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B6YRV8 | MKIRIGFGYDVHPLVMNYNLWLGGIKIPYEKGLKGHSDADVLIHALCDALLGAADIGNIGTNFPNTNKKLRNIDSKILLKQTMSFIYSKNYELNNADITVCIEQPKLNPFIPQMKTCLAEIMQTDKGNISIKATTSEKMGFIGREEGIAVFATVLITPINEIGISCQ | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 18447
Sequence Length: 167
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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Q1IVA8 | MIRVGLGFDSHEFREGIPLRIGGLTIPHTHGLSGHSDGDVLLHAITDALLGAVAAGDIGAFFPPSDPKWKGANSVVFIEEAMRHIETAGYRVGNVDCSLVLNAPKIGPHAKAIQESVAKLLKIEPTAVGIKAKTPEGLNLDGTALAHVVVLLEKR | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 16321
Sequence Length: 155
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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C5CGG7 | MYRVGIGFDAHPLEANKKGLYLGGVKVSEEYSSIGHSDGDALIHAIVDAILGATNAGNIGIWFPENEENRGRRSTEFLEIIRKKILAGKYEILNIDSVIIIDKVRMNPHIENIRLKLARILGISKGNINVKPKSGNTLYGNSVSVYAVCMLKKVGT | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 17106
Sequence Length: 156
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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Q8F0A5 | MYRIGNGIDFHKLEINLNRPLILGGIECESEFALVGHSDADIILHAISDAILGALALGDIGQYFPDTDPSLKNIDSKIILVKCLELMKEKNFDLVNIDCTVIGERPKITPLKDRITKSLSNLLNLPLDCISVKATTTEKMGALGRQEGIGTFCSILLEKRS | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 17652
Sequence Length: 161
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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Q8YAB4 | MIRIGQGYDVHKLAYDRDLIIGGVKIPYEKGLLGHSDADVLLHAITDAIIGAIGAGDIGHFFPDTDMVFKDADSAELLAEIWQKVEADGFRLGNLDATIIAEKPKMAPYVEQMKLRIAELLHADSAQVNVKATTTEKLGFTGREEGIASLAVVLLEK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 17030
Sequence Length: 157
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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Q8RG40 | MERNTRVVKVANLKIGGNNPIIIQSMTNTNSADVEATVKQINNLEKVGCQLVRMTINNIKAAEAIKEIKKKVSLPLVADIHFDYRLALLAIKNGIDKLRINPGNIGSDENVKKVVEAAKEKNIPIRIGVNSGSIEKEILEKYGKPCVDALVESAMYHIRLLEKFDFFDIIVSLKSSNVKMMVEAYRKISSLVDYPLHLGVTEAGTKFQGTVKSAIGIGALLVDGIGDTLRVSLTENPVEEIKVAKEILKVLDLSDEGVEIISCPTCGRTEIDLIGLAKQVEEEFRTKKNKFKIAVMGCVVNGPGEAREADYGIAAGRGIGILFKKGEIIKKVSESNLLEELKKMISEDLENKKD | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin]
Sequence Mass (Da): 38859
Sequence Length: 354
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6.
EC: 1.17.7.3
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Q7NS59 | MTKTIMLANPRGFCAGVDRAIAIVERAIELYGAPIYVRHEVVHNRFVVDDLRGKGAVFIEELKDVPPGSTLIYSAHGVPLSVRAEAEALGLTVFDATCPLVTKVHVEVKRMNKAGMEIIMIGHAGHPEVEGTMGQVDAGIYLVQTVDDVATLRVVNEDQLSYVSQTTLSVDETRDIIAALKARFPNIHSPKKDDICYATQNRQDAVKLLADQCDIVVVVGSPNSSNSNRLREVAALKGVDAYMVDNASLLEPEWFAGKRRVGVTAGASAPEVLVQAVIDRIKAFDVTQVTELPGVEESTVFALPPALRPLF | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 33697
Sequence Length: 311
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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B5E9S9 | MQVILAKHAGFCFGVKRATQLAFQAANIGSETYTLGPIIHSPQVVQRLEEMGVIPVDNVSEVETGGTIIIRSHGVAAEELEAAVRANLEVVDATCPFVKKAQEHVATLSKEGYDIVVVGDAVHPEVQGIVSYAAGRVYVVSSHKDVERLPRMSKIGVVAQTTQSFEHLHEVVAACLARGGEARVYNTICDATAVRQEEAKKLAGAVDCMVVIGGFNSANTMRLAQICLELLPRTHHVETASQIDEQWFKGVKKVGVTAGASTPKWIIDEVIDRISAIDKDKIS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 30493
Sequence Length: 283
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q97I09 | MRKVMLAEKAGFCFGVKRAVDMALLTQKEYNKKIYTLGELIHNNDVVDKLKDNNVYPIGIEDIDNLKENDVILIRSHGISEEIYKILLSKGLTVINATCPFVTKIQEKVKKYNELGYDIVIVGDKYHPEVIGINGWCDNKAIISKQGENLENITSESKVCIVSQTTEKLENWEKVLKEVKNRAIEVISFNTICNATSERQKIAKDLSNKVDFMVVIGGKQSSNTTKLYEICKSNCNETIHVENSGEIPENILKNKNCVIGVTAGASTPDWIIEEAISKMSENQISNETNNEMADAMKFIAENEGKIYVGASVTGEIIQVSEKEVFLNINYKRDGVIPKSEIDDDGKDLKELFTVGDKIVAKIIKLKDADNYVVLSVKELQREQGYKEIKEAFENKTTLNVVVKEDVKGGIIASYKGIRIFIPASHVELFHVDNLKEYIGKSFDVAIIEYSTKKRQTKIVASRRALLSKEKEKVEETVWNKLEEGQVVEGEVKRLTDFGAFVEIEGVDGLLHVSEISWGRVEKPADVLKIGDKIKVYVLSVDKENKKLSLSVKKLTENPWNNVEEKYPVGSVVLGKVIRFADFGAFVKLEPGVDGLVHISEISHKRIAKPSDALNVGEEIKAKILEVSSEEKKIGLSIREVEE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 71989
Sequence Length: 642
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q187C6 | MNIKIAKNAGFCFGVKRAMKMAWDEVEKNDSGIYALGPLIHNKQAVAKYEEKGLKTVNEIDTIPNHENMIIRSHGVPENIYKEAKDKKLKIVDTTCPFVKKIHTVVSEYHNKGYEIIVIGDMKHPEVIGINGWCENSAIIIKTLEQMENMEFDNSKRYCLVAQTTINPELYISIVNKLSDKLEEIVFNDTICSATKTRQESAKELAKEVDCMIVIGGKHSSNTQKLVKVCEDLVPTFAIETKDELDVNTLKKYKNLGITAGASTPNWIIEEVVTFLENL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 31466
Sequence Length: 279
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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P58675 | MERNVILAKNAGFCFGVKRAVDEAIKYQKEFGKKIYTLGPLIHNNDVVNYLEDNNIFAIELSDADSLKKGDVVLIRSHGVKESVIKDLTDKGLIVKNATCPYVTNIQLKVKKCYEQGYKIIIVGDKNHPEVIGINGWCNDSAIITNGKTELENIPAKVCVVSQTTEKKETWNKVLNEIVRASKEIVAFNTICSATDVRQKSVQELSKEADLVFVIGGKNSSNTTKLYEICKKECPKSYHIENVKELDESLLEDESVKTIGITAGASTPDWIINEVISKIKEL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 31409
Sequence Length: 282
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q11YY5 | MDVIIDKNSGYCFGVEFAIQMAEDEMATGEPLFCLGDIVHNSMEVERLAKKGLKIIDREELKKLSDCKVLIRAHGEPPETYQLALENNIELVDASCPVVLKLQNRVKASFDAIDSKDGQIVIYGQEGHAEVIGIAGQTGDKAIVITTEKDLDKIDFEKPVTLYSQTTKSTQGFYKMKDLIEARVAEAGKNVDENFEYNDSICRQVSNREPQLRKFSKEFDVVIFVSGKKSSNGKALYGVCKQENERSYFVENETEIEPSWIRATDNVGICGATSTPMWLMEKVQNYIQAHSWN | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 32940
Sequence Length: 293
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q7ULU1 | MTPMKIILAAPRGFCAGVNMAIDSLDLTLQKFGPPVYVYHEIVHNQFVVKTFREKGAVFVDTIDEVPEGGVLLFSAHGVSPEIRKAAQARKLHALDATCPLVTKVHLEAIKYAKAGYTIILIGHEGHDEVLGTMGEAPEAIVLVEDEADVDRLEFEPGTQLAYLTQTTLSVDDAGRVIRRLRERFPEIHSPPKDDICYATQNRQEAVKLLREDADVIVVLGSQNSSNSQRLKELAAEQGKRAMLVDGPQDLAVDQFSDDDRVLITAGASAPESVVQSTIDWLKENFDASVDTQVVREEDVQFPLPKPLRAFAAEQAAAK | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 35009
Sequence Length: 319
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q5LNJ7 | MTKSPLTLYLAAPRGFCAGVDRAIKIVEMAIEKWGAPVYVRHEIVHNKFVVDGLRAKGAVFVEELDECPDDRPVIFSAHGVPKAIPAEAERRQMVYVDATCPLVSKVHIEAERHAEHGLQIIMIGHRGHPETIGTMGQLPEGEVLLVETVADVARIAVRDPARLAFVTQTTLSVDDTRDIVAALQARFPQIVGPHKEDICYATTNRQEAVKAVAPKSDALLVVGAPNSSNSRRLVEVAAKAGCSYAQLVQRADDIDWRALDGIATIAVSAGASAPELLVNEVIDAFRARFDVTVEVVETAVEHVEFKVPRVLRQPA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 34351
Sequence Length: 316
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
EC: 1.17.7.4
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Q97SR4 | MFGFFKKDKAVEVEVPTQVPAHIGIIMDGNGRWAKKRMQPRVFGHKAGMEALQTVTKAANKLGVKVITVYAFSTENWTRPDQEVKFIMNLPVEFYDNYVPELHANNVKIQMIGETDRLPKQTFEALTKAEELTKNNTGLILNFALNYGGRAEITQALKLISQDVLDAKINPGDITEELIGNYLFTQHLPKDLRDPDLIIRTSGELRLSNFLPWQGAYSELYFTDTLWPDFDEAALQEAILAYNRRHRRFGGV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 28705
Sequence Length: 252
EC: 2.5.1.-
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Q9X1B8 | MRIPQHVAIIMDGNGRWAKKRGLPRIKGHQRGAEVLHNTVKWSLELGIKYLTAFSFSTENWKRPKEEVEFLMDLFVQMIDREMELLRRERVRVRILGRKEGLPEKVLKKWQEVEEKTKEFDRMTLIIAFNYGGRREILDAVEFILKDVSHGKKIELTEETFRQYLYLPDVPDPDLIIRTSGEMRLSNFLLWQSAYSELYFFKKLWPDFTKRDFLRAIESYSKRERRFGGLING | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27859
Sequence Length: 233
EC: 2.5.1.-
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Q5SH15 | MVRRLLALSRPLYWLYEKRLLREVKRGPMPRHLGLILDGNRRYARALGLSPTKGHEFGVQKAYEVLEWCLEMGIKTVTVWVFSTDNFKRPPEEVETLMNLFLREAERMAEDHRILEHQVRVRFIGRREGFSPEVVRAIERLERRTEGHRGMFLNIAMGYGGREEIVDAVKRLLLEAEARGLSPKEVAEGLTPEDIARHLYTAGLPDPDFIIRTSGEIRLSGFLLWQSAYSEFYFADVLWPEFRKIDFLRALRSYQARERRFGR | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 30893
Sequence Length: 263
EC: 2.5.1.-
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Q73K76 | MSDELKHIAIVMDGNGRWAKKRGLPRSMGHKEGLNTVKRITKAVSDLGIPYITLYIFSTENWKRTEAEVGFLMGLIKQHLKAELKFYADNNIRIEHIGNLSGLPQDIQDEINSVRDKTSAYTGTAIVLGINYGAHDEILRAIKKLNSDELASINEESFSLKLDTGKIPPVDLLIRTGGEKRLSNFLLWQSAYAELYFTDTLWPDWTVENLYEAIEDYKKRNRRYGNA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 25879
Sequence Length: 227
EC: 2.5.1.-
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O83612 | MQHVAIIMDGNGRWAERRGLRRSAGHRRGLQTAREIVAALCAIRVPFVTLYVFSTENWKRSAHEVHFLMNLIRWYLKKEMSFYVEHAIRVVHLGCAQTLPPDVRSQIEYVVERTRSHRGTTVALAINYGGKDEILRAVKKVLCSTSCPDGELLTEEAFGACLDAPQLPSVDFLIRTGGQQRMSNFLLWQSAYAEFYFTDILWPDFRVEDMLRALDEYRLRTRTFGGLE | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 26270
Sequence Length: 228
EC: 2.5.1.-
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Q9X5F1 | MIAPLANSAVKPHKSASFVPRHVAIIMDGNGRWASARHLPRIAGHKKGADAVKTTVRAAAEMGIEVLTLYAFSSENWRRPASEVADLMGLLRLCLRQEMHNIKERGICLKVIGDYTRLDQDLVALLNQAIEITANNTRLTLVFALNYGAQDELVHVTKRIAEKAKEGQLDPENIDVGTIESLLYTHDLPPLDLVIRTSGEKRLSNFLLWQAAYAELLFIDTLWPDFGSETLKAAVEEYARRERRYGGL | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27715
Sequence Length: 248
EC: 2.5.1.-
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Q863C4 | MGIELLCLFFLFLGRNDHVQGGCAMGGAETCEDCLLIGPQCAWCSQENFTHLSGVGERCDTPANLLAKGCQLTFIENPVSQVEILTNKPLSIGRQKNSSNIVQISPQSLALKLRPGLEQTLQVQVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSLLSKEMSKLTSNFRLGFGSFVEKPISPFMKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTILEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGVLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNSGVPFPHQKKCSHMKVGDTASFNVTVSLPNCERRSRHVILKPVGLGDALEILVSPECSCDCQKEVEVNSSKCSNGNGSFQCGVCACNPGHVGHHCECGEDTLSTESCKEAPELPSCSGRGDCYCGQCVCHLSPYGNIYGPYCQCDNFSCVRHKGLLCGDNGDCDCGECVCRSGWTGEYCNCTTSTDPCVSEDGILCSGRGDCVCGKCICTNPGASGPACERCPTCSDPCNSKRNCIECYLSADGQAQEECVDKCKLAGATINEEEDFSKDSSVSCSLQGENECLITFLLTTDNEGKTVIHSIEKDCPKPPNIPMIMLGVSLAILLIGVALLCIWKLLVSFHDRKEVAKFEAERSKAKWQTGTNPLYRGSTSTFKNVTYKHKEKQKVDLSTDG | Function: Integrin alpha-V:beta-6 (ITGAV:ITGB6) is a receptor for fibronectin and cytotactin (By similarity). It recognizes the sequence R-G-D in its ligands (By similarity). ITGAV:ITGB6 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85746
Sequence Length: 787
Domain: The VWFA domain (or beta I domain) contains three cation-binding sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent MIDAS site (ADMIDAS). This domain is also part of the ligand-binding site.
Subcellular Location: Cell membrane
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P26010 | MVALPMVLVLLLVLSRGESELDAKIPSTGDATEWRNPHLSMLGSCQPAPSCQKCILSHPSCAWCKQLNFTASGEAEARRCARREELLARGCPLEELEEPRGQQEVLQDQPLSQGARGEGATQLAPQRVRVTLRPGEPQQLQVRFLRAEGYPVDLYYLMDLSYSMKDDLERVRQLGHALLVRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLRHPCPTRLERCQSPFSFHHVLSLTGDAQAFEREVGRQSVSGNLDSPEGGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGKLGGIFMPSDGHCHLDSNGLYSRSTEFDYPSVGQVAQALSAANIQPIFAVTSAALPVYQELSKLIPKSAVGELSEDSSNVVQLIMDAYNSLSSTVTLEHSSLPPGVHISYESQCEGPEKREGKAEDRGQCNHVRINQTVTFWVSLQATHCLPEPHLLRLRALGFSEELIVELHTLCDCNCSDTQPQAPHCSDGQGHLQCGVCSCAPGRLGRLCECSVAELSSPDLESGCRAPNGTGPLCSGKGHCQCGRCSCSGQSSGHLCECDDASCERHEGILCGGFGRCQCGVCHCHANRTGRACECSGDMDSCISPEGGLCSGHGRCKCNRCQCLDGYYGALCDQCPGCKTPCERHRDCAECGAFRTGPLATNCSTACAHTNVTLALAPILDDGWCKERTLDNQLFFFLVEDDARGTVVLRVRPQEKGADHTQAIVLGCVGGIVAVGLGLVLAYRLSVEIYDRREYSRFEKEQQQLNWKQDSNPLYKSAITTTINPRFQEADSPTL | Function: Integrin ITGA4/ITGB7 (alpha-4/beta-7) (Peyer patches-specific homing receptor LPAM-1) is an adhesion molecule that mediates lymphocyte migration and homing to gut-associated lymphoid tissue (GALT) (Probable). Integrin ITGA4/ITGB7 interacts with the cell surface adhesion molecules MADCAM1 which is normally expressed by the vascular endothelium of the gastrointestinal tract . Interacts also with VCAM1 and fibronectin, an extracellular matrix component (Probable). It recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin (Probable). Interactions involve the tripeptide L-D-T in MADCAM1, and L-D-V in fibronectin (Probable). Integrin ITGAE/ITGB7 (alpha-E/beta-7, HML-1) is a receptor for E-cadherin .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 86903
Sequence Length: 798
Domain: The VWFA domain (or beta I domain) contains three cation-binding sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent MIDAS site (ADMIDAS) . This domain is also part of the ligand-binding site . The MIDAS site is required for both rolling and adhesion . The ADMIDAS site is required for rolling and mediates the negative regulatory effects of higher Ca(2+) concentration on ligand binding . The LIMBS site is required for adhesion and mediates the positive regulatory effects of low Ca(2+) concentrations on ligand binding .
Subcellular Location: Cell membrane
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P26012 | MCGSALAFFTAAFVCLQNDRRGPASFLWAAWVFSLVLGLGQGEDNRCASSNAASCARCLALGPECGWCVQEDFISGGSRSERCDIVSNLISKGCSVDSIEYPSVHVIIPTENEINTQVTPGEVSIQLRPGAEANFMLKVHPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSRKMAFFSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGTIAGEIESKAANLNNLVVEAYQKLISEVKVQVENQVQGIYFNITAICPDGSRKPGMEGCRNVTSNDEVLFNVTVTMKKCDVTGGKNYAIIKPIGFNETAKIHIHRNCSCQCEDNRGPKGKCVDETFLDSKCFQCDENKCHFDEDQFSSESCKSHKDQPVCSGRGVCVCGKCSCHKIKLGKVYGKYCEKDDFSCPYHHGNLCAGHGECEAGRCQCFSGWEGDRCQCPSAAAQHCVNSKGQVCSGRGTCVCGRCECTDPRSIGRFCEHCPTCYTACKENWNCMQCLHPHNLSQAILDQCKTSCALMEQQHYVDQTSECFSSPSYLRIFFIIFIVTFLIGLLKVLIIRQVILQWNSNKIKSSSDYRVSASKKDKLILQSVCTRAVTYRREKPEEIKMDISKLNAHETFRCNF | Function: Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for fibronectin . It recognizes the sequence R-G-D in its ligands . Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs) (Probable). Required during vasculogenesis (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85632
Sequence Length: 769
Domain: The VWFA domain (or beta I domain) contains two cation-binding sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS) and the metal ion-dependent adhesion site (MIDAS) . Unlike in the other beta integrins, the cation-binding site adjacent MIDAS site (ADMIDAS) in ITGB8 is not functional due to the presence of two Asn residues instead of 2 Asp residues . This domain is also part of the ligand-binding site .
Subcellular Location: Cell membrane
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Q27591 | MTSLGGRAFLWIYLVFLIAEISHSDADSIDDQCRHADSCERCLSAHLECAWCTDKEYQVGYRCLSRRQLLNYNCSETDIYENQPVLDVLQDKPLKDYETSDQAVQVTPQRAYLKLVKGNTQRMKLSYRTARNNPLDLYVLMDLTWTMRDDKKTLEELGAQLSQTLKNLTGNYRLGFGSFADKPTLPMILPQHRENPCAAERATCEPTYGYRHQLSLTDDIPAFTSAVANSKITGNLDNLEGGLDALMQVIVCTKEIGWKEQARKVVILVTDGFMHLAGDGLLAGIIQRNDKQCHLNKAGEYTGSLNYDYPSLEEIYRELLRRKINVIFAVTEEVVSSYWELSALMKEISYVDILSADSSNILELIKKSYESLIKRTQFADNSPDFIDMAYYTDCGGQFPSLQKRNYCNNVTLGKQIDFYVDVTLKKYPDNQVYTHKIRVEETSLSEFMDLDVELQRPCPCQETPDPENEEGRFLCDYKGYLYCGMCECDEGWTGTYCNCPTDATNVTSNEALLQKCRQPFSDKSTSELVCSNHGDCDCGTCLCDPGYTGPFCECRECLDCDEKLADCFCGQCVCKYGWSGSKCNCDGDTDACVGPTGEICSERGTCQCEECQCEEPYLGKFCEIDPEKDNKLCLFYEPCVTCLIEQKQGMGVCENLTEICSSLDRQETYPYNFVHELDPEQDQCLVRLVNKHGIQCDSFFVYQVIDHSNFLTIQAVDCEPPDYVALVGYISAFTLLIGLLIIFIILWYIRAKDAREYAKFEEDQKNSVRQENPIYRDPVGRYEVPKALSVKYDENPFAS | Function: Contributes to endodermal integrity and adhesion between the midgut epithelium and the surrounding visceral muscle. Essential for migration of the primordial midgut cells and for maintaining, but not establishing, cell polarity in the midgut epithelium. Can only partially compensate for the loss of beta-PS integrin during primordial midgut cell migration. The two beta subunits mediate midgut migration by distinct mechanisms: beta-PS requires rhea/Talin and beta-nu does not. Integrin alpha-PS3/beta-nu is required for effective phagocytosis of apoptotic cells during embryonic development and for the phagocytic elimination of S.aureus by mediating the binding of S.aureus peptidoglycan to larval hemocytes, which probably activates a signaling pathway involving Rac1 and Rac2. Not required for the production of antimicrobial peptides during S.aureus. Upon activation by LanA, integrin alpha-PS3/beta-nu activates Fak in presynapsis to suppress neuromuscular junction (NMJ) growth during larval development and during low crawling activity, but not during higher-crawling conditions. Mediates, together with LanA, glutamate receptor-modulated NMJ growth.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 90842
Sequence Length: 799
Subcellular Location: Membrane
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Q3ZBM4 | MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKSLEGPLDLINYIDVAQQDGKLPFVPLEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGSGKSLLALKTTDANNQEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP | Function: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter (By similarity).
PTM: Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion. The degree of phosphorylation is regulated by integrin-dependent cell-matrix interaction (By similarity).
Sequence Mass (Da): 21871
Sequence Length: 200
Subcellular Location: Nucleus
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O14713 | MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP | Function: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter.
PTM: Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion. The degree of phosphorylation is regulated by integrin-dependent cell-matrix interaction.
Sequence Mass (Da): 21782
Sequence Length: 200
Subcellular Location: Nucleus
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Q5R5S7 | MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNSNSDTCAEFRIKYVGAIEKLKLSEGKDLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP | Function: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter (By similarity).
PTM: Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion. The degree of phosphorylation is regulated by integrin-dependent cell-matrix interaction (By similarity).
Sequence Mass (Da): 21813
Sequence Length: 200
Subcellular Location: Nucleus
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P11584 | MILERNRRCQLALLMIAILAAIAGQTDAQKAAKLTAVSTCASKEKCHTCIQTEGCAWCMQPDFKGQSRCYQNTSSLCPEEFAYSPITVEQILVNNKLTNQYKAELAAGGGGSAMSGSSSSSYSSSSSSSSFYSQSSSGSSSASGYEEYSAGEIVQIQPQSMRLALRVNEKHNIKISYSQAEGYPVDLYYLMDLSKSMEDDKAKLSTLGDKLSETMKRITNNFHLGFGSFVDKVLMPYVSTIPKKLEHPCENCKAPYGYQNHMPLNNNTESFSNEVKNATVSGNLDAPEGGFDAIMQAIACRSQIGWREQARRLLVFSTDAGFHYAGDGKLGGVIAPNDGECHLSPKGEYTHSTLQDYPSISQINQKVKDNAINIIFAVTASQLSVYEKLVEHIQGSSAAKLDNDSSNVVELVKEEYRKISSSVEMKDNATGDVKITYFSSCLSNGPEVQTSKCDNLKEGQQVSFTAQIQLLKCPEDPRDWTQTIHISPVGINEVMQIQLTMLCSCPCENPGSIGYQVQANSCSGHGTSMCGICNCDDSYFGNKCECSATDLTSKFANDTSCRADSTSTTDCSGRGHCVCGACECHKRPNPIEIISGKHCECDNFSCERNRNQLCSGPDHGTCECGRCKCKPGWTGSNCGCQESNDTCMPPGGGEICSGHGTCECGVCKCTVNDQGRFSGRHCEKCPTCSGRCQELKDCVQCQMYKTGELKNGDDCARNCTQFVPVGVEKVEIDETKDEQMCKFFDEDDCKFMFKYSEQGELHVYAQENKECPAKVFMLGIVMGVIAAIVLVGLAILLLWKLLTTIHDRREFARFEKERMNAKWDTGENPIYKQATSTFKNPMYAGK | Function: Integrin alpha-PS1/beta-PS is a receptor for laminin . Integrin alpha-PS2/beta-PS is a receptor for Tig, wb and Ten-m . Contributes to endodermal integrity and adhesion between the midgut epithelium and the surrounding visceral muscle . Essential for migration of the primordial midgut cells and for maintaining, but not establishing, cell polarity in the midgut epithelium . The two beta subunits mediate midgut migration by distinct mechanisms: beta-PS requires rhea/talin and Itgbn does not . Required for rhea/talin correct cellular localization in the midgut . Required for many embryonic (dorsal closure and somatic muscle attachments) and postembryonic developmental processes (attachment between cell layers of imaginal disks, organization of ommatidial arrays and flight muscle development) . Involved in the function and/or development of the olfactory system . In the testes, essential for shv-dependent maintenance of somatic hub cells and their localization to the apical tip . Plays a role in timely border cell migration during oogenesis .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 92656
Sequence Length: 846
Subcellular Location: Apical cell membrane
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Q96J02 | MSDSGSQLGSMGSLTMKSQLQITVISAKLKENKKNWFGPSPYVEVTVDGQSKKTEKCNNTNSPKWKQPLTVIVTPVSKLHFRVWSHQTLKSDVLLGTAALDIYETLKSNNMKLEEVVVTLQLGGDKEPTETIGDLSICLDGLQLESEVVTNGETTCSENGVSLCLPRLECNSAISAHCNLCLPGLSDSPISASRVAGFTGASQNDDGSRSKDETRVSTNGSDDPEDAGAGENRRVSGNNSPSLSNGGFKPSRPPRPSRPPPPTPRRPASVNGSPSATSESDGSSTGSLPPTNTNTNTSEGATSGLIIPLTISGGSGPRPLNPVTQAPLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEPLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATSQSKEFDPLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQGQLNEKPLPEGWEMRFTVDGIPYFVDHNRRTTTYIDPRTGKSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQHIKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRHYARTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVGKENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE | Function: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . Catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation . Involved in the control of inflammatory signaling pathways . Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways . Promotes the association of the complex after TNF stimulation . Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains . This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1 . Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways . Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response . Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages . Mediates JUN ubiquitination and degradation (By similarity). Mediates JUNB ubiquitination and degradation . Critical regulator of type 2 helper T (Th2) cell cytokine production by inducing JUNB ubiquitination and degradation (By similarity). Involved in the negative regulation of MAVS-dependent cellular antiviral responses . Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation . Following ligand stimulation, regulates sorting of Wnt receptor FZD4 to the degradative endocytic pathway probably by modulating PI42KA activity . Ubiquitinates PI4K2A and negatively regulates its catalytic activity . Ubiquitinates chemokine receptor CXCR4 and regulates sorting of CXCR4 to the degradative endocytic pathway following ligand stimulation by ubiquitinating endosomal sorting complex required for transport ESCRT-0 components HGS and STAM . Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination . Ubiquitinates SNX9 . Ubiquitinates MAP3K7 through 'Lys-48'-linked conjugation (By similarity). Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP . Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID . Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 . Inhibits the replication of influenza A virus (IAV) via ubiquitination of IAV matrix protein 1 (M1) through 'Lys-48'-linked conjugation resulting in M1 proteasomal degradation . Ubiquitinates NEDD9/HEF1, resulting in proteasomal degradation of NEDD9/HEF1 .
PTM: On T-cell activation, phosphorylation by the JNK cascade on serine and threonine residues surrounding the PRR domain accelerates the ubiquitination and degradation of JUN and JUNB. The increased ITCH catalytic activity due to phosphorylation by JNK1 may occur due to a conformational change disrupting the interaction between the PRR/WW motifs domain and the HECT domain and, thus exposing the HECT domain (By similarity). Phosphorylation by FYN reduces interaction with JUNB and negatively controls JUN ubiquitination and degradation.
Location Topology: Peripheral membrane protein
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 102803
Sequence Length: 903
Domain: The WW domains mediate interaction with PPxY motif-containing proteins.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cell membrane
EC: 2.3.2.26
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Q8C863 | MSDSGPQLDSMGSLTMKSQLQITVISAKLKENKKNWFGPSPYVEVTVDGQSKKTEKCNNTNSPKWKQPLTVIVTPTSKLCFRVWSHQTLKSDVLLGTAGLDIYETLKSNNMKLEEVVMTLQLVGDKEPTETMGDLSVCLDGLQVEAEVVTNGETSCSESTTQNDDGCRTRDDTRVSTNGSEDPEVAASGENKRANGNNSPSLSNGGFKPSRPPRPSRPPPPTPRRPASVNGSPSTNSDSDGSSTGSLPPTNTNVNTSTSEGATSGLIIPLTISGGSGPRPLNTVSQAPLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEPLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATSQNKEFDPLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQGQLNEKPLPEGWEMRFTVDGIPYFVDHNRRATTYIDPRTGKSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQHIKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECGLEMYFSVDKEILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRHYTRTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVGKENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE | Function: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation (By similarity). Involved in the control of inflammatory signaling pathways (By similarity). Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways (By similarity). Promotes the association of the complex after TNF stimulation (By similarity). Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains (By similarity). This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1 (By similarity). Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways (By similarity). Regulates the transcriptional activity of several transcription factors involved in immune response . Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages (By similarity). Mediates JUN ubiquitination and degradation . Mediates JUNB ubiquitination and degradation . Critical regulator of type 2 helper T (Th2) cell cytokine production by inducing JUNB ubiquitination and degradation . Involved in the negative regulation of MAVS-dependent cellular antiviral responses (By similarity). Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation (By similarity). Following ligand stimulation, regulates sorting of Wnt receptor FZD4 to the degradative endocytic pathway probably by modulating PI42KA activity (By similarity). Ubiquitinates PI4K2A and negatively regulates its catalytic activity (By similarity). Ubiquitinates chemokine receptor CXCR4 and regulates sorting of CXCR4 to the degradative endocytic pathway following ligand stimulation by ubiquitinating endosomal sorting complex required for transport ESCRT-0 components HGS and STAM (By similarity). Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination . Ubiquitinates SNX9 (By similarity). Ubiquitinates MAP3K7 through 'Lys-48'-linked conjugation . Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP (By similarity). Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID . Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (By similarity). Ubiquitinates NEDD9/HEF1, resulting in proteasomal degradation of NEDD9/HEF1 (By similarity).
PTM: On T-cell activation, phosphorylation by the JNK cascade on serine and threonine residues surrounding the PRR domain accelerates the ubiquitination and degradation of JUN and JUNB. The increased ITCH catalytic activity due to phosphorylation by JNK1 may occur due to a conformational change disrupting the interaction between the PRR/WW motifs domain and the HECT domain and, thus exposing the HECT domain. Phosphorylation by FYN reduces interaction with JUNB and negatively controls JUN ubiquitination and degradation. Interacts directly with LDLRAD3; this interaction promotes ITCH auto-ubiquitination leading to its degradation .
Location Topology: Peripheral membrane protein
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 98994
Sequence Length: 864
Domain: The WW domains mediate interaction with PPxY motif-containing proteins.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cell membrane
EC: 2.3.2.26
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J9VTS6 | MSDEKNYGISLAAPARPDLGSRTASQLEKATASHVEFATPKDPGALHDATLMAGERTEKLTKFVVGLALFASVSGFCFGFDTGVISAALVSIKDDFGHILDDTEKEWISAATSCGALVGALSSGALADRVGRKWTLAVGDVWFTLGAIIICSSFSVVQMIVGRAVLGLGVGTAAAIAPLYIAEVAPTRFRGALVTVQSIAITGGQFFSYCIGIPLTGHNGWRIQFAIGIVPAVVQAAVVHFLPESPRYDLLRGQREAALATIHRSYKGMSEDYIAVKFAALEEVVGISADFNRGHTLGQKMRLVLTEGKYRKPAITALGIGIFQQLCGFNSLMYYAATIFSYAGFDNPTSVGLIVSGTNWFFTFVAMMILDRVGKRRILLSTYPGMIAGLALASVAFWKMTGSTGHRLVEGTEYPQQWSNMMLGMMVVFIAFYATGSGNITWTVGEMFPLEMRGIGASILAGGVWAANIVISATFLTLMNAIGPTPTFALYAGICLAGLIFIYFCYPEPSGLSLEEIQIIYNYGFGVQKSREIRAEHKLKAQEMRDRANSHIGGSATASDDQLNKV | Function: Major transporter for myo-inositol . Plays a role in the traversal of the host blood-brain barrier .
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60694
Sequence Length: 566
Subcellular Location: Cell membrane
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A0A1D8PH98 | MGSSTNNTQSKATPSVLENEVNSSKSSVVSSTSSAKGLLRETTNHGTMETSSVQISESESRPSKMVLVLTLASSISGFMFGYDTGYISSALVQIGTDLSNKILTSGEKEFITSATSLGALLGAVVGGVLANLIGRRRVLLGSNIIFVVGTIIQLAARTVWTMIAGRFVLGWGVGIASLIAPLMISELAPAKYRGRLIVTNVIFITGGQLIAYFINWGLTRVSHGWRVSVGLCMVPPVLQFVLFWFLPDTPRFYVMNGNFEKARQVLRKVHVDPSDEFVNATIDEMIASDSTVPGNGPLQKAWKSIKIIHTTPGNFRALILACGLQGIQQFTGFNSLMYFSATIFETIGFHNATAVSIIIAATNFVFTGIAICIIDKVGRRRILLVGMPCMCISLIVCAVAFHYLNVDFSTGTVVSRGINGWGIVVIIGMILYVASYAIGIGNAAWVGVELFSDVNVRSIGAMYAACTNWAGSLVIASTFLTMLENITPTGTFSFFAGLCFIAFFFVYFLLPDTAGLELEETTDFLSNGFNVKQAAQLSKERKKHSKFAKSKPTV | Function: Major transporter for myo-inositol.
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59703
Sequence Length: 554
Subcellular Location: Cell membrane
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J9VHZ4 | MSARPAQPNIYAPIRTSLSGYPSPTHSGSSTPASLEFSDGRLPENNVERDMSKVVERVALLGEADEGAVIVEGEDKVTKFVWMLVSAAAISGLLFGYDTAAISGMLVIIKDDLGTILSSWQKEVITSATTLGALLGGLAAGCVSDFTGRRLVIVFANVAFIGGSICQAACHTVAAMIAGRFIVGLGVGLASCIVPLYIGELAPTMIRGRLVTINCVAVTLGQVVAYAIGASFQNVHNGWRWIVGLGAMPSFVQLAAIGFLPESPRILLLRSDVAGARAITAKIYPLATIEQVDRKIEIMKAAVDQSIEYNANSTWFERLKSLVMVGTNRRALIIGCGLQAAQQLCGFNTLMYYSATIFAMLGFNNATAVGLIVATVNVLFTLVALKIVDPVGRRRTMLFTLPIMILALVFAAIFFYYLTLSTNGILIEDHDYPRSLSILVLLSMLLYVAGYATGLGNIPWQQGELFRLEVRGIGTSICTAVNWSCNMLIAGTFLSLMDAATPSGAFGIYAGFCVIGWVFCWMLYPETSGLSLEEVYFVFEEGFGIKKSQQLRKQKLVEAAKLKAIFE | Function: May function as a transporter or as a sensor for myo-inositol.
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60983
Sequence Length: 567
Subcellular Location: Cell membrane
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Q10286 | MSISSKDFQNVTSAGFADDTFAADTFAADKKSPFESSVFENKTQVLPVDSVSRLSNGARSRSNSNISLSEPHALNDTVEDQPVSKWVWVLAFAAGIGGLLFGYDTGVISGALVVIGTSLGGHELTNGGKEFITSATSLGALLGGIIAGALADFFGRKPVIAIASIIIIVGSIVQVTAHHLWHMIVGRFVIGWGVGIASLIIPLYLSEIAPSKIRGRLVIIYVLLITAGQVIAYGIDTAFEHVHNGWRWMVGLAMVPAAFQLFILIWLPESPRLLVKKERSQEAYNTLARIYPTAHPYEIKTKLYLIQEGVRDPFSGSRWQKIVKTFKELYFNPSNFRALILACGLQAMQQLSGFNSLMYFSSTIFEVVGFNNPTATGLIIAATNFVFTIVAFGVIDFFGRRILLLLTVWGMIAALIVCAVAFHFLPKDENGNYTSGQSNAWAIVVLISMIVYVASYASGLGNLPWQQSELFPMSVRGLGTGMSTAVNWAGNLGIGASFLTLMSEITPTGTFALYGGLCFLGWLGALFCYPDLTDYTIEEIGELLKHGFGVRESMRHLKRVRQERAWSREDKEQNN | Function: Transporter for myo-inositol.
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62758
Sequence Length: 575
Subcellular Location: Golgi apparatus membrane
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Q43667 | MAAFVESARAGAGADEVIQLVSDGVNEYSEKMMEGVVACPRILMPCKVNDDCLRGCKCLSNGYCG | Function: Inhibits trypsin.
Sequence Mass (Da): 6877
Sequence Length: 65
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q9US46 | MLEVEVESDNKHLVADELIALQSIYPEIHLDGNNYGRLNIPVNTESDYFLSFKSPDESTLTDTIVVRHFPDLVMEFFLPEAYPFNSPPTFFLKSSWLPLKQKRVLTSSLIKLWNEIHDCVLFDAIEHVRSIATIAFHLPTEMVFPGGFDDLKKEILAFDKNAKLLEFQIRKFQCNVCFDEFNGTDCFQLTRCGHVSCQSCLRDYYTMCIQEGMFSQIKCIDLDCGKDAPVLTLKELESIVGVQLTNRYKELEEKRRYENDSNIIFCPRSFCQGPSKRDPGQKLAICQKCDFAFCSFCQATWHGDLSPCKLEGDSKKLVEMYLNYQENEPEKALELEKRYGKRIIDRLVEQVKNDEEAEKWVLLNGQRCPTCDRVVERIDGCCHMNCLCGTHFCFLCGAYLMEQNPYKHFNDPVSSCYGMLFASAAEKQRFSENWT | Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 50297
Sequence Length: 435
Domain: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain.
Subcellular Location: Cytoplasm
EC: 2.3.2.31
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Q04638 | MALTQFENDLEILRDMYPELEMKSVKVEEEGEFPQRINGKLLFKISLLADVNIEFGEQHMLLSNLSNECVEFTIYSCHYPDIRRCVVMDIKSLWISTDEKKMLIDKALRLVEETVDMSIEFADSFTSILILIFGFLIDDTAILLFPNGIRKCLTQDQYDLFKQISEEATLQKVSRSNYHCCICMEMEKGVRMIKLPCENANVEHYLCRGCAKSYFTAMIQENRISSVRCPQCEYKELKLEDFKSYKKMLKALFTPLIPVSFLKEVIDTELCERYEKMFYNQAATRLSKYCPYACVTCRRCDSWCTKEDLDDAMIQCQKCHFVFCFDCLHAWHGYNNKCGKKVSLSTDIIEEYLDDTVTSYERKRKLEAKYGRRVLELEVNDYLAEKMLDLAIKKEGSNLQRCPKCKVVVERSEGCNKMKCEVCGTLFCFICGVLLYPEDPYEHFREAYSGCYGRLFEGMPGTET | Function: Modulates the efficiency of translation termination, resulting in the readthrough of all three types of nonsense codons UAA, UAG and UGA.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 54096
Sequence Length: 464
Domain: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain.
EC: 2.3.2.31
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Q47316 | MILPSEKSATDVAAQCFLNALIRETKDWQLAEYPPDELIIPLDEQKSLHFRVAYFSPTQHHRFAFPAHLVTASGSYPVDFTTLSRLIIDKLRHQLFLPVPLCETFHQRVLESYAHTQQTIDARHDWAILREKALNFGEAEQALLTGHAFHPAPKSHEPFNRQEAERYLPDMAPHFPLRWFSVDKTQIAGESLHLNLQQRLTRFAAENAPQLLNELSDNQWLFPLRPWQGEYLFQQVWCQALFAKGLIRDLGEAGTSWLPTTSSRSLYCATSRDMIKFSLSVRLTNSVRTLSVKEVERGMRLARLAQTDGWQMLQARFPTFRVMQEDDWTGLRDLNGNIMQESLFSPAWKTLLLEQPQSQTNVLVSLTQAGPHGGDSLLVSAVKRLSDRLGITVQQAAHAWVDAYCQQVLKPLFTAEADYGLVLLAHQQNILVQMLGDLPVGFIYRDCQGSAFMPHATEWLDTIDEAQAENIFTREQLLRYFPYYLLVNSTFAVTAALGAAGLDSEANLMARVRTLLAEVRDQVTHKTCLNYVLESPYWNVKGNFFCYLNDHNENTIVDPSVIYFDFANPLQAQEV | Function: Catalyzes the attachment of a first N-acetyl-N-hydroxylysine to a carboxylic group of citric acid to yield N-citryl-N-acetyl-N-hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Catalytic Activity: ATP + citrate + N(6)-acetyl-N(6)-hydroxy-L-lysine = AMP + diphosphate + H(+) + N(2)-citryl-N(6)-acetyl-N(6)-hydroxy-L-lysine
Sequence Mass (Da): 65570
Sequence Length: 575
Pathway: Siderophore biosynthesis; aerobactin biosynthesis.
EC: 6.3.2.38
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Q76BS7 | MHRNNERINLEKSNDWANTNEPSIACFLNSLARESQSVQLLWGEDGKRVYRLPLANSDSINIPLSYFSSLGSHEYCLPALLHTQDSIKTLSVEQLIEHIVNEPALVGIVSEAKKAIFTKRVLESHRNTEQAIEHSPYQEQLFTEQLDFKTAEQGLLIGHSFHPAPKSREQFSLSDAKLYSPELGGQFKLFWLSVEQSLLTSGSSADIHFNQRFEALVAHDPKLVEALQNAQQQGHELLPVHPWQWHVMVENPSIKGYIATKQIQNLGQLGATWYPTSSTRSLYAPGLPYMLKFSLSVKLTNSIRNLSLKECDSWNDLNDLFQHPQLAQQLGNGRGFQLMQEPAYIGLKDLNGKIIDESLVAFRDNPLMNNPAEEAVVLATLTQQNPYGGSSLVAARIEHYATQQHLSLHQAASLWFDAYCRHAVVPLFHLQANFGIVFLAHQQNIVMQLEQGFPVGMYYRDCQGTGYTDLAFKLFGEQLGDRKEALENYWNQDKVRRYFAYYLIINSTFNLISAICANLDVEESELIEILYHNLNALLQSGVKDDLCLRYVLTSEALCCKGNFFCYLQNFNENSIPDPAVIYFDLPNPLARVEEIAHV | Function: Catalyzes the attachment of a first N-acetyl-N-hydroxylysine to a carboxylic group of citric acid to yield N-citryl-N-acetyl-N-hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Catalytic Activity: ATP + citrate + N(6)-acetyl-N(6)-hydroxy-L-lysine = AMP + diphosphate + H(+) + N(2)-citryl-N(6)-acetyl-N(6)-hydroxy-L-lysine
Sequence Mass (Da): 67795
Sequence Length: 598
Pathway: Siderophore biosynthesis; aerobactin biosynthesis.
EC: 6.3.2.38
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Q47317 | MSGPNIVHSGYGLRCEKLDKPLNLGWGLDNSAVLHWPGELPTGWLCDALDQIFIAAPQLSAVVLPWSEWCEEPQALTLFGQVQSDIIHRSAFWQLPLWLSSPANRASGEMVFDAEREIYFPQRPPRPQGEVYRRYDPRIRRMLSFRIADPVSDAERFTRWMNDPRVEYFWEQSGSLEVQIAYLERQLTSKHAFPLIGCFDDRPVSNIEIYWAAEDRIGRHYSWQPFDRGLHLLVGEQQWRGAHYVQSWLRGVTHYLLLNEPRTQRTVLEPRTDNQRLFRHLEPAGYRTIKEFDFPHKRSRMVMADRHHFFTEVGL | Function: Catalyzes the transfer of acetyl from acetyl-CoA to the N-hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Catalytic Activity: acetyl-CoA + N(6)-hydroxy-L-lysine = CoA + N(6)-acetyl-N(6)-hydroxy-L-lysine
Sequence Mass (Da): 37029
Sequence Length: 315
Pathway: Siderophore biosynthesis; aerobactin biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.102
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Q47318 | MNHKDWDLVNRRLVAKMLSELEYEQVFHAESQGDDRYCINLPGAQWRFIAERGIWGWLWIDAQTLRCADEPVLAQTLLMQLKQVLSMSDATVAEHMQDLYATLLGDLQLLKARRGLSASDLINLNADRLQCLLSGHPKFVFNKGRRGWGKEALERYAPEYANTFRLHWLAVKREHMIWRCDNEMDIHQLLTAAMDPQEFARFSQVWQENGLDHNWLPLPVHPWQWQEKIATDFIADFGEGRMVSLGEFGDQWLAQQSLRTLTNASRRGGLDIKLPLTIYNTSCYRGIPGRYIAAGPLASRWLQQVFATDATLVQSGAVILGEPAAGYVSHEGYAALARAPYRYQEMLGVIWRENPCRWLKPDESPFLMATLMEWDENNQPLAGAYIDRSGLDAETWLTQLFRVVVVPLYHLLCRYGVALIAHGQNITLAMKEGVPQRVLLKDFQGDMRLVKEEFPEMDSLPQEVRDVTSRLSADYLIHDLQTGHFVTVLRFISPLMVRLGVPERRFYQLLAAVLSDYMKKHPQMSERFALFSLFRPQIIRVVLNPVKLTWPDLDGGSRMLPNYLEDLQNPLWLVTQEYES | Function: Catalyzes the attachment of the second N-acetyl-N-hydroxylysine to the carboxylic group of N-citryl-N-acetyl-N-hydroxylysine to yield aerobactin. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Catalytic Activity: ATP + N(2)-citryl-N(6)-acetyl-N(6)-hydroxy-L-lysine + N(6)-acetyl-N(6)-hydroxy-L-lysine = aerobactin + AMP + diphosphate + H(+)
Sequence Mass (Da): 66846
Sequence Length: 580
Pathway: Siderophore biosynthesis; aerobactin biosynthesis.
EC: 6.3.2.39
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Q76BS5 | MVMDQLALHRYWAVANQKMVGKILSEFAYEQAFQFEPTAQGYQLNLENGTRYCFAGEENIWGQVMIDPTSITRHAEIEADEPISAALLMRDLQPLLKMPDDAFAEHLEDLNATLLGDCKLMQRNEAITARDLAMLPCEQQQTYFDGHPKFVFNKGRRGWGSDDLKRYAPEAERVSNWVGSRFITRFCSSPPTMKSHGKPCCKAPSRPMKSSRWTVCWLPISLDSTIIVMFRFILWQWSNKLALLFVREIATKQLVYLGEFGDHFLPQLSLRTLSNVTRPAGYDIKLPLTVMNTSCYRGIPGRYILAGPTASDWIDQVFKSDPLLIAKQAEVLQEPAAAFAAQADYALLPNAPYRYHELLGVIWRESAASKLKAGERAILMAALMESDNQGQPLIAEYVQASGLTLEAWLSKLFDAVVIPYYHLLCNYGVSLIAHGQNVTLVLENHAPKRILLKDFQGDMRLVSREYPEQASLDDSVKKVTVRLPEHLIIHDLQTGHFVTTLRFISPLVAKLGFSEPQFYRLLGDRLKAYMAAHREYQPRFEQFDLFKPRILRIGLNLAKFRHSTDASASRMLPDMDDMLNNPLTKALEHQG | Function: Catalyzes the attachment of the second N-acetyl-N-hydroxylysine to the carboxylic group of N-citryl-N-acetyl-N-hydroxylysine to yield aerobactin. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Catalytic Activity: ATP + N(2)-citryl-N(6)-acetyl-N(6)-hydroxy-L-lysine + N(6)-acetyl-N(6)-hydroxy-L-lysine = aerobactin + AMP + diphosphate + H(+)
Sequence Mass (Da): 67163
Sequence Length: 591
Pathway: Siderophore biosynthesis; aerobactin biosynthesis.
EC: 6.3.2.39
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P11295 | MKKSVDFIGVGTGPFNLSIAALSHQIEELDCLFFDEHPHFSWHPGMLVPDCHMQTVFLKDLVSAVAPTNPYSFVNYLVKHKKFYRFLTSRLRTVSREEFSDYLRWAAEDMNNLYFSHTVENIDFDKKRRLFLVQTSQGEYFARNICLGTGKQPYLPPCVKHMTQSCFHASEMNLRRPDLSGKRITVVGGGQSGADLFLNALRGEWGEAAEINWVSRRNNFNALDEAAFADEYFTPEYISGFSGLEEDIRHQLLDEQKMTSDGITADSLLTIYRELYHRFEVLRKPRNIRLLPSRSVTTLESSGPGWKLLMEHHLDQGRESLESDVVIFATGYRSALPQILPSLMPLITMHDKNTFKVRDDFTLEWSGPKENNIFVVNASMQTHGIAEPQLSLMAWRSARILNRVMGRDLFDLSMPPALIQWRSGT | Function: Flavoprotein monooxygenase required for N-hydroxylation of lysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced by the organism under iron-stressed conditions.
Catalytic Activity: L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+)
Sequence Mass (Da): 48726
Sequence Length: 425
Pathway: Siderophore biosynthesis; aerobactin biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.14.13.59
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Q27546 | MPKKIILDCDPGLDDAVAILLAHGNPEIELLAITTVVGNQTLAKVTRNAQLVADIAGITGVPIAAGCDKPLVRKIMTAGHIHGESGMGTVAYPAEFKNKVDERHAVNLIIDLVMSHEPKTITLVPTGGLTNIAMAARLEPRIVDRVKEVVLMGGGYHEGNATSVAEFNIIIDPEAAHIVFNESWQVTMVGLDLTHQALATPPILQRVKEVDTNPARFMLEIMDYYTKIYQSNRYMAAAAVHDPCAVAYVIDPSVMTTERVPVDIELTGKLTLGMTVADFRNPRPEHCHTQVAVKLDFEKFWGLVLDALERIGDPQ | Function: Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, but has a preference for inosine and uridine as substrates. Is not active on thymidine and 2'-deoxynucleosides. Functions in purine salvage from the blood of the host, a fundamental pathway since protozoan parasites such as C.fasciculata are incapable of de novo purine biosynthesis.
Catalytic Activity: H2O + inosine = D-ribose + hypoxanthine
Sequence Mass (Da): 34326
Sequence Length: 315
Pathway: Purine metabolism; purine nucleoside salvage.
EC: 3.2.2.2
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P83851 | MPRKIILDCDPGIDDAVAIFLAHGNPEIELLAITTVVGNQSLEKVTQNARLVADVAGIVGVPVAAGCTKPLVRGVRNASHIHGETGMGNVSYPPEFKTKLDGRHAVQLIIDLIMSHEPKTITLVPTGGLTNIAMAVRLEPRIVDRVKEVVLMGGGYHTGNASPVAEFNVFIDPEAAHIVFNESWNVTMVGLDLTHQALATPAVQKRVREVGTKPAAFMLQILDFYTKVYEKEHDTYGKVHDPCAVAYVIDPTVMTTERVPVDIELNGALTTGMTVVDFRYPRPKNCRTQVAVKLDFDKFWCLVIDALERIGDPQ | Function: Catalyzes the hydrolysis of the N-glycosidic bond of all of the commonly occurring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates. Likely functions in purine salvage from the host, a fundamental pathway since protozoan parasites such as L.major are incapable of de novo purine biosynthesis.
Catalytic Activity: H2O + inosine = D-ribose + hypoxanthine
Sequence Mass (Da): 34310
Sequence Length: 314
Pathway: Purine metabolism; purine nucleoside salvage.
EC: 3.2.2.2
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P14542 | MMISKKYTLWALNPLLLTMMAPAVAQQTDDETFVVSANRSNRTVAEMAQTTWVIENAELEQQIQGGKELKDALAQLIPGLDVSSRSRTNYGMNVRGRPLVVLVDGVRLNSSRTDSRQLDSIDPFNMHHIEVIFGATSLYGGGSTGGLINIVTKKGQPETMMEFEAGTKSGFSSSKDHDERIAGAVSGGNEHISGRLSVAYQKFGGWFDGNGDATLLDNTQTGLQYSDRLDIMGTGTLNIDESRQLQLITQYYKSQGDDDYGLNLGKGFSAIRGTSTPFVSNGLNSDRIPGTDGHLISLQYSDSAFLGQELVGQVYYRDESLRFYPFPTVNANKQVTAFSSSQQDTDQYGMKLTLNSKPMDGWQITWGLDADHERFTSNQMFFDLAQASASGGLNNKKIYTTGRYPSYDITNLAAFLQSGYDINNLFTLNGGVRYQYTENKIDDFIGYAQQRQIGAGKATSADAFWRLSRLRHFLFNAGLLMHITEPQQAWLNFSQGLELPDPGKYYGRGIYGAAVNGHLPLTKSVNVSDSKLEGVKVDSYELGWRFTGNNLRTQIAAYYSISDKSVVANKDLTISVVDDKRRIYGVEGAVDYLIPDTDWSTGVNFNVLKTESKVNGTWQKYDVKTASPSKATAYIGWAPDPWSLRVQSTTSFDVSDAQGYKVDGYTTVDLLGSYQLPVGTLSFSIENLFDRDYTTVWGQRAPLYYSPGYGPASLYDYKGRGRTFGLNYSVLF | Function: Receptor for cloacin DF13/aerobactin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81014
Sequence Length: 732
Subcellular Location: Cell outer membrane
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A0A1W7HCY1 | MSGHSFFEHLFEHSQHVTPYLHGAIKPRPERCAEHGFIHIEHASSDHIRALYESLKLAHPEAGAAYWLTRTWTLLCWQPLYVAFIAIYSCQGLPKLSSMGQHVQPRFVSGYQFDDDEYRQGSEQELIAHAGKELCALFDYFRQEMSLWTRIRPGFTQHLFADGVFGCLVKLSQFYPTLSGDYFLEQARLWLAACQLPEKLIQSLRYDETSRQLSLVRTSCCLVYKCQGRELCRDCPRHPDNKRE | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB . Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)-enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)-nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Catalyzes also reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor .
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Sequence Mass (Da): 28349
Sequence Length: 244
Subcellular Location: Cytoplasm
EC: 1.16.1.10
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Q7NN81 | MMRFLILATNNQGKLQELRRLLAGTGWVVQAAPPDFAVEETGTTFAENARLKALAAAERTGEWSVGDDSGLAVDALGGAPGVYSARYGRNDGERISRLLAALAGQADRGARFICAIALAEPGRVLKEVEAECRGVILHAPRGNGGFGYDPIFLVPELDKTFAELDIVEKERHSHRGRAVRKLLSGCSRGTFIVDH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 20985
Sequence Length: 195
EC: 3.6.1.66
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Q7VLS3 | MNRTKIVLATSNKGKVKEMADVLSAFGFEVIAQSEFGLVSPPETGLTFVENALLKARYASKMTGLPAIADDSGLAVDALAGAPGLYSARYAGIEDDDTANRRKLLAEMQNVPDGQRAAKFVSCIVMLKHETDPTPKIAFGECFGEILREERGQNGFGYDALFFYPAKQCTFAELDSTEKKQISHRALALVALQKQL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21297
Sequence Length: 196
EC: 3.6.1.66
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P44598 | MKQKIVLATGNKGKVKEMADVLSDFGFEVIAQTDLGIESPEETGLTFVENALLKARYASEKSGLPAIADDSGLVVSALNGAPGLYSARYAGEEGNDAKNREKLLAELAHIAQEQRQAKFVSCIVFLQHPTDPSPIIAEGECCGVIGFEEKGENGFGYDSLFFSPEQGCTFAELETAEKKKISHRAKALSVLKSKL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 20972
Sequence Length: 195
EC: 3.6.1.66
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Q7VF43 | MVIVLASANQHKICEFQAMLKNVKEKVKVYAYGELLETFEIAENGNSFKENATLKVKAIYQALYTLSQSTMQENIRNLFAQPLAIIAEDSGLCVPVLNGEPGIYSARYAHHKQFASMQYKNTDEANLYCLLNALTHCAPTPAFFVAHIALIFIKPYFCTYTLPPLEQCVIEHFEGILNGEVINEMRGNEGFGYDPLFIPAEHNPQSLTLAEFDMSAKNTISHRKKALSQCINRLFDKS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 26793
Sequence Length: 238
EC: 3.6.1.66
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B4U8R9 | MKLMICTSNKKKFEEISSILESLKKDENLDLEFVKPPKEIEVEEYANTFLSNAYLKAKAYYNAFGIPALADDSGLVVEAFSDNLERPGVYSARFYKDSFGSHVLKEEDFKLSKDELNNLKVLRLLEKEENRKAKFVSVVAIVLSNNYGIFGEGELKGHIAKEPFGNFGFGYDPIFIPEGYNTTLANIENKDKISHRRQALEAVFFMLKKML | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 24059
Sequence Length: 211
EC: 3.6.1.66
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A2BJY7 | MEARVILIATTNKHKIEEINEVLQSCGYRVEPAAASKLEVQSNRLEDVAAYAAIQAYLALQRPVIVEDAGLFVEALGGFPGPYSSYVFKTIGIRGLLKLLEDVENRRAYFKSVIALAHSGGVEVFTGTVHGVIAEKPRGDRGFGYDPVFIPEGSSKTFAEMETQEKNKFSHRGKAARELCRWLRQYGPPR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21059
Sequence Length: 190
EC: 3.6.1.66
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A8A8W1 | MVSKKVYFLTSNPHKAKEVSDVLSQFSIEVVPLKGEKLEIQADSVEEVARFAAEEAKKRFKERPLLLEDSGLFVDALKGFPGPYSNYVYRTLGLEGLLKLMEGVEDRRARFVCAAALVKEDDKIVIEVGEVEGEIAYEPRGDKGFGFDPIFVPLGYEKTFAELGEEVKKRISHRARAFMKIAKHLSGE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21114
Sequence Length: 188
EC: 3.6.1.66
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B1L6T7 | MIFASSNRHKYEEFRRMLSDLIDLKFLEVDYLEPQGEDTREIVVTSAKWLSNYIREPFFIEDSGLFIEALNGFPGPYSSYVFKKIGNEGVLKLMNGVENRRAFFISVIALSYGRGIEVFEGRVQGTIAREVRGGGWGFDPIFIPNGSNKTYGELGDEKDRFSHRGASCRKLREFLMRFGSDRLP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21100
Sequence Length: 184
EC: 3.6.1.66
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Q5FLV7 | MSQKILFATGNKGKARELKEAFKTAGVDVEIITNSDLDNPPHPIESGRTFEANAKIKAHELADYSKLPTIADDSGLMVDALNGEPGVRSARYAGEAHNDAKNNAKLLANLGGIPDEKRTAKFWTTIVVSMPGEFEKDLVVSGTCSGRILAAPRGDDGFGYDPLFFVPKKDKTFAQMTTDEKNEISHRGNVVRELLKVLPALA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21884
Sequence Length: 202
EC: 3.6.1.66
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Q9CG29 | MEKTLIIATRNSGKTKEFKKLFADFGYEIKDLTDYPELSEIEETGTTFEENARLKAEQIAEITGQVVIGDDSGLCVDVLGGLPGIWSHRFSAPDPTDEKNIAKLLHELAPTAITPERRSAHFHTTLVAAKPGRESLVVEADWDGYIALAPKGENGFGYDPIFMVDAFRTAAELSEKEKNQVSHRGQALRKLMAELPEWLYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 22380
Sequence Length: 201
EC: 3.6.1.66
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Q88V20 | MTKPQTLIIATNNANKAREFSAMLAPYDITIKTLADFPNIPEIKENGITFEENATKKATVVVEATGLPAIADDSGLMVKALHGDPGVFSARYAGDHDDAANNAKLLANLGGVPEAERTATFHTTLVALKPSGEKLVVNGELAGRILIAPRGDNGFGYDPLFWSSKFQKSLAELTPAQKNQISHRGAALRQLMTKFDEWWAKA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = diphosphate + H(+) + XMP
Sequence Mass (Da): 21791
Sequence Length: 202
EC: 3.6.1.66
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E9FR69 | MENYVPFLVSHWRTVGLISVSIAAGVALGQLNQTHERAANKSQRVHTNSSIKAKQVKRESAIEQINEIEDDDEQSLEDQDVLPILFQYEKPSEADSIRRSEEFYRRMNQRRSVREISSDPVALEVIENIIKTGGTSPSGAHTEPWTFVVVSNLEMKQQIRQIIEAEEEINYKQRMGDVWVQDLQPVGTTWVKEYLTEAPWLILIFKQVHGFKRNGQKKIHYYNEISVSIATGFLLAAIQEAGLVTVTTTPLNCGPSIRVLLGRPVNEKLLLLLPVGYPKVGATVPDFKRKPLHDIMVHYQ | Function: Catalyzes the dehalogenation of halotyrosines such as 3,5-diiodo-L-tyrosine . Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity).
PTM: May be cleaved at Gln-55 . The cleaved form retains catalytic activity .
Location Topology: Single-pass membrane protein
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Sequence Mass (Da): 34084
Sequence Length: 300
Subcellular Location: Membrane
EC: 1.21.1.1
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E1JIB2 | MDVDELISSSKLLKHWPSLFITLALIWIVKRLFFKGNRVLKTYNLDEQVEEEVEHFADLGDELQPALEDKPHVPFVPGQNLNPNGAKRLYELMRGRRSIRSFNSHPKPDLSVIEDCIRAAGTAPSGAHTEPWTYCVVQEPELKRSIREIVEQEELVNYSQRMHPQWVTDLRPLQTNHVKEYLTEAPYLILIFKQTYGLSENGKRMRRHYYNEISTSIAAGILLCALQAAGLASLVTTPLNCGPALRNLLGRPVNEKLLILLPVGYPKDGCTVPDLARKNLSNIMVTF | Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine . Activity towards 3-fluoro-L-tyrosine is weak . Important for male and female fertility . May be involved in maintaining the viability of sperm, both during development in the testes and storage in the female spermatheca .
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32597
Sequence Length: 287
Subcellular Location: Cell membrane
EC: 1.21.1.1
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F4KU78 | MKQKPAFIPYAGAQFEPEEMLSKSAEYYQFMDHRRTVREFSNRAIPLEVIENIVMTASTAPSGAHKQPWTFVVVSDPQIKAKIRQAAEKEEFESYNGRMSNEWLEDLQPFGTDWHKPFLEIAPYLIVVFRKAYDVLPDGTQRKNYYVQESVGIACGFLLAAIHQAGLVALTHTPSPMNFLQKILQRPENERPFLLVPVGYPAEGAMVPDLQRKDKAAVMVVY | Function: Catalyzes the dehalogenation of halotyrosines such as 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine . Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity). Activity towards 3-iodo-L-tyrosine is much stronger than activity towards 3,5-diiodo-L-tyrosine and 2-iodophenol .
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Sequence Mass (Da): 25308
Sequence Length: 222
EC: 1.21.1.1
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T2MBC4 | MFDNLSGVSYGLLAGILAMLIHLVYQKITELKRRKDELKERESHPTDDLFPKEDFIPYHPSRYSEEEMIKRSNDFYLSMNARRSVRFFSNEDVPDEVIDNIIRTAGTSPSGAHTEPWTFVVIKNKLLKAKVREIIEEEEELNYKQRMGQKWVDDLKPLKTNWIKEYLTEAPYLILVFKQTYGITEDGQKKTHYYNEISASISCGFLLAAIQNAGLVALTSTPLNAGSKLRNLVGRGPNEKIVILLPVGYPSKNCQVPNLKRKPLNEIMIKFD | Function: Catalyzes the dehalogenation of halotyrosines such as 3,5-diiodo-L-tyrosine . Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity).
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31256
Sequence Length: 272
Subcellular Location: Membrane
EC: 1.21.1.1
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A7S5D9 | MEVFKALFKSKEAYTVDVDPMKDSDEHDLPRDPLSIRVTGEEEVNHIPYPYFDEIPTEEEMKKKSAEFYKSMKKRRTVRKISSEPVPLEVIENIVRVAGTSPSGAHTEPWTYVVIRDPDLKKQIKEVVEEEEQLNYARRMGEKWVQDLSILKTTWSKPYIETAPYLILIFKQVYGIKPDGDKKVHYYNEISVCISCGLLLAAIQNAGLVTVTSTPMNAGPRLRVLLNRPQNEKLIMLLPVGYPAKDAEVPNLTRKPLEEIMVLK | Function: Catalyzes the dehalogenation of halotyrosines such as 3,5-diiodo-L-tyrosine . Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity).
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Sequence Mass (Da): 30275
Sequence Length: 264
EC: 1.21.1.1
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B9K712 | MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF | Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine . Activity towards 2-iodophenol is weak .
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Sequence Mass (Da): 22028
Sequence Length: 186
EC: 1.21.1.1
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Q753H5 | MSEERGMKEQTISEMAQEMAHTTSEGLKKRIRKLYTFDELPAWQKDNELILSGYVRETNSVKECLRAMTYFNNESINIYTHLIPGVAYLVLFLIFADLVLAQLLPGLDAGEHRMLRFYLLGAFTCLACSSCFHCLKQHSEPHSRLWSKVDYLGILAQITCSTISLLYYGYHSYPSHFVFFSTLTVALCSACAVLVLNDSFNTVAFRPLRAFLFMAFGLSGVIPVLAGSYQFGFAEWAARIQLKYVLYEAVFYITGALVYGFRIPERFAPGKFDMVGHSHQIFHLLVVLGTLCHFRAVTGSYIFICTGKHYSSLLMFI | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35981
Sequence Length: 317
Subcellular Location: Endoplasmic reticulum membrane
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Q03419 | MSITTTRRRNQDSVCCKATRASIKVEAVSGQTVFEKQKLLHNFDELPEWQKDNDKILTGYVRETLSWKKCLYSLFYWNNETVNIYTHLVPAIVYFVFAITLTNYFLIPVFPSTSWSDYTVINIFLMGAFSCLMCSSCFHCMKQHSEKQSNFWSKLDYLGIISLISCSMIPIIYFGYFDHISYFSLFTIVTLVLATFCTVCVLHDKFNTSTFRPFRAMFFILFGFSGLLPLTTGFFKFGIQGVLNRIKVSFVFWEALFYISGAVIYGFRIPETLAPGKFDFFGSSHQIFHIMVVLGSVCHLKAIIDSYKLMHSHIHP | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36492
Sequence Length: 316
Subcellular Location: Endoplasmic reticulum membrane
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Q12442 | MSTLLERTKSVQELKKRAAGKTSANPAEVAKAKKVLRRLYSWDEIPEWQRDNDFILHGYVKETSSFIETFKSLFYLHNESVNIYSHLIPALGFFTVLLLDKSTIKVFATTTWLDHMVIDLFYSGAFACLILSSSFHCLKSHSLRIATLGNKLDYLGICILIVTSMVSILYYGYFEKFSLFCLFALITVSFGIACSIVSLKDKFRKREWRPYRAGLFVCFGLSSIIPIFSGLYCYSFSEIWTQIQLFWVLLGGVLYIIGAVLYGMRFPEKICPGKFDIWGHSHQLFHFLVVIAALCHLRGLLNSYELVHIKMENGIVS | Function: Probable receptor, which is involved in metabolic pathways that regulate lipid metabolism such as fatty acid oxidation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36279
Sequence Length: 317
Subcellular Location: Membrane
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Q75F81 | MSHPNTHMPRTHAVHGRAAPQRRGCRTSVEKTDQSGHSRSSLAESAMEQAQLRSRGEAGGGRSVLCASGEPGSAHKWAGAVTCSGAEEQPLHWAESRARGLARHLHYWELPYAWRENRYIIYGHRFYHSHRKSLLSVLNAYGWHNETINIWSHLVGAAVLAYLLCWGWPRSDVYRAAQVPRLAKWAIGAFLACGVKCMASSVAWHTFNGTCHLKLRSRFVCVDYTGITLLVTASVVTTVAVTLYGLSRPLMYAYMVASIGLGTAAGVMNWSPHFDRPEARPLRIAVYVGLAALGLVSFVHVWMQVRWASAHLMAPLVYKSLVWYGIGVVFYATLVPERWRSDVTLDCCSGPVHEAACRQFRDLPPVARKDRQFWSLWWVDYFCHSHFLWHVFVVLGVVGHYRAVLQMSRIVWLDAGRAF | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47153
Sequence Length: 419
Subcellular Location: Endoplasmic reticulum membrane
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Q07959 | MMDSSSKSLTQYIPSPMGSLSRLKQKGVDNFQKVKKSGKSIYNYNYSKFVPHPFSTIDESVKHSESGRYDDLEIIRPTKEKEVTSSVYKRNSGKSLNTESQFSLGDSDAATLVNSVATFKLNNASTSTSLVSSSSTVCSQAKSSLRSPTSRLNDTKIKEENNYISSVKDYCGPMRKSMVKTEILIEEPLNPTTDIKSFINSYNHGKAYSLGETQHLHYYQLPFPWRENRYIIHGYRFYNTHSKSLLSIFNWYGWHNETSNIWSHLLGAIYIIYLAIYDFPQSEVWRNSQVPPQARWIVFMFLAAALKCMLSSVFWHTFNGTSFLKLRSKFACVDYSGITILITASILTTEFVTMYSCYWAMYTYMSISLALGVFGVFMNWSPRFDRPEARPLRIRFFILLATMGVLSFLHLIFLTDLHYAATLFSPVTYKSVVWYLVGVVFYGSFIPERFRSDVQVDKTIPTNYELSTDLEIITKQREIHFREVPTAHSKCSSCPSHAKSFKSLWWVDYFGCSHTFWHFFVVLGVIGHYRAILDMFAKRWILS | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62571
Sequence Length: 543
Subcellular Location: Endoplasmic reticulum membrane
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Q99393 | MVSLTTIEQSPVKCETTTEKESNDTRGTDSNENAETKETKKGFPFHDLAKLQKQYKNKSSRNESLVALIYLLGSMLSFCLLIFFTDFYLIPLFPTTTTMTDYIVFNFYLLNVFVFCMVHFIYHFVKNISLQQHLEHWQKFSYLSNINLLISSQITILYYLFYDYVFFFKIFTLLMNFIGLVAYFFILTDKLISSKRFNKTVFFISVSVVCCSLPLLTAIITFDGLENLKERIKVNAITWELVALVAASIIYVTRFPESLFRRNKKEEGWNHSEYLFHLLISGTAFYHFFILIQSYILMHSSLNQPELINFKS | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36608
Sequence Length: 312
Subcellular Location: Endoplasmic reticulum membrane
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Q8IYV9 | MGPHFTLLCAALAGCLLPAEGCVICDPSVVLALKSLEKDYLPGHLDAKHHKAMMERVENAVKDFQELSLNEDAYMGVVDEATLQKGSWSLLKDLKRITDSDVKGDLFVKELFWMLHLQKETFATYVARFQKEAYCPNKCGVMLQTLIWCKNCKKEVHACRKSYDCGERNVEVPQMEDMILDCELNWHQASEGLTDYSFYRVWGNNTETLVSKGKEATLTKPMVGPEDAGSYRCELGSVNSSPATIINFHVTVLPKMIKEEKPSPNIVTPGEATTESSISLQPLQPEKMLASRLLGLLICGSLALITGLTFAIFRRRKVIDFIKSSLFGLGSGAAEQTQVPKEKATDSRQQ | Function: Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'. Acts a ligand for the human-specific oolemma epitope FCRL3/MAIA during fertilization . FCRL3/MAIA replaces IZUMO1R/JUNO as IZUMO1 receptor after sperm-egg adhesion, which permits species-specific gamete fusion .
PTM: N-glycosylated. Glycosylation is not essential for fusion and for proper protein trafficking in sperm.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38930
Sequence Length: 350
Domain: The extracellular domain assumes a distinct boomerang shape when not bound to IZUMO1R/JUNO . Interaction with IZUMO1R/JUNO triggers a conformation change, so that the IZUMO1 extracellular domain assumes an upright conformation .
Subcellular Location: Cell membrane
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Q9D9J7 | MGPHFTLLLAALANCLCPGRPCIKCDQFVTDALKTFENTYLNDHLPHDIHKNVMRMVNHEVSSFGVVTSAEDSYLGAVDENTLEQATWSFLKDLKRITDSDLKGELFIKELLWMLRHQKDIFNNLARQFQKEVLCPNKCGVMSQTLIWCLKCEKQLHICRKSLDCGERHIEVHRSEDLVLDCLLSWHRASKGLTDYSFYRVWENSSETLIAKGKEPYLTKSMVGPEDAGNYRCVLDTINQGHATVIRYDVTVLPPKHSEENQPPNIITQEEHETPVHVTPQTPPGQEPESELYPELHPELYPELIPTVAQNPEKKMKTRLLILLTLGFVVLVASIIISVLHFRKVSAKLKNASDEVKPTASGSKSDQSLSQQMGLKKASQADFNSDYSGDKSEATEN | Function: Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg . The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion . The ligand-receptor interaction probably does not act as a membrane 'fusogen' .
PTM: N-glycosylated. Glycosylation is not essential for fusion and for proper protein trafficking in sperm.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 44885
Sequence Length: 397
Domain: The extracellular domain assumes a distinct boomerang shape when not bound to IZUMO1R/JUNO (By similarity). Interaction with IZUMO1R/JUNO triggers a conformation change, so that the IZUMO1 extracellular domain assumes an upright conformation (By similarity).
Subcellular Location: Cell membrane
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Q8WYK2 | MMPGQIPDPSVTTGSLPGLGPLTGLPSSALTVEELKYADIRNLGAMIAPLHFLEVKLGKRPQPVKSELDEEEERRKRRREKNKVAAARCRNKKKERTEFLQRESERLELMNAELKTQIEELKQERQQLILMLNRHRPTCIVRTDSVKTPESEGNPLLEQLEKK | Function: Component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Involved in a variety of transcriptional responses associated with AP-1 such as UV-induced apoptosis, cell differentiation, tumorigenesis and antitumogeneris. Can also function as a repressor by recruiting histone deacetylase 3/HDAC3 to the promoter region of JUN. May control transcription via direct regulation of the modification of histones and the assembly of chromatin.
PTM: Phosphorylation of Thr-148 by MAPK8 in response to different stress conditions such as, UV irradiation, oxidatives stress and anisomycin treatments.
Sequence Mass (Da): 18704
Sequence Length: 163
Subcellular Location: Nucleus
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P97875 | MMPGQIPDPSVTAGSLPGLGPLTGLPSSALTTEELKYADIRNIGAMIAPLHFLEVKLGKRPQPVKSELDEEEERRKRRREKNKVAAARCRNKKKERTEFLQRESERLELMNAELKTQIEELKLERQQLILMLNRHRPTCIVRTDSVRTPESEGNPLLEQLDKK | Function: Component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Involved in a variety of transcriptional responses associated with AP-1, such as UV-induced apoptosis, cell differentiation, tumorigenesis and antitumogeneris. Can also function as a repressor by recruiting histone deacetylase 3/HDAC3 to the promoter region of JUN. May control transcription via direct regulation of the modification of histones and the assembly of chromatin (By similarity).
PTM: Phosphorylation of Thr-148 by MAPK8 in response to different stress conditions such as, UV irradiation, oxidatives stress and anisomycin treatments.
Sequence Mass (Da): 18675
Sequence Length: 163
Subcellular Location: Nucleus
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P9WJW8 | MTPRQRLTVLATGLGIFMVFVDVNIVNVALPSIQKVFHTGEQGLQWAVAGYSLGMAAVLMSCALLGDRYGRRRSFVFGVTLFVVSSIVCVLPVSLAVFTVARVIQGLGAAFISVLSLALLSHSFPNPRMKARAISNWMAIGMVGAASAPALGGLMVDGLGWRSVFLVNVPLGAIVWLLTLVGVDESQDPEPTQLDWVGQLTLIPAVALIAYTIIEAPRFDRQSAGFVAALLLAAGVLLWLFVRHEHRAAFPLVDLKLFAEPLYRSVLIVYFVVMSCFFGTLMVITQHFQNVRDLSPLHAGLMMLPVPAGFGVASLLAGRAVNKWGPQLPVLTCLAAMFIGLAIFAISMDHAHPVALVGLTIFGAGAGGCATPLLHLGMTKVDDGRAGMAAGMLNLQRSLGGIFGVAFLGTIVAAWLGAALPNTMADEIPDPIARAIVVDVIVDSANPHAHAAFIGPGHRITAAQEDEIVLAADAVFVSGIKLALGGAAVLLTGAFVLGWTRFPRTPAS | Function: Involved in resistance to ethambutol and isoniazid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53479
Sequence Length: 508
Subcellular Location: Cell inner membrane
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Q9PTT2 | MKGLVIFFCLFYGCHVAGATGKTIMLFPQKTDTDYVTLKPTERVLNQITVCLKSYTELIKEHSLFSLAMQGSGKDNTLLIYPYPPNNISISIHNEDIYFKVDPEVLQWKRTCVTWDSKTGLLQLWINGKLYPRRITKSRSPIGPQISVILGQEQDSYGGSFDINQAFVGEMSDVNVWDYVLPPENIKAYFSDDYTLDGNFYSWDGGNYTINGLIVVLRNQFIPKL | Cofactor: Binds 2 calcium ions per subunit.
Function: Calcium-dependent beta-galactose specific lectin.
PTM: Glycosylated.
Sequence Mass (Da): 25618
Sequence Length: 225
Subcellular Location: Secreted
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P40358 | MILISGYCLLVYSVILPVLISASKLCDLAELQRLNKNLKVDTESLPKYQWIAGQLEQNCMTADPASENMSDVIQLANQIYYKIGLIQLSNDQHLRAINTFEKIVFNETYKGSFGKLAEKRLQELYVDFGMWDKVHQKDDQYAKYLSLNETIRNKISSKDVSVEEDISELLRITPYDVNVLSTHIDVLFHKLAEEIDVSLAAAIILDYETILDKHLASLSIDTRLSIHYVISVLQTFVLNSDASFNIRKCLSIDMDYDKCKKLSLTISKLNKVNPSKRQILDPATYAFENKKFRSWDRIIEFYLKDKKPFITPMKILNKDTNFKNNYFFLEEIIKQLIEDVQLSRPLAKNLFEDPPITDGFVKPKSYYHTDYLVYIDSILCQASSMSPDVKRAKLAAPFCKKSLRHSLTLETWKHYQDAKSEQKPLPETVLSDVWNSNPHLLMYMVNSILNKSRSKPHSQFKKQLYDQINKFFQDNGLSESTNPYVMKNFRLLQKQLQTYKEHKHRNFNQQYFQQQQQQQQHQRHQAPPAAPNYDPKKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKANHNDKQESIHETMSQINEAYETLSDDDKRKEYDLSRSNPRRNTFPQGPRQNNMFKNPGSGFPFGNGFKMNFGL | Function: Acts as a DnaJ-like chaperone required for nuclear membrane fusion during mating.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 75144
Sequence Length: 645
Subcellular Location: Endoplasmic reticulum membrane
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P36035 | MSSSITDEKISGEQQQPAGRKLYYNTSTFAEPPLVDGEGNPINYEPEVYNPDHEKLYHNPSLPAQSIQDTRDDELLERVYSQDQGVEYEEDEEDKPNLSAASIKSYALTRFTSLLHIHEFSWENVNPIPELRKMTWQNWNYFFMGYFAWLSAAWAFFCVSVSVAPLAELYDRPTKDITWGLGLVLFVRSAGAVIFGLWTDKSSRKWPYITCLFLFVIAQLCTPWCDTYEKFLGVRWITGIAMGGIYGCASATAIEDAPVKARSFLSGLFFSAYAMGFIFAIIFYRAFGYFRDDGWKILFWFSIFLPILLIFWRLLWPETKYFTKVLKARKLILSDAVKANGGEPLPKANFKQKMVSMKRTVQKYWLLFAYLVVLLVGPNYLTHASQDLLPTMLRAQLGLSKDAVTVIVVVTNIGAICGGMIFGQFMEVTGRRLGLLIACTMGGCFTYPAFMLRSEKAILGAGFMLYFCVFGVWGILPIHLAELAPADARALVAGLSYQLGNLASAAASTIETQLADRYPLERDASGAVIKEDYAKVMAILTGSVFIFTFACVFVGHEKFHRDLSSPVMKKYINQVEEYEADGLSISDIVEQKTECASVKMIDSNVSKTYEEHIETV | Function: Essential to lactate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69376
Sequence Length: 616
Subcellular Location: Membrane
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Q9GYI4 | MSLGRDRYSLPRTYKRVSHAKDKARPELRKFGWETLGYSESFNLPPFRDSIQRVDGNNLTVEEFRRDFERPRIPVIITGLTDNWAAKDKWTVERLSKKYRNQNFKCGEDDNGNSVRMKMKYYHDYMLNNKDDSPLYIFDSSFAERRKTKKLSEDYSVPKFFEDDLFHYADDKKRPPHRWFVMGPARSGTAIHIDPLGTSAWNSLLQGHKRWVLIPPIAPRDLVKPMAHEKGKHPDEGITWFQTVYKRVRSPSWPKEYAPIECRQGPGETMFVPSGWWHVVINEEYTIAVTHNYCSVENLHLVWPKTVKGRPKLSKHWVKRLTEQRPELLEIIKSASEIPLYDMNESSSDSSSSSSSSDDSSDESDCDDSGRCGGRKRKNDDRSNECPEKMSTTYFQNSLV | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase.
Sequence Mass (Da): 46618
Sequence Length: 400
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q6PFM0 | MNHKSKKRIKEAKRSARPELKDSSDWTKHEYCKSFDLSHRSVKDNVERADVQRLSPEEFIQRFEKPYKPVVLLNVEDSWPAREKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYVEYLESTHDDSPLYIFDSSFGEHAKRRKLLEDYQVPLFFRDDLFQFAGEKRRPPYRWFVMGPARSGTGIHIDPLGTSAWNALVQGHKRWCLFPTHTPRELIKVTRDEGGNQQDEAITWFNVIYPRTQQSTWPDEFRPLEILQRPGETVFVPGGWWHVVLNLDTTIAVTQNFASTTNFPIVWHKTVRGRPKLSRKWYRILKQERPDIAAIADKVDLQESTGIASDSSSDSSSSSSSSSSDSDSEADSGSEGDAMTHRRKKRRTGGMMGNGDITSQDDCASKERSSSR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as u2af2/u2af65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylation of u2af2/u2af65, affecting the pre-mRNA splicing activity of u2af2/u2af65. Hydroxylates its own N-terminus, which is required for homooligomerization. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation. Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. In collaboration with brd4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. Demethylates other arginine methylated-proteins such as esr1. Has no histone lysine demethylase activity (By similarity). Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation (By similarity).
PTM: Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization.
Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = (5S)-5-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 46687
Sequence Length: 403
Domain: The nuclear localization signal motifs are necessary and sufficient to target it into the nucleus.
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q6NYC1 | MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEHPELAVLADSVDLQESTGIASDSSSDSSSSSSSSSSDSDSECESGSEGDGTVHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase . Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65 . Hydroxylates its own N-terminus, which is required for homooligomerization . Plays a role in the regulation of nucleolar liquid-liquid phase separation (LLPS) by post-translationally modifying LIAT1 at its lysine-rich domain which inhibits LIAT1 nucleolar targeting (By similarity). In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA . Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation . Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code . However, histone arginine demethylation may not constitute the primary activity in vivo . In collaboration with BRD4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. On distal enhancers, so called anti-pause enhancers, demethylates both histone H4R3me2 and the methyl cap of 7SKsnRNA leading to the dismissal of the 7SKsnRNA:HEXIM1 inhibitor complex. After removal of repressive marks, the complex BRD4:JMJD6 attract and retain the P-TEFb complex on chromatin, leading to its activation, promoter-proximal polymerase II pause release, and transcriptional activation . Demethylates other arginine methylated-proteins such as ESR1 . Has no histone lysine demethylase activity . Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65 (By similarity). Seems to be necessary for the regulation of macrophage cytokine responses .
PTM: Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization.
Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = (5S)-5-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 46462
Sequence Length: 403
Domain: The nuclear localization signal motifs are necessary and sufficient to target it into the nucleus.
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q6Q4H1 | MDKRTDDAVRETKLKARPELKGDEGWTRLGYANNFDLSYQHIKDTLPRIHCKSISHDEFIARYEKPRIPVILTGCTDSWLANQKWKLSSLAKKYRNQKFKVGEDNDGFSVKMKMKYYIEYLKHQKDDSPLYIFDGSYGEHPKKRKLLDDYHPPSFFQDDLFKYAGEKRRPPYRWIVIGPARSGTGIHIDPLGTSAWNALISGHKRWMMFPTETPKHLLEVSKQDGQHQSGEGIQWFVKVYPKVKSPTWPKEYAPLEIIQHPGETVFVPGGWWHVVLNLDQTVAVTQNFSSPTNFHVVWHKTVRGRPKLSQKWLRALKIYRPEIARIAAEVDLLRQSGLASDSSSDSSSSSSSSSSEESNSESEESTADSIPEQSESKRRKVDAVE | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase.
Sequence Mass (Da): 44240
Sequence Length: 385
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q9ERI5 | MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESYPLNPAAVPDNVERADALQLSVKEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTNTPRELIKVTREEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEHPELAVLADAVDLQESTGIASDSSSDSSSSSSSSSSDSDSECESGSEGDGTTHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization (By similarity). Plays a role in the regulation of nucleolar liquid-liquid phase separation (LLPS) by post-translationally modifying LIAT1 at its lysine-rich domain which inhibits LIAT1 nucleolar targeting . In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation. Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. In collaboration with BRD4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. On distal enhancers, so called anti-pause enhancers, demethylates both histone H4R3me2 and the methyl cap of 7SKsnRNA leading to the dismissal of the 7SKsnRNA:HEXIM1 inhibitor complex. After removal of repressive marks, the complex BRD4:JMJD6 attract and retain the P-TEFb complex on chromatin, leading to its activation, promoter-proximal polymerase II pause release, and transcriptional activation. Demethylates other arginine methylated-proteins such as ESR1. Has no histone lysine demethylase activity (By similarity). Required for differentiation of multiple organs during embryogenesis . Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65 . Seems to be necessary for the regulation of macrophage cytokine responses (By similarity).
PTM: Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization.
Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = (5S)-5-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 46567
Sequence Length: 403
Domain: The nuclear localization signal motifs are necessary and sufficient to target it into the nucleus.
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q6AYK2 | MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESYPLSPAAVPDNVERADALQLSVKEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTNTPRELIKVTREEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEHPELAVLADAVDLQESTGIASDSSSDSSSSSSSSSSDSDSECESGSEGDGTTHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization (By similarity). Plays a role in the regulation of nucleolar liquid-liquid phase separation (LLPS) by post-translationally modifying LIAT1 at its lysine-rich domain which inhibits LIAT1 nucleolar targeting (By similarity). In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation. Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. In collaboration with BRD4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. On distal enhancers, so called anti-pause enhancers, demethylates both histone H4R3me2 and the methyl cap of 7SKsnRNA leading to the dismissal of the 7SKsnRNA:HEXIM1 inhibitor complex. After removal of repressive marks, the complex BRD4:JMJD6 attract and retain the P-TEFb complex on chromatin, leading to its activation, promoter-proximal polymerase II pause release, and transcriptional activation. Demethylates other arginine methylated-proteins such as ESR1. Has no histone lysine demethylase activity (By similarity). Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65 (By similarity). Seems to be necessary for the regulation of macrophage cytokine responses (By similarity).
PTM: Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization.
Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = (5S)-5-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 46540
Sequence Length: 403
Domain: The nuclear localization signal motifs are necessary and sufficient to target it into the nucleus.
Subcellular Location: Nucleus
EC: 1.14.11.-
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P0C870 | MAEAALEAVRSELREFPAAARELCVPLAVPYLDKPPTPLHFYRDWVCPNRPCIIRNALQHWPALQKWSLPYFRATVGSTEVSVAVTPDGYADAVRGDRFMMPAERRLPLSFVLDVLEGRAQHPGVLYVQKQCSNLPSELPQLLPDLESHVPWASEALGKMPDAVNFWLGEAAAVTSLHKDHYENLYCVVSGEKHFLFHPPSDRPFIPYELYTPATYQLTEEGTFKVVDEEAMEKVPWIPLDPLAPDLARYPSYSQAQALRCTVRAGEMLYLPALWFHHVQQSQGCIAVNFWYDMEYDLKYSYFQLLDSLTKASGLD | Function: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase . Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation . Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4 . After initial cleavage, continues to digest histones tails via its aminopeptidase activity . Additionally, may play a role in protein biosynthesis by modifying the translation machinery . Acts as Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) .
Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = (3S)-3-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 35932
Sequence Length: 316
Subcellular Location: Nucleus
EC: 1.14.11.63
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P0C872 | MAEAALEAVRRALQEFPAAARDLNVPRVVPYLDEPPSPLCFYRDWVCPNRPCIIRNALQHWPALQKWSLSYLRATVGSTEVSVAVTPDGYADAVRGDRFVMPAERRLPISHVLDVLEGRAQHPGVLYVQKQCSNLPTELPQLLSDIESHVPWASESLGKMPDAVNFWLGDASAVTSLHKDHYENLYCVVSGEKHFLLHPPSDRPFIPYNLYTPATYQLTEEGTFRVVDEEAMEKVPWIPLDPLAPDLTQYPSYSQAQALHCTVRAGEMLYLPALWFHHVQQSHGCIAVNFWYDMEYDLKYSYFQLMDTLTRATGLD | Function: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (By similarity). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation . Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity . Additionally, may play a role in protein biosynthesis by modifying the translation machinery. Acts as Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) (By similarity).
Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = (3S)-3-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 35917
Sequence Length: 316
Subcellular Location: Nucleus
EC: 1.14.11.63
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Q96S16 | MAPASRLLALWALAAVALPGSGAEGDGGWRPGGPGAVAEEERCTVERRADLTYAEFVQQYAFVRPVILQGLTDNSRFRALCSRDRLLASFGDRVVRLSTANTYSYHKVDLPFQEYVEQLLHPQDPTSLGNDTLYFFGDNNFTEWASLFRHYSPPPFGLLGTAPAYSFGIAGAGSGVPFHWHGPGYSEVIYGRKRWFLYPPEKTPEFHPNKTTLAWLRDTYPALPPSARPLECTIRAGEVLYFPDRWWHATLNLDTSVFISTFLG | Function: Functions as a positive regulator of TNF-induced NF-kappa-B signaling . Regulates angiogenesis and cellular metabolism through interaction with PKM .
PTM: N-glycosylated.
Sequence Mass (Da): 29509
Sequence Length: 264
Subcellular Location: Endoplasmic reticulum lumen
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A0A061FBW2 | MEVMQVLHMNKGNGETSYAKNSTVQSKIISVGKPIIEEAVHEISCNNLLESMGIADLGCSSGPNTLSVISEIMDMVQTTSRRLGRPVPEFRVYLNDLYSNDFNYIFMSLPAFYHRLKEEKGIGCGSCYISGVAGSFYGRLFPSKSLHFVHSSSSLHWLSQVPPGLESKALAPLNKGKVYISKSSPQSVLNAYSLQFQNDFSMFIESRSQELVPGGRMVLSFMGRRSTDPTTEESCHHWELLAQAIMSLVREGLIEEAKVDSFNAPYYAPCAEEIKVEIQKVGSFVIDRLEGFEIDWDGGAVSDVQTAQGKLLIGQRVAKTIRAVVESMLESHFGIGQDIMDDLFSRYAEIVGNHLSKTRTKYINLVISLIKKG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the methylation of jasmonate into methyljasmonate, a plant volatile that acts as an important cellular regulator mediating diverse developmental processes and defense responses.
Catalytic Activity: jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41388
Sequence Length: 373
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.141
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Q9AR07 | MEVMRVLHMNKGNGETSYAKNSTAQSNIISLGRRVMDEALKKLMMSNSEISSIGIADLGCSSGPNSLLSISNIVDTIHNLCPDLDRPVPELRVSLNDLPSNDFNYICASLPEFYDRVNNNKEGLGFGRGGGESCFVSAVPGSFYGRLFPRRSLHFVHSSSSLHWLSQVPCREAEKEDRTITADLENMGKIYISKTSPKSAHKAYALQFQTDFWVFLRSRSEELVPGGRMVLSFLGRRSLDPTTEESCYQWELLAQALMSMAKEGIIEEEKIDAFNAPYYAASSEELKMVIEKEGSFSIDRLEISPIDWEGGSISEESYDLVIRSKPEALASGRRVSNTIRAVVEPMLEPTFGENVMDELFERYAKIVGEYFYVSSPRYAIVILSLVRAG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the methylation of jasmonate into methyljasmonate, a plant volatile that acts as an important cellular regulator mediating diverse developmental processes and defense responses.
Catalytic Activity: jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 43443
Sequence Length: 389
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.141
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Q8N9B5 | MSFALEETLESDWVAVRPHVFDEREKHKFVFIVAWNEIEGKFAITCHNRTAQRQRSGSREQAGARGGAEAGGAASDGSRGPGSPAGRGRPEATASATLVRSPGPRRSSAWAEGGSPRSTRSLLGDPRLRSPGSKGAESRLRSPVRAKPIPGQKTSEADDAAGAAAAAARPAPREAQVSSVRIVSASGTVSEEIEVLEMVKEDEAPLALSDAEQPPPATELESPAEECSWAGLFSFQDLRAVHQQLCSVNSQLEPCLPVFPEEPSGMWTVLFGGAPEMTEQEIDTLCYQLQVYLGHGLDTCGWKILSQVLFTETDDPEEYYESLSELRQKGYEEVLQRARKRIQELLDKHKNTESMVELLDLYQMEDEAYSSLAEATTELYQYLLQPFRDMRELAMLRRQQIKISMENDYLGPRRIESLQKEDADWQRKAHMAVLSIQDLTVKYFEITAKAQKAVYDRMRADQKKFGKASWAAAAERMEKLQYAVSKETLQMMRAKEICLEQRKHALKEEMQSLRGGTEAIARLDQLEADYYDLQLQLYEVQFEILKCEELLLTAQLESIKRLISEKRDEVVYYDTYESMEAMLEKEEMAASAYLQREELQKLQQKARQLEARRGRVSAKKSYLRNKKEICIAKHNEKIQQRTRIEDEYRTHHTVQLKREKLHDEEERKSAWVSQERQRTLDRLRTFKQRYPGQVILKSTRLRLAHARRKGAASPVLQEDHCDSLPSVLQVEEKTEEVGEGRVKRGPSQTTEPQSLVQLEDTSLTQLEATSLPLSGVTSELPPTISLPLLNNNLEPCSVTINPLPSPLPPTPPPPPPPPPPPPPPPLPVAKDSGPETLEKDLPRKEGNEKRIPKSASAPSAHLFDSSQLVSARKKLRKTAEGLQRRRVSSPMDEVLASLKRGSFHLKKVEQRTLPPFPDEDDSNNILAQIRKGVKLKKVQKDVLRESFTLLPDTDPLTRSIHEALRRIKEASPESEDEEEALPCTDWEN | Function: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions . In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments . Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments . Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. Upon nutrient stress, directly recruited by MAP1LC3B to the phagophore membrane surfaces to promote actin assembly during autophagy . The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location (By similarity).
PTM: Ubiquitinated by MDM2, leading to its subsequent degradation by the proteasome. In case of DNA damage, the interaction with MDM2 is altered, preventing degradation and allowing interaction with p300/EP300 and its function in p53/TP53 stress response (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 111445
Sequence Length: 988
Domain: The N-terminal region is involved in actin binding and actin nucleation activity.
Subcellular Location: Nucleus
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Q9HCI6 | MGDPGSEIIESVPPAGPEASESTTDENEDDIQFVSEGPSRPVLEYIDLVCGDDENPSAYYSDILFPKMPKRQGDFLHFLNVKKVKTDTENNEVSKNHCRLSKAKEPHFEYIEQPIIEEKPSLSSKKEIDNLVLPDCWNEKQAFMFTEQYKWLEIKEGKLGCKDCSAVRHLGSKAEKHVHVSKEWIAYLVTPNGSNKTTRQASLRKKIREHDVSKAHGKIQDLLKESTNDSICNLVHKQNNKNIDATVKVFNTVYSLVKHNRPLSDIEGARELQEKNGEVNCLNTRYSATRIAEHIAKEMKMKIFKNIIEENAKICIIIDEASTVSKKTTLVIYLQCTIQSAPAPVMLFVALKELVSTIAECIVNTLLTTLNDCGFTNEYLKANLIAFCSDGANTILGRKSGVATKLLENFPEIIIWNCLNHRLQLSLDDSISEIKQINHLKIFIDKIYSIYHQPNKNQTKLLGTVAKELETEIIKIGRVMGPRWAACSLQAATAVWHAYPILYMHFSHSYSGLAKRLANINFLQDLALMIDILEEFSVLSTALQSRSTNIKKAQKLIKRTIRALENLKIGTGKYESQIEDLIKSDKFKDIPFNKNNKFNALPRSILLDNIIQHMNLRLLSDRNHEDIFNYFDLLEPSTWPYEEITSPWIAGEKTLFHLCKILKYEVDLNDFREFVNNNIKSNNVSIPTTIYKAKKIVSTIAINSAEAERGFNLMNIICTRVRNSLTIDHVSDLMTINLLGKELADWDATPFVKSWSNCNHRLATDTRVRQKSTKVFHENQLAIWNLK | Function: E3 SUMO-protein ligase; facilitates UBE2I/UBC9-mediated SUMO2 modification of target proteins .
Sequence Mass (Da): 89673
Sequence Length: 787
Domain: Binds UBE2I/UBC9 and two SUMO2 molecules via its N-terminus. The most N-terminal region interacts with the SUMO2 chain that is covalently bound to the UBE2I/UBC9 active site, while the second region interacts with another SUMO2 that is non-covalently associated with the same UBE2I/UBC9 chain.
Pathway: Protein modification; protein sumoylation.
EC: 2.3.2.-
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Q9QR69 | MKTLIFFWNLWLWALLVCFWCITLVCVTTNSIDTMASLLVMCILFVSAINKYTQAISSNNPKWPSSWHLGIIACIVLKLWNLSTTNSVTYACLITTAILSLVTAFLTLIKHCTACKLQLEHGILFTSTFAVLMTNMLVHMSNTWQSSWIFFPISFTLSLPFLYAFATVKTGNIKLVSSVSFICAGLVMGYPVSCCKTHTCTATAAGLSLSSIYLGFTGIISTLHKSWAPPKRGILTFLLLQGGVLTTQTLTTELLAITSTTGNIKGHEILLLVCLIFLWCLYVWQSFNKASLVTGMLHLIAAWSHTGGCVQLVMLLPSGLTRGILTMIICISTLFSTLQGLLVFYLYKEKKVVAVNSYRQRRRRIYTRDQNLHHNDNHLGNNVISPPPLPPFFRQPVRLPSHVTDRGRGSQLLNEVELQEVNRDPPNVFGYASILVSGAEESREPSPQPDQSGMSILRVDGGSAFRIDTAQAATQPTDDLYEEVLFPRN | Function: Plays a crucial role for reactivation of the virus from latency, early viral gene expression and virus production. Modulates host signaling pathways including activation of MAP kinases c-JUN-N-terminal kinase (JNK), ERK2, and NF-kappa-B resulting in the activation of AP-1 and NFAT-dependent gene expression in B-lymphocytes. When expressed in epithelial cells, induces the expression of several inflammatory and angiogenic genes. Interferes also with B-lymphocytes signaling through interaction with host LYN kinase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54316
Sequence Length: 489
Subcellular Location: Host cell membrane
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P04264 | MSRQFSSRSGYRSGGGFSSGSAGIINYQRRTTSSSTRRSGGGGGRFSSCGGGGGSFGAGGGFGSRSLVNLGGSKSISISVARGGGRGSGFGGGYGGGGFGGGGFGGGGFGGGGIGGGGFGGFGSGGGGFGGGGFGGGGYGGGYGPVCPPGGIQEVTINQSLLQPLNVEIDPEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRTHNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESRMSGECAPNVSVSVSTSHTTISGGGSRGGGGGGYGSGGSSYGSGGGSYGSGGGGGGGRGSYGSGGSSYGSGGGSYGSGGGGGGHGSYGSGSSSGGYRGGSGGGGGGSSGGRGSGGGSSGGSIGGRGSSSGGVKSSGGSSSVKFVSTTYSGVTR | Function: May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK.
PTM: Undergoes deimination of some arginine residues (citrullination).
Sequence Mass (Da): 66039
Sequence Length: 644
Subcellular Location: Cell membrane
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P13647 | MSRQSSVSFRSGGSRSFSTASAITPSVSRTSFTSVSRSGGGGGGGFGRVSLAGACGVGGYGSRSLYNLGGSKRISISTSGGSFRNRFGAGAGGGYGFGGGAGSGFGFGGGAGGGFGLGGGAGFGGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPSIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLSGEGVGPVNISVVTSSVSSGYGSGSGYGGGLGGGLGGGLGGGLAGGSSGSYYSSSSGGVGLGGGLSVGGSGFSASSGRGLGVGFGSGGGSSSSVKFVSTTSSSRKSFKS | Function: Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress (By similarity). Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokines, macrophage inflammatory cytokines and CTNND1 localization in keratinocytes (By similarity).
PTM: Phosphorylated by CDK1, AURKB and Rho-kinase, phosphorylation is regulated by the cell cycle (By similarity). Thr-24 phosphorylation, mediated by CDK1, peaks during prometaphase or metaphase cells with phosphorylated filamentous structures evident throughout the cytoplasm during early mitosis (By similarity). CDK1 phosphorylates Thr-24 in mitotic cells at the site of injury (By similarity).
Sequence Mass (Da): 62378
Sequence Length: 590
Subcellular Location: Cytoplasm
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Q922U2 | MSRQSSVSFRSGGSRSFSAASAITPSVSRTSFSSVSRSGGGGGGRISLGGACGAGGYGSRSLYNVGGSKRISYSSGGGSFRNQFGAGGFGFGGGAGSGFGFGGGAGSGFGFGGGAGFGGGYGGAGFPVCPPGGIQEVTVNQNLLTPLNLQIDPTIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTIKQNLDPLFEQYINNLRRQLDGVLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEARVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGELALKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLSGEGVGPVNISVVTNSVSSGYGGGSSIGVGSGFGGGLGSGFAGGLGPRFTRGGGGLGLGSGLSVGGSGFSAGSSQGGMSFGSGGGSGSSVKFVSTTSSSRRSFKS | Function: Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress . Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokines, macrophage inflammatory cytokines and CTNND1 localization in keratinocytes .
PTM: Phosphorylated by CDK1, AURKB and Rho-kinase, phosphorylation is regulated by the cell cycle . Thr-24 phosphorylation, mediated by CDK1, peaks during prometaphase or metaphase cells with phosphorylated filamentous structures evident throughout the cytoplasm during early mitosis . CDK1 phosphorylates Thr-24 in mitotic cells at the site of injury .
Sequence Mass (Da): 61767
Sequence Length: 580
Subcellular Location: Cytoplasm
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P35028 | MKIGIVTGIPGVGKSTVLAKVKEILDNQGINNKIINYGDFMLATALKLGYAKDRDEMRKLSVEKQKKLQIDAAKGIAEEARAGGEGYLFIDTHAVIRTPSGYLPGLPSYVITEINPSVIFLLEADPKIILSRQKRDTTRNRNDYSDESVILETINFARYAATASAVLAGSTVKVIVNVEGDPSIAANEIIRSMK | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21110
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q975K4 | MKIGIVTGIPGVGKTTVLSKVKEILEEKKINNKIVNYGDYMLMTAMKLGYVNNRDEMRKLPVEKQKQLQIEAARGIANEAKEGGDGLLFIDTHAVIRTPSGYLPGLPKYVIEEINPRVIFLLEADPKVILDRQKRDTSRSRSDYSDERIISETINFARYAAMASAVLVGATVKIVINVEGDPAVAANEIINSML | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21447
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q9HIT1 | MRSVITGVAGVGKTTVLDIVSKETGIKIVNYGTLMFDLAKKRGLVENRDQMRKLSRDIQIDLQKNAATEIGRMEDVIVDTHMSIKTPFGYLPGLPEWVLREINASAFIIIEADPELILRRRQNDPTRARDEDSVESIREHQEINRAFAAAYSIFSGATVKIITNEEGKPDKAAHDIIKVIAVD | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20445
Sequence Length: 183
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
Q5JJH2 | MPFVVVITGIPGVGKSTITKLALKKTRAKFRLVNFGDLMFEEAVNMGLVKHRDEMRKLDPLTQKELQLKVAQRIVEIARKEPVLLDTHATIRTPAGYLLGFPREVIEILNPNFIVIIEAAPSEILGRRLRDLKRDRDVETEEQIARHQDLNRAAAIAYAMHSNALIKIIENHEDKGLEEAVNELVKVLDLAVSEYA | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22138
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q54CT8 | MALNLLRNYSTKIRMDHLRMTIIGAPGSGKGTQSEKLKKDYNLPIISTGQILREVSEQNTKSGIEIKSKLAAGELISDAIMSDIITEHLTKTGNSWLLDGYPRNTEQAKGLDKYLNVKMALNVVLHLDVPEKVLAERVQDRWVHPGSGRVYNSVFSPPKVKGIDDVTGEPLVRRSDDKDEEVFRNRIQTFKNNTLPLLKYYEDRGVLYTIDSPNSDEGYVKIKQILDSILTK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 26172
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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