ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O23920 | MGKKQSEAEILSSNSSNTSPATFKLVGFNNFVRANPKSDHFAVKRFHHIEFWCGDATNTSRRFSWGLGMPLVAKSDLSTGNSVHASYLVRSANLSFVFTAPYSPSTTTSSGSAAIPSFSASGFHSFAAKHGLAVRAIALEVADVAAAFEASVARGARPASAPVELDDQAWLAEVELYGDVVLRFVSFGREEGLFLPGFEAVEGTASFPDLDYGIRRLDHAVGNVTELGPVVEYIKGFTGFHEFAEFTAEDVGTLESGLNSVVLANNEEMVLLPLNEPVYGTKRKSQIQTYLEHNEGAGVQHLALVSEDIFRTLREMRKRS... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 48148
Sequence Length: 442
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
Subcellular Location: Cytoplasm
EC: 1... |
Q76NV5 | MEGFDHVTFWVGNALQAATYYIARFGFQNLAYSGLETGNRQFATHVIHQNNIIMAFTSPLTGDNKDYADHMMRHGDGVKDIAFNVKDVQHIYDEAVKAGAQSVKEPHQIKDEHGIVTLATIMSPYGETTHTFVDRSQYKGAFLPGFTYKVASDPLSNITEPVGLNLIDHVVSNHADKMMEPVVQWYEKVLQFHRFWSVDDKTIHTEYSSLRSVVVADKSEKVKLPINEPANGIRKSQIQEYVDFYNGAGVQHIALKTDNIIDAISKLRSRGVSFLTVPKTYYTSLREKLQHSSLEIKEDLDTLEKLHILIDYDDKGYLLQ... | Cofactor: Binds 1 Fe cation per subunit.
Function: Key enzyme in the degradation of tyrosine.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 41738
Sequence Length: 367
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylala... |
O48604 | MPPTPTTPAATGAAAAVTPEHARPHRMVRFNPRSDRFHTLSFHHVEFWCADAASAAGRFAFALGAPLAARSDLSTGNSAHASQLLRSGSLAFLFTAPYANGCDAATASLPSFSADAARRFSADHGIAVRSVALRVADAAEAFRASRRRGARPAFAPVDLGRGFAFAEVELYGDVVLRFVSHPDGTDVPFLPGFEGVTNPDAVDYGLTRFDHVVGNVPELAPAAAYIAGFTGFHEFAEFTAEDVGTTESGLNSVVLANNSEGVLLPLNEPVHGTKRRSQIQTFLEHHGGPGVQHIAVASSDVLRTLRKMRARSAMGGFDFL... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 46550
Sequence Length: 434
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
Subcellular Location: Cytoplasm
EC: 1... |
P32754 | MTTYSDKGAKPERGRFLHFHSVTFWVGNAKQAASFYCSKMGFEPLAYRGLETGSREVVSHVIKQGKIVFVLSSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAKIMREPWVEQDKFGKVKFAVLQTYGDTTHTLVEKMNYIGQFLPGYEAPAFMDPLLPKLPKCSLEMIDHIVGNQPDQEMVSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRHLRERGLEFLSVPSTYYKQLREKLKTAKIKVKENIDALEEL... | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to homogentisic acid, one of the steps in tyrosine catabolism.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 44934
Se... |
Q96X22 | MSPSAITESPRNSVVDHTSGLQVDSLAVQGPFPSFHGYDHVTWWVGNAKQAASYYNTLFGMKIIAYRGLETGSRYFASYLVGKEDVRFVFTSPIRSHVHLPEDEPISDEDRALLKEMHAHLEKHGDAVKDVCFEVDNVQGVYERAVQQGAVSIAPPKTLSDKEHGSVTMAVIQTYGDTTHTLLSRDNFRGTFLPGFRDVNRQPAAYSALAPVPLQRIDHCVGNQDWDDMRAACDFYERCLSFHRFWSVDDNQISTDFSALNSIVMASPNNVVKMPINEPAKGKKRSQIEEYVTFNSGAGVQHIALLTSDIITTVEAMRSR... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 47576
Sequence Length: 419
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
|
Q872T7 | MSPSAISSEYSNCNGTPDYALQSSEVSNFNGYDHVTWWVGNAKQAASYYNTVFGFKTLAYRGLETGSRYFASYVVGNADVRFVFTSPIRSQKCLPEEEPISDADRKLLQECHEHLEKHGDAVKDVAFEVDNVDGVFHKAVAAGADVVQEPTTLTDKMHGSVRTAVIRTYGDTTHTLISRADYNGPFLPGFRTAAPSSATVQLPSVPLARIDHCVGNQDWNEMVSACAFYEQCLSFHRFWSVDDSQICTEFSALNSIVMASENNLVKMPINEPAPGKKKSQIEEYVVFNSGAGVQHIALLTPDIISTVSAMRARGVEFINV... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 46029
Sequence Length: 412
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
|
Q02110 | MTSYSDKGEKPERGRFLHFHSVTFWVGNAKQAASYYCSKIGFEPLAYKGLETGSREVVSHVVKQDKIVFVFSSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAIIVREEVCCAADVRGHHTPLDRARQVWEGTLVEKMTFCLDSRPQPSQTLLHRLLLSKLPKCGLEIIDHIVGNQPDQEMESASQWYMRNLQFHRFWSVDDTQIHTEYSALRSVVMANYEESIKMPINEPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRSLRERGVEFLAVPFTYYKQLQEKLKSAKIRVKESIDVLEEL... | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to homogentisic acid, one of the steps in tyrosine catabolism.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45064
Se... |
Q9ARF9 | MGQESTAAAAVVPAEFKLVGHKNFVRSNPMSDHFPVHRFHHVEFWCGDATNTSRRFSWGLGMPLVAKSDLSTGNSAHASYLLRSGELSFVFTAPYSPSLAEPSSASIPTFSFSDHRAFTSSHGLAVRAVAIQVDSASSAYSAAVSRGAKPVSPPVVLADCETAIAEVHLYGDTVLRFVSCGSGADGWFLPGFEVVGDGVSCQELDYGIRRLDHAVGNVPKLEPVVDYLKKFTGFHEFAEFTAEDVGTAESGLNSVVLANNNENVLFPLNEPVYGTKRKSQIQTYLDHNEGAGVQHLALITEDIFRTLREMRKRSEVGGFE... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 47736
Sequence Length: 436
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
Subcellular Location: Cytoplasm
EC: 1... |
Q9I576 | MNAVAKIEQHNPIGTDGFEFVEFTAPDAKGIEQLRQLFNMMGFTETAKHRSKEVFLFQQNDINIVLNGSPTGHVHEFALKHGPSACAMAFRVKNASQAAAYAESQGAKLVGSHANFGELNIPSLEGIGGSLLYLVDRYGDRSIYDVDFEFIEGRSANDNSVGLTYIDHLTHNVKRGQMDVWSGFYERIANFREIRYFDIEGKLTGLFSRAMTAPCGKIRIPINESADDTSQIEEFIREYHGEGIQHIALTTDDIYATVRKLRDNGVKFMSTPDTYYEKVDTRVAGHGEPLEQLRELNLLIDGAPGDDGILLQIFTDTVIG... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 39913
Sequence Length: 357
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
|
P80064 | ADLYENPMGLMGFEFIELASPTPNTLEPIFEIMGFTKVATHRSKDVHLYRQGAINLILNNEPHSVASYFAAEHGPSVCGMAFRVKDSQKAYKRALELGAQPIHIETGPMELNLPAIKGIGGAPLYLIDRFGEGSSIYDIDFVFLEGVDRHPVGAGLKIIDHLTHNVYRGRMAYWANFYEKLFNFREIRYFDIKGEYTGLTSKAMTAPDGMIRIPLNEESSKGAGQIEEFLMQFNGEGIQHVAFLSDDLIKTWDHLKSIGMRFMTAPPDTYYEMLEGRLPNHGEPVGELQARGILLDGSSESGDKRLLLQIFSETLMGPVF... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 40061
Sequence Length: 357
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
|
C0CMQ8 | MKIVVLDGYCLNPGDLDWKGLEALGECIVYDRTSLTDMEEVISRIGDADIVYTNKTPMPREVFEKCPNIRFVGVLATGYNVVDVNTAKEKGIPVANIPTYGTASVGQFAIALLLEICHHVGHHNQVVHEGKWESNPDWCFWDYPLIELDGKNMGIIGYGRIGQATGKIAQALGMKVLAYDAYKNPALENENCRYVELDELLSQSDVIALHCPLFPETEGIVNKENIAKMKDGVIILNNSRGPLIVEQDLVDALNSGKVAAAGLDVVSTEPIKGDNPLLGAKNCIITPHISWAPKESRKRLMDIAVNNLEEFLKGSPVNVV... | Function: Involved in catabolism of D-apiose. Catalyzes the reduction of 3-hydroxypyruvate to glycerate.
Catalytic Activity: (R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH
Sequence Mass (Da): 35325
Sequence Length: 322
Pathway: Carbohydrate metabolism.
EC: 1.1.1.81
|
Q9X1C1 | MARYRVHVNDPLDKEATQLLMNKEELEVTSEHLEKDELMKIIPEVDVLVVRSATKVTADIIEAGKNLKIIARAGIGLDNIDVQKAKEKGIKVLNTPGASAPSVAELAMGLMLACARHIARATVSLKEGKWEKKALKGKELLGKTLGLIGFGNIGQEVAKRALAFGMKIIAYDPAKPETDLPVEYVDLDTLFKESDFISLHVPLTESTRHIINRESIAKMKDGVIIVNTARGGTIDEEALYEEVVSGKVYAAGLDVFEVEPPTDEIRRKLLSLDNVVATPHIGASTAEAQRRVGIELVEKIFKELGI | Function: Involved in the degradation of L-serine via 3-hydroxypyruvate. Catalyzes the non-reversible reduction of 3-hydroxypyruvate to yield D-glycerate.
Catalytic Activity: (R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH
Sequence Mass (Da): 33451
Sequence Length: 306
EC: 1.1.1.81
|
Q52473 | MVAFAGLTSKLTNLGNSAVGGVGGALQGVNTVASNATLQKNILLGTGDSLSVDAQAKASKESDANGAKLIAMQAQETMKKQTMDVLNAIQAGKEDSTNKKISATATNAKGISY | Function: Major structural protein of the Hrp pilus, which is a component of the type III secretion system (T3SS, Hrp secretion system) required for effector protein delivery, parasitism, and pathogenicity. Required for secretion of virulence proteins such as HrpW and AvrPto. The Hrp pilus functions as a conduit for pr... |
P35654 | MSSLFVWLNRLAISAMQRSEVVGAAIVMSIVFMMIIPLPTGLIDVLIALNICISSLLIVLAMYLPKPLAFSTFPSVLLLTTMFRLALSISTTRQILLQQDAGHIVEAFGNFVVGGNLAVGLVIFLILTVVNFLVITKGSERVAEVAARFTLDAMPGKQMSIDSDLRAGLIEAHQARQRRENLAKESQLFGAMDGAMKFVKGDAIAGLVIVFINMIGGFAIGVLQNGMEAGAAMHIYSVLTIGDGLIAQIPALLISLTAGMIITRVSADGQQVDANIGREIAEQLTSQPKAWIMSAAGMLGFALLPGMPTAVFVIISAIAL... | Function: Involved in the secretion of harpin; a proteinaceous elicitor of the hypersensitivity response in plants.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79505
Sequence Length: 715
Subcellular Location: Cell inner membrane
|
O14792 | MAALLLGAVLLVAQPQLVPSRPAELGQQELLRKAGTLQDDVRDGVAPNGSAQQLPQTIIIGVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSHGLGWYLSQMPFSWPHQLTVEKTPAYFTSPKVPERVYSMNPSIRLLLILRDPSERVLSDYTQVFYNHMQKHKPYPSIEEFLVRDGRLNVDYKALNRSLYHVHMQNWLRFFPLRHIHIVDGDRLIRDPFPEIQKVERFLKLSPQINASNFYFNKTKGFYCLRDSGRDRCLHESKGRAHPQVDPKLLNKLHEYFHEPNKKFFELVGRTFDWH | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan . Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact) . This modification is a crucial step in the biosynthesis of anticoa... |
O35310 | MTLLLLGAVLLVAQPQLVHSHPAAPGPGLKQQELLRKVIILPEDTGEGTASNGSTQQLPQTIIIGVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSQGLGWYLTQMPFSSPHQLTVEKTPAYFTSPKVPERIHSMNPTIRLLLILRDPSERVLSDYTQVLYNHLQKHKPYPPIEDLLMRDGRLNLDYKALNRSLYHAHMLNWLRFFPLGHIHIVDGDRLIRDPFPEIQKVERFLKLSPQINASNFYFNKTKGFYCLRDSGKDRCLHESKGRAHPQVDPKLLDKLHEYFHEPNKKFFKLVGRTFDWH | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan . Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact) . This modification is a crucial step in the biosynthesis of anticoa... |
Q9Y278 | MAYRVLGRAGPPQPRRARRLLFAFTLSLSCTYLCYSFLCCCDDLGRSRLLGAPRCLRGPSAGGQKLLQKSRPCDPSGPTPSEPSAPSAPAAAVPAPRLSGSNHSGSPKLGTKRLPQALIVGVKKGGTRAVLEFIRVHPDVRALGTEPHFFDRNYGRGLDWYRSLMPRTLESQITLEKTPSYFVTQEAPRRIFNMSRDTKLIVVVRNPVTRAISDYTQTLSKKPDIPTFEGLSFRNRTLGLVDVSWNAIRIGMYVLHLESWLQYFPLAQIHFVSGERLITDPAGEMGRVQDFLGIKRFITDKHFYFNKTKGFPCLKKTESS... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate . Catalyzes the O-sulfation of glucosamine in GlcA2S-GlcNS . Unlike HS3ST1/3-OST-1, does not convert non-... |
Q673U1 | MAYRVLGRAGPPQPRRARRLLFAFTLSLSCTYLCYSFLCCCDGLGQSRLLGAPRCLRGPSASGQKLLAKSRPCDPPGPTPSEPSAPSAPAAAAPAPRLSGSNHSGSPKPGTKRLPQALIVGVKKGGTRAVLEFIRVHPDVRALGTEPHFFDRNYGRGLDWYRSLMPRTLETQITLEKTPSYFVTQEAPRRIFNMSRDTKLIVVVRNPVTRAISDYTQTLSKKPDIPTFEGLSFRNRSLGLVDVSWNAIRIGMYALHLESWLRYFPLAQIHFVSGERLITDPAGEMGRIQDFLGIKRFITDKHFYFNKTKGFPCLKKPEST... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate (By similarity). Catalyzes the O-sulfation of glucosamine in GlcA2S-GlcNS (By similarity). Unlike HS3ST1/... |
Q9Y661 | MARWPAPPPPPPPPPPLAAPPPPGASAKGPPARKLLFMCTLSLSVTYLCYSLLGGSGSLQFPLALQESPGAAAEPPPSPPPPSLLPTPVRLGAPSQPPAPPPLDNASHGEPPEPPEQPAAPGTDGWGLPSGGGGAQDAWLRTPLAPSEMITAQSALPEREAQESSTTDEDLAGRRAANGSSERGGAVSTPDYGEKKLPQALIIGVKKGGTRALLEAIRVHPDVRAVGVEPHFFDRNYEKGLEWYRNVMPKTLDGQITMEKTPSYFVTNEAPKRIHSMAKDIKLIVVVRNPVTRAISDYTQTLSKKPEIPTFEVLAFKNRT... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate (By ... |
Q8IZT8 | MLFKQQAWLRQKLLVLGSLAVGSLLYLVARVGSLDRLQPICPIEGRLGGARTQAEFPLRALQFKRGLLHEFRKGNASKEQVRLHDLVQQLPKAIIIGVRKGGTRALLEMLNLHPAVVKASQEIHFFDNDENYGKGIEWYRKKMPFSYPQQITIEKSPAYFITEEVPERIYKMNSSIKLLIIVREPTTRAISDYTQVLEGKERKNKTYYKFEKLAIDPNTCEVNTKYKAVRTSIYTKHLERWLKYFPIEQFHVVDGDRLITEPLPELQLVEKFLNLPPRISQYNLYFNATRGFYCLRFNIIFNKCLAGSKGRIHPEVDPSV... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagu... |
Q96QI5 | MAGSGGLGGGAGGGQGAGAGQGAALRASRAPMLLVALVLGAYCLCALPGRCPPAARAPAPAPAPSEPSSSVHRPGAPGLPLASGPGRRRFPQALIVGVKKGGTRALLEFLRLHPDVRALGSEPHFFDRCYERGLAWYRSLMPRTLDGQITMEKTPSYFVTREAPRRIHAMSPDTKLIVVVRNPVTRAISDYAQTLSKTPGLPSFRALAFRHGLGPVDTAWSAVRIGLYAQHLDHWLRYFPLSHFLFVSGERLVSDPAGEVGRVQDFLGLKRVVTDKHFYFNATKGFPCLKKAQGGSRPRCLGKSKGRPHPRVPQALVRRL... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to heparan sulfate. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes Simplex Virus-1 (HSV-1) and permits its entry. Unlike 3-... |
Q9Y663 | MAPPGPASALSTSAEPLSRSIFRKFLLMLCSLLTSLYVFYCLAERCQTLSGPVVGLSGGGEEAGAPGGGVLAGGPRELAVWPAAAQRKRLLQLPQWRRRRPPAPRDDGEEAAWEEESPGLSGGPGGSGAGSTVAEAPPGTLALLLDEGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYDKGLAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQTLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLRHFPIRQMLFVSGERLISDPA... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate . Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2 . The substrate-sp... |
Q8BKN6 | MAPSGPTGAQPSPAEPLSRSIFRKFLLMLCSLLTSLYVFYCLAERCPPGSGPVAGVPGRGVPAGPRELAMWPAGAPRKRLLQLRQRRRRGRSGPGDSSDQEEQSPGLAAAPGGSGAGSSVAEAQPGTLALLLDEGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYHKGLAWYRDLMPRTLEGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQTLSKRPDIPSFESLTFRNRSAGLIDTSWSAIQIGLYAKHLEPWLRHFPLGQMLFVSGERLVSDPAGELRRVQDFLGLK... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. Unlike HS3ST1/3-OS... |
A4FUZ6 | MLPNTGKLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQAHPKLPGTIYTAAEEIKAAGGKALPCIVDVRDEEQISSAVEKAVEKFGGIDILVNNASAISLTNTLETPTKKVDLMMNVNTRGTYLTSKACIPYLKKSKVAHILNLSPPLNLNPLWFKQHCAYTIAKYGMSMCVLGMAEEFKGEIAVNALWPRTAIHTAAMDMLGGSGVESQCRKVDIMADAAYCIFKKPKSFTGNFIIDENILKEEGIKNFDVYAITPGHPLLPDFFLDEQPAMVTKKADSYGAVPELKEEKTQPPPKARSGAVEETFRIVKDS... | Function: Has apparently no steroid dehydrogenase activity.
Sequence Mass (Da): 45150
Sequence Length: 418
Subcellular Location: Peroxisome
EC: 1.-.-.-
|
Q6P5L8 | MLQNTGKLAGCTIFITGASRGIGKAIALKAAQDGANVVIAAKTADPHPKLPGTIYTAAAEIEAAGGKALPCIVDVRDEKQINDAVEQAVEKFGGIDILVNNASAINLTGTLQTPMKKADLMLGINLRGTYLTSKLCIPHLLKSKNPHILNLSPPLNLNPIWFKNHTAYTIAKYGMSMCVLGMAEEFRGSIAVNALWPKTAIQTAAMDMLGGSEVGKQCRKVEIMADAAYAIFKQPTSFTGQFVIDEDILKKEGIKDFDVYAVEPGHPLLPDFFLDGQPEDLVKHMEAHGATPAFTTAKADPVAAGPVSEMFNTIRGIISP... | Function: Has apparently no steroid dehydrogenase activity.
Sequence Mass (Da): 44421
Sequence Length: 415
Subcellular Location: Peroxisome
EC: 1.-.-.-
|
Q6YN16 | MLPNTGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQHCAYTIAKYGMSMYVLGMAEEFKGEIAVNALWPKTAIHTAAMDMLGGPGIESQCRKVDIIADAAYSIFQKPKSFTGNFVIDENILKEEGIENFDVYAIKPGHPLQPDFFLDEYPEAVSKKVESTGAVPEFKEEKLQLQPKPRSGAVEETFRIVKDS... | Function: Has apparently no steroid dehydrogenase activity.
Sequence Mass (Da): 45395
Sequence Length: 418
Subcellular Location: Peroxisome
EC: 1.-.-.-
|
Q2TPA8 | MLPNTGKLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTTQKHPKLLGTIYTAAEEIEAAGGTALPCVVDVRDEQQINSAVEKAVEKFGGIDILVNNASAISLTNTLDTPTKRVDLMMNVNTRGTYLTSKACIPFLKKSKVGHILNLSPPLNLNPLWFKQHCAYTIAKYGMSMCVLGMAEEFRGEIAVNALWPRTAIHTAAMDMLGGSGVENQCRKVDIIADAAYSIFKRPKSFTGNFIIDENILKEEGIKNFDVYAIAPGHPLLPDFFLDEHPDAVMEEKESNDSVPEVKEEKLQLQEESQLQKQPQLQEQPQLQ... | Function: Has apparently no steroid dehydrogenase activity.
Sequence Mass (Da): 54208
Sequence Length: 490
Subcellular Location: Peroxisome
EC: 1.-.-.-
|
Q4V8F9 | MLPNTGKLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTTQRHPKLLGTIYTAAEEIEAAGGKALPCVVDVRDEQQINSAVEKAVERFGGIDILVNNASAISLTNTLETPTKRVDLMMSVNTRGTYLTSKACIPFLKKSKVAHILNLSPPLNLNPMWFKQHCAYTIAKYGMSMCVLGMAEEFRGEIAVNALWPRTAIHTAAMDMLGGAGVESQCRKVDIIADAAYSIFKRPKSFTGNFIIDENILKEEGIKDFDIYAITPGHPLLPDFFLDEHPDAVMEEKESYDPVPEVKEEKLQLQEQPQLQEQPQLQEKPQLQ... | Function: Has apparently no steroid dehydrogenase activity.
Sequence Mass (Da): 58344
Sequence Length: 524
Subcellular Location: Peroxisome
EC: 1.-.-.-
|
Q3AC32 | MSDYLVKGMAGEFIRFTGVSSRQTVEEARKRHNLSRLATAALGRALTATIILASDLKNPGDLLTLRIFGDGPLGGIVCSAGNDGMVRGYLFNPEVELPLNDANKLDVGRGIGKGHLYVTKDLGLKEPYTGTVQLVSGEIAEDVAYYLYYSEQRPNVFNLGVLVNPDGSVAQAGGCLIEILPGAPEEIISTLEQNLGEQQSLTYQLQQGKHIEEIIQEVVNPYKTEIYVKKPVGFLCSCSREKLLPHLIGLYSEVKDEEIVEAVCHFCREKYTFSGKEIKEYKEKNT | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
P58097 | MTDIAPDTGVLDDVVSAFQIENLPVRGRVVRLGAAIDEVLTRHDYPEPVANLLGEACALAALVGSSLKFEGRLIVQAQGDGPVRYVVVDYDTSGGLRGYCRFDPEEVAAVSEGFVRPGAKTLLGGGVFIMTLDQGPDMDRYQGVTPIEGETLALCAEQYFAQSEQTPTRVRLAVGQADTGQGATWRAGGILIQVIAGDQARGETQDAWTHVQALFETTGEDELIDPTVSTPTLLWRLFNEDGVRLLDEKPLKAFCRCSEDRIGVVMDSFSAEEVAEMVEPDGKIHVTCEYCSRIYKLDPPGA | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q1QU53 | MTDQIQRFLFDETNVRGEIVGLQQAYADVLDKHAYPAAVRRQLGELLGAVALLTETVKLDGTVSLEVRGQGAVRLLMAESNPGGELRAIARLDDEAALPEENASLTALVGEAQIVITLDPRDGQRYQGIVAVEADTLAACLEDYFARSEQLATRLWLAADGDRAAGMLLQQLPDDASNRDPDAWERTVHLATTLSDAELLDLDQRELLYRLFHEEQARVFEPKALRFGCTCTRERIASALHGLGADELRHIVREQGAVETQCHFCHSHYRFTAADIETLIESPGAGAPTLH | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q7NWI9 | MNMNHHDKLQRFLFDGAPVRGALVRLDGAWQQVLARRAYPQALKTVLGEMMAASVLMAANLKFDGSLILQIHGTGALKLAVVECNNDRTVRATAKWDGDLDGKPLKALLGEGGKFVLTLEPRLDKNQTWQGIVALEGDSVGQMLENYMLRSEQLDTALVLASGDEAAAGMLLQRLPEGHGEAEGWDRVQMLGRTLKAEELLGLGAEDILHRLFHEEQVRVFEQETVSFNCNCSRERVSNMLTMLGGQEVGDVLLEQGSVEIVCDYCNQRYVFDEEDANQLFDYDVVAAAREARH | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
B5EC90 | MTDYLVRAIAKSGSVRALACVTTATVGAICKRHDTLPTATAALGRGITAGALMGALLKTGQRVAMRFEGNGPLKKIVIEADANGSVRGYVGDPKVHLLRPDGALDVNNALGRAGFLTVAKDLGLKEPYRGTVQLYTSGIAEDLALYLVESEQIPSAVGIAEFIEQDGTVAAAGGFLIQAVPPVDPLVIEELMTRIEQLPPLSELLHKGGNPEQILEQLLAGIPYDILEKRNIAFACSCSRERIERVLLSMGKKELSSMKKDQHGSEVTCEFCGEHYLFDEADLDRIIAEIAKQEG | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q17ZW5 | MRDYVLRATSGNGQVRAFVATTRNTVEEARRLHETTKVATAALGRTLTATSIMGLMMKNDSDKLTVIIKGGGPIGTIIATSDSKGMVKGYVGNPQVEVEDYPNGKLNVAAAVGTEGVVKVIKDLGLREPYNGTYPLVSGEIAEDFTYYFAVSEQTPSVVALGVLTKEDEVEFAGGFIVQLMPDAEEETIAKLEENVAKLPSITNMLKEGKSPEDILNIVLDGLEPKILDTCEVGFMCECSKERVKTALVAIGKKSLAQIIEEDKKAEVGCQFCNKKYMYSEEELLEILKEM | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q5SJV8 | MGRILRGLAGEGDLRVVAAETTDVVEEARLRHGLSPTATAALGRAMTGALLLAQLLLKTPKERITLRVEGTGPLGGLVVEADAFGHVRGYVKNPRAEVPLREDGKLNVGELVGAGALRVDRSLPSGEVYTSTVPLVSGEIAEDLAHYLWQSEQIPSAVLLGVRVKGEGEVEVAGGVAVQVMPGAREEVLDRLEANLKDLPGLTPLLRERGLEGALEALLAGLGFERTDLRALGYFQNEIPARFRCRCNREKALEALVFFTPEEREDMIVKDGGAEVVCHWCGEVYRFSPEEVRSLVAEVRCPDCGTLWLYPKGDGTLARI... | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
B5YJH3 | MDEVVKGLIKNEHVLVVATICTETVEYARKIHDTWPTATAAMGRVIAGSVLLASTLKDRQKIMVQIKGDGPLNEVVAEADSFYRVRAYVKRPHIYMGLKNEKIDVGRGVGKGFLNVIRDLGLREYYQSSVELQTGEIARDLAYYLNVSEQIPSAVSLGVYVEPDNSVKAAGGFMIQTMPETRTEIVEFLERKLSETQSTSSMILQGMDSLQILEEVVGLPIEVLHRGTVTYFCPCTKDRVINAIVTLGREEIQKMIEEGKTVDVECYFCKKKYEVTVEELKILLREI | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q112R6 | MADQLIRAMAAEGGIRAVGVITTRLTEEARQRHKLSWVASVVLGRTMAAGLLLASSMKTPESRVNIRVQGNGPLGEVLVDAGLDGTVRGYVNNPTIELLPNKIGKHDIGKAVGNQGYLYIVRDIGYGYPYSGTVELVSGEIGDDITHYLAKSEQTPSALVLGVFVDKEGVQTAGGILLQVMPKVAIDEELVQVLESRIASLSGFTSLLHSGKTLPEIFQELLGDMGLNILPEAQIVRFKCDCSMEKVLRALRMFGVDELQNMIEEDKGAEVTCEFCSQLYQASPKELTQIIQDLQQPSTEVPLGQLRRSSH | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q9KNK2 | MANNMLHRYLFKDLSVRGELVQLDDTYQQMISSQEYPAAVQHLIGELLVATSLLTATLKFEGSITLQLQGNGPVSLVVINGDNNQQVRGVARWKGDIADDASLHDMLGKGHLVITIEPKQGERYQGVVGLEGDTLAQVLEGYFERSEQLKTRLWIRVGKHDGKACAAGMLLQIVPDGKGSAEDFEHLEQLTNTIKDEELFALPAEELLYRLYNQETVQLFTPQQISFRCGCSRERSAAAIVTVAREEINDILAQDGAVALHCDYCGTTYSFDSAQVAELYAPSSANGSTLH | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q62EZ9 | MEQFHGTTILSVRRGDKVALGGDGQVTLGNIVMKGGARKVRRIYNNQVLVGFAGGTADAFSLLDRFEAKLEKHQGNLTRAAVELAKDWRTDRLLRRLEAMLIAADATTTLVITGNGDVLDPEGGICAIGSGGSYAQAAARALAENTDLSPREIVEKALGIAGDMCIYTNHNRIIETIE | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 19053
Sequence Length: 178
Subcellular Location: Cytoplasm
EC: 3.4.25.2
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Q72RY8 | MPENKIRSTTILCVRKNGKVAIGGDGQVSMGNTVMKNTAKKIRRLYDGKILSGFAGSAADAFTLFELFEKKVQEFGGSLSRSAVELAREWRTDRMLRRLEALLIVADKEESFLISGTGDVISPDEGVIAIGSGGNYALAAARALYDHTNLSPKEIVESSMKIAADICIYTNNHITLEEIL | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 19585
Sequence Length: 180
Subcellular Location: Cytoplasm
EC: 3.4.25.2
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Q92C74 | MELHATTIFAVQHDGKAAMAGDGQVTLGESVVMKHTAKKVRRLFHDKVIAGFAGSVADAFTLFEKFEAKLNEYNGNLERAAVELAQQWRSDSVLRKLEAMLIVMDKDTLLLVSGTGEVIEPDDGILAIGSGGNYALAAGRALKRHNGGQMEAKDIARHALEIASEICVFTNDHITVEEL | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 19390
Sequence Length: 179
Subcellular Location: Cytoplasm
EC: 3.4.25.2
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Q2VYI5 | MSESSLPSWHGTTILCLRKDGRVVIAGDGQVSLGATVIKGNARKVRKVGGGSILVGFAGATADAFTLLERLEAKLEKHPGQLTRACVELAKDWRTDRYLRRLEAMMAVADKDVSLVLTGQGDVLEPEDGIIGIGSGGNYALAAARALIDIDGLDAETIARKAMAIAAGICVYTNGNMIVESL | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 19124
Sequence Length: 182
Subcellular Location: Cytoplasm
EC: 3.4.25.2
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P49617 | MTTIVCVRKDGKVAIGGDGQATLGNCIEKGTVRKVRRLYKDKVVTGFAGSTADAFILRDLFEKKLELHQGHLVKSAVELAKEWRTERALRRLEAMMIVANDSEFLLVSGSGDVIEPEQDVLAIGSGGNYAKAAALALLRTENNLSAKEIVAEALKIAGDIDIYSNYNHVIEEV | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 18817
Sequence Length: 173
Subcellular Location: Cytoplasm
EC: 3.4.25.2
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Q9LNB6 | MAEEAKAKGNAAFSSGDFTTAINHFTEAIALAPTNHVLFSNRSAAHASLHQYAEALSDAKETIKLKPYWPKGYSRLGAAHLGLNQFELAVTAYKKGLDVDPTNEALKSGLADAEASVARSRAAPNPFGDAFQGPEMWTKLTSDPSTRGFLQQPDFVNMMQEIQKNPSSLNLYLKDQRVMQSLGVLLNVKFRPPPPQGDEAEVPESDMGQSSSNEPEVEKKREPEPEPEPEVTEEKEKKERKEKAKKEKELGNAAYKKKDFETAIQHYSTAIEIDDEDISYLTNRAAVYLEMGKYNECIEDCNKAVERGRELRSDYKMVAR... | Function: Mediates the association of the molecular chaperones HSP70 and HSP90. Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 64585
Sequence Length: 572
Domain: The tetratricopeptide repeat (TPR) domain, forming... |
Q43468 | MAEEAKAKGNAAFSAGDFAAAVRHFSDAIALSPSNHVLYSNRSAAHASLQNYAEALADAQKTVDLKPDWPKAYSRLGAAHLGLRRHRDAFSAYKTGLQLDPDNAALKSGLADAQAAASRPPPTSPFATAFSGPDMWARLTADPTARANLQDPEFVKIMQDIQKDPNKFNLHLSDQRVMHAIGVLLNVKIQTPNHDENDHDADDDVSEDEVVSQPEPEHEPEAAVEVAEEEEEEEKETRDRKGQAQKEKEAGNAAYKKKDFETAIGHYSKALELDDEDISYLTNRAAVYLEMGKFEDCIKDCEKAVERGKELRSDYKMIAR... | Function: Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting (By similarity). Mediates the association of the molecular chaperones HSP70 and HSP90.
PTM: Phosphorylated.
Sequence Mass (Da): 64178
Sequence Length: 572
Domain: The tetratricopeptide repeat (TPR) domain, forming... |
Q5XEP2 | MADEAKAKGNAAFSSGDFNSAVNHFTDAINLTPTNHVLFSNRSAAHASLNHYDEALSDAKKTVELKPDWGKGYSRLGAAHLGLNQFDEAVEAYSKGLEIDPSNEGLKSGLADAKASASRSRASAPNPFGDAFQGPEMWSKLTADPSTRGLLKQPDFVNMMKEIQRNPSNLNLYLQDQRVMQALGVLLNIQIRTQQAGDDMEIGEEEMAVPSRKEPEVEKKRKPEPEPEPEPEFGEEKQKKLKAQKEKELGNAAYKKKDFETAIQHYSTAMEIDDEDISYITNRAAVHLEMGKYDECIKDCDKAVERGRELRSDYKMVAKA... | Function: Mediates the association of the molecular chaperones HSP70 and HSP90. Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 64520
Sequence Length: 571
Domain: The tetratricopeptide repeat (TPR) domain, forming... |
Q9STH1 | MAEEAKSKGNAAFSSGDYATAITHFTEAINLSPTNHILYSNRSASYASLHRYEEALSDAKKTIELKPDWSKGYSRLGAAFIGLSKFDEAVDSYKKGLEIDPSNEMLKSGLADASRSRVSSKSNPFVDAFQGKEMWEKLTADPGTRVYLEQDDFVKTMKEIQRNPNNLNLYMKDKRVMKALGVLLNVKFGGSSGEDTEMKEADERKEPEPEMEPMELTEEERQKKERKEKALKEKGEGNVAYKKKDFGRAVEHYTKAMELDDEDISYLTNRAAVYLEMGKYEECIEDCDKAVERGRELRSDFKMIARALTRKGSALVKMAR... | Function: Mediates the association of the molecular chaperones HSP70 and HSP90. Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting (By similarity). Involved in acclimation to heat.
PTM: Phosphorylated.
Sequence Mass (Da): 63706
Sequence Length: 558
Domain: The tetratricopep... |
Q8ILC1 | MVNKEEAQRLKELGNKCFQEGKYEEAVKYFSDAITNDPLDHVLYSNLSGAFASLGRFYEALESANKCISIKKDWPKGYIRKGCAEHGLRQLSNAEKTYLEGLKIDPNNKSLQDALSKVRNENMLENAQLIAHLNNIIENDPQLKSYKEENSNYPHELLNTIKSINSNPMNIRIILSTCHPKISEGVEKFFGFKFTGEGNDAEERQRQQREEEERRKKKEEEERKKKEEEEMKKQNRTPEQIQGDEHKLKGNEFYKQKKFDEALKEYEEAIQINPNDIMYHYNKAAVHIEMKNYDKAVETCLYAIENRYNFKAEFIQVAKL... | Function: Acts as a co-chaperone and mediates the association of the chaperones HSP70 and HSP90 probably facilitating substrate transfer from HSP70 to HSP90 . Stimulates HSP70 ATPase activity and, in contrast, inhibits HSP90 ATPase activity .
Sequence Mass (Da): 66057
Sequence Length: 564
Domain: The TPR repeats form 3... |
P25407 | MVNKEEAQRLKELGNKCFQEGKYEEAVKYFSDAITNDPLDHVLYSNLSGAFASLGRFYEALESANKCISIKKDWPKGYIRKGCAEHGLRQLSNAEKTYLEGLKIDPNNKSLQDALSKVRNENMLENAQLIAHLNNIIENDPQLKSYKEENSNYPHELLNTIKSINSNPMNIRIILSTCHPKISEGVEKFFGFKFTGEGNDAEERQRQQREEEERRKKKEEEERKKKEEEEMKKQNRTPEQIQGDEHKLKVMN | Function: Acts as a co-chaperone and mediates the association of the chaperones HSP70 and HSP90 probably facilitating substrate transfer from HSP70 to HSP90. Stimulates HSP70 ATPase activity and, in contrast, inhibits HSP90 ATPase activity.
Sequence Mass (Da): 29324
Sequence Length: 252
Domain: The TPR repeats form 3 d... |
F8RP11 | MADEAKAKGNAAFSAGRFEEAAGHFSDAIALAPANHVLYSNRSAALASIHRYSDALADAEKTVELKPDWAKGYSRLGAAHLGLGDAASAAAAYEKGLALDPSNEGLKAGLADAKKAAAAPPRRAPSGGADAIGQMFQGPELWTKIASDPATRAYLDQPDFMQMLREVQRNPSSLNTYLSDPRMMQVLSLMLNIKIQTPQDSDFSQSSSPSQPPPQQQKQQPETKAREMEPEPQPEPMEVSDEEKERKERKAAALKEKEAGNASYKKKDFETAIQHYTKALELDDEDISYLTNRAAVYIEMGKYDECIEDCDKAVERGREL... | Function: Mediates the association of the molecular chaperones HSP70 and HSP90 (By similarity). Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting.
PTM: Phosphorylated.
Sequence Mass (Da): 65097
Sequence Length: 581
Domain: The tetratricopeptide repeat (TPR) domain, forming... |
P25619 | MNDTLSSFLNRNEALGLNPPHGLDMHITKRGSDWLWAVFAVFGFILLCYVVMFFIAENKGSRLTRYALAPAFLITFFEFFAFFTYASDLGWTGVQAEFNHVKVSKSITGEVPGIRQIFYSKYIAWFLSWPCLLFLIELAASTTGENDDISALDMVHSLLIQIVGTLFWVVSLLVGSLIKSTYKWGYYTIGAVAMLVTQGVICQRQFFNLKTRGFNALMLCTCMVIVWLYFICWGLSDGGNRIQPDGEAIFYGVLDLCVFAIYPCYLLIAVSRDGKLPRLSLTGGFSHHHATDDVEDAAPETKEAVPESPRASGETAIHEP... | Function: Probably cooperates with other heat shock proteins in the translocation of polypeptides through membranes. It may counteract the altering effect of heat shock on the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37045
Sequence Length: 332
Subcellular Location: Membrane
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O74914 | MASEGKVLLVASSYYGPFYPDGMNTGVHFAELLIPYQVFREAGYEVQLTSETGKCKFDDHSIKKSALGEVERDAFDNKDNEFWYALKDIKPADKINYKEFCIMFIAGGHAAMFDLPHATNLQTLAQQIYASNGVLAAVCHGPVMLPFVDDTKSPEGRSVVYGKKVTAFNSTGELVMGVSSALRERNMQDLNSLFREAGAEFVDPPTPMSDFTQVDGRIVTGVNPMSAKSTAEAAIKVSQSLRKT | Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step . May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS) (By similarity).
Catalytic Activity: H2O + methylglyoxal = (R)-lactate + H(+)... |
Q04432 | MAPKKVLLALTSYNDVFYSDGAKTGVFVVEALHPFNTFRKEGFEVDFVSETGKFGWDEHSLAKDFLNGQDETDFKNKDSDFNKTLAKIKTPKEVNADDYQIFFASAGHGTLFDYPKAKDLQDIASEIYANGGVVAAVCHGPAIFDGLTDKKTGRPLIEGKSITGFTDVGETILGVDSILKAKNLATVEDVAKKYGAKYLAPVGPWDDYSITDGRLVTGVNPASAHSTAVRSIDALKN | Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals . Involved in protection against reactive oxygen species (ROS) . Important for viability in stationary phase. May negatively regulate TORC1 ... |
Q08992 | MTPKRALISLTSYHGPFYKDGAKTGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHYLPKSFIGGEDKMNFETKNSAFNKALARIKTANEVNASDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLFDGLIDIKTTRPLIEGKAITGFPLEGEIALGVDDILRSRKLTTVERVANKNGAKYLAPIHPWDDYSITDGKLVTGVNANSSYSTTIRAINALYS | Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS) (By similarity). Important for viability in stationary phase. May negatively r... |
O43084 | MPAKTRNVLIACSDYYGPFYKDGENTGAFFLELLHPYLVFRDACFNVDIVTESGKIQFDDHSVAGPAIDKGSKGEEFLSYDDHIASGPELSKAEKYVLENKDDMFWRIVQNSKTADEVNPDKYDIFFVAGGHATLFDFPKATNLQKLGTSIYENGGVVAAVCHGPTLLPFMKRQTSDGSVSIVCGKDVTAFDRVAEDKSKLMEALKKYNLEVLDDMLNDAGANFIKSPNPFGDFVIADGRLVTGSNPASATSTAKTALRVL | Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS).
Catalytic Activity: H2O + methylglyoxal = (R)-lactate + H(+)
Sequence Mass (D... |
Q10092 | MVLFMKTVQRPEHISLKSCIPFKSLQRQGIVFRLSVRMVMLADDHSISDSALSDSDKNAFKDKNNDFWKAIKNAKNASDINFSDYSIFFAAGGHGTLFDFPSATNLHKGAAKIYSMGGVIAAVCHGPVILPCIKDSTGFSIVKGKTVTAFNEIAEQQMNLMPTFEKYHFKTLNKLFQEAGSNFVDPQEPFDDFVKTDGKLVTGANPASAASTAKAALNSLNS | Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS).
Catalytic Activity: H2O + methylglyoxal = (R)-lactate + H(+)
Sequence Mass (D... |
Q09918 | MDERHEAAGETSEKPKVLFLLNSYYGPFYDDGDNTGVNVVDLYEAFKVFEENGFDIVIASDTGDYGFDDKSFRDPAIVDETQSIFSNPDCSLMKKLKNIARLDRLNPSDYVIVYIPGGYGCSFDFPHAKVVQDFLYRFYETKGIICAVAQANIALAYTTNSDGQALCTNRRVTGCTWKDEVQNGVLNVMNRLNFYSFGHIAENIGAIFESPPVYVEDPFIVEDGQLFTGSNTNSAKGVAMEAVRAVLNYDG | Function: May catalyze the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS).
Catalytic Activity: H2O + methylglyoxal = (R)-lactate + H(+)
Sequence Mass... |
Q5EBG6 | MEIPVPVQPSWLRRASAPLPGFSAPGRLFDQRFGEGLLEAELASLCPAAIAPYYLRAPSVALPTAQVSTDSGYFSVLLDVKHFLPEEISVKVVDDHVEVHARHEERPDEHGFIAREFHRRYRLPPGVDPAAVTSALSPEGVLSIQATPASAQAQLPSPPAAK | Function: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contrac... |
Q5EAC9 | MADGQMPFPCHYTSRRRRDPFRDSPLSSRLLDDGFGMDPFPDDLTASWPDWALPRLSSAWPGTLRSGMVPRGPTAMTRFGVPAEGRSPPPFPGEPWKVCVNVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVDPVTVFASLSPEGLLIIEAPQVPPYSPFGESSFNNELPQDGQEVTCT | Function: Displays temperature-dependent chaperone activity.
PTM: Phosphorylated.
Sequence Mass (Da): 21673
Sequence Length: 196
Subcellular Location: Cytoplasm
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F8G0M4 | MSMKQRVIIVGGGPVGLLTALGLAKAGTNVVVLEAESQPSDSPRALVYHFPVLPHLKRLGVLDDCVAAGLMRQNFAWRVHSTSEMIFWDLSCLEGDVELPYALHLGQDKLSRILIEHLKALPNVEVRYSSPVVDCEVGPRSVRVVLGGESPGVIVEGDWLIGADGANSFVRREVLNQNFFGITWPQRYVATNTRFDFDKLGFGKTTMQVDDVYGSVICNIDADSLWRVTFMEDPNLPMEGIRGRIDQVFKELLPTNDPYEVVAFSPYRMHQRVTDRMRNGRVILIGDAAHVTNPTGGLGLTGGMFDAFALTSVLNQVIHD... | Cofactor: Binds 1 FAD per subunit.
Function: Involved in the nicotine degradation. Catalyzes the cleavage of 6-hydroxy-3-succinoylpyridine (HSP) by incorporation of oxygen at the 3-position to produce to 2,5-dihydroxypyridine (DHP) and succinic semialdehyde.
Catalytic Activity: 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate ... |
I6YBZ8 | MAIDPNSIGAVTEPMLFEWTDRDTLLYAIGVGAGTGDLAFTTENSHGIDQQVLPTYAVICCPAFGAAAKVGTFNPAALLHGSQGIRLHAPLPAAGKLSVVTEVADIQDKGEGKNAIVVLRGRGCDPESGSLVAETLTTLVLRGQGGFGGARGERPAAPEFPDRHPDARIDMPTREDQALIYRLSGDRNPLHSDPWFATQLAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAARFTKPVFPGETLSTVIWRTEPGRAVFRTEVAGSDGAEARVVLDDGAVEYVAG | Function: Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase activity . In vitro, can hydrate various enoyl-CoA such as (2E)-hexenoyl-CoA, (2E)-octenoyl-CoA, (2E)-decenoyl-CoA, (2E)-dodecenoyl-CoA and (2E)-hexadecenoyl-CoA . May contribute to the persistence of the tuberculosis infection by inducing COX-2 ex... |
Q7U2S5 | MRTFESVADLAAAAGEKVGQSDWVTITQEEVNLFADATGDHQWIHVDPERAAAGPFGTTIAHGFMTLALLPRLQHQMYTVKGVKLAINYGLNKVRFPAPVPVGSRVRATSSLVGVEDLGNGTVQATVSTTVEVEGSAKPACVAESIVRYVA | Function: Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase activity.
Catalytic Activity: a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 16007
Sequence Length: 151
EC: 4.2.1.-
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Q99081 | MNPQQQRMAAIGTDKELSDLLDFSAMFSPPVNSGKTRPTTLGSSQFSGSGIDERGGTTSWGTSGQPSPSYDSSRGFTDSPHYSDHLNDSRLGAHEGLSPTPFMNSNLMGKTSERGSFSLYSRDTGLPGCQSSLLRQDLGLGSPAQLSSSGKPGTAYYSFSATSSRRRPLHDSAALDPLQAKKVRKVPPGLPSSVYAPSPNSDDFNRESPSYPSPKPPTSMFASTFFMQDGTHNSSDLWSSSNGMSQPGFGGILGTSTSHMSQSSSYGNLHSHDRLSYPPHSVSPTDINTSLPPMSSFHRGSTSSSPYVAASHTPPINGSD... | Function: Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis .
Sequence Mass (Da): 72965
Sequence Length: 682
Domain: ... |
O67798 | MSEREFLRFGDELDVKNCNTSRSFNGLLMAIGGIIGGTAGMLIALIIAGFMNFMSYWFSDKIVLSMYGAREIPYEEAPWLHQIVEELARRANMPKPKIYLVPMEQPNAFATGRGPGHAAVAVTRGILEILDQEELKGVLAHELAHIKNRDVLVATIAATIAGAIGFLANMAQWALFFGGLNRNEEEEGGGFAEMIGAILMIIIVPIIATIVQLAISRSREYFADETGAKICGCPVALARALKKIEEYVMQVPANVNPGTAHLFIENPLKGGGIMELLSTHPSTEKRIQRLCELARKMGQECI | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33031
Sequence Length: 302
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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O30004 | MMLYFFDPVYMMLAVLGYFVMLLLASTIAPKVASRVSGKFSLFTSMVLLAGMILAISAAIIYLILAYAGVYISFYGLIIFLLIINLLMYLLSPYIINLSYGAQRDERLQMVVNSVARRLNVKPPKAVVVRSPPNAFAYGNFLTGKFVAVSESLMRMLSQEELEAVIGHEIGHHKHRDNAVMLLFGLLPSVIFYLGYALLHSSMRDDRRGAQLAAIGIAAVIVSFIVQILVLAFSRLREYYADFEGVRATNKDAMQRSLAKIHLFYHRYPDYLAPIQDSKFRTLFIYAFTNAVAEPITRADIEALKNMKVSPIQEFLSTHP... | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37855
Sequence Length: 335
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
Q64V41 | MQYVGIQTQQSRNNLRSGILLILFPCLVAVLTYLFCYLLITFTVEDDYGQYNTLAMTNQMFINLIPYIIGGVLVWFIIAYFTNSSIIKAATGARPLERKENKRIYNLVENLCMSQGMKMPKINIIDDDSLNAYASGINEQTYTITLSKGIIEKLNDEELEGVIAHELTHIRNHDVRLLIISIVFVGIFSMLAQIALRSVYYSSWTRSRNDKNNGAILILVLAMIVAAIGYFFATLMRFAISRKREYMADAGAAEMTKNPLALASALRKISADPDIEAVEREDVAQLFIQHPGKQAKSALSGLSGLFATHPPIEKRIAILE... | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36129
Sequence Length: 322
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
O31657 | MAKRIFLFILTNILVLTTIGIVLSVLSSVTGVGTYFTADGGIDPMALLVFSLVVGFVGSFTSLAISRWMAKTMMGVRVLNPKKHSLSYEEQQLVDRVHRLSRSAGLTKMPEVGIYRSPEVNAFATGPSKRRSLVAVSSGLLEQMDDAAVEGVLAHEVAHITNGDMVTMTLLQGIVNTFVVFLSRIAAWIASRFVKEDLAPIVHFIAMIIFQIVFSILGSLVVFAYSRHREFHADRGGADLAGKDKMIHALRTLKSYSSRILEDDQTAVQTLKINGKKRSSLFSTHPDLDERIRRLEAK | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32865
Sequence Length: 298
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q1LTF8 | MMRIVIFLLTNLAVMVVFGILLTCVGTHSSNTVRLMIISGLFGFCGAFISLLMSKFIALRSVGGKVISQPQNETEHWLLNIILNQAQKIGITMPQVAIYNAPDMNAFATGPSRNNSLVAVSTGLLQNMPRTEIEAVIAHEISHISNGDMVTITLISGIVNTFVIFISRFLAQLTAGFIGSNNEESNNGNKLVYMIVSTILELAFGILASIIVLWFSRYREFYADAGSANIVGCDKMIAALQRLKTSYEPKVTNNIKIFCINGYQKSLSEFFMSHPPLNKRIEALRYGTYMK | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32134
Sequence Length: 291
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q8G6T7 | MHGHFNGLKTTLLFALMWAIIMLIWWATGGSRQTLSIYIVIGLITTFGTYWFSDKLAIASMGAREVSEQEAPEIYQIVRELSAKAGKPMPRIYIAPTMSPNAFATGRNERHAAVCCTQGILQILNARELRGVLGHELMHVYNHDILTSAIASAMATVISYLGYSLMYFGGGSRDDRDSSGGLGLIGALLSVILAPIAASLIQMAISRTREYDADEDGSLLTGDPEALASALNKISYGAQTTPMRKTAGTQSVSAMMIANPFSAVGFSRLFSTHPPTDERIARLMQMANEMNGTPIAPPTYSTRVGR | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33100
Sequence Length: 306
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q92743 | MQIPRAALLPLLLLLLAAPASAQLSRAGRSAPLAAGCPDRCEPARCPPQPEHCEGGRARDACGCCEVCGAPEGAACGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDANTYANLCQLRAASRRSERLHRPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELFRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKHRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTD... | Function: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of p... |
Q9R118 | MQSLRTTLLSLLLLLLAAPSLALPSGTGRSAPAATVCPEHCDPTRCAPPPTDCEGGRVRDACGCCEVCGALEGAACGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDAKTYTNLCQLRAASRRSEKLRQPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELYRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKNRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTD... | Function: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of p... |
O06291 | MDTRVDTDNAMPARFSAQIQNEDEVTSDQGNNGGPNGGGRLAPRPVFRPPVDPASRQAFGRPSGVQGSFVAERVRPQKYQDQSDFTPNDQLADPVLQEAFGRPFAGAESLQRHPIDAGALAAEKDGAGPDEPDDPWRDPAAAAALGTPALAAPAPHGALAGSGKLGVRDVLFGGKVSYLALGILVAIALVIGGIGGVIGRKTAEVVDAFTTSKVTLSTTGNAQEPAGRFTKVAAAVADSVVTIESVSDQEGMQGSGVIVDGRGYIVTNNHVISEAANNPSQFKTTVVFNDGKEVPANLVGRDPKTDLAVLKVDNVDNLTV... | Function: Essential protein that may act as a regulatory protease that is conditionally activated upon appropriate environmental triggers.
Catalytic Activity: Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.
Loca... |
A6YFB5 | MTMLWLAVLLTCGAPAALLPTSGVGCPARCDPSSCSPAPTNCQSGETALRCGCCSVCAAAENERCGEGPEDPLCASGLRCVRNGGVTRCQCPSNQPVCGSDGKTYSSLCRLQAESKAVQGRGVAAIIPIQRGDCQQGQKDPDSPRYKYNFIADVVEKIAPAVVHIELFRILPFFKREVPAASGSGFIVSEDGLILTNAHVVTNKHRLKVERSDGSTYDAQIIDVDEKADIALIKIKAKGKLPVLLLGRSEELRPGEFVVAIGSPFSLQNTVTTGIVSTAQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVVG... | Function: Serine protease with a variety of targets, including extracellular matrix proteins and proteoglycans such as biglycan, syndecan-4 and glypican-4. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular spac... |
Q9VFJ3 | MALRGSHRLEVIFKRCIASPVLHSHAANRRSSQLAIKEGDPNSNGNSGQYQQNGEQKEKGWRRLVRFFVPFSLGAVVSAAIIQREDLTPTIAASKMTGRRRDFNFIADVVAGCADSVVYIEIKDTRHFDYFSGQPITASNGSGFIIEQNGLILTNAHVVINKPHTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQVNNLSVMRLGKSSTLRSGEWVVALGSPLALSNTVTAGVISSTQRASQELGLRNRDINYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVTAGISFAIPIDYVKVFLERAAEKRKKGSAYKTGYP... | Function: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-inde... |
O43464 | MAAPRAGRGAGWSLRAWRALGGIRWGRRPRLTPDLRALLTSGTSDPRARVTYGTPSLWARLSVGVTEPRACLTSGTPGPRAQLTAVTPDTRTREASENSGTRSRAWLAVALGAGGAVLLLLWGGGRGPPAVLAAVPSPPPASPRSQYNFIADVVEKTAPAVVYIEILDRHPFLGREVPISNGSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGV... | Function: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-inde... |
Q9RZ06 | MILDRDLNLEQFISVVRHGEQVELSAAARERIARARTVIEQIVEGDTPIYGVNTGFGKFENVQIDRSQLAQLQHNLIVSHAIGMGEPLPAEVVRGMLLLRAQSLSLGHSGVRVEVVELLLALLNADALPVVPSQGSVGASGDLAPLAHLALGLIGLGDIEYQGQVRPAADVLAELGLSPVQLQAKEGLALINGTQLMGSLLALALHDAQVLLGTANLAAAMTVEARYGSHRPFQPDVVGLRPHPGALAVAAELREFLAGSEIAPSHLTGDGKVQDAYSLRAVPQVHGATWDALAQAERVLAVEFASVTDNPLIFPETGEV... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 55536
Sequence Length: 524
Pathway: Amino-acid degradation; L-histidine degradation in... |
Q6AKP3 | MNSKIEIKPGRLTLAELRRMAKAPVGVRLEEKCKGKINASVQTVGEVIRQGRVIYGINTGFGLLANTIIPNEELEHLQRSLILSHAAGVGAFMADSTVRLMMVLKINSLARGYSGIRLEVIEALVQLLNAEVYPSVPQKGSVGASGDLAPLAHMSIVLLGEGEASYRGQRLSGREGLELAGLSPITLGPKEGLALLNGTQASTAFALQGLFAAEELFATAMVSGSLSLDAALGSRRPFNPLIHAVRGHKSQIDVAASYRQLLEHSEIERSHKFCEAVQDPYSLRCQPQVMGACLNQIRNAAEVIGTEANAVSDNPLVFCK... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 54631
Sequence Length: 512
Pathway: Amino-acid degradation; L-histidine degradation in... |
Q54JI7 | MSTTDKIVYLNGNTLKIEDLINIGYRGYNVSITQEVEELIQKGRNVIDDILKSEKTVYGINTGFGLFSDVIIPPDQVKMLQVNLIRSHSSGVGTPLTPERTRMLLALRINVLTKGYSGITLETVKRAIKILNGNCLPLVPEKGTVGASGDLAPLSHLALGMMGEGKMYDFGDSGNTFTSNLDVDVLEYRNFKFSPANEILKRQNLTPIELNAKEGLALINGTQLITSLGAEAVYRCKVLAETANIITAMTFEALKGLTAAYHPLIHAARPHSGQGRVAAFLRSVLHSDQYPSEITLANKDTKKVQDSYTLRCVPQVHGIV... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 58946
Sequence Length: 539
Pathway: Amino-acid degradation; L-histidine degradation in... |
Q7NCB3 | MKLLTDWLVLDGCSLAVDDLVAVARGGVPVRLSPASLELVRRSRAFVEALLEGDEIVYGITTGFGYFKNRRIPRSAVEQLQQNLLMSSAAGLGEPFGREVVRAMLLLRANTLAQGYSGVRPETLQLLVAMLNRGVHPVVPCRGSVGASGDLAPLAHLALVLTGEGEAEVGGEVLPGAAALARAGLEPIRLGAKEGLALINGTQAMSALGALTVHRAQRLAKLADLACAMTLEATLGSRSAFLPHFHRLRPHPGQQSSARNLLVLTEDSALIASHAGCDRVQDAYSLRCAPQVHGASLDAISYAAGVIAIEINSVTDNPLI... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 54037
Sequence Length: 514
Pathway: Amino-acid degradation; L-histidine degradation in... |
Q9RZ05 | MSETLYTGISQLATPRPGPQRGAAMGDLHIIEDAALLVRGGVIQWVGPRAAAPTATHVHDLGGRAVVPGLVDPHTHAVWAGDRLSDWEAKLQGATYEEILARGGGIRSTMRATAAADVAELVALARPRLASLRASGATTTEVKSGYGLDFDAELRMLRAVRELQAEFELRPTLLIHVPPQEGRAEYVVGVCAELIPQVAREGLAEALDVFCEKEAFSVEETRTMFAAAQAHGLRVKLHADQFHAIGGTELACEVGALSVDHLEASGAAQIAALAASETVATILPGVTLHLGLPAAPGRQLIDSGAIVAIGTDLNPGSSPL... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
Q6AKP5 | MSHQLFRNTRIYSPMDSGQPSAGKAQGKLAHFPNGALLVADGLIVAMGDEEAVLAVAKGGAEVEEVDCGGRCMIPGFVDPHTHMCFAAPREAEFAQRIAGTSYLQILSEGGGILSSVRAVALAGEDELYKSTLHRVQTALSFGTTSLEIKSGYGLDTDNELKMLRVIGRVAVDSCLDIVATFLGAHAIPGQYKTDADAFITMIVEEMLPRVREQGIARFCDVFCERGVFSIEQSRILLKAARAMGLGLKIHADEVTDLGGAGLAAELGACSADHLLAASDTNIRAMSQAGVIATLLPATAYSLRKDYARARVMIENRVAV... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
Q55CY3 | MGFDFKLKISNASQLVVISKGKPFLIGKEMSNIEIIENGTMIIDENGIIFDIGTFKEMEEKYKDKSFEKVLDCTGKSVLPGFVDGHTHPVFSGDRVHEFAMKLAGATYLDVHKAGGGIQFTISHTKNSTEDELYQLLIPRLNRMLKNGTTLIEAKSGYGLETETEMKMLKVLDRASKQFQGVEIVSTYLGGHAIPKGMNASEATDDIINKQIPELKRLKDAGEISPANIDVFLEKGFFEYEDTKRILQAGKDIGLECNFHGDELSYMKSGELAGELGCRAISHLEKVSEDGMKAMAATPTFAVLLPTTAYILRLECPPAR... | Cofactor: Binds 1 zinc or iron ion per subunit.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate
Sequence Mass (Da): 46887
Sequence Length: 426
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
EC: 3.5.2.7
|
A6H0H4 | MKTLIINIKELLQVRDNHIDKVSGTEMGVLPKIDDAFLLIEDNLIANFGSMSNCPTIKTDQTIDAKGKIVLPTWCDSHTHIVYAGNRIQEFVDRIKGLSYEEIANRGGGILNSAKNLNQTSEEDIYNQSKVRLEEIMQQGTGAVEIKSGYGLTVDGEIKMLRVIKKLAANYPIKIKATFLGAHAFPSEYKENHADYINLIVNEMLPKIAAEKLADYIDVFLETGYFSVQETEKIIEAGKKYGLIPKIHVNQFTAIGGIKSCVKHEALSVDHLEIVTNEDIENLKGSKTMPVALPSCSYFISIPYTPARKMIAAGLPLALA... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
Q5L083 | MRPLFVRRARQLVTLAGSSAAPLVKEKMSDLGIIENGSVWIENGTIVAVGPDDELVRRFADRLAEAEVIDAKGKTVTPGLIDPHTHLVYAGSREHEWTMRLHGATYMEIMNAGGGIHATTKATREASEEALYEESKRRLDQFLLHGVTTVEAKSGYGLSLEHEIKQLEIAKRLHDTHPVDIVSTFLGAHAVPPEWKHDPDEYVRLVIDEMIPEVSRRGLAEFNDVFCERGVFTPDQARRMLEAGKASGLTPKIHADEIEPYGGAELAAEVGAISADHLLRASDEGIRRMADGGVIGVLLPGTAFFLMTKAADARRLIDAG... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
Q5FRS2 | MWDTLWTDIHVATADPALISDQDGYGCIHNAAIGIENGRISWIGAARDLPDAPQNLAHKIHSGNGLWMTPGLVDAHTHVIYAGDRSLEFAERLNGVSYEEIARKGGGIISTVNATRHVSEDELFDVTARRVRRMIAEGTTTLEMKSGYGLTLQDELKQLRVARAIGTALPVRVHATFLGAHALPSEFKDRQDDYVSHLITDILPQAVEEKLIDSIDGFCENIAFTPDQIERLFIAANDLKIPVRLHSEQLSNSGGTKLAARYGALSTDHLEYVVEDDVIDLAHAGTVAMLLPGAFYFIRETRMPPVDLFRKHNVPMGLAT... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
Q9KBE4 | MVQHFDTLLVNIGQLLPMESKGPKRGKEMSELQLLEHAALGIRDGKVAFIGTMVEADTFTANQMIDCQGKLVTPGLVDPHTHLIFGGSREHEMALKQQGVPYLEILKNGGGILATVEATRAASEEELITKAICHLNRMLSYGVTTIEAKSGYGLDRETEWKQLRAAKAVGEQHPIDIVSTFLGAHAIPTSHRNDPDRFLDEMADMLGEIKEQNLAEFVDIFTETGVFTVEQSRTFLQKAKERGFGLKLHADEIDPLGGAELAGELGAISADHLVGASDQGIQKMAAAGTIACLLPGTTFYLGKDTYARARDMIDQGLAVT... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
Q5V1C1 | MTTLDAVVYGADELVAGPATDGRRLETYEDGAVAIVDGTVAAVGPTTEVTAEYPPESANHAVDADGQAVIPGFVDPHTHALFAGDRSDEFAAKLRGKSYQDILAEGGGILRTVRAVRDADEETLLSNLLAHLDTMLAHGTTTVEVKSGYGLDTETELQMLRVIDSADAVHPVDVVPTFMGAHAVPEGWDTDDYTAAVVDEQVPAVESQGIAEFCDVFCEEGVFSVAQSRRVLEAGAAAGLTPKVHAEELAHIGGTQLAADVGAASADHLLHATGEDIDALVDAAVTPVLLPGTAFGLGAAYADATAFRDRGAPVAVATDF... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
A9AW17 | MPHADQLITNIGRLVTGPQAPLRGQQLAQLTAIDQAVVAVQAGNIVALGSQAELSAWTADQTIDAGGYLAIPGFVDPHTHACYAGDRAHEFELRIKGASYSELMAAGGGIMSTVHATRAASKAELVAQTRPRLDQLLAHGTTTVEIKSGYGLDTATELTMLEAIAELAQTHPIGIVPTFMGAHAIPAEYRDNPEAFVDLVVDEMLPAVAAWWQQQTIWQEPLACDIFCENGAFSVAQSQRILVKAKALGFRLKLHVDEFEPLGGTPLAVELGAISVDHLVATPPEHIAILANSETVGVSLPGTPFGLGKSQFSPARSLIE... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
Q96NU7 | MASGHSLLLENAQQVVLVCARGERFLARDALRSLAVLEGASLVVGKDGFIKAIGPADVIQRQFSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMKLAGATYMEIHQAGGGIHFTVERTRQATEEELFRSLQQRLQCMMRAGTTLVECKSGYGLDLETELKMLRVIERARRELDIGISATYCGAHSVPKGKTATEAADDIINNHLPKLKELGRNGEIHVDNIDVFCEKGVFDLDSTRRILQRGKDIGLQINFHGDELHPMKAAELGAELGAQAISHLEEVSDEGIVAMATARCSAILLPTTAYMLRLKQPRAR... | Cofactor: Binds 1 zinc or iron ion per subunit.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate
Sequence Mass (Da): 46743
Sequence Length: 426
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
EC: 3.5.2.7
|
P31269 | MATTGALGNYYVDSFLLGADAADELSVGRYAPGTLGQPPRQAATLAEHPDFSPCSFQSKATVFGASWNPVHAAGANAVPAAVYHHHHHHPYVHPQAPVAAAAPDGRYMRSWLEPTPGALSFAGLPSSRPYGIKPEPLSARRGDCPTLDTHTLSLTDYACGSPPVDREKQPSEGAFSENNAENESGGDKPPIDPNNPAANWLHARSTRKKRCPYTKHQTLELEKEFLFNMYLTRDRRYEVARLLNLTERQVKIWFQNRRMKMKKINKDRAKDE | Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation.
PTM: Methylated on Arg-1... |
P09631 | MATTGALGNYYVDSFLLGADAADELGAGRYAPGTLGQPPRQAAALAEHPDFSPCSFQSKAAVFGASWNPVHAAGANAVPAAVYHHHHHPYVHPQAPVAAAAPDGRYMRSWLEPTPGALSFAGLPSSRPYGIKPEPLSARRGDCPTLDTHTLSLTDYACGSPPVDREKQPSEGAFSENNAENESGGDKPPIDPNNPAANWLHARSTRKKRCPYTKHQTLELEKEFLFNMYLTRDRRYEVARLLNLTERQVKIWFQNRRMKMKKINKDRAKDE | Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation (By similarity).
PTM: Met... |
P0AEW0 | MTDVLLCVGNSMMGDDGAGPLLAEKCAAAPKGNWVVIDGGSAPENDIVAIRELRPTRLLIVDATDMGLNPGEIRIIDPDDIAEMFMMTTHNMPLNYLIDQLKEDIGEVIFLGIQPDIVGFYYPMTQPIKDAVETVYQRLEGWEGNGGFAQLAVEEE | Function: Protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3.
Catalytic Activity: This enzyme specifically removes a 32-amino acid peptide from the C-terminus of the precursor of the large subunit of E.coli hydrogenase 3 by cleavage at the C-terminal side of Arg-537.
Sequence Mas... |
E7FI44 | MKNLYLPITIDHIARVEGKGGVEIIIGDDGVKEVKLNIIEGPRFFEAITIGKKLEEALAIYPRICSFCSAAHKLTALEAAEKAVGFVPREEIQALREVLYIGDMIESHALHLYLLVLPDYRGYSSPLKMVNEYKREIEIALKLKNLGTWMMDILGSRAIHQENAVLGGFGKLPEKSVLEKMKAELREALPLAEYTFELFAKLEQYSEVEGPITHLAVKPRGDAYGIYGDYIKASDGEEFPSEKYRDYIKEFVVEHSFAKHSHYKGRPFMVGAISRVINNADLLYGKAKELYEANKDLLKGTNPFANNLAQALEIVYFIER... | Cofactor: Binds 1 nickel ion per heterotetramer.
Function: Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The alpha and delta subunits... |
Q8U2E5 | MRYVKLPKENTYEFLERLKDWGKLYAPVKISDKFYDFREIDDVRKIEFHYNRTIMPPKKFFFKPREKLFEFDISKPEYREVIEEVEPFIIFGVHACDIYGLKILDTVYLDEFPDKYYKVRREKGIIIGISCMPDEYCFCNLRETDFADDGFDLFFHELPDGWLVRVGTPTGHRLVDKNIKLFEEVTDKDICAFRDFEKRRQQAFKYHEDWGNLRYLLELEMEHPMWDEEADKCLACGICNTTCPTCRCYEVQDIVNLDGVTGYRERRWDSCQFRSHGLVAGGHNFRPTKKDRFRNRYLCKNAYNEKLGLSYCVGCGRCTA... | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The beta and gamma subunits form the sul... |
Q8QHJ9 | MAGSRRLAHFFMASCLFLCYTASVNGGKRGNSDKCSYKQGTQTSSMDEGARKLGVTFRYDNCSVNWSPLGKHAIHEVNNISFSHLSCDSQAAVVVHWMASPLGIEHVKGFRVYLEDKNPERKQCQHLILKDPRQLNFSYKTIRMSSQPFSSLAFETDYMVRIVPFPTFLNDSFFPPSFLRTNSCEVLLGPDNLVCKPFWKPKMLNVSQLGSNLHVVFDHAPSTFGFSIYYLYYKLRQEGPFRLKRCKPEQNGPKTTCVLQDVTPGTYAIELRDDSNNTRRQTQYHVSQVHSPWAGPIRAMAITVPLVIMSAFATLFTVMC... | Function: Feedback inhibitor of fibroblast growth factor mediated Ras-MAPK signaling and ERK activation. May inhibit FGF-induced FGFR1 tyrosine phosphorylation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 83391
Sequence Length: 745
Subcellular Location: Membrane
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Q8NFM7 | MAPWLQLCSVFFTVNACLNGSQLAVAAGGSGRARGADTCGWRGVGPASRNSGLYNITFKYDNCTTYLNPVGKHVIADAQNITISQYACHDQVAVTILWSPGALGIEFLKGFRVILEELKSEGRQCQQLILKDPKQLNSSFKRTGMESQPFLNMKFETDYFVKVVPFPSIKNESNYHPFFFRTRACDLLLQPDNLACKPFWKPRNLNISQHGSDMQVSFDHAPHNFGFRFFYLHYKLKHEGPFKRKTCKQEQTTETTSCLLQNVSPGDYIIELVDDTNTTRKVMHYALKPVHSPWAGPIRAVAITVPLVVISAFATLFTVM... | Function: Feedback inhibitor of fibroblast growth factor mediated Ras-MAPK signaling and ERK activation . Regulates the nuclear ERK signaling pathway by spatially blocking nuclear translocation of activated ERK without inhibiting cytoplasmic phosphorylation of ERK . Mediates JNK activation and may be involved in apopto... |
Q8NFR9 | MGSSRLAALLLPLLLIVIDLSDSAGIGFRHLPHWNTRCPLASHTDDSFTGSSAYIPCRTWWALFSTKPWCVRVWHCSRCLCQHLLSGGSGLQRGLFHLLVQKSKKSSTFKFYRRHKMPAPAQRKLLPRRHLSEKSHHISIPSPDISHKGLRSKRTQPSDPETWESLPRLDSQRHGGPEFSFDLLPEARAIRVTISSGPEVSVRLCHQWALECEELSSPYDVQKIVSGGHTVELPYEFLLPCLCIEASYLQEDTVRRKKCPFQSWPEAYGSDFWKSVHFTDYSQHTQMVMALTLRCPLKLEAALCQRHDWHTLCKDLPNAT... | Function: Specific functional receptor for IL17C. May be signaling through the NF-kappa-B and MAPK pathways. May require TRAF3IP2 /ACT1 for signaling. May be a crucial regulator in innate immunity to bacterial pathogens. Isoform 2 and isoform 4 may be either cytoplasmic inactive or dominant active forms. Isoform 3 and ... |
Q8BH06 | MGSPRLAALLLSLPLLLIGLAVSARVACPCLRSWTSHCLLAYRVDKRFAGLQWGWFPLLVRKSKSPPKFEDYWRHRTPASFQRKLLGSPSLSEESHRISIPSSAISHRGQRTKRAQPSAAEGREHLPEAGSQKCGGPEFSFDLLPEVQAVRVTIPAGPKASVRLCYQWALECEDLSSPFDTQKIVSGGHTVDLPYEFLLPCMCIEASYLQEDTVRRKKCPFQSWPEAYGSDFWQSIRFTDYSQHNQMVMALTLRCPLKLEASLCWRQDPLTPCETLPNATAQESEGWYILENVDLHPQLCFKFSFENSSHVECPHQSGSL... | Function: Specific functional receptor for IL17C, signaling through the NF-kappa-B and MAPK pathways. Requires TRAF3IP2 /ACT1 for signaling. Crucial regulator in innate immunity to bacterial pathogens, such as Citrobacter rodentium. Isoform 4 and isoform 5 may be either cytoplasmic inactive or dominant active forms. Is... |
O95998 | MTMRHNWTPDLSPLWVLLLCAHVVTLLVRATPVSQTTTAATASVRSTKDPCPSQPPVFPAAKQCPALEVTWPEVEVPLNGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLWEGSTSRERGSTGTQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHVVLAQLWAGLRATLPPTQEALPSSHSSPQQQG | Function: Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response.
PTM: N- and O-glycosylated. O-glycosylated with core 1-like and core 2-like glycans. O-glycan heterogeneity at Ser-53: HexHexNAc (major) and Hex2HexNAc2 (minor). N-glycan heterogeneity at Asn-103:... |
O95256 | MLCLGWIFLWLVAGERIKGFNISGCSTKKLLWTYSTRSEEEFVLFCDLPEPQKSHFCHRNRLSPKQVPEHLPFMGSNDLSDVQWYQQPSNGDPLEDIRKSYPHIIQDKCTLHFLTPGVNNSGSYICRPKMIKSPYDVACCVKMILEVKPQTNASCEYSASHKQDLLLGSTGSISCPSLSCQSDAQSPAVTWYKNGKLLSVERSNRIVVDEVYDYHQGTYVCDYTQSDTVSSWTVRAVVQVRTIVGDTKLKPDILDPVEDTLEVELGKPLTISCKARFGFERVFNPVIKWYIKDSDLEWEVSVPEAKSIKSTLKDEIIERN... | Function: Within the IL18 receptor complex, does not mediate IL18-binding, but involved in IL18-dependent signal transduction, leading to NF-kappa-B and JNK activation . May play a role in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells (Probable).
PTM: N-glycosylated.
Location Topology: Single-pass type I mem... |
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