Length: 454
EC: 3.5.1.-
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A0A0E4AFG7 | MSGVAGHAEVVGGGIGGLSAAIALGKRGWTVRLHERNDEIRASGSGIYLWDNGLAALDYLGALDSTLVGAHFGARMQTRDAHNALVASSEVNRAGGPRVVTVARERLINALLASADAVGVEVVTGSTVTRVDAAGRIEFDNGHADADLIVVADGIGSRSRDQLGVKTRRRQLNQKCARVLLPREPGMVPSEWVDEYVTFYSGQRFLLYTPCSADLLYLALVCPSDDAPATGDPLPREAWIASFPQLAPLIDRIGPTPRWDEFEMLTLDSWSSGRVAILGDAAHAQPPSLGQGGGCAMLSALGLAHSLSKNYDLTTALGEWESSERSVIQRTQWFSYWLARANKLPDRPRSLLLSAAGHSSLYRNNRMRAALTTPTGITSSK | Function: Could be involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4-quinolone) to anthranilic acid. May catalyze the hydroxylation of HHQ to PQS (2-heptyl-3-hydroxy-4-quinolone).
Catalytic Activity: 2-heptyl-4(1H)-quinolone + H(+) + NADH + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + H2O + NAD(+)
Sequence Mass (Da): 40799
Sequence Length: 381
EC: 1.14.13.182
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B1MFK1 | MSSGHAEVVGGGIGGLTAATALALRGWTVRLHERDTRIRTVGAGIYVWDNGLEALDTIGAAAEGLDDAYEAPAITVRASDGRPLYRIDVNQPGGARCVTLLRDRLIGALHVAAEHAGVEVCTGSAAVSATADGTVEFSTGTSTRADLVVAADGVHSLLRDRLGISYRRIRMRQGAARVMVSGERPFIPGMDVDQHHEFLGGRRRLLYTPCTATQTYLAFVADNDDTATVGPELDLAAWARAFPLLVPVFDAARGRALIRWDNFELIRLSTWSHGRVAVLGDAAHAQPPYVGQGGGTAMNSAVGLAAAVSESADVEDGLNRWEQALRPPIEKAQTTSYRMRLIGSVPEVLRGPLLGALGRSRSSATSQLIKKRSAA | Function: Involved in the degradation pathway of the Pseudomonas aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4(1H)-quinolone) to anthranilate. Catalyzes the hydroxylation of HHQ to PQS (2-heptyl-3-hydroxy-4(1H)-quinolone).
Catalytic Activity: 2-heptyl-4(1H)-quinolone + H(+) + NADH + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + H2O + NAD(+)
Sequence Mass (Da): 39751
Sequence Length: 375
EC: 1.14.13.182
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A0A0E4AE72 | MNMPQLSTIQIGDHELAYLDNKLTSAVTPTIVMLPGWCGDHHSFSELIPQLNDTHRVVAVNWRGHAPVPHDVSDFGYAEQAQDALAILDAIGVDEFLPVSASHGGWALVQLLVDAGPARARAGVVLDWLMRRPTPEFTAALLSLQDPEGWVDSCRALFHTWRPNDSDWVESRVERAKEFGFDMWARSGRVISGAYGEHGTPLEFMKTITPERHIRHLFSTPSDSDYVAPQEAFASENEWFSYALLGGTSHFPHLEMPDRVAAHIVELAKNTYQAGAMR | Function: Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Catalyzes the cleavage of PQS to form N-octanoylanthranilic acid and carbon monoxide.
Catalytic Activity: 2-heptyl-3-hydroxy-4(1H)-quinolone + O2 = CO + H(+) + N-octanoylanthranilate
Sequence Mass (Da): 30938
Sequence Length: 278
EC: 1.13.11.-
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B1MFK2 | MITTKTVNGVQIAFDDQGHEPGPVFVTLSGWAHDLRAYDGMLPYLRAAQRTVRVCWRGHGPDRNLVGDFGIDEMAADTIGLLDALEVDSFVPIAHAHGGWAALEIADRLGAQRVPAVMILDLIMTPAPREFVAALHGIQDPERWKEGRDGLVQSWLAGTTNQAVLDHVRYDSGGHGFDMWARAGRVIDEAYRTWGSPMRRMEALAEPCAIRHVFSHPKIGEYDALHDDFAARHPWFSYRRLGGETHFPGIELPQQVAAEAIDLLAGARI | Function: Ring-cleaving dioxygenase involved in the degradation pathway of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4(1H)-quinolone) to anthranilate. Catalyzes the cleavage of PQS to form N-octanoylanthranilate and carbon monoxide. Thus, leads to the inactivation of PQS that plays a central role in the regulation of virulence factor production by P.aeruginosa, thereby quenching the production of antimicrobials, which may contribute to the competitiveness of M.abscessus in presence of P.aeruginosa . In vitro, can also use other 2-alkyl-3-hydroxy-4(1H)-quinolone (AHQ) substrates with shorter alkyl substituents at C2, but with lower efficiency .
Catalytic Activity: 2-heptyl-3-hydroxy-4(1H)-quinolone + O2 = CO + H(+) + N-octanoylanthranilate
Sequence Mass (Da): 29760
Sequence Length: 269
EC: 1.13.11.-
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Q7MIV9 | MNKYLAELFGTFWLVLGGCGSAVLAAAFPDVGIGLLGVSLAFGLTVLTMAFAIGHISGCHLNPAVTIGLWAGGRFEAKEIVPYILAQVIGGVIAGGVLYTIASGQMGFDATSSGFASNGYGEHSPGGYSLTSALVTEIVMAMMFLLVILGATDQRAPQGFAPIAIGLCLTLIHLISIPVTNTSVNPARSTGVALYVGDWATAQLWLFWVAPILGALLGAVAYKLISGSNKD | Function: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Catalytic Activity: H2O(in) = H2O(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23752
Sequence Length: 231
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 inner membrane
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Q9NHW7 | MTESAGVKQLVGVADITENRNIWRMLVAEFLGTFFLVSIGIGSTMGWGGDYAPTMTQIAFTFGLVVATLAQAFGHVSGCHINPAVTIGLMITADISILKGAFYIVSQCVGAIAGAALIKAATPSDVIGGLGVTGIDPRLTAGQGVMIEALITFILVFVVHGVCDNRRSDIKGSAPLAIGLSITAGHLSAIKYTGASMNPARSFGPAVVMGNWTDQWVYWVGPIVGGILAGAVYRLFFKVRKGDEESYDF | Function: Forms a water-specific channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26093
Sequence Length: 249
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: Membrane
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Q23808 | MAADKSVDNTKKIIGIDDITDTKTIWRCLAAELIGTLLLVLIGTGSCTGVQISEGDVVVRIALTFGFIIATMVQCIGHVSGCHINPAVTCGLLVTGHISILKAIFYIIVQCVGAIAGSAILKVITPAEFRGTLCMTSLAPGVTPPMGFLVEACITFVLILLVQSVCDDRRKNLGNAAPVAVGLAITCCHLAAIKYTGSSMNPARSFGPAVNGDDNWANHWVYWAGPIVGGVVAGITYRALFRARKPEEEASSYDF | Function: Forms a water-specific channel. May be involved in the transfer of excess sap dietary water from the initial midgut to the terminal midgut and the proximal part of the malpighian tubules.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26885
Sequence Length: 255
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: Membrane
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Q9V5Z7 | MVEKTEMSKFVGVADITENKKIWRMLLGELVGTFFLIFVGVGSTTSGSVPQIAFTFGLTVATIAQGLGHLSGCHINPAVTLGFLIVGEISILKAAFYIIVQCVGAIAGAAVIKVALDGVAGGDLGVSSFDPSLNCAQAVLIEALITFILVFVVKAVSDPGRQDIKGSAPLAVGLAIAAGHLCAIKLSGASMNPARSFGPAVVQGVWTYHWVYWVGPIAGGLLAGIIYRLIFKVRKGDDETDSYDF | Function: Forms a water-specific channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25575
Sequence Length: 245
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: Membrane
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Q8SRK2 | MTRETLKTLQSTFGEMVASFVFGFAVYSALLGSALTEQSAARVIVGLTVGFSGICVIYSFCDVTVAHFNPAITLAAILTCKLGVLRGIGYIVAQYIGFILAVCALLPCSPVGYKETLNIIRPTPSPFGGDNLNVFFTEFFLTAILVHVAFATAVNPYKPKTDTEGKFVDPDEEEPVDRRITAPLCIGLTLGFLAFLGLASSGGAFNPGLTLAPVIMSNTWNHFWAYFAGQYLGGFVGGLLQVLVLYKLSF | Function: Water channel required to facilitate the transport of water across membranes. Involved in osmotolerance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26795
Sequence Length: 250
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). In microsporidia, the second signature motif differs slightly and is Asn-Pro-Gly (NPG).
Subcellular Location: Cell membrane
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B7XIC4 | MNTSTKLICQKLFAEMLCSCIFGFAVYSAILNTKASNSSISSTTVGLTVCFSSISLIYTFCDHSVAHFNPAITIAAICTGKLDILLGIGYVIAQLIGFILATLLTVVCFPYGYLKTMEFIASARISDDISTVNLFFTEFILSFILVFIAFEVGINAIREPGVTLFVGIKQIDRSKFAPLTIGITLGFLAFLASTTSGGAFNPGIVWGPAIMGGNFDDFVIYIISELSGGLLGAFIQVFLLFK | Function: Water channel required to facilitate the transport of water across membranes. Involved in osmotolerance (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25999
Sequence Length: 242
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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C4VBN2 | MTRKWIKKLQSYIGEFFASFIFGFAVYTSIIGSAQTGQSAGPIIVALTIALSGVAIIYSFCDITVAHFNPAITFSAMCFRRLPFFGGIFIIIFQVAGFIIAGLASVAVLPGKYKNKLEIARPKRVADNVSRGRIFGTEFFLTAILVYVAFAVGVNPYTPPKDEHGDQLDPDEGLTEGRKITAPLAIGFTLGFCALLGIASSGGAFNPGIVLSPMILTGTWDFWWVYLLGQFSGGLLGGGLQRFLLYKIF | Function: Water channel required to facilitate the transport of water across membranes. Involved in osmotolerance (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26936
Sequence Length: 249
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). In microsporidia, the second signature motif differs slightly and is Asn-Pro-Gly (NPG).
Subcellular Location: Cell membrane
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P53943 | MSRSNSIYTEDIEMYPTHNEQHLTREYTKPDGQTKSEKLNFEGAYINSHGTLSKTTTREIEGDLDSETSSHSSDDKVDPTQQITAETKAPYTLLSYGQKWGMVAILTMCGFWSSLGSPIYYPALRQLEKQFNVDENMVNVTVVVYLLFQGISPTVSGGLADCFGRRPIILAGMLIYVIASIGLACAPSYGVIIFLRCIQSIGISPTIAISSGVVGDFTLKHERGTFVGATSGFVLLGQCFGSLIGAVLTARWDWRAIFWFLTIGCGSCFLIAFLILPETKRTIAGNLSIKPKRFINRAPIFLLGPVRRRFKYDNPDYETLDPTIPKLDLSSAGKILVLPEIILSLFPSGLLFAMWTLMLSSISSGLSVAPYNYHLVIIGVCYLPGGIGGLMGSFFTGRIIDMYFKRKIKKFEQDKANGLIPQDAEINMFKVRLVCLLPQNFLAVVAYLLFGWSIDKGWRIESILITSFVCSYCAMSTLSTSTTLLVDLYPTKSSTASSCFNFVRCSLSTIFMGCFAKMKAAMTVGGTFTFLCALVFFFNFLMFIPMKYGMKWREDRLLKQQRQSWLNTLAVKAKKGTKRDQNDNHN | Function: Probable transporter that confers resistance to short-chain monocarboxylic acids and quinidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65296
Sequence Length: 586
Subcellular Location: Membrane
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P0CD91 | MSSNDSNDTDKQHTRLDPTGVDDAYIPPEQPETKHHRFKISRDTLRDHFIAAVGEFCGTFMFLWCAYVICNVANHDVALVAAPDGSHPGQLIMIAIGFGFSVMFSIWCFAGVSGGALNPAMSLSLCLARAVSPTRCVVMWVSQIVAGMAAGGAASAMTPGEVLFANSLGLGCSRTRGLFLEMFGTAILCLTVLMTAVEKRETNFMAALPIGISLFIAHVALTAYTGTGVNPARSLGAAVAARYFPHYHWIYWIGTLLGSILAWSVWQLLQILDYTTYVTAEKAASTKEKAQKKGETSSSSAVAEV | Function: Water channel required to facilitate the transport of water across membranes. Involved in sporulation, freeze tolerance and osmotolerance (By similarity). Is non-functional in most laboratory strains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32713
Sequence Length: 305
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: Endoplasmic reticulum membrane
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Q49V87 | MTYSIGIDFGTGSGRVFLVNTENGEIIGQYVQTYAHGTIEGELNGHKLPQSYALQNANDYMEVIETGIPEILAKTNIDAKDIVGIGIDFTSSTVIFVDDQMEPMHNNPKFYNNPHAYVKLWKHHGAQAEADLLFNTAIEEKNRWLGYYGFNVSSEWMIPKIMEVNDKAPEVMTETADIMEAGDWIVNRLTGENVRSNCGLGFKSFWESSTGFHYDLFDKVDDNLSDIVRTKVEAPIVSIGESVGTVSAEMAHKLGLSPETVVSPFIIDAHSSLLGIGAEKDKEMTMVMGTSTCHLMLNKEQHKVPGISGSVKGAIIPDLYAYEAGQTAVGDLFEYVANQSPYEYVKTAEDRGISIFELLNEKASQRYPGESGLIALDWHNGNRSVLSDSNLKGSLFGLSLQTKHEDIYRAYMEATAFGTKMIMQQYQGWQMEVERVFACGGIPKKNHLLMEIYANVLNKKITVIDSEYAPAIGAAILGAICGGAHPNFSSAIQAMKEPVLYQVEPDHAQVLIYKKLFNAYKELHDLLGYKKARIMRNVSALM | Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+)
Sequence Mass (Da): 60094
Sequence Length: 542
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3.
EC: 2.7.1.16
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B7GGV9 | MGKKYVIGIDYGTESGRAVLVDLEGNEIADHVTPYPHGVIDEVLPESNVQLEPDWALQHPGDYIEVLATAVPAVLQKSGVNPADVIGVGIDFTACTMLPIAGSGEPLCLKPEFKHRPHSWVKLWKHHAAQDEANLLNEMAAKRGEAFLPRYGGKISSEWMIAKIWQILNEDPDIYDQTDLFLEATDWVIFKMTGQLVRNSCTAGYKSIWHKQDGYPSKEFFRALDPRLEHVTETKLRGSIVPLGTRAGVLTKEMAAMMGLLPGTAVAVGNVDAHAAVPGVGVVEPGKMVMAMGTSICHMLLGTEEKYVEGMCGVVEDGIIPGYFGYEAGQSAVGDIFAWYVEQSVPAYVKEAAEKEGVSVHEWLEKRAAAYRPGETGLLALDWWNGNRSVLVDTDLTGLIIGYTLLTKPEEIYRALLEATAFGTRKIIDAFVESGINVDELYACGGLPQKNKLLMQIYADVTNREIKIAASKQTPAVGAAMFAAVAAGKENGGYESIIEAARNMGKVREETFKPIPENVAIYEQLYQEYTKLHDYFGRGENDVMKRLKHWKETARAVKESISLS | Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+)
Sequence Mass (Da): 61968
Sequence Length: 564
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3.
EC: 2.7.1.16
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P94524 | MAYTIGVDFGTLSGRAVLVHVQTGEELAAAVKEYRHAVIDTVLPKTGQKLPRDWALQHPADYLEVLETTIPSLLEQTGVDPKDIIGIGIDFTACTILPIDSSGQPLCMLPEYEEEPHSYVKLWKHHAAQKHADRLNQIAEEEGEAFLQRYGGKISSEWMIPKVMQIAEEAPHIYEAADRIIEAADWIVYQLCGSLKRSNCTAGYKAMWSEKAGYPSDDFFEKLNPSMKTITKDKLSGSIHSVGEKAGSLTEKMAKLTGLLPGTAVAVANVDAHVSVPAVGITEPGKMLMIMGTSTCHVLLGEEVHIVPGMCGVVDNGILPGYAGYEAGQSCVGDHFDWFVKTCVPPAYQEEAKEKNIGVHELLSEKANHQAPGESGLLALDWWNGNRSTLVDADLTGMLLGMTLLTKPEEIYRALVEATAYGTRMIIETFKESGVPIEELFAAGGIAEKNPFVMQIYADVTNMDIKISGSPQAPALGSAIFGALAAGKEKGGYDDIKKAAANMGKLKDITYTPNAENAAVYEKLYAEYKELVHYFGKENHVMKRLKTIKNLQFSSAAKKN | Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+)
Sequence Mass (Da): 61010
Sequence Length: 560
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3.
EC: 2.7.1.16
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P58541 | MAIAIGLDFGSDSVRALAVDCTTGEEIATSVEWYPRWQKGQFCDAPNNQFRHHPRDYIESMEAALKTVLAELSVEQRAAVVGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWKDHTAVEEAEEITRLCHAPGNVDYSRYIGGIYSSEWFWAKILHVTRQDSAVAQSAASWIELCDWVPALLSGTTRPQDIRRGRCSAGHKSLWHESWGGLPPASFFDELDPILNRHLPSPLFTDTWTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGAQPNALVKVIGTSTCDILIADKQSVGERAVKGICGQVDGSVVPGFIGLEAGQSAFGDIYAWFGRVLGWPLEQLAAQHPELKEQIDASQKQLLPALTEAWAKNPSLDHLPVVLDWFNGRRTPNANQRLKGVITDLNLATDAPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARKNQVIMQACCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMASAVEKTLQPRSEQAQRFEQLYRRYQQWAMSAEQHYLPTSAPAQAAQAVPTL | Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+)
Sequence Mass (Da): 61228
Sequence Length: 566
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3.
EC: 2.7.1.16
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P94529 | MKPVKTGTVHPVPSAAKQSGWRDLFYSKKAAPYLFTAPFVLSFLVFFLYPIISVFIMSFQRILPGEVSFVGLSNYTALNNPTFYTALWNTLEYTFWTLIVLIPVPLLLAIFLNSKLVKFRNIFKSALFIPALTSTIVAGIIFRLIFGEMETSLANSILLKLGFSPQNWMNNEHTGMFLMVLLASWRWMGINILYFLAGLQNVPKELYEAADIDGANTMKKFLHITLPFLKPVTVYVLTISIIGGFRMFEESYVLWQNNSPGNIGLTLVGYLYQQGLAYNEMGYGAAIGIVLLIVILVVSLISLKLSGSFKGEG | Function: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides. Transports alpha-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units . Responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35035
Sequence Length: 313
Subcellular Location: Cell membrane
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P94530 | MLRHSPQFSVYRIALTLFFMMLSLLYLFPIFCLLLGSLKPSSELLRVGLNLDIDPKVMSFDNYTFLFNGGSIYFKWFFNSLVLGLFTTVLTLFFSSMIGYGLAVYDFKGRNIIFVLVLIIMMVPLEVMMLPLFKLTVGLHLIDSYTGVILPFIVSPVAVFFFRQYALGLPRDLLDSARMDGCTEFGIFFRIMAPLMKPAFGAMIILQSLNSWNNFLWPLIVLRSKEMFTLPIGLSSLLSPYGNNYDMLISGSVFAILPVIIIFLFFQKYFISGLTVGGVKG | Function: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides. Transports alpha-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units . Responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31846
Sequence Length: 281
Subcellular Location: Cell membrane
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O80885 | MLLNISSSPISHRNPHFLSNFNNPISYFPRRSKTHLSKSHFFPKFTPLSNQSLKNRVLFGNKRYPDGERFDFRSRAISGIDLGSFESVLEAIAVLTTIIVVHESGHFLAASLQGIHVSKFAIGFGPILAKFDYNNVEYSLRAFPLGGFVGFPDNDPDSEIPIDDENLLKNRPTLDRSIVVSAGIIANVIFAYAIIFVQVLSVGLPVQEAFPGVLVPEVKTFSAASRDGLLSGDVILAVDGTELSKTGPDAVSKIVDIVKRNPKSNVVFRIERGGEDFDIRVTPDKNFDGTGKIGVQLSPNVRITKVRPRNIPETFRFVGREFMGLSSNVLDGLKQTFFNFSQTASKVAGPVAIIAVGAEVARSNIDGLYQFAALLNINLAVINLLPLPALDGGTLALILLEAVRGGKKLPVEVEQGIMSSGIMLVIFLGLFLIVKDTLSLDFIKEML | Function: Metalloprotease essential for chloroplast and plant development. May be involved in regulated intramembrane proteolysis (RIP).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48726
Sequence Length: 447
Subcellular Location: Plastid
EC: 3.4.24.-
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H3ZPL1 | MELEKRLKEKLEAPTLDYEKYFSEKALGMKASEIRELLKLVETSDVISLAGGLPAPETFPVEIIGEITKEVLEKHAAQALQYGTTKGFTPLRLALAEWMRERYDIPISKVDIMTTSGSQQALDLIGRVFINPGDIIVVEAPTYLAALQAFKYYEPEFVQIPLDDEGMNVDLLEEKLQELEKEGKKVKIVYTIPTFQNPAGVTMNEKRRKRLLELASQYDFIIVEDNPYGELRYSGEPVKPIKAWDEEGRVIYLGTFSKILAPGFRIGWIAAEPHFIRKLEIAKQSVDLCTNTFSQVIAWKYVEGGYLDKHIPKIIEFYKPRRDAMLKALEEFMPDGVKWTKPEGGMFVWATLPEGIDTKLMLEKAVAKGVAYVPGEAFFAHRDVKNTMRLNFTYVPEEKIREGIKRLAETIKEEMKK | Function: Catalyzes the transamination of phenylalanine, tyrosine and tryptophan. Shows virtually no activity towards aspartic acid, alanine, valine or isoleucine.
Catalytic Activity: 2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate
Sequence Mass (Da): 47610
Sequence Length: 417
EC: 2.6.1.57
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H3ZPU1 | MALSDRLEMVNPSEIRKLFDLAQGIEGIISLGIGEPDFDTPEHIKEYAKEALDKGLTHYSPNIGILELREAVAEKFKKHNGIDADPKTQIMITVGTNQQILMGLATFLKDNEEVLIPSPMFVSYAPAVILAGGKPVEVPTYEENEFRLSVDELEKYVTPKTRALIINTPNNPTGAVLTKKDLEEIADFAVEHDLMILSDEVYEYFVYDGVKNYSIASLDGMFERTITMNGFSKTFAMTGWRLGFLAAPEWVVEKMVRFQMYNATCPVTFIQYAAAKALRDERSWQAVEEMRREYERRRNLVWKRLNEMGLPTVKPKGAFYIFPRIKDTGLSSKEFSELMIKEAKVVVVPGSAFGQAGEGYVRISYATAYEKLEEAMDRMEKVLKEKKLV | Function: Catalyzes the transamination of phenylalanine, tyrosine and tryptophan. Shows virtually no activity towards aspartic acid, alanine, valine or isoleucine.
Catalytic Activity: 2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate
Sequence Mass (Da): 44105
Sequence Length: 389
EC: 2.6.1.57
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P40024 | MPPVSASKAKRDAKKAEREAKKAAAGKTIRKLGRKKEAAAEESEVDAAAREIKMMKLQQDKDGLSDRVVTGVLSSLETSRDIKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSALDYVVTEAQHELKRIEDLVEKTILEDGPESELLEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHKTRSELETNQMKQYNKQQEEIQHIKKFIASAGTYANLVKQAKSRQKILDKMEADGLVQPVVPDKVFSFRFPQVERLPPPVLAFDDISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQDQLDLTKSALEFVRDKYSNISQDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKTATRWDGSILQYKNKLAKNVVL | Function: ATPase that stimulates 40S and 60S ribosome biogenesis . Also involved in ribosome-associated quality control (RQC) pathway, a pathway that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation: localizes to the ribosomal E-site and stimulates VMS1-dependent tRNA cleavage .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68377
Sequence Length: 610
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P95470 | MPTHHPITRQHWHHSWLSALALLCASLACGAKQVDVHDPVMTREGDTWYLFSTGPGITIYSSKDRVNWRYSDRAFGTEPTWAKRVSPSFDGHLWAPDIYQHKGLFYLYYSVSAFGKNTSAIGVTVNKTLNPASPDYRWEDKGIVIESVPQRDLWNAIDPAIIADDHGQVWMSFGSFWGGLKLFKLNDDLTRPAEPQEWHSIAKLERSVLMDDSQAGSAQIEAPFILRKGDYYYLFASWGLCCRKGDSTYHLVVGRSKQVTGPYLDKTGRDMNQGGGSLLIKGNKRWVGLGHNSAYTWDGKDYLVLHAYEAADNYLQKLKILNLHWDGEGWPQVDEKELDSYISQRLK | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of the terminal alpha-(1->5)-arabinofuranosyl bonds of linear arabinan and carboxymethylarabinan to produce almost exclusively arabinotriose.
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Sequence Mass (Da): 39432
Sequence Length: 347
Pathway: Glycan metabolism; L-arabinan degradation.
Subcellular Location: Secreted
EC: 3.2.1.55
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P0C0B4 | MTAQTPIHVYSEIGKLKKVLLHRPGKEIENLMPDYLERLLFDDIPFLEDAQKEHDAFAQALRDEGIEVLYLETLAAESLVTPEIREAFIDEYLSEANIRGRATKKAIRELLMAIEDNQELIEKTMAGVQKSELPEIPASEKGLTDLVESNYPFAIDPMPNLYFTRDPFATIGTGVSLNHMFSETRNRETLYGKYIFTHHPIYGGGKVPMVYDRNETTRIEGGDELVLSKDVLAVGISQRTDAASIEKLLVNIFKQNLGFKKVLAFEFANNRKFMHLDTVFTMVDYDKFTIHPEIEGDLRVYSVTYDNEELHIVEEKGDLAELLAANLGVEKVDLIRCGGDNLVAAGREQWNDGSNTLTIAPGVVVVYNRNTITNAILESKGLKLIKIHGSELVRGRGGPRCMSMPFEREDI | PTM: Glycosylated.
Catalytic Activity: H2O + L-arginine = L-citrulline + NH4(+)
Sequence Mass (Da): 46297
Sequence Length: 411
Pathway: Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 1/2.
Subcellular Location: Cytoplasm
EC: 3.5.3.6
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Q7LC44 | MELDHRTSGGLHAYPGPRGGQVAKPNVILQIGKCRAEMLEHVRRTHRHLLAEVSKQVERELKGLHRSVGKLESNLDGYVPTSDSQRWKKSIKACLCRCQETIANLERWVKREMHVWREVFYRLERWADRLESTGGKYPVGSESARHTVSVGVGGPESYCHEADGYDYTVSPYAITPPPAAGELPGQEPAEAQQYQPWVPGEDGQPSPGVDTQIFEDPREFLSHLEEYLRQVGGSEEYWLSQIQNHMNGPAKKWWEFKQGSVKNWVEFKKEFLQYSEGTLSREAIQRELDLPQKQGEPLDQFLWRKRDLYQTLYVDADEEEIIQYVVGTLQPKLKRFLRHPLPKTLEQLIQRGMEVQDDLEQAAEPAGPHLPVEDEAETLTPAPNSESVASDRTQPE | Function: Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer in the nervous system. ARC protein is released from neurons in extracellular vesicles that mediate the transfer of ARC mRNA into new target cells, where ARC mRNA can undergo activity-dependent translation. ARC capsids are endocytosed and are able to transfer ARC mRNA into the cytoplasm of neurons. Acts as a key regulator of synaptic plasticity: required for protein synthesis-dependent forms of long-term potentiation (LTP) and depression (LTD) and for the formation of long-term memory. Regulates synaptic plasticity by promoting endocytosis of AMPA receptors (AMPARs) in response to synaptic activity: this endocytic pathway maintains levels of surface AMPARs in response to chronic changes in neuronal activity through synaptic scaling, thereby contributing to neuronal homeostasis. Acts as a postsynaptic mediator of activity-dependent synapse elimination in the developing cerebellum by mediating elimination of surplus climbing fiber synapses. Accumulates at weaker synapses, probably to prevent their undesired enhancement. This suggests that ARC-containing virion-like capsids may be required to eliminate synaptic material. Required to transduce experience into long-lasting changes in visual cortex plasticity and for long-term memory (By similarity). Involved in postsynaptic trafficking and processing of amyloid-beta A4 (APP) via interaction with PSEN1 (By similarity). In addition to its role in synapses, also involved in the regulation of the immune system: specifically expressed in skin-migratory dendritic cells and regulates fast dendritic cell migration, thereby regulating T-cell activation (By similarity).
PTM: Palmitoylation anchors the protein into the membrane by allowing direct insertion into the hydrophobic core of the lipid bilayer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45316
Sequence Length: 396
Domain: The protein is evolutionarily related to retrotransposon Gag proteins: it contains large N- and C-terminal domains that form a bi-lobar architecture similar to the capsid domain of human immunodeficiency virus (HIV) gag protein. It contains structural elements found within viral Gag polyproteins originated from the Ty3/gypsy retrotransposon family and retains the ability to form virion-like capsid structures that can mediate mRNA transfer between cells. Tetrapod and fly Arc protein-coding genes originated independently from distinct lineages of Ty3/gypsy retrotransposons.
Subcellular Location: Extracellular vesicle membrane
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C7R400 | MTETHNDPEELARRVASLSAQNERLAQILVEARSKIVGLQQQIDDLAQPPSTYATFIRSYSDGTADVMVQGRKMRLTSLPAAMVSTARPGQQVRLNEAMAIVETMTYDHTGELVTVKELIGTHRAMVVGRGDDERVVNLAGSLIGRDGPTIRTGDSVLVDLKAGYALEKIDKSEVEELVLEEVPRVAYEDIGGLSRQIDTIKDAVELPFLHPDLYREHGLKAPKGILLYGPPGCGKTLIAKAVAHSLAQTVGQGNNTPTDDTRGYFLNIKGPELLNKYVGETERQIRLIFTRARDKAAQGHPVVVFFDEMESLFRTRGTGLSSDVETTIVPQLLAEIDGVERLDNVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAEAALDIFSKYLTPDLPIHPVDLAEHGGNAQDAVTAMGQRVVEHMYATTPDNQFLEVTYASGDKETLYFKDFSSGAMIQNIVDRAKKAAIKGYLSHGTRGLQVEHLLAACDDEFQENEDLPNTTNPDDWARISGKKGERIVFIRTIVQRKGEGKNPTPAKAIETPHNTGPYL | Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.
Sequence Mass (Da): 60449
Sequence Length: 550
Domain: Consists of three main regions, an N-terminal coiled-coil domain that binds to protein Pup and functions as a docking station, an interdomain involved in ARC hexamerization, and a C-terminal ATPase domain of the AAA type.
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
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Q9WV31 | MELDHMTTGGLHAYPAPRGGPAAKPNVILQIGKCRAEMLEHVRRTHRHLLTEVSKQVERELKGLHRSVGKLENNLDGYVPTGDSQRWKKSIKACLCRCQETIANLERWVKREMHVWREVFYRLERWADRLESMGGKYPVGSEPARHTVSVGVGGPEPYCQEADGYDYTVSPYAITPPPAAGELPEQESVEAQQYQSWGPGEDGQPSPGVDTQIFEDPREFLSHLEEYLRQVGGSEEYWLSQIQNHMNGPAKKWWEFKQGSVKNWVEFKKEFLQYSEGTLSREAIQRELELPQKQGEPLDQFLWRKRDLYQTLYVDAEEEEIIQYVVGTLQPKLKRFLRHPLPKTLEQLIQRGMEVQDGLEQAAEPSGTPLPTEDETEALTPALTSESVASDRTQPE | Function: Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer in the nervous system (By similarity). ARC protein is released from neurons in extracellular vesicles that mediate the transfer of ARC mRNA into new target cells, where ARC mRNA can undergo activity-dependent translation (By similarity). ARC capsids are endocytosed and are able to transfer ARC mRNA into the cytoplasm of neurons (By similarity). Acts as a key regulator of synaptic plasticity: required for protein synthesis-dependent forms of long-term potentiation (LTP) and depression (LTD) and for the formation of long-term memory . Regulates synaptic plasticity by promoting endocytosis of AMPA receptors (AMPARs) in response to synaptic activity: this endocytic pathway maintains levels of surface AMPARs in response to chronic changes in neuronal activity through synaptic scaling, thereby contributing to neuronal homeostasis . Acts as a postsynaptic mediator of activity-dependent synapse elimination in the developing cerebellum by mediating elimination of surplus climbing fiber synapses . Accumulates at weaker synapses, probably to prevent their undesired enhancement (By similarity). This suggests that ARC-containing virion-like capsids may be required to eliminate synaptic material (By similarity). Required to transduce experience into long-lasting changes in visual cortex plasticity and for long-term memory . Involved in postsynaptic trafficking and processing of amyloid-beta A4 (APP) via interaction with PSEN1 . In addition to its role in synapses, also involved in the regulation of the immune system: specifically expressed in skin-migratory dendritic cells and regulates fast dendritic cell migration, thereby regulating T-cell activation .
PTM: Ubiquitinated by UBE3A, leading to its degradation by the proteasome, thereby promoting AMPA receptors (AMPARs) expression at synapses.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45321
Sequence Length: 396
Subcellular Location: Extracellular vesicle membrane
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A0QZ54 | MSESERSEGFPEGFAGAGSGSLSSEDAAELEALRREAAMLREQLENAVGPQSGLRSARDVHQLEARIDSLAARNAKLMDTLKEARQQLLALREEVDRLGQPPSGYGVLLATHDDDTVDVFTSGRKMRLTCSPNIEVKELKQGQTVRLNEALTVVEAGNFEAVGEISTLREILADGHRALVVGHADEERIVWLAEPLVAAKDLPDEPTDYFDDSRPRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVSYNDIGGLGRQIEQIRDAVELPFLHKDLYKEYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKMAEVRGDDAREAKSYFLNIKGPELLNKFVGETERHIRLIFQRAREKASEGTPVIVFFDEMDSIFRTRGTGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAEAAQDIFSKYLTEDLPVHADDLTEFNGDRALCIKAMIEKVVDRMYAEIDDNRFLEVTYANGDKEVMYFKDFNSGAMIQNVVDRAKKYAIKSVLETGQKGLRIQHLLDSIVDEFAENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKSSSASRAIDTESNLGQYL | Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.
Sequence Mass (Da): 67964
Sequence Length: 613
Domain: Consists of three main regions, an N-terminal coiled-coil domain that binds to protein Pup and functions as a docking station, an interdomain involved in ARC hexamerization, and a C-terminal ATPase domain of the AAA type.
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
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Q9SKN5 | MEQEKSLDPQLWHACAGSMVQIPSLNSTVFYFAQGHTEHAHAPPDFHAPRVPPLILCRVVSVKFLADAETDEVFAKITLLPLPGNDLDLENDAVLGLTPPSSDGNGNGKEKPASFAKTLTQSDANNGGGFSVPRYCAETIFPRLDYSAEPPVQTVIAKDIHGETWKFRHIYRGTPRRHLLTTGWSTFVNQKKLIAGDSIVFLRSESGDLCVGIRRAKRGGLGSNAGSDNPYPGFSGFLRDDESTTTTSKLMMMKRNGNNDGNAAATGRVRVEAVAEAVARAACGQAFEVVYYPRASTPEFCVKAADVRSAMRIRWCSGMRFKMAFETEDSSRISWFMGTVSAVQVADPIRWPNSPWRLLQVAWDEPDLLQNVKRVSPWLVELVSNMPTIHLSPFSPRKKIRIPQPFEFPFHGTKFPIFSPGFANNGGGESMCYLSNDNNNAPAGIQGARQAQQLFGSPSPSLLSDLNLSSYTGNNKLHSPAMFLSSFNPRHHHYQARDSENSNNISCSLTMGNPAMVQDKKKSVGSVKTHQFVLFGQPILTEQQVMNRKRFLEEEAEAEEEKGLVARGLTWNYSLQGLETGHCKVFMESEDVGRTLDLSVIGSYQELYRKLAEMFHIEERSDLLTHVVYRDANGVIKRIGDEPFSDFMKATKRLTIKMDIGGDNVRKTWITGIRTGENGIDASTKTGPLSIFA | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression.
Sequence Mass (Da): 76721
Sequence Length: 693
Domain: Interactions between auxin response factors (ARFs) and Aux/IAA proteins occur through their C-terminal dimerization domains III and IV.
Subcellular Location: Nucleus
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Q01K26 | MASSQEKAKTGVLRNAAALLDEMQLMGETQGAKKVINSELWHACAGPLVCLPQRGSLVYYFPQGHSEQVAATTRKIPNSRIPNYPNLPSQLLCQVHNITLHADKDTDEVYAQMTLQPVNSETDVFPIPTLGAYTKSKHPTEYFCKNLTASDTSTHGGFSVPRRAAEKLFPQLDYSMQPPNQELIVRDLHDNMWTFRHIYRGQPKRHLLTTGWSLFVGAKRLKAGDSVLFIRDEKSQLLLGVRRATRQQTMLSSSVLSTDSMHIGVLAAAAHAASSGSSFTIYYNPRTSPSPFVIPVARYNKATYMQPSVGMRFAMMFETEESSKRRYTGTVVGISDYDPMRWPNSKWRNLQVEWDEHGYGERPERVSIWDIETPENTLVFPSSTLNSKRQCLPGYGVSVPGMEIGSANMSSFPRAQGNPYGSLQHIPAVGSELAIMLLNQSGQTLGSPLSFHQSSYSSIIQNVKQNYIPPLTVSTSACLTKQESLPSDDAQHQFHMANMQNGDLEGSEVQPVIDSISESKLNATSRDPRNTDSYTSRSTSEQNSKGEPRGKTRRSKKGLPHKTVSEKSDLSSAPSWICDNQQVGLESKLVGCDEQVNCGNIEDSSGALTQGNFVGQPHGHQVEQKGVLSPPKVESSKSPDGGKSVNSFPNQGCFSQFIDGLDWMTQPSYYQDSNVIQPAGVSENIFSSSADIPPSMIADTMETFQASCLSDCLPNSIQEFISSPDLNSLTFLSPDMQNLEVQLQHDGSNLPSTSNSFVQMSFSEESASQSANLSGLHMESTHRSINTTSCSQPMSTGGFDAGMYSKLPRLKESQILSLPEIHTNSMGTSACSMDATEYSLDRSAKPMKPPVRTYTKVQKQGSVGRSIDVTGFRNYHELRSAIACMFGLQGKLEHPGSSEWKLVYVDYENDVLLVGDDPWEEFINCVRCIRILSPSEVQQMSENGMHVLNDCIQAA | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
Sequence Mass (Da): 105224
Sequence Length: 955
Domain: Interactions between auxin response factors (ARFs) and Aux/IAA proteins occur through their C-terminal dimerization domains III and IV.
Subcellular Location: Nucleus
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Q0J951 | MSSSSAASIGPPQPPPPPAPPEEEKKCLNSELWHACAGPLVCLPTVGTRVVYFPQGHSEQVAASTNKEVEGHIPNYPNLPAQLICQLHDVTMHADVETDEVYAQMTLQPLNPQEQNDAYLPAEMGIMSKQPTNYFCKTLTASDTSTHGGFSVPRRAAERVFPPLDFTQQPPAQELIARDIHDIEWKFRHIFRGQPKRHLLTTGWSVFVSAKRLVAGDSVLFIWNEKNQLLLGIRRASRPQTVMPSSVLSSDSMHIGLLAAAAHAAATNSRFTIFYNPRASPSEFVIPLSKYIKAVFHTRISVGMRFRMLFETEESSVRRYMGTITEVSDADPVRWPSSYWRSVKVGWDESTAGERPPRVSLWEIEPLTTFPMYPSLFPLRVKHPWYSGVASLHDDSNALMWLRGVAGEGGFQSLNFQSPGIGSWGQQRLHPSLLSSDHDQYQAVVAAAAASQSGGYLKQQFLHLQQPMQSPQEHCNLNPLLQQQILQQASQQQIINPDAQNIQTMLSPSAIQQQLQQLQQMQQVQNDQKQKIQPDQSYQVPTSAVLPSPTSLPSHLREKFGFSDPNANSSSFITSSSSDNMLDSSFLQGSSKAVDLSRFNQPVASEQQQQQQQAWKQKFMGSQSVSFGGSVLHNSPTSKDGSVENKIGRDVQNQSLFSPQVDSSSLLYNMVPNLTSNVSDGNLSTIPSGSTYLQNAMYGCLDDSSGLLQNTGENDPATRTFVKVYKSGSVGRSLDITRFSNYAELREELGQMFGIKGQLDDPDRSGWQLVFVDRENDVLLLGDDPWESFVNSVWYIKILSPEDVHKMGKQGNDPRYLS | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
Sequence Mass (Da): 90901
Sequence Length: 818
Domain: Interactions between auxin response factors (ARFs) and Aux/IAA proteins occur through their C-terminal dimerization domains III and IV.
Subcellular Location: Nucleus
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P53367 | MAQESPKNSAAEIPVTSNGEVDDSREHSFNRDLKHSLPSGLGLSETQITSHGFDNTKEGVIEAGAFQGSPAPPLPSVMSPSRVAASRLAQQGSDLIVPAGGQRTQTKSGPVILADEIKNPAMEKLELVRKWSLNTYKCTRQIISEKLGRGSRTVDLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQRQLGDAFADLSLKSLELHEEFGYNADTQKLLAKNGETLLGAINFFIASVNTLVNKTIEDTLMTVKQYESARIEYDAYRTDLEELNLGPRDANTLPKIEQSQHLFQAHKEKYDKMRNDVSVKLKFLEENKVKVLHNQLVLFHNAIAAYFAGNQKQLEQTLKQFHIKLKTPGVDAPSWLEEQ | Function: Plays a role in controlling biogenesis of secretory granules at the trans-Golgi network . Mechanistically, binds ARF-GTP at the neck of a growing secretory granule precursor and forms a protective scaffold . Once the granule precursor has been completely loaded, active PRKD1 phosphorylates ARFIP1 and releases it from ARFs . In turn, ARFs induce fission . Through this mechanism, ensures proper secretory granule formation at the Golgi of pancreatic beta cells .
PTM: Phosphorylated by PRKD1; phosphorylation delocalizes ARFIP1 from the Golgi and disrupts its ability to inhibit the activity of ADP-ribosylation factor, an important component of the vesicle scission machinery.
Sequence Mass (Da): 41738
Sequence Length: 373
Subcellular Location: Golgi apparatus
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Q5WEW9 | MATVVIKIGGSTLEALEEGFYEGVVKRASLGDKIMIVHGGGPAINNLLQAMAVESQFVNGLRKTTAEVLTAAETALSGQINKQLVRSLYQAGGKAIGLSGSDGHLLKTIPIDTDKLGFVGAVESVNVDVLFNVAKAGYIPVIAPIGMDANYQPYNINADTAAAAVAKASKAEELVFVTDVDGVQKDGKVIKEMDEVLAKHYIEEGVIYGGMVPKVNACLDSLSGALTKARIVNGKKAYHPSAGTAIVKQSNVLTSGA | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 26714
Sequence Length: 257
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
|
A6TTJ1 | MNLSPNQKADVLIESLPYIKKFYNEIVVIKYGGSAMVNDELKESIIKDIVLMKYVGMHPVVVHGGGPEITNMLKVFDKESKFVDGLRVTDQATMEITEMVLLGKVCQEIVTRINQNGVRSIGICGKDGSMIKTVPKDPELGLVGGITSIDTDLIKTIIEKGYIPVISPIGCGPAGESHNINADEVAGKLAAALGAKKLMLITDVAGVLRDQHDEASLISDIKTNEIEEYIETGVIKGGMIPKISCCFDAVANGVERAHIIDGRKSHSMLLEIFTDQGVGTMITHGGDQNGNSKNNKQWKSIFNEHLWENAYSLPGR | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 34334
Sequence Length: 316
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
|
B4S0H7 | MSVSPIVIKVGGALLDDAAAMTRLFLSVKDVQATRPVVVVHGGGPLVETLMASLGLKSTKIDGLRVTPDEHMPYICGALAGSANKQLCAAALASGLTPVGLSLLDGNMVVCEPLADQYGAVGVPSTADAAFLKSVLAQSTLPIISSIGSSPQGRLLNVNADQAATVIAELLNAELLLLSNVDGVLDGNKALISALNANSIAQYASEGVITDGMKVKVDAALASAESLSRPVYIASWAADITDILNKTTGTQIVPTTLAAENGNAGEI | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 27086
Sequence Length: 267
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
|
O67848 | MNELIEKAKVLQEALPYIREFHGKVFVIKYGGSAMHDEELRESFARDVVLLKYVGINPVIVHGGGPQISKTLEKFGIKPKFVGGMRKTDEETMHVVEMVLSGDINKDIVALINRYSGEKIYAVGLSGRDGRLLKAKKLDKERYFSELGLPVPEEDIGFVGEIVDVNEELIFTLLSHNFIPVIAPVGVGEEGEAYNVNADLAASEIAGEIKAEKLIYLTDTKGVLDEKGELISSLSKDKAEELIKKGVIREGMIPKVRSALRALEKGVKKVHIIDGRVKHSILLEVFTKEGVGTEITLE | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 32908
Sequence Length: 298
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
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O28988 | MENVELLIEALPYIKDFHSTTMVIKIGGHAMVNDRILEDTIKDIVLLYFVGIKPVVVHGGGPEISEKMEKFGLKPKFVEGLRVTDKETMEVVEMVLDGKVNSKIVTTFIRNGGKAVGLSGKDGLLIVARKKEMRMKKGEEEVIIDLGFVGETEFVNPEIIRILLDNGFIPVVSPVATDLAGNTYNLNADVVAGDIAAALKAKKLIMLTDVPGILENPDDKSTLISRIRLSELENMRSKGVIRGGMIPKVDAVIKALKSGVERAHIIDGSRPHSILIELFTKEGIGTMVEP | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 31664
Sequence Length: 290
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
|
B6YS18 | MERLTIVKVGGEIIRIPEVRDSFLKDFSIIAGYKILVHGGGSMLTELARNLDIETQMIDGRRVTTEKILKLAVMVYAGLINKEIVVGLQALGVDALGFTGADSNIICSEKRPIRDSIDYGLVGDIQEINVQLLNEFLNKGHTPIFAPITHNGGGQLLNTNADSIAGELAKVLVYDYNVRLVYCFDKKGVLYDEGDENSFISVLSYTDFQRYKENGIIGGGMLPKLDSAFNALSAGVKEVIITCASNIKHTGSGTHLKL | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 28108
Sequence Length: 258
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
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Q7NEE9 | MSQDAPSCFTAIISPADRVQVLAEALPYIQRFAGKTIVVKYGGAAMVKENLRDLVIRDIVFLATVGIKPVVVHGGGPEINSWLERLNIPVQFVGGLRVTDKITMEVVEMVLAGKVNKSIVQMINQAGGSAVGLCGRDGSIIEARPHQSAQLQPDIGFVGDIQSVNPKLIQSLLKEGHIPVLSSVASDENGQAYNINADTAAGELAAALDAEKLILLTDTPGILLDKDHPRSLIRKLDIYQARKLIAEGVVDGGMIPKVQCCVRALAQGVRAAHIVDGRQMHALLLEVLTDQGIGSMLVASELV | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 32258
Sequence Length: 303
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Cytoplasm
EC: 2.7.2.8
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