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O46584 | SVVKSEDYALPSYVDRRDYPLPDVAHVRHLSASQKALKEKEKASWSSLSMDEKVELYRIQFKESFAEMNRGSNEWKTVVGAAMFFIGFTAILIILEKRYVYGPLPHTFDKEWVAMQTKRMLDLKVNPVDGLASKWDYDKKEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16824
Sequence Length: 144
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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P13073 | MLATRVFSLVGKRAISTSVCVRAHESVVKSEDFSLPAYMDRRDHPLPEVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRGSNEWKTVVGGAMFFIGFTALVIMWQKHYVYGPLPQSFDKEWVAKQTKRMLDMKVNPIQGLASKWDYEKNEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19577
Sequence Length: 169
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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P19783 | MLASRALSLIGKRAISTSVCLRAHGSVVKSEDYAFPTYADRRDYPLPDVAHVTMLSASQKALKEKEKADWSSLSRDEKVQLYRIQFNESFAEMNRGTNEWKTVVGMAMFFIGFTALVLIWEKSYVYGPIPHTFDRDWVAMQTKRMLDMKANPIQGFSAKWDYDKNEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19530
Sequence Length: 169
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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Q95283 | MLATRVFNLIGRRAISTSVCVRAHGSXVKSEDYALPVYVDRRDYPLPDVAHVKNLSASQKAXKEKEKASWSSLSMDEKVELYRLKFNESFAEMNRST | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11048
Sequence Length: 97
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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Q9TTT8 | MLPTRLLSFSGSRAISTSFCLRAHGSVVKSEDYALPSYVDRRDYPLPDVAHVKQLSAGQKALKEKEKAPWGSLTRDEKVELYRIQFNESFAEMNRGTNEWKTVVGTALFFIGFTALILIWEKHYVYGPIPHTFDKEWVAMQTKRMLDMKVSPIQGFSAKWDYNKNEWRK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19599
Sequence Length: 169
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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P10888 | MLATRALSLIGKRAISTSVCLRAHGSVVKSEDYALPSYVDRRDYPLPDVAHVKLLSASQKALKEKEKADWSSLSRDEKVQLYRIQFNESFAEMNKGTNEWKTVVGLAMFFIGFTALVLIWEKSYVYGPIPHTFDRDWVAMQTKRMLDMKVNPIQGFSAKWDYNKNEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19515
Sequence Length: 169
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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O46582 | SVVKSEDYARPSYVDRRDYPLPDVAHVRHLSASQKALKEKEKASWSSLSMDEKVEKTVVGAAMFFIGFTAILVILEKRYVYGPLPHTFDKEWVAMQTKRMLDLKMNPIDGLASKWDYEKKEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14426
Sequence Length: 124
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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O46581 | SVVKSEDFTLPAYVDRRDYPLPDVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRRSNEWKTVVGTAMFFFGITALIVMWEKRYVYGPLPQTFDKEWVAMQTKRMLDMKVNPIQGLASKWDYEKNEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17037
Sequence Length: 144
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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Q9RM98 | MSVLDQNAVDINPRISEAEVGDYIALLKPRVMSLVIFTALVGMAMAPGHFHPVLAITSLLCIAVGAGASGALNMALEGDIDAKMSRTANRPIPRGRITRPEAMTFGMTLAFFSVMTLGILVNWIAGALLAFTIFFYVVIYTMWLKRWTAQNIVIGGAAGALPPVVAWAAVTGTVDVEPLLLFAIIFFWTPPHFWALALFRSDDYARAGIPMLPNVAGPDATRLQILLYTIVLIAVAAAPWALGYFDAVYGVVSLILGAGMLVLAINVYMRRERSQSLRATRKLFAFSILYLFALFATLLAEVVFRALAPMAGGA | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33884
Sequence Length: 314
Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Subcellular Location: Cell inner membrane
EC: 2.5.1.141
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Q829U3 | MLTTSSSRGQRPFGARVKAFVALTKPRIIELLLITTVPVMFLAEQGVPSLRLVLLTCLGGYLSAGGANALNMYIDRDIDALMERTSQRPLVTGMVSPRECLAFGITLAVVSTLLFGLTVNWLSAWLSLGALLFYVVVYTMILKRRTSQNIVWGGIAGCLPVLIGWSSVTDSMSWAPVILFLVMFFWTPPHYWPLSMKVKDDYARVGVPMLPVVASNKVVARQIVIYSWVMVGVSLLLTPLGYTGWFYTLVALLAGGFWLWEAHGLQNRAKAEVTGGKLKEMRLFHWSITYVSILFVAVAVDPFLR | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33796
Sequence Length: 305
Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Subcellular Location: Cell membrane
EC: 2.5.1.141
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Q9XAC2 | MTAVESRPAGVIGTSQSPSHRPFGARVKAFVALTKPRIIELLLITTVPVMFLAEQGVPNLKLVLLTCVGGYLSAGGANALNMYIDRDIDALMDRTSQRPLVTGMVSPVECLVFGITLAIVSTLLFGFTVNWLSAWLSLGALLFYVVVYTMILKRRTSQNIVWGGIAGCLPVLIGWSAVTNSMSWAPVILFGVMFFWTPPHYWPLSMKVKEDYARVGVPMLPVIASNKVVARQIVIYSWVMVVVSLLLQPLGYTGWFYTAVALAAGGMWLWEAHGLQNRAKAEVTGGKLKEMRLFHWSITYVSVLFLAIAVDPFLR | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34669
Sequence Length: 315
Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Subcellular Location: Cell membrane
EC: 2.5.1.141
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Q67ML5 | MFAQARDRLQSGQVVRDYVALTKPRIVILLLITGFAAMWVAAGGPPPLGLTVVTMIGLALSCGAANAINMWYDRDIDAVMARTRRRPLPAGRLTPEQALRFGVITGALSFLVLLTVNLLTALLATAGLLFYVLVYTMWLKRSTVHNIVIGGAAGAAPPLVGWAAVTGRLDWAAVIMFLVVFLWTPPHFWALALFRSEDYERAGVPMLPVVRGERATKWQILLYSLLLIPSAALLYWTGTVGRLYLWTSVVLGCAMVSASVGLLRERAPQMDWAHRTYGWSLLYLFVIFLAMMLDVTRA | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32820
Sequence Length: 298
Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Subcellular Location: Cell membrane
EC: 2.5.1.141
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Q31JY9 | MTLSSDSRLRFPLEEVGAQLLAYWQLTKPRIILLLLITTAAGMGLAAQGPLDPRLAIATLIGGGLAAAAANTLNCLYDRDIDAIMERTRWRPLPSGRIQPFEAWAFALSLAALSFILLDWQANQLAAGLALAGIVFYVVIYTHGLKRHSSQNIVIGGAAGAIPPLVGWAAVTGELAWPAWILFAIVCLWTPPHFWALALMIRDDYAAVKVPMLPVVVGNAATAQQILAYAGLLLPTTLALAWPLGAAGPFYSATALLLGLELLRRSRQLCQAPDSRPLARSLFKFSIFYLMLLCGAIAMDCLPGAPSLSQAIAAWPGF | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34054
Sequence Length: 318
Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Subcellular Location: Cell inner membrane
EC: 2.5.1.141
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P9WPL7 | MTSTSIPTFPFDRPVPTEPSPMLSELRNSCPVAPIELPSGHTAWLVTRFDDVKGVLSDKRFSCRAAAHPSSPPFVPFVQLCPSLLSIDGPQHTAARRLLAQGLNPGFIARMRPVVQQIVDNALDDLAAAEPPVDFQEIVSVPIGEQLMAKLLGVEPKTVHELAAHVDAAMSVCEIGDEEVSRRWSALCTMVIDILHRKLAEPGDDLLSTIAQANRQQSTMTDEQVVGMLLTVVIGGVDTPIAVITNGLASLLHHRDQYERLVEDPGRVARAVEEIVRFNPATEIEHLRVVTEDVVIAGTALSAGSPAFTSITSANRDSDQFLDPDEFDVERNPNEHIAFGYGPHACPASAYSRMCLTTFFTSLTQRFPQLQLARPFEDLERRGKGLHSVGIKELLVTWPT | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43731
Sequence Length: 400
Subcellular Location: Cell membrane
EC: 1.14.-.-
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P9WPL5 | MTEAPDVDLADGNFYASREARAAYRWMRANQPVFRDRNGLAAASTYQAVIDAERQPELFSNAGGIRPDQPALPMMIDMDDPAHLLRRKLVNAGFTRKRVKDKEASIAALCDTLIDAVCERGECDFVRDLAAPLPMAVIGDMLGVRPEQRDMFLRWSDDLVTFLSSHVSQEDFQITMDAFAAYNDFTRATIAARRADPTDDLVSVLVSSEVDGERLSDDELVMETLLILIGGDETTRHTLSGGTEQLLRNRDQWDLLQRDPSLLPGAIEEMLRWTAPVKNMCRVLTADTEFHGTALCAGEKMMLLFESANFDEAVFCEPEKFDVQRNPNSHLAFGFGTHFCLGNQLARLELSLMTERVLRRLPDLRLVADDSVLPLRPANFVSGLESMPVVFTPSPPLG | Function: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection . Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate . In vitro, Cyp142 catalyzes with equal preference the oxidation of both (25R)- and (25S)-26-hydroxycholest-4-en-3-one diastereomers to the corresponding carboxylic acid which is a prerequisite for entry into the beta-oxidation pathway . Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one .
Catalytic Activity: cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = (25R)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 44399
Sequence Length: 398
Pathway: Steroid metabolism; cholesterol degradation.
EC: 1.14.15.28
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Q01741 | KFLQIAVEEHYQSFDKNNIRDVTDSLWRSKKTKPRGAADPNEKIINLVNDIFGAGFDTVTTALSWSLMYLVTQPHSQKKIQESELDTAIGRERRSWLSERSMLPYKEAFILETVPTWQFVPFTIPHSTTRDTTLNGFHIPKECCVFVNQWQVNHEAELWEDPFVFRTERFLTDDSTAIDKTLSEKVMGKQVGLAWKSALGTRQWEVSFYLSTLTPNWSSAPGGESKKDRVRPIYGLSMKHKRCEHFQVKKRFSMKSSN | Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29914
Sequence Length: 258
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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P05177 | MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLSDRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPELWEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLEFSVPPGVKVDLTPIYGLTMKHARCEHVQARLRFSIN | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) . Catalyzes the hydroxylation of carbon-hydrogen bonds . Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2 . Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis . May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid . Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer . Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA . May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) . Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin . Metabolizes caffeine via N3-demethylation (Probable).
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58407
Sequence Length: 516
Pathway: Cofactor metabolism; retinol metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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Q92109 | MVLMILPIIGSVSASEGLVAMVTLCLVYMIMKYMHTEIPEGLKRLPGPKPLPIIGNMLEVHNNPHLSLTAMSERYGSVFQIQIGMRPVVVLSGNETVRQALIKQGEDFAGRSDLYSFKFINDGKSLAFSTDKAGVWRARRKLAMSALRSFATLEGTTPEYSCALEEHVLKEGEYLVKQLTSVMDVSGSFDPFRHIVVSVANVICGMCFGRRYSHDDQELLGLVNMSDEFGQVVGSGNPADFIPILRYLPNRTMKRFMDINDRFNNFVQKIVSEHYESYDKDNIRDITDSLIDHCEDRKLDENANIQVSDEKIVGIVNDLFGAGFDTISTALSWAVVYLVAYPETQERLHQELKEKVGMIRTPRLSDKINLPLLEAFILEIFRHSSFLPFTIPHCTIKDTSLNGYFIPKDTCVFINQWQVNHDPELWKEPSSFNPDRFLSADGTELNKLEGEKVLVFGMGKRRCIGEAIGRNEVYLFLAILLQRLRFQEKPGHPLDMTPEYGLTMKHKRCQLKASMRPWGQEE | Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59273
Sequence Length: 522
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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P79761 | MGPEEVMVQASSPGLISATEVLVAAATFCLLLLLTQTRRQHAPKGLRSPPGPRGLPMLGSVLELRKDPHLVLTRLSRKYGDVMEVTIGSRPVVVLSGLETIKQALVRQAEDFMGRPDLYSFRHITDGQSLTFSTDTGEMWKARRKLAQNALKNFSIAASPTASSSCLLEEHVSTEASYLVTKFLQLMEEKQSFDPYRYMVVSVANVICAICFGKRYDHDDQELLSVVNVVDEFVDVTAAGNPADFIPLLRYLPSRNMDSFLDFNKRFMKLLQTAVEEHYQTFDKNNIRDVTDSLIEQCVEKKAEANGATQIPNEKIINLVNDIFGAGFDTVTTALSWSLMYLVTYPHMQKKIQAELDQTIGRERRPRLSDRGMLPYTEAFILEMFRHSSFMPFTIPHSTTRDTVLNGYYIPKDRCVFINQWQVNHDEKLWKDPQAFNPERFLNAEGTEVNKVDAEKVMTFGLGKRRCIGENIGKWEVFLFLSTLLQQLEFSIQDGKKADMTPIYGLSMKHKRCEHFQVKKRFSMKSSN | Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60071
Sequence Length: 528
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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Q16678 | MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLIGNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAFASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVALLVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSLVDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSAEKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAELDQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVVFVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQLFLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKETCQ | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) . Exhibits catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2- and 4-hydroxy E1 and E2. Displays a predominant hydroxylase activity toward E2 at the C-4 position . Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites . May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid . Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system . Additionally, displays dehydratase activity toward oxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2 . Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products . Plays an important role in retinal vascular development. Under hyperoxic O2 conditions, promotes retinal angiogenesis and capillary morphogenesis, likely by metabolizing the oxygenated products generated during the oxidative stress. Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression (By similarity).
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60846
Sequence Length: 543
Pathway: Steroid hormone biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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Q64429 | MATSLSADSPQQLSSLSTQQTTLLLLFSVLAAVHLGQWLLRQWQRKPWSSPPGPFPWPLIGNAAAVGQASHLYFARLARRYGDVFQIRLGSCPVVVLNGESAIHQALVQQGSIFADRPPFASFRVVSGGRSLAFGHYSEHWKTQRRSAYSTMRAFSTRHPRSRGLLEGHALAEARELVAVLVRRCAGGAFLDPTQPVIVAVANVMSAVCFGCRYNHDDAEFLELLSHNEEFGRTVGAGSLVDVLPWLQLFPNPVRTTFRKFEQLNRNFSNFVLDKFLRHRESLVPGAAPRDMTDAFILSAEKKASGAPGDDSSGLDLEDVPATITDIFGASQDTLSTALLWLLILFTRYPDVQARVQAELDQVVGRDRLPCMSDQPNLPYVMAFLYESMRFSSFLPVTIPHATTANTFVLGYYIPKNTVVFVNQWSVNHDPAKWPNPEDFDPARFLDKDGFINKALASSVMIFSVGKRRCIGEELSKMLLFLFISILAHQCNFKANQNESSNMSFSYGLTIKPKSFRIHVSLRESMELLDNAVKKLQTEEGCK | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (By similarity). Exhibits catalytic activity for the formation of hydroxyestrogens from 17beta-estradiol (E2), namely 2- and 4-hydroxy E2 . Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites (By similarity). May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid . Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system . Additionally, displays dehydratase activity toward oxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2 (By similarity). Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products (By similarity). Plays an important role in retinal vascular development. Under ambient/hyperoxic O2 conditions, promotes angiogenesis and capillary morphogenesis of retinal endothelial cells and pericytes, likely by metabolizing the oxygenated products symptomatic of oxidative stress . Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression .
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60537
Sequence Length: 543
Pathway: Steroid hormone biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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P98187 | MSLLSLSWLGLRPVAASPWLLLLVVGASWLLARILAWTYAFYHNGRRLRCFPQPRKQNWFLGHLGLVTPTEEGLRVLTQLVATYPQGFVRWLGPITPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPSEYITAIMELSALVVKRNNQFFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFLQAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSRVIPKGNVCNINIFAIHHNPSVWPDPEVYDPFRFDPENAQKRSPMAFIPFSAGPRNCIGQKFAMAEMKVVLALTLLRFRILPDHREPRRTPEIVLRAEDGLWLRVEPLG | Function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous polyunsaturated fatty acids (PUFAs) and their oxygenated derivatives (oxylipins). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon hydrogen bonds, with preference for omega-1 and omega-2 positions . Hydroxylates (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) predominantly at omega-2 position to form (18R)-hydroxyeicosatetraenoic acid (18R-HETE) . Exhibits omega-1 hydroxylase activity toward prostaglandin (PG) H1, PGH2 and PGI2 . Catalyzes the epoxidation of double bonds of PUFAs, including docosahexaenoic and docosapentaenoic acids . Shows little activity against PGD2, PGE1, PGE2, PGF2alpha, and leukotriene B4.
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59995
Sequence Length: 520
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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Q9HCS2 | MSLLSLPWLGLRPVATSPWLLLLLVVGSWLLARILAWTYAFYNNCRRLQCFPQPPKRNWFWGHLGLITPTEEGLKNSTQMSATYSQGFTVWLGPIIPFIVLCHPDTIRSITNASAAIAPKDNLFIRFLKPWLGEGILLSGGDKWSRHRRMLTPAFHFNILKSYITIFNKSANIMLDKWQHLASEGSSRLDMFEHISLMTLDSLQKCIFSFDSHCQERPSEYIATILELSALVEKRSQHILQHMDFLYYLSHDGRRFHRACRLVHDFTDAVIRERRRTLPTQGIDDFFKDKAKSKTLDFIDVLLLSKDEDGKALSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDRDPKEIEWDDLAQLPFLTMCVKESLRLHPPAPFISRCCTQDIVLPDGRVIPKGITCLIDIIGVHHNPTVWPDPEVYDPFRFDPENSKGRSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALMLLHFRFLPDHTEPRRKLELIMRAEGGLWLRVEPLNVSLQ | Function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous polyunsaturated fatty acids (PUFAs). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon hydrogen bonds, with preference for omega-2 position. Metabolizes (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) toward 18-hydroxy arachidonate . Catalyzes the epoxidation of double bonds of PUFAs such as docosapentaenoic and docosahexaenoic acids . Has low omega-hydroxylase activity toward leukotriene B4 and arachidonate . Involved in the metabolism of xenobiotics. Catalyzes the hydroxylation of the antihistamine drug ebastine .
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 60309
Sequence Length: 524
Pathway: Lipid metabolism; arachidonate metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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Q6NT55 | MLPITDRLLHLLGLEKTAFRIYAVSTLLLFLLFFLFRLLLRFLRLCRSFYITCRRLRCFPQPPRRNWLLGHLGMYLPNEAGLQDEKKVLDNMHHVLLVWMGPVLPLLVLVHPDYIKPLLGASAAIAPKDDLFYGFLKPWLGDGLLLSKGDKWSRHRRLLTPAFHFDILKPYMKIFNQSADIMHAKWRHLAEGSAVSLDMFEHISLMTLDSLQKCVFSYNSNCQEKMSDYISAIIELSALSVRRQYRLHHYLDFIYYRSADGRRFRQACDMVHHFTTEVIQERRRALRQQGAEAWLKAKQGKTLDFIDVLLLARDEDGKELSDEDIRAEADTFMFEGHDTTSSGISWMLFNLAKYPEYQEKCREEIQEVMKGRELEELEWDDLTQLPFTTMCIKESLRQYPPVTLVSRQCTEDIKLPDGRIIPKGIICLVSIYGTHHNPTVWPDSKVYNPYRFDPDNPQQRSPLAYVPFSAGPRNCIGQSFAMAELRVVVALTLLRFRLSVDRTRKVRRKPELILRTENGLWLKVEPLPPRA | Function: A cytochrome P450 monooxygenase involved in epidermal ceramide biosynthesis. Hydroxylates the terminal carbon (omega-hydroxylation) of ultra-long-chain fatty acyls (C28-C36) prior to ceramide synthesis . Contributes to the synthesis of three classes of omega-hydroxy-ultra-long chain fatty acylceramides having sphingosine, 6-hydroxysphingosine and phytosphingosine bases, all major lipid components that underlie the permeability barrier of the stratum corneum . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) .
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + triacontanoate = H(+) + H2O + omega-hydroxy-triacontanoate + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 61958
Sequence Length: 531
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.177
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Q9GLL1 | MLELSVSRLGFGLVAASPWLLLLVVGASWLLARVLAWTYTFYNNCRLLQCFPQPPKQNWFFAHLYLVPPTEQGLRKSTQLAANYSHGYLIWFGPITPMIVFCHPDMLRSIANASAAVAPKNMDFYKFLKPWLGDGLLLSAGDKWSRHRHLLTPTFHFNILKPYMKIFTKSTDIMHTKWERLITQGHTRLDMFEHLSLLTLDSLQKCVFSFDSNCQELSSCRKPSKYITAILELSELVAKRNRQIFLHADFLYFLTLDGWRFLRACRLVHDFTDAVIQERCRTLPENVDDFLKAKAKTKTLDFIDVLLLTKDEDGKRLSDEDIRAEADTFMFEGHDTTASGLSWILYNLAKHPEYQERCRQEVQELLRDRESKEIEWDNLAQLPFLTMCIKESLRLHPPVTIISRCCTQDIVLPNGWVIPKGVICIIDIFGTHHNQSVWPDPEVYDPFRFDQENIKGRSPLAFIPFSAGPRNCIGQTFAMTEMKVVLALTLLRFRFLPDKEEPRRKRELILRAEGGLWLQVEPLSASPQ | Function: A cytochrome P450 monooxygenase that catalyzes the omega-hydroxylation of prostaglandin E2. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Catalytic Activity: O2 + prostaglandin E2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy prostaglandin E2 + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 61113
Sequence Length: 528
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.-
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Q9V3S0 | MAVEVVQETLQQAASSSSTTVLGFSPMLTTLVGTLVAMALYEYWRRNSREYRMVANIPSPPELPILGQAHVAAGLSNAEILAVGLGYLNKYGETMKAWLGNVLLVFLTNPSDIELILSGHQHLTKAEEYRYFKPWFGDGLLISNGHHWRHHRKMIAPTFHQSILKSFVPTFVDHSKAVVARMGLEAGKSFDVHDYMSQTTVDILLSTAMGVKKLPEGNKSFEYAQAVVDMCDIIHKRQVKLLYRLDSIYKFTKLREKGDRMMNIILGMTSKVVKDRKENFQEESRAIVEEISTPVASTPASKKEGLRDDLDDIDENDVGAKRRLALLDAMVEMAKNPDIEWNEKDIMDEVNTIMFEGHDTTSAGSSFALCMMGIHKDIQAKVFAEQKAIFGDNMLRDCTFADTMEMKYLERVILETLRLYPPVPLIARRLDYDLKLASGPYTVPKGTTVIVLQYCVHRRPDIYPNPTKFDPDNFLPERMANRHYYSFIPFSAGPRSCVGRKYAMLKLKVLLSTIVRNYIVHSTDTEADFKLQADIILKLENGFNVSLEKRQYATVA | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62971
Sequence Length: 556
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9V558 | MIILWLILALSALLYWLHRANKDYHILSFFTKRIRLKDGTPVEIIAPIAKGKTIFGNTLDLYGRDHAGVFNYSRERAKEMGTSYIEYVFGKAIYNIIDADSAENVLNHPNLITKGLVYNFLHPFLRTGLLTSTGKKWHARRKMLTPTFHFNILNQFQEIFKTESQKFLLQFEGQDEVTITLHDVIPRFTLNSICETAMGVKLDEMAEKGDRYRENFSQIEECFIRRLSNPLLWGDKLFEMFAAKDFASALDVVHRFSSEIIAKRRDLLKDELDKSSSTADDDGFVSKKRFAMLDTLIYAEKDGLIDHIGICEEVDTLMFEGYDTTSIGLIFGLMNMSLNPDKQELCYQEIQEHIDDDLSNLDVGQLNKLKYLEYFMKETTRLFPSVPIMGREAVQETELANGLILPKGAQITIHVFDIHRNAKYWDSPEEFRPERFLPENVQDRHTYAYVPFSAGQRNCIGKKYAMQEMKTLMVVLLKQFKVLKAIDPQKIVFHTGITLRTQDKIRVKLVRRT | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59433
Sequence Length: 513
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9V557 | MMICLLWISVAILVVIHWIYKVNKDYNILAFFARRVQTKDGKPLDSLVPMIKGRTVFANCFDLLGKDTDQVFTHLRQLAKNSGDSYLQYSMGFSNFNVIDAHNAANILNHPNLITKGVIYNFLHPFLRTGVLTATEKKWHTRRSMLTRTFHLDILNQFQEIFIAESLKFVSQFQGQNEVVVSLKDRISRFTLNSICETAMGIKLDEMAEKGDRYRANFHIIDEGLTRRIVNPLYWDDCVYNMFTGHKYNAALKVVHEFSREIIAKRRVLLEEELENRRATQTADDDICVIRKKRFAMLDTLICAEKDGLIDDIGISEEVDTLMAEGYDTTSIGLVFGLMNMSLYAAEQELCYQEIQEHILDDLSNLNLSQLSKLNYLGYFIKETMRLYPSIPIMGRQTLQETELENGLILPKRSQINIHVFDIHRNPKYWESPEEFRPERFLPQNCLKRHPYAYIPFSAGQRNCIGQKYAMQEMKTLMVVILKHFKILPVIDPKSIVFQVGITLRFKNKIKVKLVRRNCV | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60459
Sequence Length: 520
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9VXY0 | MSTLALVAFVLWAAFLRYLPKILNFLRLQRFAKTLPGPTIGELIANVKKGEILNWLKELREKHGPVFRIWFGKDLMVMFTDPEDIKQLLGNNQLLTKSRNYELLEPWLGKGLLTNGGESWHRRRKLLTPGFHFRILSEFKEPMEENCRILVRRLRTKANGESFDIYPYITLFALDAICETAMGIKKHAQLQSDSEYVQAVQSICRVMHKQSFSFWQRLNVFFKHTKPGKEREAALKVLHDETNRVIRLRREQLIQERNEWKPEAEQDDVGAKRRLAFLDMLLLTQMEGGAELSDTDIREEVDTFMFEGHDTTSSAIAFALSLLSKNPDVQQRAFEEASELEGREKESMPYLEAVIKETLRIYPSVPFFSRKVLEDLEVGKLTVPKGASISCLIYMLHRDPKNFPDPERFDPDRFLVNEKQMHPFAFAAFSAGPRNCIGQKFAMLELKTSLAMLLRSYRFLPDKDHQPKPLAELVTKSGNGIRLRILPRDENGTTA | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57189
Sequence Length: 495
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q6ZWL3 | MAGLWLGLVWQKLLLWGAASALSLAGASLVLSLLQRVASYARKWQQMRPIPTVARAYPLVGHALLMKPDGREFFQQIIEYTEEYRHMPLLKLWVGPVPMVALYNAENVEVILTSSKQIDKSSMYKFLEPWLGLGLLTSTGNKWRSRRKMLTPTFHFTILEDFLDIMNEQANILVKKLEKHINQEAFNCFFYITLCALDIICETAMGKNIGAQSNDDSEYVRAVYRMSEMIFRRIKMPWLWLDLWYLMFKEGWEHKKSLQILHTFTNSVIAERANEMNANEDCRGDGRGSAPSKNKRRAFLDLLLSVTDDEGNRLSHEDIREEVDTFMFEGHDTTAAAINWSLYLLGSNPEVQKKVDHELDDVFGKSDRPATVEDLKKLRYLECVIKETLRLFPSVPLFARSVSEDCEVAGYRVLKGTEAVIIPYALHRDPRYFPNPEEFQPERFFPENAQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILSCILRHFWIESNQKREELGLEGQLILRPSNGIWIKLKRRNADER | Function: A cytochrome P450 monooxygenase involved in fatty acid metabolism in the eye. Catalyzes the omega-hydroxylation of polyunsaturated fatty acids (PUFAs) docosahexaenoate (DHA) and its precursor eicosapentaenoate (EPA), and may contribute to the homeostasis of these retinal PUFAs . Omega hydroxylates saturated fatty acids such as laurate, myristate and palmitate, the catalytic efficiency decreasing in the following order: myristate > laurate > palmitate (C14>C12>C16) . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Catalytic Activity: dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60724
Sequence Length: 525
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
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Q9DBW0 | MLWLWLGLSGQKLLLWGAASAVSLAGATILISIFPMLVSYARKWQQMRSIPSVARAYPLVGHALYMKPNNAEFFQQLIYYTEEFRHLPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRMKMPWLWFDLWYLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDWTGAGRGPIPSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNQKREELGLAGDLILRPNNGIWIKLKRRHEDDP | Function: A cytochrome P450 monooxygenase involved in fatty acid metabolism in the eye. Catalyzes the omega-hydroxylation of polyunsaturated fatty acids (PUFAs) docosahexaenoate (DHA) and its precursor eicosapentaenoate (EPA), and may contribute to the homeostasis of these retinal PUFAs. Omega hydroxylates saturated fatty acids such as laurate, myristate and palmitate, the catalytic efficiency decreasing in the following order: myristate > laurate > palmitate (C14>C12>C16). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Catalytic Activity: dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60939
Sequence Length: 525
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
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Q8N118 | MEFSWLETRWARPFYLAFVFCLALGLLQAIKLYLRRQRLLRDLRPFPAPPTHWFLGHQKFIQDDNMEKLEEIIEKYPRAFPFWIGPFQAFFCIYDPDYAKTLLSRTDPKSQYLQKFSPPLLGKGLAALDGPKWFQHRRLLTPGFHFNILKAYIEVMAHSVKMMLDKWEKICSTQDTSVEVYEHINSMSLDIIMKCAFSKETNCQTNSTHDPYAKAIFELSKIIFHRLYSLLYHSDIIFKLSPQGYRFQKLSRVLNQYTDTIIQERKKSLQAGVKQDNTPKRKYQDFLDIVLSAKDESGSSFSDIDVHSEVSTFLLAGHDTLAASISWILYCLALNPEHQERCREEVRGILGDGSSITWDQLGEMSYTTMCIKETCRLIPAVPSISRDLSKPLTFPDGCTLPAGITVVLSIWGLHHNPAVWKNPKVFDPLRFSQENSDQRHPYAYLPFSAGSRNCIGQEFAMIELKVTIALILLHFRVTPDPTRPLTFPNHFILKPKNGMYLHLKKLSEC | Function: A cytochrome P450 monooxygenase that selectively catalyzes the epoxidation of the last double bond of the arachidonoyl moiety of anandamide, potentially modulating endocannabinoid signaling. Has no hydroxylase activity toward various fatty acids, steroids and prostaglandins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Catalytic Activity: N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + N-(14,15-epoxy-5Z,8Z,11Z-eicosatrienoyl)-ethanolamine + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58875
Sequence Length: 509
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.-
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Q86W10 | MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEFYPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESWVGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELFQHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFSSQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFSEADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLSQMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWEDPQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHSRPPQPVRQVVLKSKNGIHVFAKKVC | Function: A cytochrome P450 monooxygenase that catalyzes the in-chain oxidation of fatty acids . Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates lauric and myristic acids predominantly at the omega-4 and omega-2 positions, respectively . Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Displays an absolute stereoselectivity in the epoxidation of arachidonic acid producing the 14(S),15(R)-epoxyeicosatrienoic acid (EET) enantiomer . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) .
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 59086
Sequence Length: 505
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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Q56686 | MFKNKLAVLFTCLSVFSFSAQSGSFDTVTLGSKGGIQDGNLTAFLIKSEADSNFVMLDAGSVVNGLIVSEQKGAFKDITVPDSSPYTKVGYLLKDRIKGYFISHAHLDHVAGLIISSPDDSKKPIYGLAATNKDLMKNYFNWSAWPNFGNKGEGFKLNKYNYVDLQPGVWSPVAETTMSVVSLPLSHSGGQSTVFILKDSEGDVFAYFGDTGPDEVEKSSAMRTAWSVLAPFVKQGKLKGIIIEVSFTNETPDKSLFGHLTPNWLVKELSVLEDMNGKGSLKDLNVAISHIKYSLKNSEDPKVIIKKQLVEVNDLGVNFIFPEQGDSLQF | Function: Seems to allow the organism to grow on cAMP.
Catalytic Activity: a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+)
Sequence Mass (Da): 36089
Sequence Length: 330
Subcellular Location: Periplasm
EC: 3.1.4.17
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Q8ZD92 | MKYLSIKSASDKIKSGLLKTGVILSFSLFSSLSTAAFEVVALGVDGGVSDGNLTSYLIRNDSQPLYLGLDAGSVLPGIARALEKGHFAAITDAMAAPLTRQGYIFRQSINSYFISHAHLDHVSGLIIGSPDDSKKTIYASADTIDVLRNYYFNWRVWPNFTDSGSGARLGTYRMQVVRPAQSLSLGLTRLTGEMYPLSHDKSPSSMLLISSNNEFFAYFGDTGPDDVEKSKNLDTVWRKLAEKVTQQQLKGMIIEVSYPNDVADNKLFGHMTPTWLLKELKKLEQYSGEGQPLKGLPVVISHIKPSFQQGQDVRKLILSELQQGNDMGIEFILMEQGDSQKFQ | Catalytic Activity: a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+)
Sequence Mass (Da): 37874
Sequence Length: 343
Subcellular Location: Periplasm
EC: 3.1.4.17
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Q2YIF7 | MKRILLAEDDNDMRRFLVKALEKAGYHVTHFDNGASAYERLQEEPFSLLLTDIVMPEMDGIELARRATEIDPDLKIMFITGFAAVALNPDSDAPRDAKVLSKPFHLRDLVNEIEKMLIAA | Function: Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. CpdR is a response regulator substrate of ChpT. Unphosphorylated CpdR controls steady-state levels of CtrA in the B.abortus cell, likely via CtrA destabilization and activation of its proteolysis.
PTM: Is phosphorylated by ChpT-P on Asp-52.
Sequence Mass (Da): 13586
Sequence Length: 120
Subcellular Location: Cytoplasm
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O04147 | MEEVKKDVYSVWALPDEESEPRFKKLMEALRSEFTGPRFVPHVTVAVSAYLTADEAKKMFESACDGLKAYTATVDRVSTGTFFFQCVFLLLQTTPEVMEAGEHCKNHFNCSTTTPYMPHLSLLYAELTEEEKKNAQEKAYTLDSSLDGLSFRLNRLALCKTDTEDKTLETWETVAVCNLNP | Function: Hydrolyzes ADP-ribose 1'',2''-cyclic phosphate (Appr>1) that is produced during tRNA splicing into ADP-ribose 1''-phosphate (Appr-1''p) . Acts also on nucleoside 2',3'-cyclic phosphates .
Catalytic Activity: ADP-alpha-D-ribose 1'',2''-cyclic phosphate + H2O = ADP-alpha-D-ribose 1''-phosphate + H(+)
Sequence Mass (Da): 20514
Sequence Length: 181
Subcellular Location: Cytoplasm
EC: 3.1.4.37
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Q9BZB8 | MALSLEEEAGRIKDCWDNQEAPALSTCSNANIFRRINAILDNSLDFSRVCTTPINRGIHDHLPDFQDSEETVTSRMLFPTSAQESSRGLPDANDLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTHSVLSMLHNPLGNVLGKPPLSFLPLDPLGSDLVDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSLSGGGPRDPLKMGVGSRMDQEQAALAAVTPSPTSASKRWPGASVWPSWDLLEAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGNMPKGYVYLVFELEKSVRSLLQACSHDPLSPDGLSEYYFKMSSRRMRCKEVQVIPWVLADSNFVRSPSQRLDPSRTVFVGALHGMLNAEALAAILNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVSAAFVEIKTTKFTKKVQIDPYLEDSLCHICSSQPGPFFCRDQVCFKYFCRSCWHWRHSMEGLRHHSPLMRNQKNRDSS | Function: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism . In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses (By similarity). Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation (By similarity). Induces the assembly of stress granules in the absence of stress. Required for cell cycle progression, specifically for prophase entry .
PTM: Phosphorylated on serine/threonine residues by AURKA within positions 166 and 197. Phosphorylation and dephosphorylation on Thr-172 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs. Phosphorylation on Thr-172 by AURKA and CAMK2A activates CPEB1. Phosphorylation on Thr-172 may be promoted by APLP1. Phosphorylation increases binding to RNA (By similarity).
Sequence Mass (Da): 62595
Sequence Length: 566
Domain: The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA . The interdomain linker (411-429) acts as a hinge to fix the relative orientation of the 2 RRMs . The ZZ domain (509-566) coordinates 2 Zn ions and is probably implicated in mediating interactions with other proteins in addition to increasing the affinity of the RRMs for the CPEs . A continuous hydrophobic interface is formed between the 2 RRMs .
Subcellular Location: Cytoplasm
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P70166 | MAFSLEEAAGRIKDCWDNQEVPALSTCSNANIFRRINAILDDSLDFSKVCTTPINRGIHDQLPDFQDSEETVTSRMLFPTSAQESPRGLPDANGLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTQSVLSMLQNPLGNVLGKAPLSFLSLDPLGSDLDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSMTGNGPRDPLKMGVGSRMDQEQAALAAVAPSPTSAPKRWPGASVWPSWDLLGAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGNMPKGYVYLVFELEKSVRALLQACSHDPLSPDGLSEYYFKMSSRRMRCKEVQVIPWVLADSNFVWSPSQRLDPSRTVFVGALHGMLNAEALAAILNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVTAAFVEIKTTKFTKKVQIDPYLEDSLCLICSSQPGPFFCRDQVCFKYFCRSCWHWRHSMEGLRHHSPLMRNQKN | Function: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the 3'-UTR of mRNAs. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses. Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation. Induces the assembly of stress granules in the absence of stress (By similarity). Required for cell cycle progression, specifically for prophase entry (By similarity).
PTM: Phosphorylated on serine/threonine residues by AURKA within positions 165 and 196 (By similarity). Phosphorylation and dephosphorylation on Thr-171 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs. Phosphorylation on Thr-171 by AURKA in embryonic ovaries at 16.5 dpc (mostly pachytene oocytes) activates CPEB1. Not phosphorylated on Thr-171 in embryonic ovaries between 18.5 dpc (diplotene oocytes) and metaphase I. Dephosphorylation on Thr-171 by PP1 in embryonic ovaries at 18.5 dpc (mostly diplotene oocytes) inactivates CPEB1. In maturing oocytes, re-phosphorylation on Thr-171 by AURKA reactivates CPEB1. Phosphorylation on Thr-171 by CAMK2A in depolarized hippocampal neurons activates CPEB1. Dephosphorylation on Thr-171 (indirectly by PP1) in hippocampal neurons inactivates CPEB1. Phosphorylation on Thr-171 may be promoted by APLP1. Phosphorylation increases binding to RNA.
Sequence Mass (Da): 61917
Sequence Length: 561
Domain: The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA. The interdomain linker (411-429) acts as a hinge to fix the relative orientation of the 2 RRMs. The ZZ domain (509-566) coordinates 2 Zn ions and is probably implicated in mediating interactions with other proteins in addition to increasing the affinity of the RRMs for the CPEs. A continuous hydrophobic interface is formed between the 2 RRM.
Subcellular Location: Cytoplasm
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Q5R733 | MLFPTSAQESSRGLPDANDLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTHSVLSMLHNPLGNVLGKPPLSFLPLDPLGSDLVDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSLTGGGPRDPLKMGVGSRMDQEQAALAAVTPSPTSASKRWPGASVWPSWDLLEAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGYVYLVFELEKSVRSLLQACSHDPLSPDGLSEYYFKMSSRRMRCKEVQVIPWVLADSNFVRSPSQRLNPSRTVFVGALHGMLNAEALAAILNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVTAAFVEIKTTKFTKKVQIDPYLEDSLCHICSSQPGPFFCRDQVCFKYFCRSCWHWRHSMEGLRHHSPLMRNQKNRDSS | Function: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation. Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses. Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation. Induces the assembly of stress granules in the absence of stress. Required for cell cycle progression, specifically for prophase entry.
PTM: Phosphorylated on serine/threonine residues by AURKA within positions 91 and 122. Phosphorylation and dephosphorylation on Thr-97 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs. Phosphorylation on Thr-97 by AURKA and CAMK2A activates CPEB1. Phosphorylation on Thr-97 may be promoted by APLP1. Phosphorylation increases binding to RNA (By similarity).
Sequence Mass (Da): 53662
Sequence Length: 486
Domain: The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA. The interdomain linker (411-429) acts as a hinge to fix the relative orientation of the 2 RRMs. The ZZ domain (509-566) coordinates 2 Zn ions and is probably implicated in mediating interactions with other proteins in addition to increasing the affinity of the RRMs for the CPEs. A continuous hydrophobic interface is formed between the 2 RRM.
Subcellular Location: Cytoplasm
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Q7TN99 | MQDDLLMDKSKTQPQSQQQQRQQQQQQQQLQPEPGAAEAPSTPLSSEIPKPEDSSAVPALSPASAPPAPNGPDKMQMESPLLPGLSFHQPPQQPPPPQEPTAPGASLSPSFGSTWSTGTTNAVEDSFFQGITPVNGTMLFQNFPHHVNPVFGGTFSPQIGLAQTQHHQQPPPPAPQPPQPAQPPQAQPSQQRRSPASPSQAPYAQRSAAAYGHQPIMTSKPSSSSAVAAAAAAAAASSASSSWNTHQSVNAAWSAPSNPWGGLQAGRDPRRAVGVGVGVGVGVPSPLNPISPLKKPFSSNVIAPPKFPRAAPLTSKSWMEDNAFRTDNGNNLLPFQDRSRPYDTFNLHSLENSLMDMIRTDHEPLKGKHYPNSGPPMSFADIMWRNHFAGRMGINFHHPGTDNIMALNTRSYGRRRGRSSLFPFEDAFLDDSHGDQALSSGLSSPTRCQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACLEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHNDIDKRVEVKPYVLDDQMCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWASIHSRAGREFHKPLVKEGGDRPRHVPFRWS | Function: Sequence-specific RNA-binding protein which acts as a translational repressor in the basal unstimulated state but, following neuronal stimulation, acts as a translational activator . In contrast to CPEB1, does not bind to the cytoplasmic polyadenylation element (CPE), a uridine-rich sequence element within the mRNA 3'-UTR, but binds to a U-rich loop within a stem-loop structure . Required for the consolidation and maintenance of hippocampal-based long term memory . In the basal state, binds to the mRNA 3'-UTR of the glutamate receptors GRIA1 and GRIA2 and negatively regulates their translation . Also represses the translation of DLG4, GRIN1 GRIN2A and GRIN2B . When activated, acts as a translational activator of GRIA1 and GRIA2 . In the basal state, suppresses SUMO2 translation but activates it following neuronal stimulation . Binds to the 3'-UTR of TRPV1 mRNA and represses TRPV1 translation which is required to maintain normal thermoception . Binds actin mRNA, leading to actin translational repression in the basal state and to translational activation following neuronal stimulation . Negatively regulates target mRNA levels by binding to TOB1 which recruits CNOT7/CAF1 to a ternary complex and this leads to target mRNA deadenylation and decay (By similarity). In addition to its role in translation, binds to and inhibits the transcriptional activation activity of STAT5B without affecting its dimerization or DNA-binding activity. This, in turn, represses transcription of the STAT5B target gene EGFR which has been shown to play a role in enhancing learning and memory performance (By similarity). In contrast to CPEB1, CPEB2 and CPEB4, not required for cell cycle progression (By similarity).
PTM: Activated by NEURL1-mediated monoubiquitination, resulting in the growth of new dendritic spines and increased levels of GRIA1 and GRIA2. NEURL1-mediated monoubiquitination facilitates synaptic plasticity and hippocampal-dependent memory storage.
Sequence Mass (Da): 78335
Sequence Length: 716
Domain: The N-terminal Gln-rich region is required for the formation of amyloid-like oligomers and for the stability of long-term potentiation and spatial memory.
Subcellular Location: Cytoplasm
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Q28CH2 | MQDDLLMDKSKAQQRQQPQQPPSSQTQQQQKEAASVAEPPSSRESSPPTHKDKMQMESPLLPGLSFQQEPPTTPSLSPSFGSTWSTGGSNSAVDDSFFPGITPVNGTMLFQNFPHHHHVNPVFGGTFSPQMGLAHQTQQQQRRSPASPNNHTAYTQRNAYSHQPILTNKPSSSPNSSSPSPSNWNNQQNAAWNTPSNPWGAMQPGRDPRRAVGVGVGVGVGVPSPLNPISPLKKTFSSNVIAPPKFSRASPLTPKSWVEDNAFRTDNGNTLLPLQDRNRPYDSFNLHTLENSLMDMIRTDHEPLKARMGLNFHHPGTDNIMALNTRSYGRRRGRSSLFPFEDGFLGDGHGDQSLSSGLSSPTHCQNGERIERYSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACLEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHNDIDKRVEVKPYVLDDQMCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWASIHSRAGREFHKPLVKEGGDRPRHVPFHWS | Function: Sequence-specific RNA-binding protein which acts as a translational repressor in the basal unstimulated state but, following neuronal stimulation, acts as a translational activator (By similarity). Does not bind to the cytoplasmic polyadenylation element (CPE), a uridine-rich sequence element within the mRNA 3'-UTR, but binds to a U-rich loop within a stem-loop structure (By similarity). Required for the consolidation and maintenance of hippocampal-based long term memory (By similarity). Inhibits differentiation of intermediate mesoderm from an early stage to inhibit pronephric differentiation but induce neural differentiation .
Sequence Mass (Da): 70211
Sequence Length: 632
Domain: The N-terminal Gln-rich region is required for the formation of amyloid-like oligomers and for the stability of long-term potentiation and spatial memory.
Subcellular Location: Cytoplasm
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A0A3G1QTU5 | FRSTAAGRCLPVTCCVFPRHFRVSSSSILPSNAKVVGGCKKNRQIAVEAAQSLEVDSQQPMNQEEVSEKMRQLREKIRWMLQNMDDGEISVSPYDTAWVAMVEDIGGGGGPQFPTSLEWISNNQLDDGSWGDLRFLIYDRILNTLACVAVLTQWKMHLHKCQKGLRFIRENIDNLENGNDEMMPVGFEVAFPSLIQTAKKVGIKIPTDSPFMKNIYAKRDLKLRKIPMDILHTKPTTLLHSLEGMEGLDWEKLLNLRTDDGSFLMSPSSTAYVFRHTKDELCHQYLLKSVNKFNGGVPNVYPVDMFEHLWCVDRLQRLGISRYFQVEIQECLDYVYKYWTNKGICWARNTNVQDVDDTAMGFRLLRLHGYDVSTDAFKQFEKAGEFCSFPGQSTDALTGMYNLYRASQTMFNGEHILADAKEYSTNFLHKKRLANAIVDKWIITKDLPGEVGYALDVPFYASLPRLEARFFLEQYGGDDDVWIGKTLYRMLYVNCDTHLELAKLDYEKCQAVHQLEWESIQKWYRDWNLVEFGLSERSLLLAYYIAASTVFEPERSRERLAWAITAILVKTIASQRQLPLETKGESLGSILENEDGGRLIEFLINTIHQLSSEIVVAEGRDITQQLSNTWQKWLKTCKEGGDDDLGEAEARLIVHTLHLSSGLDESSFSHPKYHQLLEATSKVCGQLRLFQSRKQVDVDLATGTTFQIEAGMQELVKLVFTNSSEDLDSLTKQSFFSIARSFYYTAYCDEGAINSHIDKVLFEKID | Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities, and in the production of gibberellins phytohormones . Catalyzes the conversion of (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CPP) .
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl diphosphate
Sequence Mass (Da): 87546
Sequence Length: 766
Domain: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Plant hormone biosynthesis; gibberellin biosynthesis.
Subcellular Location: Plastid
EC: 5.5.1.13
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A0A1W6QDJ1 | MSSSSIVTSLLRPTTAADGVLPRQMAQVNSSCNIWRSKAKVGGINYFNPGNIKCVEEVHKSRQVVVAALKSLEYETEKPTNQDVVSEKMRVLSERIETMLQNMDEGEISISPYDTAWVALVEDTDGRPQFPTSLEWISNNQLADGSWGDRKFVIYDRILNTLACVVALTTWNMHPHKCNRGLRFIRDNMEKLENENEELMPIGFEVVFPSLIEAAQKLGIEIPHIDSPCIKKIQAMRDFKLKRIPMELLHKKPTSLLHSLEGMQGLVWEKLLDFRSDGSFLCSPSSTAYALQHTKDELCLQYLLKAVKKFNGGVPNVYPVDMFEHLWCVDRLQRLGICRYFRVQIKEMLDYVYKYWTDKGICWARNTNVQDVDDTAMGFRLLRMHGYDVSTDVFKQFEKAGEFCCFPGQSTHAITGMYNVYRTSQIMFDGEDILADAKNYSATFLHQKRLANELVDKWIITKDLPGEVGYALDVPFFASLPRLEARFFLEQYGGDDDVWIGKTLYRMPYVNSDTYLELAKLDYKKCQAVHQLEWKSIQKWYRDCKLGEFGLGEKRLLLAYFLAASTAFEPEKKGERLAWAKTAFLVETIASQQLSHEQKREFADEFEHGSSLNMENGGSYKTRTRLVEILSNTVSQLSFETLVAEGRDIKQQLSNTWQKWLKTWEEGGNLGEAEAQLLLQTLHLSSGLDESSFSHPKYHQLLEVTCKVCNQLRLFQNRKAHDAQGGISDLVIGTTFQIEASMQELVKLVFTKSSEDLDSITKQSFFAIARSFYYTAYCDAGAINSHIYKVLFENID | Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities . Catalyzes the conversion of (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CPP) .
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl diphosphate
Sequence Mass (Da): 91115
Sequence Length: 796
Domain: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
EC: 5.5.1.13
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Q0JF02 | MPVFTASFQCVTLFGQPASAADAQPLLQGQRPFLHLHARRRRPCGPMLISKSPPYPASEETREWEADGQHEHTDELRETTTTMIDGIRTALRSIGEGEISISAYDTSLVALLKRLDGGDGPQFPSTIDWIVQNQLPDGSWGDASFFMMGDRIMSTLACVVALKSWNIHTDKCERGLLFIQENMWRLAHEEEDWMLVGFEIALPSLLDMAKDLDLDIPYDEPALKAIYAERERKLAKIPRDVLHSMPTTLLHSLEGMVDLDWEKLLKLRCLDGSFHCSPASTATAFQQTGDQKCFEYLDGIVKKFNGGVPCIYPLDVYERLWAVDRLTRLGISRHFTSEIEDCLDYIFRNWTPDGLAHTKNCPVKDIDDTAMGFRLLRLYGYQVDPCVLKKFEKDGKFFCLHGESNPSSVTPMYNTYRASQLKFPGDDGVLGRAEVFCRSFLQDRRGSNRMKDKWAIAKDIPGEVEYAMDYPWKASLPRIETRLYLDQYGGSGDVWIGKVLHRMTLFCNDLYLKAAKADFSNFQKECRVELNGLRRWYLRSNLEKFGGTDPQTTLMTSYFLASANIFEANRAAERLGWARVALLADAVSSHFRRIGGPKNSTSNLEELISLVPFDDAYSGSLREAWKQWLMAWTAKESSQESIEGDTAILLVRAIEIFGGRHVLTGQRPDLWEYSQLEQLTSSICCKLSRRVLAQENGESTEKVEEIDQQVDLEMQELTRRVLQGCSAINRLTRETFLHVVKSFCYVAYCSPETIDSHIDKVIFQDVI | Function: Catalyzes the conversion of geranylgeranyl diphosphate to the phytoalexin precursor syn-copalyl diphosphate . Required for the biosynthesis of momilactones that exude from roots and act as allelochemicals against lowland weeds in paddy soil .
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = 9alpha-copalyl diphosphate
Sequence Mass (Da): 87217
Sequence Length: 767
Domain: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Subcellular Location: Plastid
EC: 5.5.1.14
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Q54518 | MIDIHSHIVFDVDDGPKSREESKALLAESYRQGVRTIVSTSHRRKGMFETPEEKIAENFLQVREIAKEVADDLVIAYGAEIYYTLDALEKLEKKEIPTLNDSRYALIEFSMHTSYRQIHTGLSNILMLGITPVIAHIERYDALENNEKRVRELIDMGCYTQINSYHVSKPKFFGEKYKFMKKRARYFLERDLVHVVASDMHNLDSRPPYMQQAYDIIAKKYGAKKAKELFVDNPRKIIMDQLI | Function: Dephosphorylates CpsD. Involved in the regulation of capsular polysaccharide biosynthesis.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 28354
Sequence Length: 243
Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
EC: 3.1.3.48
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Q3K0S9 | MNKIANTEVEINIFNLLKKLWKKKFLITFVAIAFATAGLFYSLFIVTPQYTSSTRIYVINPNTPNNSITAQDLQAGSFLANDYKEIITSTDVLEKVISSEKLNYPSSQLLQKITVSILKDTRVISISVEDANPKMSQKLANSVREAAVSKIKAVTQVEDITTLEKGNLPKAPSSPNIKKNVLIGFIVGAGLSTIVLVIMGILDDRVNTEEDIEKALGLTSLGIVPDLNKL | Function: Required for CpsD phosphorylation (By similarity). Involved in the regulation of capsular polysaccharide biosynthesis. May be part of a complex that directs the coordinated polymerization and export to the cell surface of the capsular polysaccharide.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25185
Sequence Length: 230
Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
Subcellular Location: Cell membrane
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B1X536 | MSASLSQLVHQLSARFNNQQQAFDNPPLYAHIVVNCRPLVHLLPGSLLIEQSYAMDPLKPYRIRVLRAQTRDEKLIIFSYSLSDEQKYWGSVYEPERMLKIEEKDLQAIEGCNYIVRKKNSNFIGEVEPGCRCLVDRKGVTTYIVSKFELTNKGEMRTLDRGHNPVTHEQLWGSLGGVFEFNRTTDFSKEIPYDWIEEWKK | Function: Covalently attaches a chromophore to Cys residue(s) of phycobiliproteins.
Sequence Mass (Da): 23416
Sequence Length: 201
Subcellular Location: Plastid
EC: 4.-.-.-
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O65220 | MASSSILIPPILTRRNLLLSTTIATVTPPPPAKPPSPDITITDRVFLDFSLCPTYFRSDPSATLSSTTPCSDSTPLGRVVLGLYGRHVPITVSTFKRMCTSSSTSYKNTPVHKIFPGQYFLAGRQGGGRRDTAEVGYSLRDLPRNTDVVNSKAFLLPHARAGVVSLCLSENDDDDDIRLDPDYRNVEFLITTGPGPSPQLDGGNIVFGTVLEGLDVVTSISSIPTYKPSENIKQFNDFAEFLGDERAQNARSLWNRPLKTVFISGCGELKVTNPSLSPTLP | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
PTM: S-nytrosylated during the hypersensitive disease resistance response.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 30505
Sequence Length: 281
Subcellular Location: Plastid
EC: 5.2.1.8
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Q6Q152 | MSTVYVLEPPTKGKVIVNTTHGPIDVELWPKEAPKSVRNFVQLCLEGYFDNTIFHRVIPGFLVQGGDPTGSGTGGDSIYGGVFADEFHSRLRFSHRGIVAMANASSPNSNGSQFFFTLDKCDWLDKKHTIFGKVTGDSIYNLLRLGEVDTSKDDRPLDPAPKILSVEVLWNPFEDIVPRVLAKTSEESAAEIKEPPTKPVKKLNLLSFGEEAEEEEKELAVVKQKIKSSHDVLNDPRLLKAEASDKERNASESKEVLSVREALNAKKEAAQKDKSFSVSDTVGNSDDDDDGEDETKFDAKMRNQVLSRRKEIGDTPSKPTQKKKSSSLKGREESTQRSDAVSSEDEKPRMEKLSLKKKGIGSEAKAEHMEKGDTDLQLYNASERARQLHKLKKRRLQGNEDSVLAKLEKFKQSISAKPFTSSNEPVVLTSSSEPVDNKEEDLSDWKNVKLKFAPERGKDKMSRRDDPDAYMVVDPLLEKGKEKFNRMQAKQKRREREWSGKSLA | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Involved in plant response to pathogen infection by increasing PAD4 expression in absence of EDS1 up-regulation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 56515
Sequence Length: 504
Subcellular Location: Nucleus
EC: 5.2.1.8
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Q8W4D0 | MEEESKNGGTTIPTEELAVVAVPPVVEEEEPMVGPGPAPRGKRKRPLQFEQAYLDSLPSANMYEKSYMHRDVVTHVAVSAAEFFISGSMDGHLKFWKKKGVGIEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYDMMAMIRLPYIPGAVEWVYKQGDVKAKLAVSDRDSLFVHIYDPRSGSNEPIASKEIHMNPIKVMKYNPVSDTMISGDTKGIIEYWSATTLQFPEDEVNFKLKSDTNLFEIIKCKTTISAIEVSPDGKQFSITAPDRRIRVFWFRTGKLRRVYDESLVVAQDLQRSDAPLYRLEAIDFGRRMAVEKELEKTESAPQPNAVFDESSNFLIYATFLGIKVINLHTNTVARILGKVESNERYLRVALYQGDQGGKKVRKIPAAAANVNESKEPLTDPTILCCAFKKHRIYMFSRREPEEPEDASQGRDVFNEKPAADELMSVSDIGNSATTSLPENVIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHDRPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNVTVPKS | Function: PPIases accelerate the folding of proteins (Probable). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides . Histone proline isomerase that increases the rate of cis-trans isomerization of the synthetic histone H3 peptides H3P30 (RKSAP30F-p-nitroanilide) and H3P30K27me3 (RKme3-SAP30F-p-nitroanilide) in the histone H3 N-terminal tail, in vitro . Histone remodeling factor involved in chromatin-based gene silencing . Reinforces H3K27 methylation . Involved in fundamental processes of chromatin assembly and histone modification by mediating the targeting of FAS1 and LHP1 on the chromatin . Required for the formation and development of leaves, for normal phyllotaxy and for the formation, maintenance and activity of root and shoot apical meristems .
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 70984
Sequence Length: 631
Subcellular Location: Nucleus
EC: 5.2.1.8
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Q91WE4 | MVCIPCIVIPVLLWIFKKFLEPYIYPVVSRIWPKKAVQQSGDKNMSKVDCKGAGTNGLPTKGPTEVSDKKKD | Function: May activate the NF-kappa-B signaling pathway.
PTM: Undergoes ER-associated degradation (ERAD).
Sequence Mass (Da): 8036
Sequence Length: 72
Subcellular Location: Endoplasmic reticulum
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B1WC88 | MVCIPCIVIPVLLWIFKKFLEPYIYPVVSRIWPRKAVQQLDNKNTGKVDCKGADTNGFSTKGPTEVSDKKKD | Function: May activate the NF-kappa-B signaling pathway.
PTM: Undergoes ER-associated degradation (ERAD).
Sequence Mass (Da): 8169
Sequence Length: 72
Subcellular Location: Endoplasmic reticulum
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A0A0M5K865 | MVKLYCAVVGVAGSAFSVRVDESDTVDDLKDAIKAKKPNDFKDIDADKLELYVAKRDGVWLTEADVKSGVADITGLVRLEVVRAKLFSVGLSDEVVSEVDAQEEAAGRGPVNVLVVVPMKKRRVDAGVDEERRFFDTRDFPPLLAPPQRGATVESPEAQWEKLLNSLEWKEPKRLCASSGQNWPYQGESELAGHLVEPLALHYTAWYLQNEDKQNHAINLVLSGPGTGKSRMLDQMKGLMCAAAARSNNRKLKERMENAFVFSVTFENGTSATGSLLDRDNPEFDISYRMLYQLSKDRPNWKKFAKTLKSYRSLELDIEAAIGILAKLKGIDDVKKMTVILCVDGLQKLVNDGTKSCDFYRVLASVCSFLNSSRAFAVCVCSATIQSPVDKALSDSPQKRVFLVPPPLRGHEVLPTKTRIEKQLVDDMGGHGRALETLQLFLSHYTKDQLEEMDPTWMFEKVCDALRLQYGDIFASPFFQDPYNCREVLAAILSRRRYKLFDRIGRTDMTVDCLRSFGLFRWGAEGHLECAFILLVLLMQKLPKKLGEVDNFDDHLTRTVLVWQRFEQFVAFYRRVKSIAYCETPVALSSFHAGARFGAIQDIIITEPTSRTVVEALRQEDTKSSSDDSTCFTNRDGGVKISDMDTIVINGASASAGDLFMRVQLKVGRQNVQCNEVIQCKLLQTKQKIHEDAYAKERAKAANESSDVFLLVTPAQATEFDLPPRCGLVSANEFGRYFGPFTSRAYRSFLEPPNINTASFHELRRLEGVGDATAAKIIAERTIRRFSNLEDALNRLVPSKKGKTAMILSRMHYDDDEADL | Function: Secreted effector that suppresses plant basal defense and promotes plant susceptibility via targeting promoters of host HSP gene and thus inhibiting their expression. CRN108 binds directly to heat shock elements (HSEs) 5'-GAAnnTTC-3' and interferes with the association of the HSE with the plant heat shock transcription factors, which initializes HSP gene expression in response to stress.
Sequence Mass (Da): 91945
Sequence Length: 820
Domain: The CRN proteins have modular architectures that include a signal peptide, a conserved N-terminus, and highly diverse C-terminal domains. The conserved CRN N-terminus harbors a distinct LXLFLAK motif, which is followed by the conserved DWL domain. A highly conserved HVLVXXP motif marks the end of the CRN N-terminal domains and forms a junction where diverse C-terminal domains are fused. The conserved CRN N-terminus mediates the translocation into the plant host cells.
Subcellular Location: Secreted
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E9M7A1 | MVKLFCAIVGVAGSAFPVDIDGGQSVGDLKKAIKAESEDITIPAKDLKLFLAKTEGGAWLPDDDQAALDLEDGKVHEDIQALIDGEKMKATWTIEDVLTANNMTKRKGRAPKSRQIHVLVVVPEGAFGSASETSKMDQLVEKVDKMYEQTVLGKRKYVHSEVTSTQGRQLLNDLDIRVEFVRTVPFDAGEGSSVDPYEWKRVIIENGEEVVLTEEQQRKRYRRYVEHNIGTVLKETQLCVIGVERGTNILTVKVPGREIELAGRTDLLILSDLVAMRPTEVQYLPGVKMLIEVKRDVKASNDFQALSELIALDLLVDDPVMALLTDLEGEWIFFWVAEKINSSARIHKAAINKPGEAFEVIRALLVQPPTAPADTDTTEIKLPYFQSPVKRLKLRKALPPIGEGGDNGGIRESIERYYDIASMLGPDIEMARAVARQVTRSIPTFSYFS | Function: Secreted effector that, with CRN63, is critical to pathogenesis by modulating host defenses . Suppresses cell death elicited by the P.sojae necrosis-inducing protein or CRN63 . CRN115 and CRN63 may share the same molecular host targets that are involved in the cell death signal transduction pathway and that their differential activities are dependent on plant nuclear localization or not .
Sequence Mass (Da): 49875
Sequence Length: 449
Domain: The CRN proteins have modular architectures that include a signal peptide, a conserved N-terminus, and highly diverse C-terminal domains. The conserved CRN N-terminus harbors a distinct LXLFLAK motif, which is followed by the conserved DWL domain. A highly conserved HVLVXXP motif marks the end of the CRN N-terminal domains and forms a junction where diverse C-terminal domains are fused. The conserved CRN N-terminus mediates the translocation into the plant host cells.
Subcellular Location: Secreted
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D0CCT2 | MYKLMKNIQTTALNRTTLMFPLALVLFEFAVYIGNDLIQPAMLAITEDFGVSATWAPSSMSFYLLGGASVAWLLGPLSDRLGRKKVLLSGVLFFALCCFLILLTRQIEHFLTLRFLQGIGLSVISAVGYAAIQENFAERDAIKVMALMANISLLAPLLGPVLGAFLIDYVSWHWGFVAIALLALLSWVGLKKQMPSHKVSVTKQPFSYLFDDFKKVFSNRQFLGLTLALPLVGMPLMLWIALSPIILVDELKLTSVQYGLAQFPVFLGLIVGNIVLIKIIDRLALGKTVLIGLPIMLTGTLILILGVVWQAYLIPCLLIGMTLICFGEGISFSVLYRFALMSSEVSKGTVAAAVSMLLMTSFFAMIELVRYLYTQFHLWAFVLSAFAFIALWFTQPRLALKREMQERVAQDLH | Function: Efflux pump that mediates resistance to chloramphenicol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45882
Sequence Length: 413
Subcellular Location: Cell inner membrane
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Q96SW2 | MAGEGDQQDAAHNMGNHLPLLPAESEEEDEMEVEDQDSKEAKKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL | Function: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 or ILF2 . Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8 . Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons . Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 . May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism (By similarity). Plays a negative role in TLR4 signaling by interacting with TRAF6 and ECSIT, leading to inhibition of ECSIT ubiquitination, an important step of the signaling .
PTM: Ubiquitinated, ubiquitination is mediated by its own DCX protein ligase complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50546
Sequence Length: 442
Domain: The CULT domain binds thalidomide and related drugs, such as pomalidomide and lenalidomide. Drug binding leads to a change in substrate specificity of the human DCX (DDB1-CUL4-X-box) E3 protein ligase complex, while no such change is observed in rodents.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q12289 | MSSDTSLSESSLLKEESGSLTKSRPPIKSNPVRENIKSFVAGGVGGVCAVFTGHPFDLIKVRCQNGQANSTVHAITNIIKEAKTQVKGTLFTNSVKGFYKGVIPPLLGVTPIFAVSFWGYDVGKKLVTFNNKQGGSNELTMGQMAAAGFISAIPTTLVTAPTERVKVVLQTSSKGSFIQAAKTIVKEGGIASLFKGSLATLARDGPGSALYFASYEISKNYLNSRQPRQDAGKDEPVNILNVCLAGGIAGMSMWLAVFPIDTIKTKLQASSTRQNMLSATKEIYLQRGGIKGFFPGLGPALLRSFPANAATFLGVEMTHSLFKKYGI | Function: Transports carnitine, acetylcarnitine, propionylcarnitine and to a much lower extent medium- and long-chain acylcarnitines.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34754
Sequence Length: 327
Subcellular Location: Mitochondrion inner membrane
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Q9FIL7 | MPMRSKTPTPLRFSNGKHQRDDSEYSWTDVGTGEKARNVSVLGAIRRAAKKVFVIIFLGQRKLKPTECRSDPGESSTHDRESTLSGWTGYSSPSSFGRSTERKVSGQYRFSGSRFQSPGKDSSSSKSWHQGPVIFSFGELQRATANFSSVHQIGEGGFGTVFKGKLDDGTIVAIKRARKNNYGKSWLLEFKNEIYTLSKIEHMNLVKLYGFLEHGDEKVIVVEYVANGNLREHLDGLRGNRLEMAERLEIAIDVAHALTYLHTYTDSPIIHRDIKASNILITNKLRAKVADFGFARLVSEDLGATHISTQVKGSAGYVDPDYLRTFQLTDKSDVYSFGVLLVEILTGRRPIELKRPRKDRLTVKWALRRLKDDEAVLIMDPFLKRNRAAIEVAEKMLRLASECVTPTRATRPAMKGIAEKLWAIRREMKETMICSSASNSSCSSTTHSFIGRDSDRYALPRIEDNENSIE | PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52879
Sequence Length: 470
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P47866 | MDAALLLSLLEANCSLALAEELLLDGWGEPPDPEGPYSYCNTTLDQIGTCWPQSAPGALVERPCPEYFNGIKYNTTRNAYRECLENGTWASRVNYSHCEPILDDKQRKYDLHYRIALIINYLGHCVSVVALVAAFLLFLVLRSIRCLRNVIHWNLITTFILRNITWFLLQLIDHEVHEGNEVWCRCVTTIFNYFVVTNFFWMFVEGCYLHTAIVMTYSTEHLRKWLFLFIGWCIPCPIIVAWAVGKLYYENEQCWFGKEPGDLVDYIYQGPIILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDDLSQIVFIYFNSFLQSFQGFFVSVFYCFFNGEVRSALRKRWHRWQDHHALRVPVARAMSIPTSPTRISFHSIKQTAAV | Function: G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels.
PTM: A N-glycosylation site within the signal peptide impedes its proper cleavage and function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47693
Sequence Length: 411
Domain: The transmembrane domain is composed of seven transmembrane helices that are arranged in V-shape. Transmembrane helix 7 assumes a sharply kinked structure (By similarity).
Subcellular Location: Cell membrane
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O42603 | MDSTIFEIIIDEFDANCSLLDAFQDSFLHSESSSFFGFEGPYCSATIDQIGTCWPRSLAGELVERPCPDSFNGIRYNTTRNVYRECFENGTWASWMNYSQCVPILDNKRKYALHYKIALIINYLGHCISILALVIAFLLFLCLRSIRCLRNIIHWNLITTFILRNIMWFLLQMIDHNIHESNEVWCRCITTIYNYFVVTNFFWMFVEGCYLHTAIVMTYSTDKLRKWVFLFIGWCIPSPIIVTWAICKLFYENEQCWIGKEPGKYIDYIYQGRVILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDDVSQIVFIYFNSFLQSFQGFFVSVFYCFLNGEVRSAARKRWHRWQDHHSLRVRVARAMSIPTSPTRISFHSIKQTAAV | Function: G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels (By similarity).
PTM: A N-glycosylation site within the signal peptide impedes its proper cleavage and function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48459
Sequence Length: 413
Domain: The transmembrane domain is composed of seven transmembrane helices that are arranged in V-shape. Transmembrane helix 7 assumes a sharply kinked structure (By similarity).
Subcellular Location: Cell membrane
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P38892 | MPKTSYLNKNFESAHYNNVRPSYPLSLVNEIMKFHKGTRKSLVDIGCGTGKATFVVEPYFKEVIGIDPSSAMLSIAEKETNERRLDKKIRFINAPGEDLSSIRPESVDMVISAEAIHWCNLERLFQQVSSILRSDGTFAFWFYIQPEFVDFPEALNVYYKYGWSKDYMGKYLNDNQREILLNYGGEKLRSLLSDRFGDIEVTIYSPSDPNASTVTAENSQFLWRAAITLNQFKEFVKSWSIYTSWARDNPSKPDIADIFINELKEICHCEDLNVPLKIEWSTFYYLCRKRE | Function: Probable S-adenosylmethionine-dependent methyltransferase which mediates cantharidin resistance.
Sequence Mass (Da): 33785
Sequence Length: 291
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q8GY82 | MAVTSLLDTVFRRRKKKSTEFISFFEFDLDTIKAATNDFSELVGRGGFGFVYKGRLQNGQEIAVKILSTSSIRTERQFHNELIILSKLKHKNLINLLGFCTKRDQHGLVYEFMPNSSLDCFILDPHRAAQLNWEMCRNIIDGIARGLRYLHEESGLWVVHRDIKPGNILLDSDLKPKIVGFELARTMQQGENAAETTEIVGTVGYLDPEYIRSGRVSVKSDVYAFGVTILTIISRRKAWSVDGDSLIKYVRRCWNRGEAIDVIHEVMREEEREYSISEILRYIHIALLCVDENAERRPNIDKVLHWFSCFSTPLPDPTFGNRFLVEEETNWPWSPSLSPGHSSVTSPISSR | Function: Forms a complex with CRK36 that may negatively control abscisic acid (ABA) and osmotic stress signal transduction . Involved in plant response to ABA during seed germination, early seedling growth and responses to abiotic stresses by inducing the expression of ABA-responsive genes and stress-inducible genes . Acts as positive regulator in disease resistance, downstream of NPR1 and WRKY70 .
PTM: Autophosphorylated and phosphorylated by CRK36.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 40231
Sequence Length: 351
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9M0G5 | MASTLISSLAVVLPLTLLAPSMSMKISRIDVLGYICNNGTVSNEEAYRRSYQINLDAIRGDMRHVKFGTHEHGDPPERMYVLSQCVSDLSSDECSLCWSRATDLLSQCFPATGGWFHLDGCFVRADNYSFYQEPVSHQDTKICASDKEKSAEFKGLVKEVTKSIVEAAPYSRGFSVAKMGIRDLTVYGLGVCWRTLNDELCKLCLADGALSVTSCLPSKEGFALNAGCYLRYSNYTFYNERGLLAMSFTKENLTYIFVISMVGVLAIAAGFWCGKCFYMRTSPKKKIKGTKTKKFHLFGHLRIEKESESICTESHLMSFEYSTLKKATNNFNESCKLGVGGYGEVFKGTLSDGREIAIKRLHVSGKKPRDEIHNEIDVISRCQHKNLVRLLGCCFTNMNSFIVYEFLANTSLDHILFNPEKKKELDWKKRRTIILGTAEGLEYLHETCKIIHRDIKASNILLDLKYKPKISDFGLAKFYPEGGKDIPASSLSPSSIAGTLGYMAPEYISKGRLSNKIDAYSFGVLVLEITSGFRNNKFRSDNSLETLVTQVWKCFASNKMEEMIDKDMGEDTDKQEMKRVMQIGLLCTQESPQLRPTMSKVIQMVSSTDIVLPTPTKPPFLHDSM | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70182
Sequence Length: 625
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9C5S8 | MSAYTSLNFLFLLTFFIGSLRVSAQLQDPTYVGHVCTNRISRNSIYFSNLQTLLTSLSSNNAYFSLGSHSLTKGQNSDMVFGLYLCKGDLSPESCRECVIFAAKDTRSRCPGGKEFLIQYDECMLGYSDRNIFMDTVTTTTIITWNTQKVTADQSDRFNDAVLSLMKKSAEEAANSTSKKFAVKKSDFSSSQSLYASVQCIPDLTSEDCVMCLQQSIKELYFNKVGGRFLVPSCNSRYEVYPFYKETIEGTVLPPPVSAPPLPLVSTPSFPPGKGKNSTVIIIAIVVPVAISVLICVAVFSFHASKRAKKTYDTPEEDDITTAGSLQFDFKVIEAATDKFSMCNKLGQGGFGQVYKGTLPNGVQVAVKRLSKTSGQGEKEFKNEVVVVAKLQHRNLVKLLGFCLEREEKILVYEFVSNKSLDYFLFDSRMQSQLDWTTRYKIIGGIARGILYLHQDSRLTIIHRDLKAGNILLDADMNPKVADFGMARIFEIDQTEAHTRRVVGTYGYMSPEYAMYGQFSMKSDVYSFGVLVLEIISGRKNSSLYQMDASFGNLVTYTWRLWSDGSPLDLVDSSFRDSYQRNEIIRCIHIALLCVQEDTENRPTMSAIVQMLTTSSIALAVPQPPGFFFRSNHEQAGPSMDKSSLCSIDAASITILAPR | Function: Involved in multiple distinct defense responses. May function as a disease resistance (R) protein.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73402
Sequence Length: 659
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9C5S9 | MSSLISFNFLFLFSFLTSSFTASAQDPFYLNHYCPNTTTYSSNSTYSTNLRTLLSSLSSRNASYSTGFQNATAGKAPDRVTGLFLCRGDVSPEVCRNCVAFSVNQTLNLCPKVREAVFYYEQCILRYSHKNILSTAITNEGEFILSNTNTISPNQKQIDGFTSFVSSTMSEAAGKAANSSRKLYTVNTELTAYQNLYGLLQCTPDLTRADCLSCLQSSINGMALSRIGARLYWPSCTARYELYPFYNESAIETPPLPPPPPPPPPRESLVSTPPISSSSLPGKSGNSTVLVVAVVVLAVLLFIALVGYCFLAKKKKKTFDTASASEVGDDMATADSLQLDYRTIQTATNDFAESNKIGRGGFGEVYKGTFSNGKEVAVKRLSKNSRQGEAEFKTEVVVVAKLQHRNLVRLLGFSLQGEERILVYEYMPNKSLDCLLFDPTKQIQLDWMQRYNIIGGIARGILYLHQDSRLTIIHRDLKASNILLDADINPKIADFGMARIFGLDQTQDNTSRIVGTYGYMAPEYAMHGQFSMKSDVYSFGVLVLEIISGRKNSSFGESDGAQDLLTHAWRLWTNKKALDLVDPLIAENCQNSEVVRCIHIGLLCVQEDPAKRPAISTVFMMLTSNTVTLPVPRQPGFFIQCRAVKDPLDSDQSTTTKSFPASIDDESITDLYPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74501
Sequence Length: 674
Subcellular Location: Membrane
EC: 2.7.11.-
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Q0D5R3 | MRRHRPYLDGVAAAAATFLLAVLLHAPLAAGEDEPPPWVLCGPYPPSGNYSKNGTYQVNLDLLSTTLPKNTSSSPAMYATGTVGDVPDKVYGLALCRGDANASACERCVAAALRDAPRRCPLVKDVLVFYDLCQLRYSNRDFFLDDDYFVTTYTLQRSRRVGAAAAAAFDAAVAVLVNATADYAAADSSRRYGTGEEEGVDGDSDRPKIYALAQCTPDKTPEVCRTCLSTVIGQLPKEFSGRTGGGMFGVWCNFRYEVFPFFSGRPLLQLPAFVETPPPPPSPSATSGEKTKNRIGTVLAIVMPAIAAILLMVVACFCCWKRIKKRRPEEQTFLSYSVSSDDIQSIDSLILDLPTIRVATDDFADTKMIGQGGFGMVYKGVLPDGQEIAVKRLCQSSRQGIGELKSELILVAKLYHKNLVRLIGVCLEQQEKILVYEYMPNGSLDIVLFDTDKNRELDWGKRFKIINGIARGLQYLHEDSQLKIVHRDLKASNILLDFDYSPKISDFGLAKIFGGDQSEDVTNRIAGTYGYMAPEYAMRGNYSIKSDVFSFGVLVLEIITGRRNTGSYDSGQDVDLLNLVWEHWTRGNVVELIDPSMGDHPPIEQMLKCIHIGLLCVQKKPASRPTISSVNIMLSSNTVRLPSLSRPAFCIQEVSASDSSNPYSERYPRPRHSGYSDNSTVVSSNDLSITELVPR | Function: Involved in disease resistance. Required for NPR1/NH1-mediated immunity to the bacterial blight pathogen Xanthomomas oryzae pv. oryzae (Xoo). Required for the benzothiadiazole (BTH)-induced immune response. Possesses kinase activity in vitro.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76461
Sequence Length: 695
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8L7G3 | MSSLFPFIFLFLFSFLTSFRASAQDPRFLAYYCPNATTYSSNSTYLTNLKTLLSSLSSRNASYSTGFQNATVGQALDRVTGLFLCRGDVSPEVCRNCVTFAVNNTFSRCPNQREAVFYYEECILRYSHKNILSTAITNEGEFILRNPNHISPIQNQINQFTNLVLSNMNQIAIEAADNPRKFSTIKTELTALQTFYGLVQCTPDLSRQNCMNCLTSSINRMPFSRIGARQFWPSCNSRYELYDFYNETAIGTPPPPLPPLASPSLSDKSGNSNVVVVAVVVPIIVAVLIFIAGYCFFAKRAKKTYGTTPALDEDDKTTIESLQLDYRAIQAATNDFSENNKIGRGGFGDVYKGTFSNGTEVAVKRLSKTSEQGDTEFKNEVVVVANLRHKNLVRILGFSIEREERILVYEYVENKSLDNFLFDPAKKGQLYWTQRYHIIGGIARGILYLHQDSRLTIIHRDLKASNILLDADMNPKIADFGMARIFGMDQTQQNTSRIVGTYGYMSPEYAMRGQFSMKSDVYSFGVLVLEIISGRKNNSFIETDDAQDLVTHAWRLWRNGTALDLVDPFIADSCRKSEVVRCTHIGLLCVQEDPVKRPAMSTISVMLTSNTMALPAPQQPGFFVRSRPGTNRLDSDQSTTNKSVTVSIDDKSMSDLDPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73925
Sequence Length: 659
Subcellular Location: Membrane
EC: 2.7.11.-
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O65468 | MYIVSMFGLAGLEALICFIFLFLFSFLTSFKASAQNPFYLNHDCPNRTTYSSNSTYSTNLKTLLSSFASRNASYSTGFQNIRAGQTPDRVTGLFLCRGDLSPEVCSNCVAFSVNESLTRCPNQREAVFYYEECILRYSHKNFLSTVTYEGELIMRNPNNISSIQNQRDQFIDLVQSNMNQAANEAANSSRKFSTIKTELTSLQTLYGLVQCTPDLARQDCFSCLTSSINRMMPLFRIGARQFWPSCNSRYELYAFYNETAIGTPSPPPLFPGSTPPLTSPSIPGKSGNSTVLVVAIVVLAVLLFIALVGYCFLAQRTKKTFDTASASEVGDDMATADSLQLDYRTIQTATNDFAESNKIGRGGFGEVYKGTFSNGKEVAVKRLSKNSRQGEAEFKTEVVVVAKLQHRNLVRLLGFSLQGEERILVYEYMPNKSLDCLLFDPTKQTQLDWMQRYNIIGGIARGILYLHQDSRLTIIHRDLKASNILLDADINPKIADFGMARIFGLDQTQDNTSRIVGTYGYMAPEYAMHGQFSMKSDVYSFGVLVLEIISGRKNSSFDESDGAQDLLTHTWRLWTNRTALDLVDPLIANNCQNSEVVRCIHIGLLCVQEDPAKRPTISTVFMMLTSNTVTLPVPRQPGFFIQSSPVKDPTDSDQSTTTKSTPASIDDELITDLYPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75412
Sequence Length: 676
Subcellular Location: Membrane
EC: 2.7.11.-
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Q04929 | MAGQFDSEDRGSWYWGRLSRGDAVSLLQGQRHGTFLVRDSGSIPGDFVLSVSESSRVSHYIVNSLGPAGGRRAGGEGPGAPGLNPTRFRIGDQEFDSLPSLLEFYKIHYLDTTTLIEPVSRSRQNSGVILRQEEVEYVRALFDFNGNDDEDLPFKKGDILKIRDKPEEQWWNAEDMDGKRGMIPVPYVEKCRPSSASVSTLTGGNQDSSHPQPLGGPEPGPYAQPSINTPLPNLQNGPFYARVIQKRVPNAYDKTALALEVGELVKVTKINMSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS | Function: May mediate attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility (By similarity). Involved in cell branching and adhesion (By similarity). May regulate the EFNA5-EPHA3 signaling (By similarity).
PTM: Phosphorylated on Tyr-222 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-222 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway (By similarity).
Sequence Mass (Da): 33806
Sequence Length: 305
Subcellular Location: Cytoplasm
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P46108 | MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVSRSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS | Function: Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1.
PTM: Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway . Isoform Crk-II: Phosphorylated by KIT (By similarity).
Sequence Mass (Da): 33831
Sequence Length: 304
Domain: The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation.
Subcellular Location: Cytoplasm
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Q64010 | MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVARSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS | Function: Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1.
PTM: Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway . Isoform Crk-II: Phosphorylated by KIT (By similarity).
Sequence Mass (Da): 33815
Sequence Length: 304
Domain: The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation.
Subcellular Location: Cytoplasm
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Q8NSP8 | MMEKIRLILLSSRPISWINTAYPFGLAYLLNAGEIDWLFWLGIVFFLIPYNIAMYGINDVFDYESDMRNPRKGGVEGAVLPKSSHSTLLWASAISTIPFLVILFIFGTWMSSLWLTLSVLAVIAYSAPKLRFKERPFIDALTSSTHFTSPALIGATITGTSPSAAMWIALGSFFLWGMASQILGAVQDVNADREANLSSIATVIGARGAIRLSVVLYLLAAVLVTTLPNPAWIIGIAILTYVFNAARFWNITDASCEQANRSWKVFLWLNYFVGAVITILLIAIHQI | Function: Catalyzes the elongation of the C(40) carotenoid all-trans-lycopene to the acyclic C(50) carotenoid flavuxanthin during decaprenoxanthin biosynthesis . Acts as a bifunctional enzyme that catalyzes the elongation of lycopene by attaching a C(5) isoprene unit at C-2, as well as the hydroxylation of the new isoprene unit. The enzyme acts at both ends of the substrate, forming the C(50) carotenoid flavuxanthin via the C(45) intermediate nonaflavuxanthin (By similarity).
Catalytic Activity: A + all-trans-lycopene + dimethylallyl diphosphate + H2O = AH2 + diphosphate + nonaflavuxanthin
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31705
Sequence Length: 287
Pathway: Carotenoid biosynthesis.
Subcellular Location: Cell membrane
EC: 2.5.1.149
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P54976 | MAFEQRIEAAMAAAIARGQGSEAPSKLATALDYAVTPGGARIRPTLLLSVATACGDDRPALSDAAAVALELIHCASLVHDDLPCFDDAEIRRGKPTVHRAYSEPLAILTGDSLIVMGFEVLARAAADQPQRALQLVTALAVRTGMPMGICAGQGWESESQINLSAYHRAKTGALFIAATQMGAIAAGYEAEPWEELGARIGEAFQVADDLRDALCDAETLGKPAGQDEIHARPNAVREYGVEGAAKRLKDILGGAIASIPSCPGEAMLAEMVRRYAEKIVPAQVAARV | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate
Sequence Mass (Da): 30229
Sequence Length: 288
Pathway: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1.
EC: 2.5.1.29
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P48368 | MKPLQTNFNLLTYLYERKEIVEDTLNKSIPRGNPTFIYDSIRYSLSAGGKRIRPILCLASCELAGGTMEMALPTACALEMIHTMSLIHDDLPAMDNDSYRRGKPTNHIIYGEDLAILAGDALLAYAFEFIATQTKNVPADLIVKVIAQVAHSVTTSGLVGGQIIDLSSEGKSDTTLETLNFIHIHKTGALLEAAVLSGALLAGAKEKDMNRFLRYAQNIGLAFQIIDDVLDIISTEEKLGKSIGKDLKTQKATYPSFWGVEESIKQAELLVEEAKEEILYFDNKAIPLIAIADFIVNRNN | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate
Sequence Mass (Da): 33008
Sequence Length: 300
Pathway: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1.
Subcellular Location: Plastid
EC: 2.5.1.29
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P22873 | MVSGSKAGVSPHREIEVMRQSIDDHLAGLLPETDSQDIVSLAMREGVMAPGKRIRPLLMLLAARDLRYQGSMPTLLDLACAVELTHTASLMLDDMPCMDNAELRRGQPTTHKKFGESVAILASVGLLSKAFGLIAATGDLPGERRAQAVNELSTAVGVQGLVLGQFRDLNDAALDRTPDAILSTNHLKTGILFSAMLQIVAIASASSPSTRETLHAFALDFGQAFQLLDDLRDDHPETGKDRNKDAGKSTLVNRLGADAARQKLREHIDSADKHLTFACPQGGAIRQFMHLWFGHHLADWSPVMKIA | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate
Sequence Mass (Da): 33242
Sequence Length: 307
Pathway: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1.
EC: 2.5.1.29
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B1XJV9 | MVVADAHTQGFSLAQYLQEQKTIVETALDQSLVITEPVTIYEAMRYSLLAGGKRLRPILCLAACEMLGGTAAMAMNTACALEMIHTMSLIHDDLPAMDNDDLRRGKPTNHKVYGEDIAILAGDALLSYAFEYVARTPDVPAERLLQVIVRLGQAVGAEGLVGGQVVDLESEGKTDVAVETLNFIHTHKTGALLEVCVTAGAILAGAKPEEVQLLSRYAQNIGLAFQIVDDILDITATAEELGKTAGKDLEAQKVTYPSLWGIEKSQAEAQKLVAEAIASLEPYGEKANPLKALAEYIVNRKN | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the sequential condensation of three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to yield geranylgeranyl diphosphate (GGPP). Thereby, is a key enzyme for the biosynthesis of terpenenoids.
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate
Sequence Mass (Da): 32477
Sequence Length: 302
Pathway: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.
EC: 2.5.1.29
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P54906 | MSALRPPARGGLGLSRLGVRLAGSRRFQLIAERVPFLRRIGRREGEELFDIVAGFVHSQVLYALVELRVLHLVAEGPQTVQALAAATGLAPERMQLLLQGGAALKLLTRRRDGQFDLAVRGAAFLAVPGLEAMVGHHHVLYRDLADPVAFLKGETEPELARFWPYVFGAGGATDPEVTAKYSRLMTESQGLVAEDALRLVDLMGVRRLMDVGGGTGAFLAAVGRAYPLMELMLFDLPVVAEAAPQRLTEAGLAGRFTVHGGSFRDDPLPLGADAISLVRVLFDHSDETVKLLLHRVREALPAGGRVIVAEAMSGGARPHRETDTYMAFYTAAMRTGRVRSAAEIAELLTGQGFSEIKIFPGLRPYVASAVTAVRPSDAP | Function: Methyltransferase that mediates the O-methylation of 1-hydroxy carotenoids. Converts hydroxyneurosporene to methoxyneurosporene or demethylspheroidene to spheroidene. Also able to produce spirilloxanthin (By similarity).
Catalytic Activity: demethylspheroidene + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + spheroidene
Sequence Mass (Da): 40788
Sequence Length: 379
Pathway: Carotenoid biosynthesis; spheroidene biosynthesis.
EC: 2.1.1.210
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D5AP78 | MPKDDHTGATADRTAQPTGTGKQPLVPGQPGAAPVQPGRVNFFTRIALSQRLHEIFERLPLMNRVTRREGEALFDIVSGFVQSQVLLAIVEFRVLHILAGASWPLPQLAERTGLAEDRLAVLMQAAAALKLVKFRRGLWQLAPRGAAFITVPGLEAMVRHHPVLYRDLADPVAFLKGDIEPELAGFWPYVFGPLAQEDAGLAERYSQLMADSQRVVADDTLRLVDLRDAKRVMDVGGGTGAFLRVVAKLYPELPLTLFDLPHVLSVADRFSPKLDFAPGSFRDDPIPQGADVITLVRVLYDHPDSVVEPLLAKVHAALPPGGRLIISEAMAGGAKPDRACDVYFAFYTMAMSSGRTRSPEEIKQMLEKAGFTKVSKPRTLRPFITSVIEAERG | Function: Methyltransferase that mediates the O-methylation of 1-hydroxy carotenoids. Converts hydroxyneurosporene to methoxyneurosporene or demethylspheroidene to spheroidene. Also able to produce spirilloxanthin.
Catalytic Activity: demethylspheroidene + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + spheroidene
Sequence Mass (Da): 43039
Sequence Length: 393
Pathway: Carotenoid biosynthesis; spheroidene biosynthesis.
EC: 2.1.1.210
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Q02861 | MASEGGSVRHVIVVGAGPGGLSAAINLAGQGFRVTVVEKDAVPGGRMKGLTLGASGEYAVDTGPSILQLPGVLEQIFRRAARRLEDYVKLLPLDVNTRVHFWDGTHLDTTRHLDRMEAELAKFGPRQASALRQWMEDGREKYGIAYQKFICTSADNLGYYAPWRLAPTLRFKPWQTLYRQLDGFFHDDRVTYALAYPSKYLGLHPTTCSSVFSVIPFLELAFGVWHVEGGFRELSRGMMRCARDLGATFRMGTPVEKVRVDAGRAVGVKLVGGEVLDADAVVVNADLAYAARSLIPAEAREGSRLTDAALERAKYSCSTFMAYYGLDTVYADLPHHLIYLSESARRTDRDALEDRHVDLEDPPFYVCNPGVTDPSGAPAGHSTLYVLVPTPNTGRPVDWVKTEQALRERIPAMLEKVGLKGVREHIREERYFTAETWRDDFNVFRGAVFNLSHTWLQLGPLRPKVKNRDIEGLYFVGGGTHPGSGLLTIMESANIAADYLTREAGKGPLPGWPYVPPLEPESPVQARAG | Function: Dehydrogenates carotenes in the trans conformation: converts all-trans-zeta-carotene into all-trans-lycopene, one of the last dehydrogenation steps of lycopene biosynthesis.
Catalytic Activity: 2 A + all-trans-zeta-carotene = 2 AH2 + all-trans-lycopene
Sequence Mass (Da): 58421
Sequence Length: 529
Pathway: Carotenoid biosynthesis; lycopene biosynthesis.
EC: 1.3.99.26
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P21334 | MAETQRPRSAIIVGAGAGGIAVAARLAKAGVDVTVLEKNDFTGGRCSLIHTKAGYRFDQGPSLLLLPGLFRETFEDLGTTLEQEDVELLQCFPNYNIWFSDGKRFSPTTDNATMKVEIEKWEGPDGFRRYLSWLAEGHQHYETSLRHVLHRNFKSILELADPRLVVTLLMALHPFESIWHRAGRYFKTDRMQRVFTFATMYMGMSPFDAPATYSLLQYSELAEGIWYPRGGFHKVLDALVKIGERMGVKYRLNTGVSQVLTDGGKNGKKPKATGVQLENGEVLNADLVVVNADLVYTYNNLLPKEIGGIKKYANKLNNRKASCSSISFYWSLSGMAKELETHNIFLAEEYKESFDAIFERQALPDDPSFYIHVPSRVDPSAAPPDRDAVIALVPVGHLLQNGQPELDWPTLVSKARAGVLATIQARTGLSLSPLITEEIVNTPYTWETKFNLSKGAILGLAHDFFNVLAFRPRTKAQGMDNAYFVGASTHPGTGVPIVLAGAKITAEQILEETFPKNTKVPWTTNEERNSERMRKEMDEKITEEGIIMRSNSSKPGRRGSDAFEGAMEVVNLLSQRAFPLLVALMGVLYFLLFVR | Function: Phytoene desaturase involved in the carotenoid biosynthesis pathway . Converts phytoene into 3,4-didehydrolycopene via the intermediates phytofluene, zeta-carotene, neurosporene and lycopene, by introducing up to five double bonds into phytoene . Is also able to desaturate 1-hydroxyneurosporene into 1-hydroxylycopene and 1-hydroxylycopene into 1-hydroxy-3,4-didehydrolycopene . Gamma-carotene and 1,19-dihydroxylycopene are not accepted as substrates . Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme al-2 first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase al-1 then introduces 5 desaturations to lead to 3,4-didehydrolycopene via the intermediates phytofluene, zeta-carotene, neurosporene and lycopene. Al-2 cyclase activity then converts 3,4-didehydrolycopene into torulene. Al-2 can also convet lycopene into gamma-carotene which in turn is converted to beta-carotene by an additional al-2 cyclization reaction. Torulene is the substrate of the dioxidase cao-2 that breaks the molecule, removing five carbon atoms to yield beta-apo-4'-carotenal, whereas the aldehyde dehydrogenase ylo-1 mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).
Catalytic Activity: 15-cis-phytoene + A = AH2 + all-trans-phytofluene
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 66367
Sequence Length: 595
Pathway: Carotenoid biosynthesis; lycopene biosynthesis.
Subcellular Location: Membrane
EC: 1.3.99.-
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P21685 | MKPTTVIGAGFGGLALAIRLQAAGIPVLLLEQRDKPGGRAYVYEDQGFTFDAGPTVITDPSAIEELFALAGKQLKEYVELLPVTPFYRLCWESGKVFNYDNDQTRLEAQIQQFNPRDVEGYRQFLDYSRAVFKEGYLKLGTVPFLSFRDMLRAAPQLAKLQAWRSVYSKVASYIEDEHLRQAFSFHSLLVGGNPFATSSIYTLIHALEREWGVWFPRGGTGALVQGMIKLFQDLGGEVVLNARVSHMETTGNKIEAVHLEDGRRFLTQAVASNADVVHTYRDLLSQHPAAVKQSNKLQTKRMSNSLFVLYFGLNHHHDQLAHHTVCFGPRYRELIDEIFNHDGLAEDFSLYLHAPCVTDSSLAPEGCGSYYVLAPVPHLGTANLDWTVEGPKLRDRIFAYLEQHYMPGLRSQLVTHRMFTPFDFRDQLNAYHGSAFSVEPVLTQSAWFRPHNRDKTITNLYLVGAGTHPGAGIPGVIGSAKATAGLMLEDLI | Function: Converts 15-cis-phytoene into all-trans-lycopene via the intermediary of all-trans-phytofluene, all-trans-zeta-carotene and all-trans-neurosporene, by the introduction of four double bonds.
Catalytic Activity: 15-cis-phytoene + 4 A = 4 AH2 + all-trans-lycopene
Sequence Mass (Da): 55008
Sequence Length: 492
Pathway: Carotenoid biosynthesis; lycopene biosynthesis.
Subcellular Location: Cell membrane
EC: 1.3.99.31
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P54982 | MAPPKHVIIIGAGAGGTATAARLAREGIKVTVVEKNNFGGGRCSLINHNGHRFDQGPSLYLMPKLFEEAFEALDEKIEDHVELLRCHNNYKVHFDDGDKIQLSSDLSRMKPEMERIEGPDGFLRFLDFMKESHTHYEGGVEMAIKQNFETIWKLIRLQYVPALFRLHIFDFVYSRAAKYFKTKKMRMAFTFQSMYMGMSPYDSPAVYNLLQYTEFAEGIWYPKGGFNTVIQKLENIATEKFGARFIYEAPVAKINTDDKGKKVTGVTLQSGEVIEADAVVCNADLVYAYHNLLPPCRWTTNTLAEKKLTSSSISFYWSLKRVVPELDVHNIFLAEAFKESFDEIFTDHKMPSELSFYVNLPSRIDPTAAPPGKDSMIVLVPIGHMKSKTNEAEDYTMIVKRARKMVLEVLERRLGLTNFIDLVEHEEVNDPSIWQKKFNLWRGSILGLSHDVLQVLWFRPSTQDSTGRYKNLFFVGASTHPGTGVPIVLAGSKLTSDQVCDHFGVKVRPSAITSSKRTYAPEDSKSFIWDIIWFLLIALFAATLVLFIAFPQYSEVNQTAASYINNLLPAAFRVPVANLSLTS | Function: Phytoene desaturase involved in the carotenoid biosynthesis pathway. Converts phytoene into 3,4-didehydrolycopene via the intermediary of phytofluene, zeta-carotene, neurosporene and lycopene, by introducing up to five double bonds into phytoene (By similarity).
Catalytic Activity: 15-cis-phytoene + 5 A = 5 AH2 + all-trans-3,4-didehydrolycopene
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65984
Sequence Length: 583
Pathway: Carotenoid biosynthesis; lycopene biosynthesis.
Subcellular Location: Membrane
EC: 1.3.99.30
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Q2XXQ9 | MILLKLYLTLAAILCQSRGTTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNIIAESAKRAALRCNQNEHTPVSGRTIGGVVCGENYFMSSNPRTWSFGIQSWFDERNYFKFGFGPTRAGVMVGHYTQKERCRPEV | Function: Blocks ryanodine receptors, and potassium channels.
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 16858
Sequence Length: 148
Subcellular Location: Secreted
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Q2XXQ7 | MILLKLYLTLAAILCQSRGTTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNTIAESAKRAALRCNQNEHTPVSGRTIGGVVCGENYFMSSNLRTWSFGIQSWFDERNYFKFGFGPTRAGVMVGHYTQVVWYKSYKMGCAINLCPNEPLKYFLVCQYCPGGNVVGRKYEPYAIGEPCAACPNNCDNGL | Function: Blocks ryanodine receptors, and potassium channels.
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 22485
Sequence Length: 200
Subcellular Location: Secreted
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Q2XXP3 | MILLKLYLTLAAILCQSRGMTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNIIAESAKRAALRCNYKEHTSIAERTIGGCGVWEKILSC | Function: Blocks ryanodine receptors, and potassium channels.
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 11533
Sequence Length: 102
Subcellular Location: Secreted
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Q2XXP2 | MILLKLYLTLAAILCQSRGMTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNIIAESAKRAALRCNYKEHTSIAERTIGGVVCGENYFMSSNPRTWSSSIQSWFDERNNFMFGFGPTIPGVMVGHYTQVVWYKSYKVGCAINLCPAQSLKYFQVCQYCPGGNVAGRKYEPYTIGEPCAARPKDCDNGLCTNPCAYNDDYTSCPDLTKQVGCHHPVTANC | Function: Blocks ryanodine receptors, and potassium channels.
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 25880
Sequence Length: 231
Subcellular Location: Secreted
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P02488 | MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKIQTGLDATHERAIPVAREEKPSSAPSS | Function: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
PTM: Acetylation at Lys-70 may increase chaperone activity.
Sequence Mass (Da): 19792
Sequence Length: 172
Subcellular Location: Cytoplasm
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P68405 | MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS | Function: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
PTM: Acetylation at Lys-70 may increase chaperone activity.
Sequence Mass (Da): 19792
Sequence Length: 173
Subcellular Location: Cytoplasm
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P24622 | MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISELMTHMWFVMHQPHAGNPKNNPVKVRSDRDKFVIFLDVKHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS | Function: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
PTM: Acetylation at Lys-93 may increase chaperone activity.
Sequence Mass (Da): 22489
Sequence Length: 196
Subcellular Location: Cytoplasm
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P02477 | MDIAIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRSVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVTSGMDAGHSERAIPVSREEKPSSAPSS | Function: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
PTM: Acetylation at Lys-70 may increase chaperone activity.
Sequence Mass (Da): 19768
Sequence Length: 173
Subcellular Location: Cytoplasm
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A0A1J4UAV9 | MNMSKTTISVKLKIIDLSSEKKEFLDNYFNEYAKATTFCQLRIRRLLRNTHWLGKKEKSSKKWIFESGICDLCGENKELVNEDRNSGEPAKICKRCYNGRYGNQMIRKLFVSTKKREVQENMDIRRVAKLNNTHYHRIPEEAFDMIKAADTAEKRRKKNVEYDKKRQMEFIEMFNDEKKRAARPKKPNERETRYVHISKLESPSKGYTLNGIKRKIDGMGKKIERAEKGLSRKKIFGYQGNRIKLDSNWVRFDLAESEITIPSLFKEMKLRITGPTNVHSKSGQIYFAEWFERINKQPNNYCYLIRKTSSNGKYEYYLQYTYEAEVEANKEYAGCLGVDIGCSKLAAAVYYDSKNKKAQKPIEIFTNPIKKIKMRREKLIKLLSRVKVRHRRRKLMQLSKTEPIIDYTCHKTARKIVEMANTAKAFISMENLETGIKQKQQARETKKQKFYRNMFLFRKLSKLIEYKALLKGIKIVYVKPDYTSQTCSSCGADKEKTERPSQAIFRCLNPTCRYYQRDINADFNAAVNIAKKALNNTEVVTTLL | Cofactor: Mg(2+) is required for dsDNA cleavage.
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids (Probable). CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), which requires a trans-encoded small RNA (tracrRNA), but not this protein (in vitro) (By similarity). Recognizes a short motif in the CRISPR repeat sequences (the 5' PAM or protospacer adjacent motif, TTAT in this organism) to help distinguish self versus nonself, as targets within the CRISPR locus do not have PAMs . Upon expression in E.coli of this protein, a mini CRISPR array and the probable tracrRNA, has dsDNA endonuclease activity. DNA cleavage is centered around positions 21 base pairs 3' of PAM. The mini system does not protect E.coli against transformation by foreign plasmids .
Sequence Mass (Da): 63904
Sequence Length: 544
Domain: Has an asymmetric bilobed structure, with a recognition (REC) lobe and nuclease (NUC) lobe; the sgRNA:target DNA is bound between the 2 lobes. The REC lobe (residues 1-312) is formed by the WED, ZF and REC domains, while the NUC lobe (residues 321-529) is formed by the RuvC and TNB domains. Has a split RuvC-like domain with the nuclease active sites.
EC: 3.1.-.-
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A0A2U3D0N8 | MIKVYRYEIVKPLDLDWKEFGTILRQLQQETRFALNKATQLAWEWMGFSSDYKDNHGEYPKSKDILGYTNVHGYAYHTIKTKAYRLNSGNLSQTIKRATDRFKAYQKEILRGDMSIPSYKRDIPLDLIKENISVNRMNHGDYIASLSLLSNPAKQEMNVKRKISVIIIVRGAGKTIMDRILSGEYQVSASQIIHDDRKNKWYLNISYDFEPQTRVLDLNKIMGIDLGVAVAVYMAFQHTPARYKLEGGEIENFRRQVESRRISMLRQGKYAGGARGGHGRDKRIKPIEQLRDKIANFRDTTNHRYSRYIVDMAIKEGCGTIQMEDLTNIRDIGSRFLQNWTYYDLQQKIIYKAEEAGIKVIKIDPQYTSQRCSECGNIDSGNRIGQAIFKCRACGYEANADYNAARNIAIPNIDKIIAESIK | Cofactor: Mg(2+) is required for dsDNA cleavage.
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids (Probable). CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), which requires a trans-encoded small RNA (tracrRNA), but not this protein (By similarity). Recognizes a short motif in the CRISPR repeat sequences (the 5' PAM or protospacer adjacent motif, YTT in this organism) to help distinguish self versus nonself, as targets within the CRISPR locus do not have PAMs. Has dsDNA endonuclease activity upon expression in E.coli of this protein, a mini CRISPR array and the probable tracrRNA. Plasmid cleavage is centered around positions 19-24 base pairs 3' of PAM. The mini system protects E.coli against transformation by foreign plasmids .
Sequence Mass (Da): 48689
Sequence Length: 422
Domain: Has an asymmetric bilobed structure, with a recognition (REC) lobe and nuclease (NUC) lobe; the sgRNA:target DNA is bound between the 2 lobes. The REC lobe (residues 1-312) is formed by the WED, ZF and REC domains, while the NUC lobe (residues 321-529) is formed by the RuvC and TNB domains. Has a split RuvC-like domain with the nuclease active sites.
EC: 3.1.-.-
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P0DW62 | MGESVKAIKLKILDMFLDPECTKQDDNWRKDLSTMSRFCAEAGNMCLRDLYNYFSMPKEDRISSKDLYNAMYHKTKLLHPELPGKVANQIVNHAKDVWKRNAKLIYRNQISMPTYKITTAPIRLQNNIYKLIKNKNKYIIDVQLYSKEYSKDSGKGTHRYFLVAVRDSSTRMIFDRIMSKDHIDSSKSYTQGQLQIKKDHQGKWYCIIPYTFPTHETVLDPDKVMGVDLGVAKAVYWAFNSSYKRGCIDGGEIEHFRKMIRARRVSIQNQIKHSGDARKGHGRKRALKPIETLSEKEKNFRDTINHRYANRIVEAAIKQGCGTIQIENLEGIADTTGSKFLKNWPYYDLQTKIVNKAKEHGITVVAINPQYTSQRCSMCGYIEKTNRSSQAVFECKQCGYGSRTICINCRHVQVSGDVCEECGGIVKKENVNADYNAAKNISTPYIDQIIMEKCLELGIPYRSITCKECGHIQASGNTCEVCGSTNILKPKKIRKAK | Cofactor: Mg(2+) is required for dsDNA cleavage.
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids (Probable). CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), which requires a trans-encoded small RNA (tracrRNA), but not this protein (By similarity). Recognizes a short motif in the CRISPR repeat sequences (the 5' PAM or protospacer adjacent motif, TTC in this organism) to help distinguish self versus nonself, as targets within the CRISPR locus do not have PAMs. Has dsDNA endonuclease activity upon expression in E.coli of this protein, a mini CRISPR array and the probable tracrRNA. Plasmid cleavage is centered around positions 24 base pairs 3' of PAM. The mini system protects E.coli against transformation by foreign plasmids .
Sequence Mass (Da): 56892
Sequence Length: 497
Domain: Has an asymmetric bilobed structure, with a recognition (REC) lobe and nuclease (NUC) lobe; the sgRNA:target DNA is bound between the 2 lobes. The REC lobe (residues 1-312) is formed by the WED, ZF and REC domains, while the NUC lobe (residues 321-529) is formed by the RuvC and TNB domains. Has a split RuvC-like domain with the nuclease active sites.
EC: 3.1.-.-
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A0A482D308 | MAKNTITKTLKLRIVRPYNSAEVEKIVADEKNNREKIALEKNKDKVKEACSKHLKVAAYCTTQVERNACLFCKARKLDDKFYQKLRGQFPDAVFWQEISEIFRQLQKQAAEIYNQSLIELYYEIFIKGKGIANASSVEHYLSDVCYTRAAELFKNAAIASGLRSKIKSNFRLKELKNMKSGLPTTKSDNFPIPLVKQKGGQYTGFEISNHNSDFIIKIPFGRWQVKKEIDKYRPWEKFDFEQVQKSPKPISLLLSTQRRKRNKGWSKDEGTEAEIKKVMNGDYQTSYIEVKRGSKIGEKSAWMLNLSIDVPKIDKGVDPSIIGGIDVGVKSPLVCAINNAFSRYSISDNDLFHFNKKMFARRRILLKKNRHKRAGHGAKNKLKPITILTEKSERFRKKLIERWACEIADFFIKNKVGTVQMENLESMKRKEDSYFNIRLRGFWPYAEMQNKIEFKLKQYGIEIRKVAPNNTSKTCSKCGHLNNYFNFEYRKKNKFPHFKCEKCNFKENADYNAALNISNPKLKSTKEEP | Cofactor: Mg(2+) is required for dsDNA cleavage . Mg(2+) and Mn(2+) support ssDNA cleavage equally .
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids (Probable). CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), which requires a trans-encoded small RNA (tracrRNA), but not this protein (in vitro) (Probable). Upon expression in E.coli of this protein, a mini CRISPR array and the probable tracrRNA, the protein associates with both RNAs . The mini system is not active in E.coli against phiX174 phage, nor is it active in protection against transformation by foreign plasmids . In vitro the purified protein-tracrRNA-crRNA complex cleaves ssDNA complementary to the crRNA; target cleavage requires both tracrRNA and crRNA, but not a protospacer adjacent motif (PAM). The tracrRNA-crRNA can be replaced by a single guide RNA (sgRNA). 2-nucleotide mismatches in the middle of the crRNA:DNA heteroduplex decrease cleavage. Cleavage occurs just downstream of the heteroduplex . Activation of this protein results in non-specific ssDNA degradation in vitro . In vitro and in E.coli (coexpressed with sgRNA) has dsDNA endonuclease activity, recognizing the 5' PAM sequence TTTR; both sgRNA and a PAM are required for activity. Cleaves the target strand 24 and the nontarget strand 22 bases upstream of the PAM (respectively), resulting in 5' overhangs . The 2 monomers interact differently with the sgRNA and target DNA. Mutagenesis of a dimeric construct shows that one of the RuvC monomers probably cleaves both DNA strands .
Sequence Mass (Da): 61517
Sequence Length: 529
Domain: Has an asymmetric bilobed structure, with a recognition (REC) lobe and nuclease (NUC) lobe; the sgRNA:target DNA is bound between the 2 lobes. The REC lobe (residues 1-312) is formed by the WED, ZF and REC domains, while the NUC lobe (residues 321-529) is formed by the RuvC and TNB domains. Has a split RuvC-like domain with the nuclease active sites.
EC: 3.1.-.-
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P35833 | MKLMVLQLLLWHSALWTVHEATPLGPARSLPQSFLLKCLEQVRKIQADGAELQERLCAAHKLCHPEELMLLRHSLGIPQAPLSSCSSQSLQLTSCLNQLHGGLFLYQGLLQALAGISPELAPTLDTLQLDVTDFATNIWLQMEDLGAAPAVQPTQGAMPTFTSAFQRRAGGVLVASQLHRFLELAYRGLRYLAEP | Function: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.
PTM: O-glycosylated.
Sequence Mass (Da): 21431
Sequence Length: 195
Subcellular Location: Secreted
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P09919 | MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP | Function: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.
PTM: O-glycan consists of Gal-GalNAc disaccharide which can be modified with up to two sialic acid residues (done in recombinantly expressed G-CSF from CHO cells).
Sequence Mass (Da): 22293
Sequence Length: 207
Subcellular Location: Secreted
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G0HV86 | MTGNSDKVRSLFLTALMVFSVFAGTIAFSGGAAAAANVSVQQAAEYDSGTVELALNGSTGSPVTTGDINIYIDGNENPSNYGVSSVDTTDDGTTGRLQFSLDQDVQPNRNLTVEVSGLTGGDNTVVAEDIDVTSQTIDADDDSGDTNAFRGEVLAIRADGGEGDADDATSSTQIVVEDSNGAVVTQDTYTANSKVYTYETENLDTGEEYEVTVGGTADENITISNLDLNVNIDDDVGDGANIDDTDTLAVNVSTTRGGEPANATLFNEDDDKVATQIKSLKGNENVVFDFGNQSADDSPYYVKVTDNQTGVSAESDQINVSESGEGDASFETSTVQDEVGDVTNITVQMGNTENAVINVGSQNDDNYVIQGQLEDDNGDGEVTVQFNSYTAGTDNNNTVLTVPGDDDLDEVEEKGSFTDSRNSLDEDVLEPQSYSINVTAGTSPDVTSPDTVGTLRLNENSVESMQTWVAPSDADIDDEDIDIYDRIGENLTQSDDVAVEDVVVHEIQASGIEGALEYEQEDNGSSDVTDAFIAAADTTPDRINDDTSASGLQLYVNRTDVGANADADPINFANSSSAVTVVDDPDNNTYFVALDTEDVEFESGNTITEEEDTEINATFSVQEGPLTDDSSSESELYTTSERNAELNLDDDGFVTVGAAAGQTVSGDTNVAPGSELEVEMESESEANPFVERPEATVGPNGTYVATEDFSDYSAGTNFTVQTLDVDGDSDFSDEEDGRIVEADTATVSISDQESDGSEVVVDSAQLSSGGFIAIHAGDASGDVVGNSEYLEAGTYNDLTITLDEPMDENFTAVAMPHQDTNGNEEYDFPGDDGPYTQNGSAVTDSANVTVSAEEPEDTPEDTPEDTPEDTPEDTPEDTPADTPEDTPDTGTETTEAEGPGFTAAIALIALVAAALLAVRRDN | Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell. In H.hispanica, the S-layer contains two different glycoproteins, Slg1 and Slg2, which share highly similar amino acid sequences.
PTM: N-glycosylated on Asn-307; this N-linked glycan is a branched trisaccharide containing 2-amino-6-sulfo-2,6-dideoxy-glucose (sulfoquinovosamine).
Sequence Mass (Da): 96911
Sequence Length: 922
Subcellular Location: Secreted
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P35206 | MSTTLLWFSSVIGYVIQTKCLSNIQSKKEISVGPNGTIATPETNGDNGNSSSLTFYLTFMYFASWLLLVPASRLWEKMRPMFVSDSDSNRNSQFDNNNSGSVTNEDVDTFSHVLDDPQPRIPAQQQKQKIISVATFKYVAKLTVLALIMIVADLTYNMALSLSPAFDVALMQNTAIFEIVTLLYGVCGISRKNYVFRNFLIMMNAVIGILIISYTKATCDMLAGKLSVNPNTGELSDPFLFDRLKGALICGLGALIMGPFAVLWNRWFCSNISKNENSAVVLVKQSTHMALIGIIGMVILLPFIPKFPSRESVESISLFYNDKSFWFSLLGSIIFGSLPSLISILELNRKAPAEYLTTCNLGAIIFMGLAEWVCEPTQTTIVRWEVIGYIMLTVSLLVLSVTLGEGKYHH | Function: Required for calcium regulation. May regulate calcium accumulation by a non-vacuole organelle. Also regulates the activity of CSH1 and SUR1 during mannosyl phosphorylinositol ceramide synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45442
Sequence Length: 410
Subcellular Location: Endoplasmic reticulum membrane
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P21158 | MRAFATNVCTGPVDVLINNAGVSGLWCALGDVDYADMARTFTINALGPLRVTSAMLPGLRQGALRRVAHVTSRMGSLAANTDGGAYAYRMSKAALNMAVRSMSTDLRPEGFVTVLLHPGWVQTDMGGPDATLPAPDSVRGMLRVIDGLNPEHSGRFFDYQGTEVPW | Function: Cell-cell signaling protein required for fruiting body formation, a multicellular developmental program that is induced in response to starvation . Necessary for rippling, cellular aggregation, spore differentiation and for gene expression that is initiated after 6 hours of starvation . In starving cells, the C-signal directly induces aggregation and sporulation, which are induced at distinct threshold levels of C-signaling . Contact with C-signaling induces cells to glide with high speed and low stop and reversal frequencies toward aggregation centers . The C-signal acts as a morphogen and induces distinct events at distinct threshold levels . A regulated increase in the level of C-signaling during development ensures the correct temporal order of aggregation and sporulation .
PTM: The mature C-signal (p17) is derived from the precursor sequence (p25) by proteolytic cleavage . The subtilisin-like protease PopC is directly responsible for cleavage of p25 to p17 . The cleavage site is probably located between amino acid residues 60 and 68 in p25 .
Sequence Mass (Da): 17741
Sequence Length: 166
Subcellular Location: Secreted
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Subsets and Splits