ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q84FH6 | MVRGIRGAITVEEDTPEAIHQATRELLLKMLEANGIQSYEELAAVIFTVTEDLTSAFPAEAARQIGMHRVPLLSAREVPVPGSLPRVIRVLALWNTDTPQDRVRHVYLREAVRLRPDLESAQ | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 13650
Sequence Length: 122
Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.4.99.5
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Q8G5X4 | MTARPRAVIIGMMGAGKTRVGKEVAHMLRLPFADADVEIEREVGMKIPSYFEEYGEPAFREVEADLIADMLEDFDGIFSLGGGAPMTPSTQHALASYIDHGGRVVYLDADPAEAMERANRGGGRPMLNGNANSRWKKLFKQRDPVFREVANVHVHTRGLTPQGAAKKVIDMVSERAVHVTGAAIEPYDVVIGEGAMNHLVDVLGPKPAKIALIHTQPVQRHSDRARALLRQGGYEVSDIVIPDAEPGKTITVANGIWERLGNEGFTRSDAVVGLGGGAATDLAGFVAATWMRGVRYVNCPTSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILHILEDHAAELRAFDGSTFLGSPLEDVVAELIERTVKVKAYHVSSDLKEKGLREFLNYGHTMGHAIEKLEHFRWRHGNAVAVGMVYAAELAHLIGYIDQDLVDYHRSLLASMGLPTSWNGGSFDDVLALMHRDKKARGNELRFVVLDEIGHVVHLDNPPAEAVEEAFRRIQQ | Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Mass (Da): 58712
Sequence Length: 540
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Subcellular Location: Cytoplasm
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P0A4Z3 | MAPKAVLVGLPGSGKSTIGRRLAKALGVGLLDTDVAIEQRTGRSIADIFATDGEQEFRRIEEDVVRAALADHDGVLSLGGGAVTSPGVRAALAGHTVVYLEISAAEGVRRTGGNTVRPLLAGPDRAEKYRALMAKRAPLYRRVATMRVDTNRRNPGAVVRHILSRLQVPSPSEAAT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 18583
Sequence Length: 176
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
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Q9CCS5 | MAPKAVLVGLPGAGKSTIGRRLSKALGVSLLDTDAAIEKQTGRSIADIFAIDGEEEFRRIEEGVVRAALVEHDGVVSLGGGAVTSPGVCAALAGHIVIYLEINAEEAMRRACGSTVRPLLAGPDRAEKFQDLMARRVPLYRRVATIRVDTNCHNLGAVVRYIMARLQAQLATPVSGGDRKSSEAERSGAPLRKSSEVVK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 21084
Sequence Length: 199
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
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B2HNC7 | MAPKAVLVGLPGSGKSTIGRRLAKALGVGLLDTDAAIEQQAGRSIAEIFATDGEEEFRRIEEEVVRAALADHDGVLSLGGGAVTSPGVRSALDGHTVVYLEISAAEGVRRTGGSNVRPLLAGPDRAEKFRALMSQRIPLYRRVSTIRVDTNRRNPGAVVRYIMSRLDDPTPNTSPSSTASGAAT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19347
Sequence Length: 184
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
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Q5FAD3 | MKNFNGKLILIGLMGAGKTTLGRQMAQRLDYRFYDSDHEIAAAAGVPIPTIFEMEGEQGFRSRETAILKKLIVLPHIVLSTGGGAVLKEENRALIRKSGTVVYLHAPPETLLERTRCDNSRPLLQVADPLAKLRELYAARDPVYRQTADFTVESANCRETVQTLLKRLSR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 18980
Sequence Length: 170
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
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Q82TC0 | MHFRYNYRMQRSKTPNTKNSDTGSIPGNIILIGMMGSGKTTVGKLLANLVGKTFIDIDHEIQRRTGVGIPVIFEIEGEAGFRKRESEVLRDIVRQQNIVLATGGGAILHPDNRALLRQHGTVVYLCAPVTELRRRTYLDKNRPLLQTGNVHAKLIELFTQRDPLYRETAHIIMDSGRQSARAFVQKLIQKLRQSNQEFTAAGSPPCVKPSE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 23703
Sequence Length: 211
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
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Q2YBB2 | MISTDAVAPAVDVKGEAGDRAATGNIFLVGMMGAGKTTVGRLLSHFLEKTFYDSDREIQKRTGVSIPTIFEIEGEEGFRRRETEILSELMNARNIILATGGGAVLSGVNRAMLKHGGTVIYLRASIDDLWRRTRHDKNRPLLQTSDPRARLAELFVQRDPLYRETAHIVVESGKRSPRHLAQSLAQQLTISSRTG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 21542
Sequence Length: 195
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
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B2IX35 | MSSLLQGVNLYLIGMMGVGKTTVGPLLAKHLGYGFLDLDGVIAKATDKSINQLFAEEGEAGFRQIESDVLSQVCAFTKLTIATGGGIVLRRENWGYLHHGLIVWLDVPVELIYRRLAEDTTRPLLQDADLKGKLRSLLEQRTPLYSQADLHITVQEGETPEDIANRIIEVIPNVLKPQASH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19959
Sequence Length: 181
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
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A4W763 | MTQPIFLVGPRGCGKTTVGLELARACQSQFVDTDHWLQTKAGRTIAEIVEKEGWETFRALETETLKAVSAPSTVIATGGGIILAEHNRGFMREHGIVIYLCAPVATLVERLEAFPEEGQRPTLTGKPISDEVSEVLAERDALYREAAHHVVDASQTPEQVVSHIVTALRLACAS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 18890
Sequence Length: 174
Domain: The LID domain closes over the active site upon ATP binding.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
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B7LMJ7 | MIQPLFLVGPRGCGKTTVGKALADALERRFVDTDQWLQANVQMTVADIVEREGWAGFRAREAAALEAVTAPATVVATGGGIILAEQNRHFMRNNGIVIYLSAPVDVLVNRLEAEPEVGLRPTLTGKSLSEEVAEVLEQRDILYRETANIIVDATYEPGQVISEIRALLDQMALRNLGGAYT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Mass (Da): 19690
Sequence Length: 181
Domain: The LID domain closes over the active site upon ATP binding.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Subcellular Location: Cytoplasm
EC: 2.7.1.71
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Q741J6 | MIVQVINGPNLGRLGRREPDVYGDTTHDQLAALIEAEAAALGLKAIVRQSDSEAELLDWIHGAADANQPVILNAGGLTHTSVALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPVATGAIVGLGVQGYLLALRYLAGRPA | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 15192
Sequence Length: 143
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
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Q1QLB8 | MARTIYVLNGPNLNMLGTREPETYGRATLADVEKLCADTAGDFGLAADCRQSNREGELIDFIHDAHAKKAAGIVINAGGYSHTSVALHDALVAVNIPTVEVHISNIHAREDFRHHSFTARAAFASLCGFGIDGYRLAINGLAAKIGAVKSGAKVKS | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 16530
Sequence Length: 156
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
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A6Q235 | MKVMVIQGPNLNMLGIREQHIYGPMKLEDIHKQMKNFADANGLDIEFFQSNLEGEIVDKIQESLGDADGIIINAGAYTHTSIAIRDAIAAVQLPTIEVHLSNVYRREEFRQKSMIAPVCAGVITGFGPFSYHLAMVAMHQIFQEIEALKAQQPQQA | Function: Catalyzes a trans-dehydration via an enolate intermediate.
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Mass (Da): 17380
Sequence Length: 156
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
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Q8N5I2 | MGRVQLFEISLSHGRVVYSPGEPLAGTVRVRLGAPLPFRAIRVTCIGSCGVSNKANDTAWVVEEGYFNSSLSLADKGSLPAGEHSFPFQFLLPATAPTSFEGPFGKIVHQVRAAIHTPRFSKDHKCSLVFYILSPLNLNSIPDIEQPNVASATKKFSYKLVKTGSVVLTASTDLRGYVVGQALQLHADVENQSGKDTSPVVASLLQKVSYKAKRWIHDVRTIAEVEGAGVKAWRRAQWHEQILVPALPQSALPGCSLIHIDYYLQVSLKAPEATVTLPVFIGNIAVNHAPVSPRPGLGLPPGAPPLVVPSAPPQEEAEAEAAAGGPHFLDPVFLSTKSHSQRQPLLATLSSVPGAPEPCPQDGSPASHPLHPPLCISTGATVPYFAEGSGGPVPTTSTLILPPEYSSWGYPYEAPPSYEQSCGGVEPSLTPES | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates . Through an ubiquitination-dependent mechanism plays for instance a role in the incorporation of SLC11A2 into extracellular vesicles . More generally, plays a role in the extracellular transport of proteins between cells through the release in the extracellular space of microvesicles . By participating in the ITCH-mediated ubiquitination and subsequent degradation of NOTCH1, negatively regulates the NOTCH signaling pathway .
PTM: Ubiquitinated . Ubiquitination by WWP2; promotes localization to extracellular microvesicles . Ubiquitinated by WWP1 .
Sequence Mass (Da): 45981
Sequence Length: 433
Domain: The PPxY motifs mediate interaction with WW domain-containing ubiquitin-protein ligases.
Subcellular Location: Cell membrane
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Q99KN1 | MGRVQLFEIRLSQGRVVYGPGEPLAGTVHLRLGAPLPFRAIRVTCMGSCGVSTKANDGAWVVEESYFNSSLSLADKGSLPAGEHNFPFQFLLPATAPTSFEGPFGKIVHQVRASIDTPRFSKDHKCSLVFYILSPLNLNSIPDIEQPNVASTTKKFSYKLVKTGNVVLTASTDLRGYVVGQVLRLQADIENQSGKDTSPVVASLLQKVSYKAKRWIYDVRTIAEVEGTGVKAWRRAQWQEQILVPALPQSALPGCSLIHIDYYLQVSMKAPEATVTLPLFVGNIAVNQTPLSPCPGRESSPGTLSLVVPSAPPQEEAEAVASGPHFSDPVSLSTKSHSQQQPLSAPLGSVSVTTTEPWVQVGSPARHSLHPPLCISIGATVPYFAEGSAGPVPTTSALILPPEYSSWGYPYEAPPSYEQSCGAAGTDLGLIPGS | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates . Through an ubiquitination-dependent mechanism plays for instance a role in the incorporation of SLC11A2 into extracellular vesicles . More generally, plays a role in the extracellular transport of proteins between cells through the release in the extracellular space of microvesicles (By similarity). By participating to the ITCH-mediated ubiquitination and subsequent degradation of NOTCH1, negatively regulates the NOTCH signaling pathway .
PTM: Ubiquitinated. Ubiquitination by WWP2; promotes localization to extracellular microvesicles. Ubiquitinated by WWP1.
Sequence Mass (Da): 46330
Sequence Length: 434
Domain: The PPxY motifs mediate interaction with WW domain-containing ubiquitin-protein ligases.
Subcellular Location: Cell membrane
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Q96B67 | MVLGKVKSLTISFDCLNDSNVPVYSSGDTVSGRVNLEVTGEIRVKSLKIHARGHAKVRWTESRNAGSNTAYTQNYTEEVEYFNHKDILIGHERDDDNSEEGFHTIHSGRHEYAFSFELPQTPLATSFEGRHGSVRYWVKAELHRPWLLPVKLKKEFTVFEHIDINTPSLLSPQAGTKEKTLCCWFCTSGPISLSAKIERKGYTPGESIQIFAEIENCSSRMVVPKAAIYQTQAFYAKGKMKEVKQLVANLRGESLSSGKTETWNGKLLKIPPVSPSILDCSIIRVEYSLMVYVDIPGAMDLFLNLPLVIGTIPLHPFGSRTSSVSSQCSMNMNWLSLSLPERPEAPPSYAEVVTEEQRRNNLAPVSACDDFERALQGPLFAYIQEFRFLPPPLYSEIDPNPDQSADDRPSCPSR | Function: Adapter protein that plays a role in regulating cell-surface expression of adrenergic receptors and probably also other G protein-coupled receptors . Plays a role in NEDD4-mediated ubiquitination and endocytosis af activated ADRB2 and subsequent ADRB2 degradation . May recruit NEDD4 to ADRB2 . Alternatively, may function as adapter protein that does not play a major role in recruiting NEDD4 to ADRB2, but rather plays a role in a targeting ADRB2 to endosomes .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 46395
Sequence Length: 414
Subcellular Location: Cytoplasm
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Q8NCT1 | MGGEAGCAAAVGAEGRVKSLGLVFEDERKGCYSSGETVAGHVLLEASEPVALRALRLEAQGRATAAWGPSTCPRASASTAALAVFSEVEYLNVRLSLREPPAGEGIILLQPGKHEFPFRFQLPSEPLVTSFTGKYGSIQYCVRAVLERPKVPDQSVKRELQVVSHVDVNTPALLTPVLKTQEKMVGCWFFTSGPVSLSAKIERKGYCNGEAIPIYAEIENCSSRLIVPKAAIFQTQTYLASGKTKTIRHMVANVRGNHIASGSTDTWNGKTLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKKLMLELPLVIGTIPYNGFGSRNSSIASQFSMDMSWLTLTLPEQPEAPPNYADVVSEEEFSRHIPPYPQPPNCEGEVCCPVFACIQEFRFQPPPLYSEVDPHPSDVEESQPVSFIL | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates (By similarity). Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (Probable). Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular vesicles (By similarity). May play a role in glucose uptake . Participates in innate immune response by promoting IFIH1/MDA5 activation through interaction with TRIM65 .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45479
Sequence Length: 418
Subcellular Location: Early endosome
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A0A0B4J1F4 | MGGEAGADGPRGRVKSLGLVFEDESKGCYSSGETVAGHVLLEAAEPVALRGLRLEAQGRATSAWGPSAGARVCIGGGSPAASSEVEYLNLRLSLLEAPAGEGVTLLQPGKHEFPFRFQLPSEPLATSFTGKYGSIQYCVRAVLERPQVPDQSVRRELQVVSHVDVNTPPLLTPMLKTQEKMVGCWLFTSGPVSLSVKIERKGYCNGEAIPIYAEIENCSSRLVVPKAAIFQTQTYLASGKTKTVRHMVANVRGNHIGSGSTDTWNGKMLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKRLMLELPLVIGTIPYSGFGRRNSSVASQFSMDMCWLALALPEQPEAPPNYADVVSEEEFSRHVPPYPQPSDCDGEACYSMFACIQEFRFQPPPLYSEVDPHPGDAQETQPVSFIL | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates . Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (By similarity). Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular vesicles . May play a role in glucose uptake (By similarity). Participates in innate immune response by promoting IFIH1/MDA5 activation through interaction with TRIM65 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 44970
Sequence Length: 415
Subcellular Location: Early endosome
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Q7TP90 | MSSQSSILVDFRPLATSFTGKYGSIQYCVRAVLERPQVPDQSVRRELQVVSHVDVNTPPLLTPMLKTQEKMVGCWLFTSGPVSLSVKIERKGYCNGEAIPIYAEIENCSSRLVVPKAAIFQTQTYLASGKTKTVRHMVANVRGNHIGSGSTDTWNGKMLKIPPVTPSILDCCIIRVYIHIPGAKKLMLELPLVIGTIPYSGFGRRNSSMASQFSMDMCWLALALPEQPEAPPNYADVVSEEEFSRHIPPYPQPSACDGEACYSMFACIQEFRFQPPPLYSESHAQLFCLQPVGPTNRAHF | Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates. Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular vesicles. May play a role in glucose uptake. Participates in innate immune response by promoting IFIH1/MDA5 activation through interaction with TRIM65.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33275
Sequence Length: 300
Subcellular Location: Early endosome
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O24972 | MRFSIFFKVVALFMITLFSFGAFAYYFVSSQISHENYQNEMRHYQFVTTINEILNNYSDYRAIEDYLYKIGFRETTIENLEKVLAKRRHQLHHRNIGYAEVFKFSDMVFILLKKDEHFVLYKDLHSVSYRNYFLAITVGLLLILFLFLFVLQSLLPLRELRSQVKPFAQGDKSVSCKSKQKDEIGDLANEFDNCILKINAMNESRVLFLRSIMHELRTPITKGKILSSMLKEELSCKRFSSIFDHLNMLIEQFARIEQLASKNYGSNKEKFLMSDLIDKIEKMLLIDEDKESPIHVSSSNYIIEADFELFSIALKNMVDNAIKYSDDKQVFLDFIGNNLVVSNKSKPLKEDFEKYLQPYFKSSNPSQAHGFGLGMYIIKNALEAMGLNLSYHYSNGRICFTIHDCVFNSFYDLEEDNEELPPPPPKI | Function: Member of the two-component regulatory system ArsS/ArsR that regulates genes involved in biofilm formation and acid adaptation by acting on major ammonia-producing pathways . Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of ArsR . In turn, ArsR binds to the upstream promoter regions of target genes including ureA, amiE and amiF to positively regulate their expression in response to acidic pH . Participates also in acidic acclimatation in a phosphorylation-independent pathway by regulating acid-induced trafficking of urease and its accessory proteins to the inner membrane .
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 49917
Sequence Length: 427
Subcellular Location: Membrane
EC: 2.7.13.3
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O27106 | MMNDKKITSFIALPDLLSMLNASSGYLSILLSIDGSLNAACILMLLAVLFDSLDGWVARKTGRIDIHGFGKNMDSLSDVISFGVAPAILIYSAAVDFRYINILVGPLIVLCGILRLSRFNVLTGGGKNFTGLPIPVAAVTISSFYLTGFYSELSAAFIMIAVSVLMISSIEYPRVDGMGASTALILIIATIISVAAVEILQAASVVAGPVAIILFIATLTYIAVPILPKRDVI | Function: Involved in the lipid biosynthesis. Catalyzes the formation of unsaturated archaetidylserine from CDP-unsaturated archaeol and L-serine. Activity with ester-linked substrate analogs containing straight aliphatic chains (typical bacterial substrates) is two to three times higher than that with the corresponding ether-type substrate (typical archaeal substrates). Both enantiomers of CDP-unsaturated archaeols with ether-linked geranylgeranyl chains and CDP-saturated archaeol with ether-linked phytanyl chains are similarly active. The enzyme also accepts D-serine, although activity is only about third of that with L-serine.
Catalytic Activity: CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + L-serine = archaetidylserine + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24618
Sequence Length: 233
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Membrane
EC: 2.7.8.38
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P14000 | MKSAPFLFLLGLLGLVTAQTQDPALLDLLRENPDLLSLLLQSNEHRAPLVKPNVVLLVADHMGSGDLTSYGHPTQEAGFIDKMAAEGLRFTNGYVGDAVCTPSRSAIMTGRLPVRIGTFGETRVFLPWTKTGLPKSELTIAEAMKEAGYATGMVGKWHLGINENSSTDGAHLPFNHGFDFVGHNLPFTNSWSCDDTGLHKDFPDSQRCYLYVNATLVSQPYQHKGLTQLFTDDALGFIEDNHADPFFLYVAFAHMHTSLFSSDDFSCTSRRGRYGDNLLEMHDAVQKIVDKLEENNISENTIIFFISDHGPHREYCEEGGDASIFRGGKSHSWEGGHRIPYIVYWPGTISPGISNEIVTSMDIIATAADLGGTTLPTDRIYDGKSIKDVLLEGSASPHSSFFYYCKDNLMAVRVGKYKAHFRTQRVRSQDEYGLECAGGFPLEDYFDCNDCEGDCVTEHDPPLLFDLHRDPGEAYPLEACGHEDVFLTVKSTVEEHKAALVKGTPLLDSFDHSIVPCCNPANGCICNYVHEPGMPECYQDQVATAARHYRP | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May be a structural component of the extracellular matrices involved in cell movement during morphogenesis.
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Catalytic Activity: an aryl sulfate + H2O = a phenol + H(+) + sulfate
Sequence Mass (Da): 60952
Sequence Length: 551
Subcellular Location: Cytoplasm
EC: 3.1.6.1
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P51691 | MSKRPNFLVIVADDLGFSDIGAFGGEIATPNLDALAIAGLRLTDFHTASTCSPTRSMLLTGTDHHIAGIGTMAEALTPELEGKPGYEGHLNERVVALPELLREAGYQTLMAGKWHLGLKPEQTPHARGFERSFSLLPGAANHYGFEPPYDESTPRILKGTPALYVEDERYLDTLPEGFYSSDAFGDKLLQYLKERDQSRPFFAYLPFSAPHWPLQAPREIVEKYRGRYDAGPEALRQERLARLKELGLVEADVEAHPVLALTREWEALEDEERAKSARAMEVYAAMVERMDWNIGRVVDYLRRQGELDNTFVLFMSDNGAEGALLEAFPKFGPDLLGFLDRHYDNSLENIGRANSYVWYGPRWAQAATAPSRLYKAFTTQGGIRVPALVRYPRLSRQGAISHAFATVMDVTPTLLDLAGVRHPGKRWRGREIAEPRGRSWLGWLSGETEAAHDENTVTGWELFGMRAIRQGDWKAVYLPAPVGPATWQLYDLARDPGEIHDLADSQPGKLAELIEHWKRYVSETGVVEGASPFLVR | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Hydrolyzes the bond between sulfate and the aromatic ring in a compound such as 4-nitrocatechol sulfate.
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Catalytic Activity: an aryl sulfate + H2O = a phenol + H(+) + sulfate
Sequence Mass (Da): 59946
Sequence Length: 536
Subcellular Location: Cytoplasm
EC: 3.1.6.1
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P28607 | MQKISIIFNLFLSLGCLAFTFNGSASETKNEWITLGTMAGPIPNAKHSQPANAMLVNGNTYVVDAGDGTAGQLAKVGLDIKNVDAVFLSHLHFDHTGGLPAILSLRWQTSARNELVVYGPPGTQQTVDGIFEYMTYGTLGHYGVPGQVPAPANTNIKVVEVEDGTQLKLPDFTVDVIRNSHYSWPKGSEEWKKFQALSFKFSLQDYTVVYTGDTGPSSAVEKLSSGVDLLVSEMMDIDHTVNMIKETNPQMPKGKFIGIHKHLSKHHLSPKQVGELAKAANVGSLVITHMAPGLDTQAEIDFYTKQVASEYKGPISVAQDLNRYELKR | Function: May function as a glycosulphohydrolase involved with desulfation of sulfated polysaccharides.
Catalytic Activity: an aryl sulfate + H2O = a phenol + H(+) + sulfate
Sequence Mass (Da): 35793
Sequence Length: 328
Subcellular Location: Periplasm
EC: 3.1.6.1
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Q10723 | MLQRLVVALCLLGFAALTAAAAHQRPNFVVIFTDDQDGIQNSTHPRYQPKLHEHIRYPGIELKNYFVTTPVCCPSRTNLWRGQFSHNTNFTDVLGPHGGYAKWKSLGIDKSYLPVWLQNLGYNTYYVGKFLVDYSVSNYQNVPAGWTDIDALVTPYTFDYNNPGFSRNGATPNIYPGFYSTDVIADKAVAQIKTAVAAGKPFYAQISPIAPHTSTQIYFDPVANATKTFFYPPIPAPRHWELFSDATLPEGTSHKNLYEADVSDKPAWIRALPLAQQNNRTYLEEVYRLRLRSLASVDELIDRVVATLQEAGVLDNTYLIYSADNGYHVGTHRFGAGKVTAYDEDLRVPFLIRGPGIRASHSDKPANSKVGLHVDFAPTILTLAGAGDQVGDKALDGTPLGLYANDDGNLLADYPRPANHRNQFQGEFWGGWSDEVLHHIPRYTNNSWKAVRVYDEDNQQAWKLIVSCTNERELYDLKTDPGELCNIYNKTRAAVRTRLEALLAVLVVCKGESCTNPWKILHPEGSVNSWNQSLDRKYDKYYANVAPFQYRTCLPYQDHNNEVSAFRSTVAAAAAAAAAAAAQQPGRRRMYTWTSAGRQLSATASAIATSPQPRSEPFVAEVERHSVPVPAEVLQSDVAKWFDNPLALA | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Is commonly produced by soil microorganisms and plays an important role in the mineralization of sulfates.
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Catalytic Activity: an aryl sulfate + H2O = a phenol + H(+) + sulfate
Sequence Mass (Da): 72287
Sequence Length: 649
Subcellular Location: Periplasm
EC: 3.1.6.1
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P18634 | MAPKISISLNPPYNGEFYSSNDQMSGIVSLQLTKALSIRKISVILKGFSETLTKIDQEYMFQQNGMMMPGQDNKSFHTLMKFEQRVFPPDNVWNALDGSSKPFKVKPGSYNYSFQFDKFPRKPECLKNHTAKTVAFVTRSNARLPPTFNSHWQEFNKIDNLDLYFYSFGKVIYMVQVQLELGKSSSWFKPFHKLIREIETFEFIPEPKDLIIEPDEDDNEELNAFSNNSRGNSMVTNNEFFNSSNLKVPSKDVKVVNGVGYIKSDRNFSQANSILIENGDIRSRPVSSVTSTRQSTRLVNGMKVFPSTYKMGLPDGESNMRIEVRSRDLKQIYRKDYLFRSGSQNFDKVYVVMEGNIASLSKMQITPLKLQLNLLETTTYLSQGIANGNYSSLKLIEIDLNQLKSNKPLLDLNEIRENFDGSMFECELRLKDHPILRKLVFNEEDYRHRGNRLYSFKTCTIKRTFSLQLLIEWGINGIRKQSEVNIDPVQIFCQVREHVEAEALPRYVPPPTYTEMAS | Function: May regulate endocytosis by recruiting RSP5 ubiquitin ligase activity to specific plasma membrane proteins in response to extracellular stimuli.
PTM: Ubiquitinated by RSP5.
Sequence Mass (Da): 59758
Sequence Length: 518
Subcellular Location: Cytoplasm
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Q9UT55 | MKFLNPPFPYSMTSDPESFGHECFTRRWGIILTGIEKDVSERLSKLASTSKDSEVVAQGKPLLNDLEAFKSDIKNDRPLVPLEGEGQDIVEYNEELKQLDNASWGNAPWLYSECYYYRRISLIFARYSEWKAYDPFFQQKDSTLKSSRAAVEELAGRYCLLEEELNSIAKKGDSHIAYMVFVEMAQISLWGNATDLSLLTNLSYEELQNLQGQKVVEESQKNILVNDFPTVWSKLKDVHNGRIDFVLDNAGFELYVDLIFAAYLLKAGIAKEIVLHPKDFPWFVSDVLPYDIEYLLTNLDTIFPTESVTKFATDLRSFSAKGQLRLRTDPFWTTAHYFGRMPDFAAGLLTELEKSDMIFFKGDLNYRKLTGDCLWPRTTPFGKTLGPIANAINACALRTCKADVVVGLPDGLYEKIAKDLPHWERTGKYAVVEFCPKA | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity).
Catalytic Activity: beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate
Sequence Mass (Da): 49895
Sequence Length: 438
Domain: Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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Q94GF1 | MASLVLSLRIAPSTPPLGLGGGRFRGRRGAVACRAATFQQLDAVAVREEESKFKAGAAEGCNILPLKRCIFSDHLTPVLAYRCLVREDDREAPSFLFESVEQGSEGTNVGRYSVVGAQPAMEIVAKANHVTVMDHKMKSRREQFAPDPMKIPRSIMEQWNPQIVEGLPDAFCGGWVGFFSYDTVRYVETKKLPFSNAPEDDRNLPDIHLGLYNDIVVFDHVEKKTHVIHWVRVDCHESVDEAYEDGKNQLEALLSRLHSVNVPTLTAGSVKLNVGQFGSALQKSSMSREDYKKAVVQAKEHILAGDIFQVVLSQRFERRTFADPFEVYRALRIVNPSPYMAYLQARGCILVASSPEILTRVEKRTIVNRPLAGTIRRGKSKAEDKVLEQLLLSDGKQCAEHIMLVDLGRNDVGKVSKPGSVKVEKLMNVERYSHVMHISSTVTGELRDDLTCWDALRAALPVGTVSGAPKVRAMELIDQMEGKMRGPYSGGFGGVSFRGDMDIALALRTIVFPTGSRFDTMYSYTDKNARQEWVAHLQAGAGIVADSKPDDEHQECLNKAAGLARAIDLAESTFVDE | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS to produce anthranilate.
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 63866
Sequence Length: 577
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Subcellular Location: Plastid
EC: 4.1.3.27
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Q9H765 | MSSSMWYIMQSIQSKYSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEKDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLIGQTPISRLVALLVRGLGTEKEDSCFELLHRAVGHFELRKNGTMPREVARDPQLCEKLTVLCSAPGTLKTLARYAVRRSLGLQYLPDAVKGLPLPASLKEYLLLLE | Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 31642
Sequence Length: 288
Domain: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q91ZT9 | MSSSMWYIMQSIQSKYSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAERDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLKGQTPISRLVALLVRGLGTEKEDSCFELLHRAVGQFELRKNGIMPREVTKDQQLCEKLTVLCSAPGTLKTLARYAVRRSLGLQYLPDAVKGLPLPVSLKDYLLLLE | Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 31735
Sequence Length: 288
Domain: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q96DX5 | MDGKQGGMDGSKPAGPRDFPGIRLLSNPLMGDAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVNQGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL | Function: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes at least two forms of creatine kinase, CKB and CKMT1A.
Sequence Mass (Da): 31858
Sequence Length: 294
Domain: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Mitochondrion
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Q91ZT8 | MDGEQRGRSDRPGGSPHLPFLSNPLMGDVVSDWSPLHDAAIHGCLLTLRNLISQGWPVNIITADHVSPLHEACLRGHLSCASVLLSHGAQVNGMTIDWRTPLFNACVSGSQDCVNLLLQHGATPHPETELASPIHEAAKRGYVKCIESLAAHGANIDYNISHLGTPLYVACKNQQVACAKKLLESGVSVNQGKGLDSPLHVVARMSSVELVHLLMDFGANAQAKNADGKRPVDLVPLESPLIQIFLQNEGPQSLRQLCRLRIRKCFGIRQHHKISELLLPEDLKRFLLHL | Function: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes at least two forms of creatine kinase, CKB and CKMT1A (By similarity).
Sequence Mass (Da): 31656
Sequence Length: 290
Domain: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Mitochondrion
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A0A0F7RJ52 | MKHAKQIAEHATIQSFLNCYLRETGSGEWITEDKRIEDIFYHLFQRDTCSTYLCCRLSAQNITLYGEVIYKSPTDRHLFGEQFYYQMGDSNSVMKADYVTVITFLIKEMSINYGEGTNPAELMLRVIRSCQNIEEFTKERKEDTSALYGFHTSFIEAEQSLLFGHLTHPTPKSRQGILEWKSAMYSPELKGECQLHYFRAHKSIVNEKSLLLDSTTVILKEELRNDEMVSKEFISKYCNEDEYSLLPIHPLQAEWLLHQPYVQDWIEQGVLEYIGPTGKCYMATSSLRTLYHPDAKYMLKFSFPVKVTNSMRINKLKELESGLEGKAMLNTAIGEVLEKFPGFDFICDPAFITLNYGTQESGFEVIIRENPFYSEHADDATLIAGLVQDAIPGERTRLSNIIHRLADLESRSCEEVSLEWFRRYMNISLKPMVWMYLQYGVALEAHQQNSVVQLKDGYPVKYYFRDNQGFYFCNSMKEMLNNELAGIGERTGNLYDDYIVDERFRYYLIFNHMFGLINGFGTAGLIREEILLTELRTVLESFLPYNREPSTFLRELLEEDKLACKANLLTRFFDVDELSNPLEQAIYVQVQNPLVREVAVRS | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Catalyzes the ATP-dependent condensation of citric acid and spermidine to form N(8)-citryl-spermidine . It can also catalyze the condensation of several di- and triamine analogs of spermidine with citric acid and the condensation of the citric acid analog tricarballylic acid with spermidine . Required for growth in iron-depleted medium and for full virulence in a mouse model of infection .
Catalytic Activity: ATP + citrate + spermidine = AMP + diphosphate + H(+) + N(8)-citryl-spermidine
Sequence Mass (Da): 69937
Sequence Length: 602
Pathway: Siderophore biosynthesis; petrobactin biosynthesis.
EC: 6.3.2.-
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Q81RQ8 | MRMDMYHTKILKAIESEDYISVRRRVLRQLVESLIYEGIITPARIEKEEQILFLIQGLDEDNKSVTYECYGRERITFGRISIDSLIVRVQDGKQEIQSVAQFLEEVFRVVNVEQTKLDSFIHELEQTIFKDTIAQYERCNKLKYTQKSYDELENHLIDGHPYHPSYKARIGFQYRDNFRYGYEFMRPIKLIWIAAHKKNATVGYENEVIYDKILKSEVGERKLEAYKERIHSMGCDPKQYLFIPVHPWQWENFIISNYAEDIQDKGIIYLGESADDYCAQQSMRTLRNVTNPKRPYVKVSLNILNTSTLRTLKPYSVASAPAISNWLSNVVSQDSYLRDESRVILLKEFSSVMYDTNKKATYGSLGCIWRESVHHYLGEQEDAVPFNGLYAKEKDGTPIIDAWLNKYGIENWLRLLIQKAIIPVIHLVVEHGIALESHGQNMILVHKEGLPVRIALKDFHEGLEFYRPFLKEMNKCPDFTKMHKTYANGKMNDFFEMDRIECLQEMVLDALFLFNVGELAFVLADKYEWKEESFWMIVVEEIENHFRKYPHLKDRFESIQLYTPTFYAEQLTKRRLYIDVESLVHEVPNPLYRARQLNIQKSVATGGNYANC | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Catalyzes the ATP-dependent condensation of spermidine with N(8)-citryl-spermidine or N(1)-(3,4-dihydroxbenzoyl)-N(8)-citryl-spermidine, two intermediates in petrobactin biosynthesis pathway .
Catalytic Activity: ATP + N(8)-citryl-spermidine + spermidine = AMP + diphosphate + H(+) + N(8),N'(8)-citryl-bis(spermidine)
Sequence Mass (Da): 72014
Sequence Length: 612
Pathway: Siderophore biosynthesis; petrobactin biosynthesis.
EC: 6.3.2.-
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Q81RQ7 | MLIVNREEYSKSDFDLRLQAYEEMEQFQEAAGNRFALCLKDPFDIITLVFFLKEKKSSVLLIHEDTPKETAIEMAKRANCIGILYGENSDFTKLEAVNYLAEEPSLLQYSSGTTGEPKLIRRAWTEVDTEIKVYNEALNCDIDEVPIVMAPVSHSYGLICGTLSAITRGSKPIIITNKNPKFALNIVRNTEKHIVYAVPLMLHIMGSFPQGTFQFHKIMTSGAPLPEALFYKLKETTTYMMQQYGCSEAGCISICHDMKSHLDLGNPLPHASISIGSDENAPEEIIVKMNDKEIFTKDLGYKSERGLHFMGRMDDVINVSGLKVFPIEVEETMLRLEGVQEAIVYRGKHPVMGEIVKAKVISHIDPVQIREWCMQHLPSYKVPHEIESVTEIPKNKTGKVSRKLLEMGEVTT | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Catalyzes the adenylation of 3,4-dihydroxybenzoate (3,4-DHBA) to the corresponding AMP ester, followed by the transfer of the activated unit to the phosphopantetheine thiol of the aryl-carrier protein AsbD .
Catalytic Activity: 3,4-dihydroxybenzoate + ATP + holo-[aryl-carrier protein] = 3,4-dihydroxybenzoyl-[aryl-carrier protein] + AMP + diphosphate
Sequence Mass (Da): 46510
Sequence Length: 412
Pathway: Siderophore biosynthesis; petrobactin biosynthesis.
EC: 6.2.1.62
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A0A0J1I1I3 | MRREALKNAVLKIMTEKMELKNVTHLEETMRLNQDLYIDSVMMLQLIVYIEMDVKLCVPEDEVDPKAFLTVGSLLDFMEELQPLQDVNVNN | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Aryl-carrier protein that activates 3,4-dihydroxybenzoate (3,4-DHBA) prior to its incorporation into petrobactin .
PTM: Activated by the transfer of a 4'-phosphopantetheine group from CoA to Ser-40.
Sequence Mass (Da): 10628
Sequence Length: 91
Pathway: Siderophore biosynthesis; petrobactin biosynthesis.
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Q81RQ5 | MTSIKVHCLVSCFCEIIKRRSDIDFRPFYFGLWDGDFDITEGGIISYHSENINHDHYLLWYEKLYGMKVNEWYDHAKDKDSNVETFLQLVENKPENRYVIVMVDMSLLPERENKFHQKPFPHYLMISETEKEEEWFMLDPDFRWEGNMEREKVLYSVQDNPFGGGYFIDVEEIQEPTAEMVASYFIETFKRNDNELTMELKNLIIKMANEEEGYLLSGLVAAVKQIPVLAIRKYSYEHAFAYFRETLQYSEQEFDYWCDRVEDIVQGFTNVQYRAIKMAMTNNKGMLLSIVEKLDEMNAIELQIKTELERQFLSWKEMKSNESVLVF | Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Transfers the activated 3,4-dihydroxybenzoate (3,4-DHBA) moiety from 3,4-DHBA-loaded AsbD to different receipient molecules, including N-citryl-spermidine, N8,N'8-citryl-bis(spermidine) and N1-(3,4-dihydroxybenzoyl)-N8,N'8-citryl-bis(spermidine) . Also catalyzes the transfer of the activated 3,4-DHBA moiety from 3,4-DHBA-loaded AsbD to spermidine to generate DHB-spermidine (DHB-SP) .
Catalytic Activity: 3,4-dihydroxybenzoyl-[aryl-carrier protein] + N(8)-citryl-spermidine = H(+) + holo-[aryl-carrier protein] + N(1)-(3,4-dihydroxybenzoyl)-N(8)-citryl-spermidine
Sequence Mass (Da): 39032
Sequence Length: 327
Pathway: Siderophore biosynthesis; petrobactin biosynthesis.
EC: 2.3.2.-
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Q81RQ4 | MKYSLCTISFRHQLISFTDIVQFAYENGFEGIELWGTHAQNLYMQEYETTERELNCLKDKTLEITMISDYLDISLSADFEKTIEKCEQLAILANWFKTNKIRTFAGQKGSADFSQQERQEYVNRIRMICELFAQHNMYVLLETHPNTLTDTLPSTLELLGEVDHPNLKINLDFLHIWESGADPVDSFQQLRPWIQHYHFKNISSADYLHVFEPNNVYAAAGNRTGMVPLFEGIVNYDEIIQEVRDTDHFASLEWFGHNAKDILKAEMKVLTNRNLEVVTS | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence . Catalyzes the conversion of 3-dehydroshikimate to 3,4-dihydroxybenzoate (3,4-DHBA) .
Catalytic Activity: 3-dehydroshikimate = 3,4-dihydroxybenzoate + H2O
Sequence Mass (Da): 32589
Sequence Length: 280
Pathway: Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 2/2.
EC: 4.2.1.118
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Q9M6A3 | MKNLDHIAASVDWEKESLPEYQDLIFLLFFALFFPVLRFILDRFVFEALAKRMIFGKKTVVNINGREERKKINKFKESAWKFVYFLSTELLALSVTCNEPWFTDSRYFWAGPGDVVWPNLKMKLKLKLLYMYAGGFYFYSIFATLYWETRRYDFAAQIIHHVTTVSLIVLSYVYGFARIGSVVLALHDGSDVFMEIAKMSKYSGFDLIADIFFSLFALVFTSLRIICYPFWIIRSTCYELLYVLDIQKERTTGIILYFVFNALLICLLVLHLFWFKIILRMVKNQILSRGHITDDVREDSESDDDHKD | Function: Mediates resistance to sphinganine-analog mycotoxins (SAMs) by restoring the sphingolipid biosynthesis. Could salvage the transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted cells after SAM exposure.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36332
Sequence Length: 308
Subcellular Location: Endoplasmic reticulum membrane
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A0A3G5BIB1 | MRFLNIFLFFAVMIAFVSASPVLEEEEIDIEPRITCDLIGNERLCVVHCLAKGFRGGWCDSRKVCNCRR | Function: The recombinant peptide moderately increases Kv11.1/KCNH2/ERG1 currents and shifts the voltage-dependence of the channel activation to hyperpolarised potentials . In vivo, induces neurotoxic effects when injected into insects (tested on L.cuprina and A.domesticus) .
Sequence Mass (Da): 7939
Sequence Length: 69
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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Q94BQ3 | MDNLSFHDGNIFNLLHTRSQDPSHEVDQRMQFHSSLVRRLSQEQELEGHQGCVNALAWNSNGSLLISGSDDLRINIWNYSSRKLLHSIDTGHTANIFCTKFVPETSDELVVSGAGDAEVRLFNTSRLSGRAEDDNAIIPSALYQCHTRRVKKLAVEPGNPNVVWSASEDGTLRQHDFRESTSCPPAGTAHQECRSVLLDLRSGAKRALADPPKQTLSLKSCDISATRPHLLLVGGSDAFARLYDRRMLPPLASSRKRMPPPPCVNYFCPMHLSERGRTNLHLTHVTFSPNGEEVLLSYSGEHVYLMNVNNGICSTGIMQYTPGDVDNLFSFSNNLHDVESPPQVSTTPQNGFHRSSNAATVKKCTELVEIAKWSLEEGTDVFYAIEAANEVLDAHSNDIESALRHECLCTRAALLLKRKWKNDAHMAVRDCHNARRIDASSFKAHYYMSEALQQLGKCKEALDFATAAQHMNPSDADIVAKVESIKRDLQAAGAEKNEETGAGTTRVLSLSDILYRSEANSDSSHDMSRSEREDSDYDEELELDIQTSLSDDEGRDTDSNSMRGSLNLRIHRVGDDKPMENTVDNASSGTASSSQNDRTSYQPEGAIDMKRRYVGHCNVGTDIKQASFLGQRGEYIASGSDDGRWFIWEKQTGRLMKVLVGDESVLNCIQCHPFDSVVATSGIDNTIKIWSPTASVPSIVAGGSAGPATANVVEVMESNQQKLSRNRENPLSVELMQRFRMQEFAEGNFHPFECTQS | Function: May function as a substrate adapter for CUL4-DDB1 E3 ubiquitin-protein ligase complex (Probable). Negative regulator of fatty acid biosynthetic process and accumulation . Acts as an abscisic acid (ABA) negative regulator . Involved in responses to salt (NaCl) and osmotic (e.g. in response to mannitol and PEG) stresses .
PTM: Farnesylated at Cys-754 by FTB/ERA1; this modification triggers an exclusion from the nucleus.
Sequence Mass (Da): 83830
Sequence Length: 757
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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P46993 | MTTLASSIEHKTKHLAAPFENDENPWMKKYCCQCKSCKMSVPVQPWLPRFFVFGILCPVFWLVNLLAWWFLQYWQPHELEFHDLQEDEYPGFYEYEAITKRTVIPIKEEVLQEIRVMQNFSDSNSEEYYESKDGMPSSFLNVNTEQVEDENDTLKKYRYAFLKKVAHDVLESHDLLRKTFRDWNLRSLLGLLIDSILIIFVVLLCKKSR | Function: Required for receptor inhibition of inappropriately expressed a-factor receptor (STE3) in MAT a cells. Inhibits signaling by relocalizing the G protein beta-gamma (STE4-STE18) subunit to intracellular membranes. May also be a mechanism for the down-regulation of the mating pheromone response after the zygotic fusion event, promoting the transition of the new diploid cell to vegetative growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24946
Sequence Length: 209
Subcellular Location: Endomembrane system
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Q5BKW9 | MLPVVVVHGGAGHIPKERTEESTIGVKEAARTGYAILQRGGSAVDAVVEAVALMETNPRFNAGRGSVLNIKGEVEMDALVMDGRTLDSGAVSAVRRIANPVQLARLVMEKTKHLCLTAEGASKFARSMGVPEVPEESLITDYAKMRWKKNLEPDANPVECQMGKMGTVGAVAVDMDGNIACATSTGGMINKMEGRVGDTPCVGCGGYADNKIGAVSPTGHGEAIMKVTLSRLVLFHMEQGKTPEEASDLALAYMKERVDGLGGVVVVDHNGTWAARFSSLQMSWAAAQQGKLHFGLFHGDHFTEPVEEHT | Function: Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.
Catalytic Activity: H2O + L-asparagine = L-aspartate + NH4(+)
Sequence Mass (Da): 32929
Sequence Length: 310
Subcellular Location: Cytoplasm
EC: 3.4.19.5
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Q9VXT7 | MPRPVLLIHGGAGDISDSRIAGKFAGIKQALRSAWGLLSPDNGSGGGSALDAVEAAVRSMELDENFNAGYGSCLNTSGQVELEASLMEGRDLRAGCITLLRDVMHPITVARRLMEKQRHTFLGGAAAQELALATGSERLQPGALVTEGARLTLKEFEDQVAQGKDPFFARTELTDDKPVPKTDPSGETVGAVAMDASGQIVVGTSTGGITGKWPGRIGDTPILGSGTYADNCRGGVSTTGHGETLMRYNLAQRILSAMEYQGLSAQAAADKECREMTKRLGGTGGAIVVGHSGDLGISFTSRRMAWGYVQDGTIFYGIEGQVVHQEPFTLST | Function: Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.
Catalytic Activity: H2O + L-asparagine = L-aspartate + NH4(+)
Sequence Mass (Da): 34861
Sequence Length: 332
EC: 3.4.19.5
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Q7L266 | MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP | Function: Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.
Catalytic Activity: H2O + L-asparagine = L-aspartate + NH4(+)
Sequence Mass (Da): 32055
Sequence Length: 308
Subcellular Location: Cytoplasm
EC: 3.4.19.5
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P08243 | MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPFLPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPKWINATDPSARTLTHYKSAVKA | Catalytic Activity: ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate
Sequence Mass (Da): 64370
Sequence Length: 561
Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.
EC: 6.3.5.4
|
Q5UQE1 | MCGIICFIQYGGQKIDLVSCLNCLDKLNNRGPDAQSYQVIELGDITIFLGFTRLAIMDTSEAGLQPFKDNNSNYSICNGEIYNYKNLAEKFNIEMQSQCDCEILLPLFNLRGFEGLLSDLDAEFATVIVDKYNSKLYAARDKYGVRPLYYGYNCEKGLIGFASELKALHSVMEYVEQVKPNQYVTIDLSFRPSIPFDLQNFVKLFQFTNYHEYYQSHKSLIDYHEPNIEQLQTSINHLLTEAVRKRLYADRQIGFLLSGGLDSSLIVAIATRLLGPTNIVCFSVGFEGSPDVAAAREVVKFLGIKNHHIVPFSVDIGLNAINDVIKTIETYDITTIRASTPQFIMAKYIQENTDIRVLLSGEGSDEIHGSYKYMRSAPNSQEFHKETIRLLEELYLFDNKRTDRTMAGNGLEVRVPFLDFNYVDFIMNIDPNLLMYKSDYIEKKIIRDAFKGYLPENILYRPKEAFSDAVSSKEINWYRSIQKITEEIYTDEKLQNSNYKFNKPEIKEALYYRDIFNSHYGGRDHIIPHYWLPRFQQNNVLDPSATILPI | Catalytic Activity: ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate
Sequence Mass (Da): 63335
Sequence Length: 550
Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.
EC: 6.3.5.4
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P78753 | MCGILAVHHVAEDIEAFKPKALHLSKQLRHRGPDWSGKAIRNQTILCHERLAIVGVESGAQPLVSDDGKLVLTVNGEIYNHLKLRENLKGNYKFKTYSDCEVILYLYREHGPACANMLDGMFSWVLYDQDKDKVVAARDPIGITTLYQGFSSDSPDTAYFASELKALHPVCDKIIAFPPGHYYDSETKQTVRYFKPSWWDENKIPSNPVDYKLLRETLEASVRKRLMAEVPYGVLLSGGLDSSLIASIAARETEKLANSTSQSEEARTITAWPKLHSFAIGLPGSPDLLAARKVADFLHTFHHEHTFTIDEGLDALRDVIYHLETYDVTTIRASTPMYLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFGNAPSREAFHSECVRRVKNLHLSDCLRANKSTMAWGLEARVPFLDKDFLEVALNIDPEEKMYINGRKEKYILRKAFDTTHDSSLQPYLPQDILWRQKEQFSDGVGYSWIDALKDTAELCISDDEFALPRREWGDDIPTTKEAFWYRKLFDEIFPRQCADTVMRWVPKAEWGCPEDPSGRYQAGHVAALK | Catalytic Activity: ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate
Sequence Mass (Da): 63241
Sequence Length: 557
Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.5.4
|
Q00624 | MRGVKLLAACLYLAAAATVVVHAEDPYFHHVWNVTYGTASPLGVPQQVILINGQFPGPNINSTSNNNVIINVFNNLDEPFLLTWNGIQHRKNCWQDGTPGTMCPIMPGTNYTYHFQPKDQIGSYFYYPTTGMHRAAGGYGGLRVNSRLLIPVPYADPEDDYTVLIGDWYTKSHTQLKKFLDGGRTIGRPDGIVINGKSGKGDGSDAPLFTLKPGKTYRVRICNVGVKTSINFRIQNHKMKLVEMEGSHVLQNDYDSLDVHVGQCFGTIVTANQEPKDYYMVASSRFLKTVITTTGLLRYEGGKGPASSQLPAGPVGWAWSLNQFRSFRWNLTASAARPNPQGSYHYGKINITRTIKLVNTQGKVDGKLRFALNGVSHTEPETPLKLAEYFGISDKVFKYDTITDDPTPEQIKNIKIEPNVLNITHRTFVEVVFENHEKSVQSWHLDGYSFFSVAVEPGTWTPEKRKNYNLLDAVSRHTVQVYPKCWAAILLTFDNCGMWNVRSENTERRYLGQQLYASVLSPEKSLRDEYNMPETSLQCGLVKNTPKPVNPYAGA | Function: Probable oxidase that may be involved in pollen tube growth.
Sequence Mass (Da): 62131
Sequence Length: 555
Subcellular Location: Secreted
EC: 1.10.3.-
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P29162 | MGSGKVTFVALLLCLSVGVIAEDPYLYFNWNVTYGTIAPLGVPQQGILINGQFPGPRINCTSNNNIVVNVFNNLDEPFLFTWNGVQHRKNSWQDGTPGTMCPIMPGQNFTYRFQVKDQIGSYSYFPTTALHRAAGGYGALNVHSRALIPVPFDNPADEYNVFVGDWYNKGHKTLKKILDGGRTIGRPDGIIINGKSAKVGEAKEPLFTMEAGKTYRYRFCNLGMRSSVNIRFQGHPMKLVELEGSHTVQNIYDSLDLHVGQCLSVLVTADQEPKDYYLVVSSRFLKQALSSVAIIRYANGKGPASPELPTPPPENTEGIAWSMNQFRSFRWNLTASAARPNPQGSYHYGQINITRTIKIFNSMSQVGGKLRYGLNGISHTNGETPLKLVEYFGATNKAFKYDLMADEAPADPSKLTIATNVKNATYRNFVEIIFENHEKTIRTYHLDGYSFFAVAVEPGRWSPEKRKNYNLVDGLSRNNIQVYPNSWAAIMLTFDNAGMWNLRSEMWEKTYLGEQLYFSVLSPSRSLRDEYNIPDNHPLCGIVKGLSMPAPYKA | Function: Probable oxidoreductase that may be involved in pollen tube growth.
Sequence Mass (Da): 62034
Sequence Length: 554
Subcellular Location: Secreted
EC: 1.10.3.-
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Q8LPL3 | MAVIVWWLLTVVVVAFHSASAAVVESTWEVEYKYWWPDCKEGIVMAINGQFPGPTIDAVAGDTVIIHVVNKLSTEGVVIHWHGIRQKGTPWADGAAGVTQCPINPGETFTYKFIVDKAGTHFYHGHYGMQRSSGLYGMLIVRSPKERLIYDGEFNLLLSDWWHQSIHAQELALSSRPMRWIGEPQSLLINGRGQFNCSQAAYFNKGGEKDVCTFKENDQCAPQTLRVEPNRVYRLRIASTTALASLNLAVQGHQLVVVEADGNYVAPFTVNDIDVYSGETYSVLLKTNALPSKKYWISVGVRGREPKTPQALTVINYVDATESRPSHPPPVTPIWNDTDRSKSFSKKIFAAKGYPKPPEKSHDQLILLNTQNLYEDYTKWSINNVSLSVPVTPYLGSIRYGLKSAYDLKSPAKKLIMDNYDIMKPPPNPNTTKGSGIYNFAFGIVVDVILQNANVLKGVISEIHPWHIHGHDFWVLGYGEGKFKPGIDEKTFNLKNPPLRNTVVLYPFGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFVEGVDRIGKMEIPDEALGCGLTRKWLMNRGRP | Cofactor: Binds 4 Cu cations per monomer.
Function: Ascorbate oxidase involved in a redox system involving ascorbic acid (AsA) . The oxidation of AsA represses responses to high salinity and oxidative stress conditions such as vegetative growth and seed production reductions . Negative regulator of defense responses toward incompatible Turnip mosaic virus (TuMV strain UK1) by preventing jasmonic acid (JA)- dependent accumulation of ascorbic acid (AsA, AS) and dehydroascobic acid (DHA) .
Catalytic Activity: 4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical
Sequence Mass (Da): 64266
Sequence Length: 573
Pathway: Cofactor degradation; L-ascorbate degradation.
Subcellular Location: Secreted
EC: 1.10.3.3
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M4DUF2 | MGMWWIVAVAILAHTASAAVREYAWEVEYKFGWPDCKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAPSSQLPTSPPPETPRWNDFDRSKNFSKKIFAAMGSPSPPETFDERLILLNTQNLIEGFTKWAINNVSLAVPGTPYLGSVKYNLRTGFNRSSPPKDYPVDYDIMTPPRNRNAKQGNVSCVFPFNVTVDVILQNANGLNANASEIHPWHLHGHDFWVLGYGEGKFKPGVDEKTYNLKNPPLRNTVALYPYGWTALRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLNRIGKVPDEALGCGLTKQFLMNRNNP | Cofactor: Binds 4 Cu cations per monomer.
Function: Ascorbate oxidase involved in a redox system involving ascorbic acid (AsA) . The oxidation of AsA represses responses to high salinity and oxidative stress conditions such as vegetative growth and seed production reductions (By similarity). Negative regulator of defense responses toward incompatible Turnip mosaic virus (TuMV strain UK1) by preventing jasmonic acid (JA)- dependent accumulation of ascorbic acid (AsA, AS) and dehydroascobic acid (DHA) .
Catalytic Activity: 4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical
Sequence Mass (Da): 63250
Sequence Length: 570
Pathway: Cofactor degradation; L-ascorbate degradation.
Subcellular Location: Secreted
EC: 1.10.3.3
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A0A2S1XB67 | MIKKVPIVLSIFCFLLLLSSSHGSIPEAFLNCISNKFSLDVSILNILHVPSNSSYDSVLKSTIQNPRFLKSPKPLAIITPVLHSHVQSAVICTKQAGLQIRIRSGGADYEGLSYRSEVPFILLDLQNLRSISVDIEDNSAWVESGATIGEFYHEIAQNSPVHAFPAGVSSSVGIGGHLSSGGFGTLLRKYGLAADNIIDAKIVDARGRILDRESMGEDLFWAIRGGGGASFGVIVSWKVKLVKVPPMVTVFILSKTYEEGGLDLLHKWQYIEHKLPEDLFLAVSIMDDSSSGNKTLMAGFMSLFLGKTEDLLKVMAENFPQLGLKKEDCLEMNWIDAAMYFSGHPIGESRSVLKNRESHLPKTCVSIKSDFIQEPQSMDALEKLWKFCREEENSPIILMLPLGGMMSKISESEIPFPYRKDVIYSMIYEIVWNCEDDESSEEYIDGLGRLEELMTPYVKQPRGSWFSTRNLYTGKNKGPGTTYSKAKEWGFRYFNNNFKKLALIKGQVDPENFFYYEQSIPPLHLQVEL | Function: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts O-acetylstemmadenine (OAS) to reactive acetylated intermediates, likely dihydroprecondylocarpine acetate.
Catalytic Activity: O-acetyl-15alpha-stemmadenine + O2 = H2O2 + precondylocarpine acetate
Sequence Mass (Da): 59214
Sequence Length: 529
Pathway: Alkaloid biosynthesis.
Subcellular Location: Endoplasmic reticulum
EC: 1.21.3.-
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P37064 | SQIRHYKWEVEYMFWAPNCNENIVMGINGQFPGPTIRANAGDSVVVELTNKLHTEGVVIHWHGILQRGTPWADGTASISQCAINPGETFFYNFTVDNPGTFFYHGHLGMQRSAGLYGSLIVDPPQGKKEPFHYDGEINLLLSDWWHQSIHKQEVGLSSKPIRWIGEPQTILLNGRGQFDCSIAAKYDSNLEPCKLKGSESCAPYIFHVSPKKTYRIRIASTTALAALNFAIGNHQLLVVEADGNYVQPFYTSDIDIYSGESYSVLITTDQNPSENYWVSVGTRARHPNTPPGLTLLNYLPNSVSKLPTSPPPQTPAWDDFDRSKNFTYRITAAMGSPKPPVKFNRRIFLLNTQNVINGYVKWAINDVSLALPPTPYLGAMKYNLLHAFDQNPPPEVFPEDYDIDTPPTNEKTRIGNGVYQFKIGEVVDVILQNANMMKENLSETHPWHLHGHDFWVLGYGDGKFSAEEESSLNLKNPPLRNTVVIFPYGWTAIRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGRIPTKALACGGTAKSLINNPKNP | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: May be involved in a redox system involving ascorbic acid.
Catalytic Activity: 4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical
Sequence Mass (Da): 61704
Sequence Length: 552
Subcellular Location: Secreted
EC: 1.10.3.3
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Q40588 | MASLGFLFFFLLPLILLELSSSRSVMAAKTRHFKWDVEYIHWSPDGEESVVMGINGQFPGPTIRAKAGDTVAVHLTNKLHTEGVVIHWHGIRQIGTPWADGTAAISQCAINPGETFLYRFKVDKAGTYFYHGHYGMQRSAGLYGSLIVEVGEGEKEPFHYDGEFNLLLSDWWHKGSHEQEVDLSSNPLRWIGEPQTLLLNGRGQYNCSLAARFSKPPLPQCKLRGGEQYAPQILRVRPNKIYRLRVASTTALGSLSLAIGGHKMVVVEADGNYVQPFSVQDMDIYSGESYSVLFKTDQDPTKNYWISINVRGREPKTPQGLTLLNYLPNSASKFPTLPPPIAPLWNDYNHSKSFSNKIFALMGSPKPPPQNHRRIILLNTQNKIDGYTKWAINNVSLVLPTQLYLGSIRYGINAFDTKPPPDNFPKDYDVLKQAPNSNSTYGNGVYMLKFNTTIDIILQNANALAKDVSEIHPWHLHGHDFWVLGYGEGKFSEKDVKKFNLKNPPLRNTAVIFPFGWTALRFVTDNPGVWAFHCHIEPHLHMGMGVIFAEGVHLVKKIPKEALACGLTGKMLMSNKHN | Cofactor: Binds 4 Cu cations per monomer.
Function: May be involved in a redox system involving ascorbic acid.
Catalytic Activity: 4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical
Sequence Mass (Da): 64865
Sequence Length: 578
Subcellular Location: Secreted
EC: 1.10.3.3
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Q03168 | MLIKSIIALVCLAVLAQADFVRVQLHKTESARQHFRNVDTEIKQLRLKYNAVSGPVPEPLSNYLDAQYYGAITIGTPPQSFKVVFDTGSSNLWVPSKECSFTNIACLMHNKYNAKKSSTFEKNGTAFHIQYGSGSLSGYLSTDTVGLGGVSVTKQTFAEAINEPGLVFVAAKFDGILGLGYSSISVDGVVPVFYNMFNQGLIDAPVFSFYLNRDPSAAEGGEIIFGGSDSNKYTGDFTYLSVDRKAYWQFKMDSVKVGDTEFCNNGCEAIADTGTSLIAGPVSEVTAINKAIGGTPIMNGEYMVDCSLIPKLPKISFVLGGKSFDLEGADYVLRVAQMGKTICLSGFMGIDIPPPNGPLWILGDVFIGKYYTEFDMGNDRVGFATAV | Function: May degrade organelles involved in the biosynthesis and secretion of vitellogenin.
Sequence Mass (Da): 41790
Sequence Length: 387
Subcellular Location: Lysosome
EC: 3.4.23.-
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O07002 | MSKQGNFQKSMSLFDLILIGMGAIFGSAWLFAVSNVASKAGPSGAFSWILGGAIILLIGLVYAELGAALPRTGGIIRYPVYSHGHLVGYLISFVTIVAYTSLISIEVTAVRQYVAYWFPGLTIKGSDSPTISGWILQFALLCLFFLLNYWSVKTFAKANFIISIFKYIVPITIIIVLIFHFQPENLSVQGFAPFGFTGIQAAISTGGVMFAYLGLHPIVSVAGEVQNPKRNIPIALIICIIVSTIIYTVLQVTFIGAIPTETLKHGWPAIGREFSLPFKDIAVMLGLGWLATLVILDAILSPGGNGNIFMNTTSRLVYAWARNGTLFGIFSKVNKDTGTPRASLWLSFALSIFWTLPFPSWNALVNVCSVALILSYAIAPISSAALRVNAKDLNRPFYLKGMSIIGPLSFIFTAFIVYWSGWKTVSWLLGSQLVMFLIYLCFSKYTPKEDVSLAQQLKSAWWLIGFYIMMLIFSYIGSFGHGLGIISNPVDLILVAIGSLAIYYWAKYTGLPKAAIDYDK | Function: Uptake of L-aspartate with the concomitant import of a proton. Can also transport aspartate hydroxamate and L-glutamate with lower affinity and efficiency.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56989
Sequence Length: 520
Subcellular Location: Cell membrane
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P83712 | NVVVLATGGTIAGAGTNAFASQXGPLGMVVEGK | Catalytic Activity: H2O + L-glutamine = L-glutamate + NH4(+)
Sequence Mass (Da): 3099
Sequence Length: 33
Subcellular Location: Periplasm
EC: 3.5.1.38
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P10182 | KEVENQQKLANVVILATGGTIAGAGASAANSATYQAAKVGVDKLIAGVPELADLANVRGEQVMQIASESITNDDLLKLGKRVAELADSNDVDGIVITHGTDTLEETAYFLDLTLNTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASNKDSRGKGVLVTMNDEIQSGRDVSKSINIKTEAFKSAWGPLGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYSYGNVTDTAYKALAQNGAKALIHAGTGNGSVSSRLTPALQTLRKTGTQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPEKARILVELAMVKTQDSKELQRIFWEY | Catalytic Activity: H2O + L-glutamine = L-glutamate + NH4(+)
Sequence Mass (Da): 36200
Sequence Length: 337
Subcellular Location: Periplasm
EC: 3.5.1.38
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O60020 | MISDTVIAILAVALVGSTVQAAPVDATATSTSGIIAVPISKSAAQLAREADPVVSLDWLKKTKAQAQYKHKQANARLHSKRATGASVLTDQGSESLWTGPITIGGQSFTVDWDTGSSDLWVPSSACSSAACNAHHKYTLTSTGKKQSGTFSISYGDGSSASGPVYKDNVVASGLQATSQVFGAVTSESSSFSSDPSDGISGLGWPALAQLSGTSYFWSLINQGTVTSPVFSFRLATTNSELYLGGINSAHYTGAITYTPVTQKAYWTIALGGVSVNGAAINPSVSSAIIDTGTTLVYGPTAGVAALYAKIPGSASMADTYGSDYQGYYTFPCSAVPTVALTFGGSSFSVPTSAFNLGTVSSGSKQCVGGIVGQGDGSWLVGDVFLQGVYSIYDVGNARVGFAKTV | Function: Possesses acidic protease activity. Hydrolyzes casein and azoalbumin in vitro.
Sequence Mass (Da): 41370
Sequence Length: 405
Subcellular Location: Secreted
EC: 3.4.23.-
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O04057 | MASYHSKAAFLCLFLLVSFNIVSSASNDGLLRVGLKKIKLDPENRLAARVESKDAEILKAAFRKYNPKGNLGESSDTDIVALKNYLDAQYYGEIAIGTPPQKFTVIFDTGSSNLWVLCECLFSVACHFHARYKSSRSSSYKKNGTSASIRYGTGAVSGFFSYDNVKVGDLVVKEQVFIEATREPSLTFLVAKFDGLLGLGFQEIAVGNAVPVWYNMVEQGLVKEPVFSFWLNRNVEEEEGGEIVFGGVDPKHYRGKHTYVPVTQKGYWQFDMGDVLIDGEPTGFCDGGCSAIADSGTSLLAGPTPVITMINHAIGAKGVVSQQCKAVVAQYGQTIMDLLLSEADPKKICSQINLCTFDGTRGVSMGIESVVDENAGKSSDSLHDGMCSVCEMTVVWMQNQLRQNQTKERIINYINELCDRMPSPMGQSAVDCGQLSSMPTVSFTIGGKIFDLAPEEYILKVGEGPVAQCISGFTAFDIPPPRGPLWILGDVFMGRYHTVFDFGKLRVGSAEAA | Function: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles.
Sequence Mass (Da): 55856
Sequence Length: 513
Subcellular Location: Vacuole
EC: 3.4.23.-
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P42210 | MGTRGLALALLAAVLLLQTVLPAASEAEGLVRIALKKRPIDRNSRVATGLSGGEEQPLLSGANPLRSEEEGDIVALKNYMNAQYFGEIGVGTPPQKFTVIFDTGSSNLWVPSAKCYFSIACYLHSRYKAGASSTYKKNGKPAAIQYGTGSIAGYFSEDSVTVGDLVVKDQEFIEATKEPGITFLVAKFDGILGLGFKEISVGKAVPVWYKMIEQGLVSDPVFSFWLNRHVDEGEGGEIIFGGMDPKHYVGEHTYVPVTQKGYWQFDMGDVLVGGKSTGFCAGGCAAIADSGTSLLAGPTAIITEINEKIGAAGVVSQECKTIVSQYGQQILDLLLAETQPKKICSQVGLCTFDGTRGVSAGIRSVVDDEPVKSNGLRADPMCSACEMAVVWMQNQLAQNKTQDLILDYVNQLCNRLPSPMGESAVDCGSLGSMPDIEFTIGGKKFALKPEEYILKVGEGAAAQCISGFTAMDIPPPRGPLWILGDVFMGPYHTVFDYGKLRIGFAKAA | Function: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles.
Catalytic Activity: Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.
Sequence Mass (Da): 54226
Sequence Length: 508
Subcellular Location: Vacuole
EC: 3.4.23.40
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C0HJJ8 | GTQTNAPWGLARLIS | Function: Protease capable of hydrolyzing gelatin and cell surface heparan sulfate proteoglycans (HSPGs) in vitro.
Sequence Mass (Da): 1585
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.21.-
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E3PJ88 | MSIKQMPGRVLISLLLSVTGLLSGCASHNENASLLAKKQAQNISQNLPIKSAGYTLVLAQSSGTTVKMTIISEAGTQTTQTPDAFLTSYQRQMCADPTVKLMLTEGINYSITINDTRTGNQYQRKLDRTTCGIVKA | Function: Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). Required for correct assembly of the type II secretion system-beta (T2SS-beta), for localization of GspD-beta to the cell outer membrane and for export of a labile enterotoxin by T2SS-beta . Each AspS2 binds to 2 GspD2 subunits and may clamp the monomers together, stabilizing structure and accelerating its assembly .
Location Topology: Lipid-anchor
Sequence Mass (Da): 14670
Sequence Length: 136
Subcellular Location: Cell outer membrane
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Q8L3K8 | MNAIGNFLVGTPVFTIFICLALGYLLGKLKIGSFTLGATVGVLIVALLIGQLGVFPRDTLLGDIFFDFFMFAIGYRVGPSFISSMKKFGAKIVYATLIFLVSAFIVAYACFKMFHIGPGIAAGIIAGGLTQSAVIGSSLETISKLPISDHLKTLYSNQIPIVYTLTYVFGTIGVLIFLRDIMPKLMHIDLKKQAVKTAKELDMIPVPVIVASTHFYTINDGSSLIGQTLGTVNTKFAKGLVAAGLNDSADMASVINAGDVLAISGGIDEIGRAVQEFNLLEVTGKTKAYVSKQVVLKKNFSADVLKNAQDKGVLVATLAGDVMDPAQFSTLKPAESVTLVGQKDAVSEVQSQLGRLRAAENIINYSWFALGIALSAALGIVGTKVSGVPIALGGGTASLIVGLVQSIYRDKHAHMDTIPDSLLEFFQSIGLNLFIATVGLSAAKTFISAIQSMGISVLLIGAVISILPHIITFVICYYLMKMEPISIIGAQTGADTLSAALNDVSERVGSDASPFFAAAVAPAYAIGNIFLTLMGPIFIVLLS | Function: Catalyzes the electrogenic exchange of aspartate with alanine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57213
Sequence Length: 543
Subcellular Location: Cell membrane
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Q1QVN0 | MSDVKKVVLAYSGGLDTSVIVKWLQETYDCEVVTFTADIGQGEEVEPARAKAQALGVKEIYIEDLREEFVRDYVYPMFRANTIYEGEYLLGTSIARPLIAKRLVEIANETGADAISHGATGKGNDQVRFELGAYALKPGVKVIAPWREWDLNSREKLMNYCEEHDIPVDFSTSKKKSPYSMDANLLHISYEGGILEDPWAEAEEDMWRWSVSPEAAPEQPTYVELTFDKGDIVAIDGEPLKPHEVLSRLNRMGGDNGIGRLDIVENRYVGMKSRGCYETPGGTIMLRAHRAIESLTLDREAAHLKDELMPKYAEVIYNGYWWSPERKMLQAAIDATQDNVNGVVRMKLYKGSATVVGRKSEQSLFDASIATFEDDAGAYDQKDAEGFIKLNALRLRIAAGKGRQAD | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 45409
Sequence Length: 406
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 6.3.4.5
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C1FU68 | MKEKVVLAYSGGLDTSIIIPWLKENYDLDVIAVCVNVGQGDDMDYVKTKAIKSGASKIYVEDVKEEFVVDYLYKAIKSEALYEQDYMLGTSFARPLMAKKLVEIAHKEQAKYICHGCTGKGNDQVRFEVGVKAQDPIIKIIAPWRIWDIKSREDAIDYAKKVGVEVPVTKKKIYSVDKNLWHVSHEGGDLEDLKNEHKEDMYFMVTPPEKAKNEPTYLEIYFEKGAPVKINGEVLNPVDIIDKLNTIGGENGIGIADIIENRLVGMKSRGIYETPAGTLLYAAHKKLESVTLDKYTYQYKKIVSAQYGELVYNGLWFTSLREAIDAFVDKTQENVTGTVQLKLYKGNIKPCSVDTEYALYDEGISSFGESELYSHKDAEGFINLFGLPSKIKALKNF | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 44742
Sequence Length: 397
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 6.3.4.5
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Q186Z6 | MKEKVVLAYSGGLDTSIIIPWLKENYEDIDVIAVCGNVGQEDKMEDVYEKALQSGASKAYVDDISEEFVTETIFKAVKAEAKYEGKYLLGTSLARPIIAKKLVEVAHKEGAKYICHGCTGKGNDQVRFEATIAALDPTIKVIAPWRIWDIKSREDAIDYAEKHNIKVTATKAKIYSVDANLWHVSTEGGDIEHLENEHKKDVYKQCVDPEDACDVAEYVEVYFEKGVPKKVNGEELSPVALIHKLNELGCKHGIGVIDIVENRLVGMKSRGIYETPGGTILYEAHNILESATLDKDTLHFKQMVSYKYGELIYNGLWYCKLRESIDAFMEQTQDNVTGTVKVKLYKGNIKPAGIFTENALYDEGISSFGNSELYDHKDAEGFINLFTLPLKIRAMKAGK | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 44624
Sequence Length: 399
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 6.3.4.5
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Q827Z1 | MQCEEKPVTERVVLAYSGGLDTSVAIGWIAEETGAEVIAVAVDVGQGGEDLDVIRKRALACGAVEAEVADAKDEFADEYCLPAVKANALYMDRYPLVSALSRPTIVKHLVAAAQKHGATTVAHGCTGKGNDQVRFEAGIVALAPGLKCIAPVRDYAMTRDKAIAFCEEKRLPIATTKKSPYSIDQNVFGRAVETGFLEDIWNAPIEDIYEYTSNPAEPREADEVVISFKEGVPVAIDGRPVTVLQAIQQLNERAGAQGVGRIDMVEDRLVGIKSREVYEAPGAIALITAHQELENVTVERELARYKRQVEQRWGELVYDGQWFSPLKRALEGFIDEANQHVNGDIRMTLHGGRAVVTGRRSETSLYDFNLATYDTGDSFDQAAAKGFIDIYSLSSKIAAKRDLA | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 44066
Sequence Length: 404
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 6.3.4.5
|
Q06734 | MSKVLTSLPAGERVGIAFSGGLDTSVAVAWMRDKGAVPCTYTADIGQYDEPDIASVPSRASAYGAEITRLVDCRAALVEEGLAALACGAFHIRSGGRPYFNTTPLGRAVTGTLLVRAMLEDGVQIWGDGSTFKGNDIERFYRYGLLANPHLRIYKPWLDADFVTELGGRKEMSEWLLAHGLPYRDSTEKAYSTDANIWGATHEAKTLEHLDTGIETVDPIMGVRFWDPSVEIATEDVTVGFEQGRPVSINGKEFASAVDLVMEANAIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIVYERLVNAIHNEDTLAAYHNEGRRLGRLMYEGRWLDPQALMIRESLQRWVGTAVTGEVTLRLRRGEDYSILDTTGPAFSYHPDKLSMERTEDSAFGPVDRIGQLTMRNLDIADSRARLEQYVGLGLVGTPHPTPIGAAQAAATGLIGAMDEGGAEAIASRGEATDEETMLDRAAMESGTD | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 52383
Sequence Length: 482
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 6.3.4.5
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Q04MW7 | MSKEKVILAYSGGLDTSVAITWLKKDYDVVAVCMDVGEGKDLDFIHDKALKVGAVESYVIDVKDEFATDYVLVAHQSHAYYEQKYPLVSALSRPLISKKLVEIAHQIGATTIAHGCTGKGNDQVRFEVSIAALDLNLKVIAPVREWKWSREEEIYYAKENGVPVPADLDNPYSVDQNLWGRANECGILENPWNQAPEEAFGITTSPEQAPDMPEYIEIEFSEGVPVSLNGEVLKLADLIQKLNEIAGKHGVGRIDHVENRLVGIKSREIYECPGAVTLLTAHKEIEDLTLVREVAHFKPIIENELSNLIYNALWFSSATQALIAYIKETQKVVNGTAKVKLYKGSAQVVARKSPSSLYDENLATYTSADTFDQDAAVGFIKLWGLPTKVHSEVQKSAK | Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
Sequence Mass (Da): 44065
Sequence Length: 398
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 6.3.4.5
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Q87Q40 | MTKSLFRQSFLTDTLDVHIDVAPAEQVLSNGVQLKLYQRGVLEVIPENPTQETKNIIISCGIHGDETAPMELVDSIIKDIESGFQKVDARCLFIIAHPESTLAHTRFLEENLNRLFDEKEHEPTKELAIADTLKLLVRDFYQDTEPKTRWHLDLHCAIRGSKHYTFAVSPKTRHPVRSKALVDFLDSAHIEAVLLSNSPSSTFSWYSAENYSAQALTMELGRVARIGENALDRLTAFDLALRNLIAEAQPEHLSKPCIKYRVSRTIVRLHDDFDFMFDDNVENFTSFVHGEVFGHDGDKPLMAKNDNEAIVFPNRHVAIGQRAALMVCEVKTRFEEGELVYD | Cofactor: Binds 1 zinc ion per subunit.
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
Catalytic Activity: H2O + N-succinyl-L-glutamate = L-glutamate + succinate
Sequence Mass (Da): 38837
Sequence Length: 342
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5.
EC: 3.5.1.96
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Q2UEK7 | MLPTLPNIAGRINTMATFLLPVAIGTIILLFLYGKYVTSTLIPGPPTLPLIGNLHQLPSDDRRHVLAQWHKKHGPIISLKFGWSSVVILGNIAVTKELFGKRSLKYGSRPRMVMARDCMTKQMQTSTLPWGEKWKIHNRIQLSLVGGPKIRSYQSLLDIESCKVLYQLLSTESLVTCFNRFKFNIIYTLAYGKDPDQNESDFHEILELADHFTQTLTNATWVVDLFPILNCLPRRLAPWKAVGDDFHRRAMGWFRRNSEAAVKSNSWNWTKHVQFNEDTGNLSVSEMQYLIGVLFEAGVDSTATVLHFFVLACTLYPDAVTKARQELDKVVGSARLPTPKDLPQLPYVKAFIQEVLRWRPITAEGLPHFTLEDDKYQGYDIPKGSTVIFNYWSGHMDEDTYQHADQFCPERWIERPDLPLGVFGYGRRACAGRRLALMSLETLIPKLLWAFDFRSPAGTDHGKSRDPGTEHQGALIKPRSFPVSWHPVSNDRRLIIERLFQERDKDLDTVLDDIGKAFERY | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate . Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene-11-ol by atsK . Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE . The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin . The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively . Finally, the O-acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59544
Sequence Length: 521
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q2UEK8 | MGEQTEFEPIQLSPLDQAIPPVYIRILLCFSVVNVDRAISQLQTGVSSLLSALPFLSGDVVRYTAPGKTKWLYQLCPPTHQVQATGVLVVKHHQMRCMVDEKRFAPSSTSHIPLSPFAEPARPAPIFRVQANAYIDGITLGFAFHHIAVDATGMGVIISELARHCRSSPPPSLLCPDYERATRQLISNSRATECSGLDHSGDYISCQALSPPAEGSEDASPSIEISTETRTFVFPAARLESLKNACIEMLPTLDQQQRQQNPCLDEPARTKVPWLSTNDVFVALLWVCLTRCRYQEDQNSGLPSDEHTRICMGVNMRSRIQPPLSADYLGNAILSLSFKLNVNVFRRTQVTNESIEGVDSKDIEHKQWLATICRVARNIRRGVNGMDDSYFRSVVSFLEDSSDCRLFDYARCDFCVPSWRHLCVYHADFGEMGRPKSLEVFDVPGDGSFCILPQHYGAAAPWELLLGLLKA | Function: O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate . Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene-11-ol by atsK . Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE . The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin . The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively . Finally, the O-acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B .
Sequence Mass (Da): 52449
Sequence Length: 471
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 2.3.1.-
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P80358 | MIVRPVTSADLPALIELARSTGTGLTTLPANEQRLQHRVSWAEKAFRGEAERGDADYLFVLEDDAGKVVGISAIAGAVGLREPWYNYRVGLTVSASQELNIHREIPTLFLANDLTGNSELCSLFLHADHRSGLNGKLLSRARFLFIAEFRHLFGDKLIAEMRGMSDEEGRSPFWESLGRHFFKMEFSQADYLTGVGNKAFIAELMPKFPLYTCFLSEEARGVIGRVHPNTEPALAMLKAEGFSYQGYVDIFDAGPAIEAETDKIRAIAESQNLVLAVGTPGDDAEPYLIHNRKREDCRITAAPARAAAGTLVVDPLTAKRLRLSAGASVRAVPLSAQKRG | Catalytic Activity: L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine
Sequence Mass (Da): 37245
Sequence Length: 340
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5.
EC: 2.3.1.109
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Q2UEK9 | MTDISTGVQLKPGIGDGTVYNGNMSKDTLVNCSPDPENPEKGQASSPRTQISVDDNEESTTEYPSSWKLAMIMISLCLAVFCLALDTTIMATAIPKIADQFNSLNDVGWYGSAYLLTTSALTLSFGKLYSFYSIKWVYLQALGMFEIGSLICGATPNSLGLIIGRAIAGSGSAGIYSGSMLIVARSAPLERRPLLTGILGGLFGVASVVGPLIGGAFTDNLSWRWCFYINLPLGAVTGLFLILFFDGAKATTQRATIRDQLSQLDLLGSLCFLPAIICVLLALQWGGTTYPWHDGRIIALFTVFGVLLLAFAGVQWWRQEKATVPPRLIANRNVWGAALFSFCLNASFIIFTYYLPMWFQSIKGVTATQSGIMNLPMVLAVVIFSIISGGLVGALGYYTPFMVIAPLIAAIGAGLLSTLRMDSNNASWIGYQILYGVGVGCGLQQPIVAVQGSLAPADLPTGTVIVMFMQTIGGAIFMSVGQNVFQNQLMRNLATQAPSVDAARVLQAGATMLRKTVSSDLLPAALRAYNSAITEAFYVAVAMAVLALPGALVMQWISVKGRQL | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . Seems not to be involved in astellolides translocation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60176
Sequence Length: 564
Subcellular Location: Membrane
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Q2UEL0 | MTRQSHYQAIILDLGNVVFEWDTSQNPPTAAPNQISLLRTSMKSPVYHSYERGQLSTEECHRLLGESLHVDPGQIKEAFDLARQSLRSNPALLDFIRQLKQTRGVAVYAMSNIPQAEIEYLKESRAGDMEVFDEVFASGYVGSRKPETEFYRRVMGEIGLKAERVVFVDDKEENVDVARGLGLYGVCFGGVEELRGHLLGI | Function: Sesquiterpene phosphatase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate . Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene-11-ol by atsK . Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE . The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin . The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively . Finally, the O-acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B .
Sequence Mass (Da): 22610
Sequence Length: 201
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 3.1.3.-
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Q2UEL1 | MSRRFPIQVAQSEIPPIAWGLWRMVYRLWLHPLSGYPGPRLAAVSNLPYFAWTCTGNLHLRLQELHKVYGDVIRIRPNALTYRTPEAWTDIYGHRKPGTLPFSKDPEFFMPAQAGSSHMINANEKDHTRQKRLLNHAFSERSLRQQEHLIMGYIDLFIQRLRGQARMGAETVNMEEWLNFLTFDIIGDLAFGEPFGCLQNSEYHPWVATIFKSIKTGAILRALNIYPILLGFIRRFLPKSLVQKRIAHYQMSKDRVTRRLQTETSRPDFISYILKYNDDRGMSTPEIEMNAALLIQAGSETTATVLAACLYFLQKNAACHRRLVQDIRSAFTQETDINFLSAAQLPYMNGVIEESLRLFPPAPGIGPRVVPKGGARICGRYVPGGVSVSVGHYSTFRSARNFTRPNEFLPQRWLDRDAESEFASDQTMALQPFSYGPRACIGRNLAYAEMRTILAKILWHFDVQLDERSADWANSKSYIVWEKGPLWLKLHPRNVPQETD | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate . Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene-11-ol by atsK . Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE . The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin . The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively . Finally, the O-acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B .
Sequence Mass (Da): 57391
Sequence Length: 500
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.-.-.-
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P42662 | MDLKMLLIFTAFLLPAVLGFPIQDNYENSTATSESTQVTTEESIYDSPSPTETDSEDDVIFNRILEVNKDSSRYLQEGDIVPRRSRSAFNCRNCYWPQSMDGIVRIPYVLDPTYEENHVRGILEAMAEFETLTCINFVKRKTERDYLIIRSADGCWSNYGKVGGGQTVSVMKGGCMWKGIIQHELDHALGFLHEHSRSDRDKYVKIMWEYISPACRPDFRKFENSNNLGLPYDYSSVMHYGPHTFTNTTGKATIVPVPDGSVHIGQRLGLSNLDVAKINKLYNCSRCSTIIDAAFGSLKSANYPRNYSDNTNCVWLIRTRSRKISLHFRDFDLRRTRGCQGDYVKVYDGSSKYSPVLMNKTCGSQIPTDVVSSSSLMLIEFVTDGRDTASGFQATFTSARMQRRFNTRN | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization (By similarity). Protease which may play a role in the breaking down of the vitelline membrane (days 0-5) and possibly, in the digestion of the egg white (days 9-12) .
Sequence Mass (Da): 46446
Sequence Length: 409
Subcellular Location: Cytoplasm
EC: 3.4.24.-
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P33879 | MSKETKKPFRQSVAEWRQFVYNPNSGEFLGRTAKSWGLILLFYLVFYGFLAALFTFTMWVMLQTLSNDIPKYRDRISSPGLMISPKPDTALEFYFNKSDAQSYAEYVSTLRKFLETYDDSKQSQNINCTPGKVFDQNDVAVKKACRFNLSELGQCSGKEDKTFGYSKGTPCVLVKMNRIIGLKPEGEPYIQCTSKEPGAVEINYFPSGGLIDLMYFPYYGKTLHAHYLQPLVAVQLAINSNSTNEEIAIECKILGSPNLKNEDDRDKFLGRIAFKVEMTE | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31859
Sequence Length: 280
Subcellular Location: Cell membrane
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P54709 | MTKNEKKSLNQSLAEWKLFIYNPTTGEFLGRTAKSWGLILLFYLVFYGFLAALFSFTMWVMLQTLNDEVPKYRDQIPSPGLMVFPKPVTALEYTFSRSDPTSYAGYIEDLKKFLKPYTLEEQKNLTVCPDGALFEQKGPVYVACQFPISLLQACSGMNDPDFGYSQGNPCILVKMNRIIGLKPEGVPRIDCVSKNEDIPNVAVYPHNGMIDLKYFPYYGKKLHVGYLQPLVAVQVSFAPNNTGKEVTVECKIDGSANLKSQDDRDKFLGRVMFKITARA | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31513
Sequence Length: 279
Domain: The C-terminal lobe folds into an immunoglobulin-like domain and may mediate cell adhesion properties.
Subcellular Location: Apical cell membrane
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Q63377 | MTKTEKKSFHQSLAEWKLFIYNPTSGEFLGRTSKSWGLILLFYLVFYGFLAALFTFTMWVMLQTLNDEVPKYRDQIPSPGLMVFPKPPTALDYTYSMSDPHTYKKFVEDLKNFLKPYSVEEQKNLTDCPGGALFHQEGPDYSACQFPVSLLQECSGVNDSNFGYSKGQPCVLVKMNRIIELVPDGAPYITCITKEENIANIVTYPDDGLIDLKYFPYYGKKRHVGYRQPLVAVQVIFGADATKKEVTIECQIDGTRNLKNKNERDKFLGRVSFKVIAHA | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31830
Sequence Length: 279
Domain: The C-terminal lobe folds into an immunoglobulin-like domain and may mediate cell adhesion properties.
Subcellular Location: Apical cell membrane
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P30716 | MAKEENKSGEQSSSEWKQFIYNPSSGEILGRTASSWALILLFYLVFYGFLAGLFTLTMWVMLQTLDDSVPKYRDRVSFPGLMISPKSAGLEISFSKSDKSHMKSILKFFTHFYHHTMTPYKLQMCSARKAITTEQEGVEEKKSCQFNRSSLGPCAGLEGNEYFGYNDGSPCVLVKMNRIIGLKPDGNPHINCTSKAENISLQYYPEYGKIDLMYYPYYGKKTHVNYVQPLVAVKITPSNSTGTSEIVLECKLYGSPNLKNNDDRDKFLGRVNFKLEIKD | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of this glycoprotein is not known. Some specific sequence of the beta subunit can modulate the activation of the Na,K-pump by extracellular potassium ions.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31678
Sequence Length: 279
Subcellular Location: Cell membrane
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P21188 | MAKEENKGSEQSGSDWKQFIYNPQKGEFMGRTASSWALILLFYLVFYGFLAGLFTLTMWVMLQTLDDSVPKYRDRVSSPGLMISPKSAGLEIKFSRSKTQSYMEYVQTLNTFLAPYNDSIQAKNEFCPPGLYFDQDEEVEKKTCQFNRTSLGICSGIEDPMFGYGEGKPCVIVKINRIIGLKPEGNPKINCTSKTEDVNLQYFPDNGKIDLMYFPYYGKKTHVNYVQPVVAVKISPSNFTSEEIAVECKIHGSRNLKNEDERDKFLGRVTFKVKITE | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31570
Sequence Length: 277
Subcellular Location: Cell membrane
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Q2HZ96 | MEPGMEMNTASEGGTRRGPENKHEEKVQDPNRGEAETKAEMGNKTWADLAGEMKTFLWNPEERTCMGRTAKSWGLILLFYFIFYTCLAGMFAFCMYVMLLTLSPYTPTYRDRVSPPGVMIRPYLNGFTIAFNVSKPSTWQPYVDSMHQFLAAYDDKVQEEKNIECISGQYFIQGGNDSEEKKACQFKRSLLQNCSGIEDPTFGFSKGQPCILLKMNRIIGYRPGAGVPVNVDCKVQKGNESDLRSVDFYPGNGTFDLMYYPYYGKLTHVNYTSPLVAMHFTDVKRNSLVHIQCKLNGKGIINDVNSDRFLGRIIFTLSIGK | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane.
PTM: Glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36363
Sequence Length: 321
Subcellular Location: Membrane
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Q9UN42 | MRRQLRSRRAPSFPYSYRYRLDDPDEANQNYLADEEEEAEEEARVTVVPKSEEEEEEEEKEEEEEEEKEEEEGQGQPTGNAWWQKLQIMSEYLWDPERRMFLARTGQSWSLILLIYFFFYASLAAVITLCMYTLFLTISPYIPTFTERVKPPGVMIRPFAHSLNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGNEDEDKKACQFKRSFLKNCSGLEDPTFGYSTGQPCILLKMNRIVGFRPELGDPVKVSCKVQRGDENDIRSISYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVKNQAVPVQCQLKGKGVINDVINDRFVGRVIFTLNIET | Function: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 41598
Sequence Length: 357
Subcellular Location: Nucleus inner membrane
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Q202B1 | MATTAGEQANYLQSADSMSDGRQHHPEEAGEKKQEEQKKSWGEWLQDLKIFIWNPEKKEVLGRDKKSWALILLFYFILYCFLAGLFALCIYGLLATISPYVPTYRDRVFPPGLTIRPQFNALYFSFNPSDRSTWSSHAESLNTFLEDYNDEIQQEKNLECTPGKYFFQPGEDHEERKACQFRRSLLKNCSGIEDPTFGFAQGKPCILLKMNRIVGYQAGSGIPIYVTCEILKADASYLGPVNFYPSDKFDLMYYPYYGKLTHVNYTSPLIAMQFTEVKNNQDINIQCKINGKDIISDHDKDRFLGRVAFTLHIG | Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane.
PTM: Glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36129
Sequence Length: 314
Subcellular Location: Membrane
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P28774 | MAKGKQKKGKDLNELKKELDIDFHKIPIEECYQRLGSNPETGLTNAQARSNIERDGPNCLTPPKTTPEWIKFCKNLFGGFALLLWTGAILCFLAYGIEASSGNEDMLKDNLYLGIVLATVVIVTGIFSYYQENKSSRIMDSFKNLVPQYALALREGQRVTLKAEELTMGDIVEVKFGDRVPADLRVLEARSFKVDNSSLTGESEPQARSPEFTNDNPLETKNLAFFSTNAVEGTMRGIVIGIGDNTVMGRIAGLASGLDTGETPIAKEIAHFIHIITGVAVFLGVTFFIIAFVLGYHWLDAVVFLIGIIVANVPEGLLATVTVCLTLTAKRMASKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDGTITEADTTEDQSGAQFDKSSAGWKALVKIAALCSRAEFKPNQSTTPILKREVTGDASEAAILKCVELTTGETEAIRKRNKKICEIPFNSANKFQVSIHENEDKSDGRYLLVMKGAPERILERCSTIFMNGKEIDMTEELKEAFNNAYMELGGLGERVLGFCDYLLPLDKYPHGFAFNADDANFPLTGLRFAGLMSMIDPPRAAVPDAVAKCRSAGIKVIMVTGDHPITAKAIAKSVGIISEGNETVEDIAARLNIPVSEVNPRDAKAAVVHGGELRDITPDALDEILRHHPEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIVYTLTSNIPEISPFLLFILFDIPLPLGTVTILCIDLGTDMVPAISLAYEEAESDIMKRRPRNPVTDKLVNERLISLAYGQIGMIQASAGFFVYFVIMAECGFLPWDLFGLRKHWDSRAVNDLTDSYGQEWTYDARKQLESSCHTAYFVSIVIVQWADLIISKTRRNSVFQQGMRNNILNFALVFETCLAAFLSYTPGMDKGLRMYPLKINWWFPALPFSFLIFVYDEARKFILRRNPGGWVEQETYY | Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Catalytic Activity: ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 110699
Sequence Length: 1004
Subcellular Location: Cell membrane
EC: 7.2.2.13
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A0A068BGA5 | MASFPPSLVFTVRRKEPILVLPSKPTPRELKQLSDIDDQEGLRFQVPVIMFYKRKLSTEGEDPVKVIREALAEALAFYYPFAGRLIEGPNRKLMVDCTSEGVLFIEADADIELNQLIGDTIDPGTYLDELLHDVPGSEGILGCPLLLIQVTRFRCGGWAFAIRLNHTMSDTLGLVQFLTTIAEFTRGAEGAPSVPPVWQREFLAARQPPFIPFQHHEYEQVIDTTPDDNKKSMTHKSFFFGPKEIRAIRSHLPLHHRSTSSTFDVLTACLWRCRTCALVLDPKKTVRISCAASGRGKHDLHVPRGYYGNVSAFPATVLRAGMISTSPLEYAMEGVKKAKARMTGEYLRSVADLMVTKGRPLYTVVGNYIVSDMTRVGLDTIDFGWGKPVYGGPARAFPLISFYGRFKDNKGEDGIVVLICLPEAAMKRFQEELKKMTGEHVDGPFDYKPIKVVSKL | Function: Involved in the biosynthesis of volatile esters which confer kiwifruit flavor . Alcohol acyl transferase that can use a wide range of alcohols as substrate to produce esters . Exhibits benzoyl-CoA:alcohol O-acyltransferase activity .
Catalytic Activity: 3-(methylsulfanyl)propanoyl-CoA + butan-1-ol = butyl 3-(methylsulfanyl)propanoate + CoA
Sequence Mass (Da): 50972
Sequence Length: 456
EC: 2.3.1.-
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A1L209 | MKMEDMSLSGLDNTKLEALAHDVYSDLVEDACLGLCFEVHRAVKQGYFFLDETDQESMKDFEIVDQPGVDIFGQVYNQWKNKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIASSNNTSKSESDQEDNDDINDNDWSYGSEKKAKKRKSEKNPNSPRRSKSLKHKNGELSGSVNPDMYKYNYSSGISYETLGPEELRSILTTQCGVVSEHTKKMCTRSQRCPQHTDEQRRAVRVFLLGPSASTLPDADTMLENEAYEPPDGQLIMSRLHWDASSDISPSDSASSKASTNNSESKRPKKKKPSTLSLTPAGERDKAQERDRIAGSGSSGSSSQNALGLSSRKKRPKLAVPPAPSIYDDLN | Function: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone H2B. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription.
Sequence Mass (Da): 40720
Sequence Length: 367
Domain: The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module.
Subcellular Location: Nucleus
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Q14CW9 | MKMEEMSLSGLDNSKLEAIAQEIYADLVEDSCLGFCFEVHRAVKCGYFFLDDTDPDSMKDFEIVDQPGLDIFGQVFNQWKSKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIANSNNMNKSESDQEDNDDINDNDWSYGSEKKAKKRKSDKNPNSPRRSKSLKHKNGELSNSDPFKYNNSTGISYETLGPEELRSLLTTQCGVISEHTKKMCTRSLRCPQHTDEQRRTVRIYFLGPSAVLPEVESSLDNDSFDMTDSQALISRLQWDGSSDLSPSDSGSSKTSENQGWGLGTNSSESRKTKKKKSHLSLVGTASGLGSNKKKKPKPPAPPTPSIYDDIN | Function: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B . The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Within the complex, it is required to recruit USP22 and ENY2 into the SAGA complex . Regulates H2B monoubiquitination (H2Bub1) levels. Affects subcellular distribution of ENY2, USP22 and ATXN7L3B .
Sequence Mass (Da): 38651
Sequence Length: 347
Domain: The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module.
Subcellular Location: Nucleus
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O14261 | MRFRLNDSFSGKSWTIDNVQWTPQNLVAWIMELNIGLSDEAKLLLPNGMSLNETVLNSESDVVIYVLDQNLLTFTYDGDKIPSIPSLKGQPISNVLTGIIADSSSDQWKDKISKCLSLLSDILESSSKIHNQLSVCHDEYSTSIVSPEVAMNYLQRRQSGMKDLLFVFYERLDRVSVSDLLHDFLALPTGSLPITPLKILSTNWTKLDSWLNSISARYAEAQKRVQQCIGAANSIIVSPFKEVPSIKEGDDAYYHLRSVAQDAANILQEILKIESTSTTSQIKPKCNYETEITDCMEKLQSNLSELKSSRKSSLISLKSFWLSFYKVSLRYDALYEYLRQIAEELDRSKFVLSQSRNIFSLYIDILMEALRRTEWQESYNVSHDSSLPLDQEKELSLRKSWLSHFSNLLFNHGQLKYLPVLTRDEISNYLLNIQAHPNYQTFHQMLSNRLSEYLGFPGSPREAVSNTVQANNSLHEKLAMYQNRCNNLEAMLSHQNGFNYNINNDGLSPNAPHPPINEQSNSSQPFYRVSPSIVPLNVIRKLTNRKTSFTDSHILRLQDEVNQLRNELDLVNKRNEDLLIELQGKEEKIQYLETENEEVLQKYENLQEELSSTRKLLTKNEAAVAEQQSNEEMHSNEPNILNLYSVFEGKVDSLQELYNAFKLQLTSLKQKGEYATLAKDAEAVQHIIEERDYALAEKADLLKLSENRKEQCKILTQKLYTIVFRCNELQSVLRECVTQPGFDSDNERDGHASIPDRQIEFNSKDLQYLYWMDGEDADRNFQEFLNRMSSLDFDSFHNFVVSVLTQAHNHELRWKREFQSNRDKALKAILDSQSKVSLRNFKQGSLVLFLPTRRTAGNKKVWAAFNVNAPHYYLNTQPHLKLESRDWMLGRVTSIEDRTADDSTDKWLRLPSGTIWHLVEAIDERF | Function: Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the preautophagosome (PAS), the site of vesicle/autophagosome formation. Required for atg9 anterograde transport from the mitochondria to the PAS (By similarity). Required for nitrogen starvation-induced sexual development and for entering the dormant G0 state (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 106770
Sequence Length: 926
Subcellular Location: Preautophagosomal structure membrane
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Q6CFR0 | MSEIRVSCASSGVSVSAARDQFSSLPHLKAWIELEFSVSVSEQLLLTVAAEQVKMAHLGTQNELFVFDRSVVGGTVSNEHKYSAPKLKTLTPGTDPSQWALTVLTHCSRLVEETKRVTAEIATIKRATNVAITQMKQHSQNLDKNLLNVKEYSKELNQGITPLLSVDLAQLRDNTRAVKLVAPAVFGKKQFLNDWLDLQQLQSIVVEFKADFPSCMDKLQTLEQDLAQLSKDTQTLVNSTDVWIGGTNSDVLCNEAVGILRKLSELTSGDHVTNEAVKSVQNCQSQILDLHKALSKAKFQTVQHSQKVLQSISQLQSRSTKLKPKLTHIGSELTKYEEKRVQAMKQVDVEFVYGCVLVEMLRRTVWSQSGGENGSVKSEIGTRVAWKKQFQDTFPFVDILNEQEDLTIDTISTSSPSIVHNLVIARPVVTDYISQVSSKEVRNNLESLLGGVTGSAAATSSFPRSLFRNGSISGSLMAERAPISSATNADDKIRGYEARIRKLEDLLYKQRMSQDTSRWSVSPGTPSAGFAVVSPGQLSSEARGSSLSPEPTETREQVKAREKAEEEARKAEEERLARDKAAAEALQSKVDQLSQSLLHTENEKNDLMANLASMESDFSRERRCLVQEISELKLRVEELEEQVETAAETSIERHQRADQETEELEQRLKAMTLAQNTVDDENSRLKITLQDMSQRLYTGYKRNCVLLESLGLQAQKEYDADGSEVVSFDIHRVKGLRKKHRGKKGEKTEKDSESDSTDDFSALYWATKTTPDSFESSYRTFLARIFLDYDLYVEKVAKRFEDLEHLARKLQKEARNYRTMTQQLDDETRSKIALNRFKVGDLVLFLPTRDPSRQPQPWAAFNVGAPHFFLKQKPGRELKDRDWLVGRITGMEERVVNGGIGDREENPFDLGQGLRWWWLEAEEE | Function: Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation. Required for the Cvt vesicles completion (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 104021
Sequence Length: 924
Subcellular Location: Preautophagosomal structure membrane
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Q6BH63 | MSDDTEWSEDILNRLNVRDQYEKKDSRYFKAFSQLSQEARTNDQASNNDKSIEYNKLLKENNQLKKDNEILTTSLNQTTISLEKSDLKINQLLKSQDQLERHNTSLNNKIKHLNLEIIEKNKSVEILNDELLLNEIQTNVLNDKITRLSDENKKLVERWIEKAKSDAEKLNDANEFLESVNRK | Function: Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21537
Sequence Length: 183
Subcellular Location: Preautophagosomal structure membrane
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Q5BH90 | MAHWREEYAAALAARDRREKANVAIYNAYSQLADRTASSMIAVSDLQSDAQRSALSTPVADPRQQQPSPASGPSPQDIILAIRADLAEAQRSRSELEEQLARVTTELEKLRRRNIQNGKRISSMESEITHLQLRLKDRDEELREKAKLLEGFQDEIATFELQLNMAEERSNRLQKENQELIDRWMARMGKEADAMNDAYQFS | Function: Stabilizes the atg5-atg12 conjugate which is necessary for autophagy. The atg5-atg12/atg16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23118
Sequence Length: 202
Subcellular Location: Preautophagosomal structure membrane
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I1RFS8 | MPNWRDQYLSGIKDAELNNPVNMELVQTCSQMADRISALEAEKNGLETLVTTNGKTTARPTEPSTNDPAVAQLKQDLAEALRSKGVAEKRLRSSEEELLQLRSKHKTNTRSIRDLTADKNSLTTRLKDREYELREKRKFIEQVQDEMIALNLQMSMAEKERDKVKKENKELVDRWMKRMAQEAEAMNLANEPIFKKGR | Function: Stabilizes the ATG5-ATG12 conjugate (By similarity). The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS) (By similarity). Recruits also ATG3 to the PAS (By similarity). Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity). Autophagy is required for proper vegetative growth, asexual/sexual reproduction, and full virulence . Autophagy is particularly involved in the biosynthesis of deoxynivalenol (DON), an important virulence determinant .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22848
Sequence Length: 198
Subcellular Location: Preautophagosomal structure membrane
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W0T661 | MEYELLESIRARDLVDKRFSQLFEEVPLVPKLEKAGEGDTNVKESSIKNLKDYLKLRDEEVYKLKDILKLKNRDTERLNDELLSANIESNLLQERLEKLQQEYDRLIERWLLKAQKEADTMNSHFK | Function: Stabilizes the ATG5-ATG12 conjugate (By similarity). The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS) . Recruits also ATG3 to the PAS (By similarity). Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15068
Sequence Length: 126
Subcellular Location: Preautophagosomal structure membrane
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Q520U5 | MSSLPDWRDEYLASIKEAEKNSPVNRDLVEACSQLQDRVAALEAERDALKASGASAGQSASDPASQSGDAAQSAVVARLRLDLAEALGTQERLQSRLGLAESELERLRAKTAEDAKTIRTLNTQCVSLSTKVKDRNEELQGKSKLVENVQDELIALTLQLNVMEQQKAKIQAENDQLVERWMKRMGQEAEAMNLANEPKFAKRG | Function: Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22465
Sequence Length: 204
Subcellular Location: Preautophagosomal structure membrane
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A7KAK0 | MSWKNDLLAKLAQRDKSMETQKDVFLSFQFLSTRIASLERQLDTVQRDDSKKTVLDLLGEIDQLKQKLDLAEDSLKHETAKNKELVKELSTVKNNLNILTDGYKKLQERHLRLQEESKIKFQNLESLNDDILSLNIENNLLNDRMAKLKQENESLIERWMKRVKQEAEVLNDANEALSRSEKSLKPEG | Function: Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21924
Sequence Length: 188
Subcellular Location: Preautophagosomal structure membrane
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