ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P93834 | MGKVAVATTVVCSVAVCAAAALIVRRRMKSAGKWARVIEILKAFEEDCATPIAKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGDETGFFYALDLGGTNFRVMRVLLGGKHDRVVKREFKEESIPPHLMTGKSHELFDFIVDVLAKFVATEGEDFHLPPGRQRELGFTFSFPVKQLSLSSGTLINWTKGFSIDDTVDKDVVGELVKAMERVGLDMLVAALVNDTIGTLAGGRYTNPDVVVAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHSLDVDSLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDIVPPKLKIPFIIRTPNMSAMHSDTSPDLKVVGSKLKDILEVQTSSLKMRKVVISLCNIIASRGARLSAAGIYGILKKIGRDATKDGEAQKSVIAMDGGLFEHYTQFSESMKSSLKELLGDEVSESVEVILSNDGSGVGAALLAASHSQYLELEDDSETS | Function: Fructose and glucose phosphorylating enzyme . May be involved in the phosphorylation of glucose during the export from mitochondrion to cytosol . Acts as sugar sensor which may regulate sugar-dependent gene repression or activation . Mediates the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism . May regulate the execution of program cell death in plant cells .
Catalytic Activity: ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54490
Sequence Length: 502
Pathway: Carbohydrate metabolism; hexose metabolism.
Subcellular Location: Mitochondrion outer membrane
EC: 2.7.1.1
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P35588 | MLKFVILVCSVACVFGAVVPGGMLPQLDGRIVGGFEADIEDFPWQVSIQRGGYHFCGGSIYSPEIIVTAAHCLEKIDASQLRVRVGGSYWDEEGSLLTVSNFKIHEKYDAMIMWYDVALLKLSSKLTYGATVKNIELAKETPPDNADAVVSGWGTIYENYPYMPVQLRSVDVKIVSREVCRSDEYGYGNAIGPTMICAYAVGKDACQGDSGGPLVVGEALVGVVSWGEGCAYPGFPGVYTDVSVVRSWITENAKSF | Function: Protease that shows preferential cleavage after Arg and Lys residues.
Sequence Mass (Da): 27711
Sequence Length: 256
Subcellular Location: Secreted
EC: 3.4.21.-
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B8NI03 | MEDLRDLSPRDLHKARGAKEEFKNVFLLADGELTVHASFSRIFTRRTNKMGTEYVAVLTGSFLTGAMMNLHLLTIPILIETTRQPAQLVHQWSRIFYSGHRKGPGIALVTGALYGYAAWAKYSVGEPWHHWMVAGVTTVSMVPYTWMFMNATNTALFHAEDQFEKGGVEISLQESVRLVGKWDWLNTVRALFPLAGSVMGMLGVCGVVRY | Function: Monooxygenase that converts norsolorinic acid anthrone to norsolorinic acid during aflatoxin biosynthesis.
Catalytic Activity: noranthrone + O2 = H2O + norsolorinic acid
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23567
Sequence Length: 210
Pathway: Mycotoxin biosynthesis; aflatoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.13.12.20
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M2WJF5 | MLRAATNLYSPPNTGKMSPKTIGSDVGIEVIPVMTGTFLSGAMMSLFLLTIPVILETTTVPSQLLNQWHRIFYRGHIQGPLISIATGLLYSYAAYQRSQRGAAWKPFAVSAAVTVAMIPFTWVFMANVNNSLFRAVAVTEKGGEGNWNEAQGLVRSWGAWNAVRALFPLSGAVLGLLSTCKIVSF | Function: Monooxygenase; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B . The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA . PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin . The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) . The next step is performed by adhA that transforms HAVN to averufin (AVF) . Averufin might then be converted to hydroxyversicolorone by cypX and avfA . Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY . VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) . Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring . Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) . DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA . Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step . It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step . Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA . However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis . Alternatively, opening of the epoxide ring could be achieved non-enzymatically . The next step is the deoxygenation of ring A to yield the 5,8-dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 . The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran . OrdB and norB might have oxidative roles here . An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20026
Sequence Length: 185
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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C7DQY0 | MMFRLTSVSCFLLVIACLNLFQVVLTSRCFPPGIYCTPYLPCCWGICCGTCRNDNSSLTFLQFCLPFFFFLRPSHPLFLLLPAR | Function: Inhibits the vertebrate voltage-gated potassium channels Kv1.1/KCNA1 and Kv1.3/KCNA3.
Sequence Mass (Da): 9627
Sequence Length: 84
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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A0A125S9E1 | MFRVTSVLLVIVLLNLVVLTNACHMDCSKMTCCSGICCFYCGRPMCPGTRRALLQRLVGHQR | Function: Probable neurotoxin.
Sequence Mass (Da): 6933
Sequence Length: 62
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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P0C615 | CRTEGMSCEENQQCCWRSCCRGECEAPCRFGP | Function: Kappa-conotoxins bind and inhibit voltage-gated potassium channels. This toxin inhibits Kv1.2/KCNA2 and Kv1.6/KCNA6. Produces stiffening of body, limbs and tail when injected intracranially into mice.
Sequence Mass (Da): 3660
Sequence Length: 32
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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Q8LAL2 | MEGCPRNREIGPKLLDLIPQGRKWYQEDKNNTDQEKKLELRLGPPGGDEEDHSAIKKKNTEIRNIKKETEDKSFHCFNGNHFSPSNKTTSVPHISQKRTAPGPVVGWPPVRSFRKNLASTSSSKLGNESSHGGQINKSDDGEKQVETKKEGMFVKINMDGVPIGRKVDLNAYNSYEQLSFVVDKLFRGLLAAQRDISDGQGEEKPIIGLLDGKGEFTLTYEDNEGDKMLVGDVPWQMFVSSVKRLRVIKSSEISSALTFGCSKQEKMMH | Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Sequence Mass (Da): 30124
Sequence Length: 269
Domain: The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
Subcellular Location: Nucleus
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Q9ZSY8 | MSVSVAAEHDYIGLSEFPTMEATTMSDKTKTRDNNNGLNFKATELRLGLPGSESPERVDSRFLALNKSSCPVSGAKRVFSDAINDSNKWVFSPGSTTATGDVGSGSGPRTSVVKDGKSTTFTKPAVPVKEKKSSATAPASKAQVVGWPPIRSFRKNSMASSQSQKPGNNSETEEAEAKSGPEQPCLYVKVSMEGAPYLRKIDLKTYKSYLELSSALEKMFSCFTIGQFGSHGGCGRDGLNESRLTDLLRGSEYVVTYEDKDSDWMLVGDVPWEMFICSCKKLRIMKSSEAIGLAPRVMEKCRSRN | Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Sequence Mass (Da): 33196
Sequence Length: 305
Domain: The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
Subcellular Location: Nucleus
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Q9XFM0 | MEEEKRLELRLAPPCHQFTSNNNINGSKQKSSTKETSFLSNNRVEVAPVVGWPPVRSSRRNLTAQLKEEMKKKESDEEKELYVKINMEGVPIGRKVNLSAYNNYQQLSHAVDQLFSKKDSWDLNRQYTLVYEDTEGDKVLVGDVPWEMFVSTVKRLHVLKTSHAFSLSPRKHGKE | Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Sequence Mass (Da): 20206
Sequence Length: 175
Domain: The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
Subcellular Location: Nucleus
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Q93WC4 | MELDLGLSLSPHKSSKLGFNFDLNKHCAIEGAASCLGTEKLRFEATFGLGNVEENCYMPKQRLFALNGQPNEEDEDPLESESSIVYDDEEENSEVVGWPPVKTCMIKYGSYHHRHIRNHHHCPYHHRGRRITAMNNNISNPTTATVGSSSSSSISSRSSMYVKVKMDGVAIARKVDIKLFNSYESLTNSLITMFTEYEDCDREDTNYTFTFQGKEGDWLLRGDVTWKIFAESVHRISIIRDRPCAYTRCLF | Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Sequence Mass (Da): 28610
Sequence Length: 251
Domain: The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
Subcellular Location: Nucleus
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P49678 | MAYEKVNELNLKDTELCLGLPGRTEKIKEEQEVSCVKSNNKRLFEETRDEEESTPPTKTQIVGWPPVRSSRKNNNSVSYVKVSMDGAPYLRKIDLKTYKNYPELLKALENMFKVMIGEYCEREGYKGSGFVPTYEDKDGDWMLVGDVPWDMFSSSCKRLRIMKGSDAPALDSSL | Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Sequence Mass (Da): 19910
Sequence Length: 174
Domain: The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
Subcellular Location: Nucleus
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P13691 | MGAMWMKSMLLVLLLCMLMVTPMTGARSDNSGPWMWCDPEMGHKVSPLTRCRALVKLECVGNRVPEDVLRDCCQEVANISNEWCRCGDLGSMLRSVYAALGVGGGPEEVFPGCQKDVMKLLVAGVPALCNVPIPNEAAGTRGVCYWSASTDT | Function: Could be involved in insect defense mechanisms. Inhibits insect-type alpha-amylase.
PTM: Five disulfide bonds, which are essential for the inhibitor activity, are probably present.
Sequence Mass (Da): 16429
Sequence Length: 152
Subcellular Location: Secreted
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P01083 | MWMKTVFWGLLVFMLVATTMAVEYGARSHNSGPWSWCNPATGYKVSALTGCRAMVKLQCVGSQVPEAVLRDCCQQLADINNEWCRCGDLSSMLRSVYQELGVREGKEVLPGCRKEVMKLTAASVPEVCKVPIPNPSGDRAGVCYGDWAAYPDV | Function: Alpha-amylase inhibitor.
PTM: The disulfide bonds are essential for the inhibitor activity.
Sequence Mass (Da): 16800
Sequence Length: 153
Subcellular Location: Secreted
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Q8H174 | MEVSNSCSSFSSSSVDSTKPSPSESSVNLSLSLTFPSTSPQREARQDWPPIKSRLRDTLKGRRLLRRGDDTSLFVKVYMEGVPIGRKLDLCVFSGYESLLENLSHMFDTSIICGNRDRKHHVLTYEDKDGDWMMVGDIPWDMFLETVRRLKITRPERY | Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Sequence Mass (Da): 18155
Sequence Length: 158
Domain: The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
Subcellular Location: Nucleus
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P10997 | MGILKLQVFLIVLSVALNHLKATPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGKRNAVEVLKREPLNYLPL | Function: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
PTM: Amyloid fibrils are degraded by IDE.
Sequence Mass (Da): 9806
Sequence Length: 89
Domain: The mature protein is largely unstructured in the absence of a cognate ligand, and has a strong tendency to form fibrillar aggregates. Homodimerization may be the first step of amyloid formation.
Subcellular Location: Secreted
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Q07333 | TQRLANFLIHSSNNFGAIFSPPN | Function: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Sequence Mass (Da): 2546
Sequence Length: 23
Domain: The mature protein is largely unstructured in the absence of a cognate ligand.
Subcellular Location: Secreted
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P12968 | MMCISKLPAVLLILSVALNHLRATPVRSGSNPQMDKRKCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTYGKRNAAGDPNRESLDFLLV | Function: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Sequence Mass (Da): 10022
Sequence Length: 93
Domain: The mature protein is largely unstructured in the absence of a cognate ligand, but contrary to the human protein, it does not easily form fibrillar aggregates.
Subcellular Location: Secreted
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Q29119 | NMATCATQHLANFLDRSRNNLGTIFSPTKVGS | Function: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Sequence Mass (Da): 3466
Sequence Length: 32
Domain: The mature protein is largely unstructured in the absence of a cognate ligand.
Subcellular Location: Secreted
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Q07334 | MCILKLPIVLLVLSVAVNHLQASPVESHQVEKRKCNTVTCATQRLANFLIHSSNNFGAIFSPPSVGS | Function: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Sequence Mass (Da): 7230
Sequence Length: 67
Domain: The mature protein is largely unstructured in the absence of a cognate ligand, and has a strong tendency to form fibrillar aggregates.
Subcellular Location: Secreted
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Q28934 | NTATCSMHRLADFLGRSSNNFGAILSPTNVGS | Function: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Sequence Mass (Da): 3340
Sequence Length: 32
Domain: The mature protein is largely unstructured in the absence of a cognate ligand.
Subcellular Location: Secreted
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A7ZTP0 | MRNFDLSPLMRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLEIQLEGTRLSVKGTPEQPKEEKKWLHQGLMNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEPIAAQRIAISERPALNS | Function: Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.
Sequence Mass (Da): 16093
Sequence Length: 142
Domain: The N- and C-terminal flexible termini are involved in oligomerization and in the binding of non-native substrate proteins, and are essential for chaperone activity.
Subcellular Location: Cytoplasm
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Q6TYB1 | MKPFKLIFISALMILIMTNATPISHLNAQANEENKKLKYEKNSALALNYHRVRKKDPLNDFISLLSGSKEIKNYSVTDQEFKSQIQWLKAHDAKFLTLKEFIKYKEKGKFPKRSVWINFDDMDQTIYDNAFPVLKKYHIPATGFLITNHIGSTNFHNLNLLSKKQLDEMYETGLWDFESHTHDLHALKKGNKSKFLDSSQSVASKDIKKSEHYLNKNYPKNERALAYPYGLINDDKIKAMKKNGIQYGFTLQEKAVTPDADNYRIPRILVSNDAFETLIKEWDGFDEEK | Function: Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. In fact, the IcaB deacetylase converts 15 to 20% of the GlcNAc residues of PNAG to glucosamine. N-deacetylation is crucial for attachment of the polysaccharide to the bacterial cell surface; it leads to the introduction of positive charges in the otherwise neutral PIA polymer, allowing electrostatic interactions. Deacetylation of the polymer is also essential for key virulence mechanisms of S.epidermidis, namely biofilm formation, colonization, and resistance to neutrophil phagocytosis and human antibacterial peptides.
Sequence Mass (Da): 33636
Sequence Length: 289
Subcellular Location: Secreted
EC: 3.5.1.-
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Q9RQP6 | MKKIRLELVYLRAIICAIIIITHLLTQITLKHENMEGGSLVLQFYIRNIVIFGTPCFIILSQLLTTLNYQKVTYRYLTTRVKYILIPYILMGLFYSYSESLLTDSSFNKQFIENVLLGQWYGYFIVVIMQFFILSYIIFKINYNLFNSKILLLLSFILQQSFLYYFTNNTAFHDTVLHYYPLSENTIIFGWIFYFFLGAYMGYNYERVLNFLERYLVIMIVLAVATYFVFIALANGDYWNVTSFSYSLTPYNSIMFIVILGICTHFKTMLFNTIQMISAFSFFIYLLHPIILDSLFAYTNIFEDNTMVFLAISLLFILGLCIGVGMILREFYIFRFIIGKQPYKLNINAY | Function: Presumably involved in the export of the biofilm adhesin polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA) across the cell membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41344
Sequence Length: 350
Subcellular Location: Cell membrane
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Q9RQP8 | MVKPRQREYPTLKSSLNIVRETALIAISCVFWIYCLVVLLVYIGTIFEIHDESINTIRVALNIENTEILDIFETMGIFAIIIFVFFTISILIQKWQRGRES | Function: Necessary for the synthesis of poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. Is required for full IcaA N-acetylglucosaminyltransferase activity (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11783
Sequence Length: 101
Subcellular Location: Cell membrane
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W4VRY9 | MNTMITFLVLFVLTAANGAPEANERKIPEAIHNEDQSLAEMAEELMFFLQQTEFEAPLLQEEEEAEXAEXRNSRERRCAMGDVPCTKGKTNCCKGYECKPKSPAWWYDTDFCQSIHSGRPIGI | Function: Ion channel inhibitor.
Sequence Mass (Da): 13958
Sequence Length: 123
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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W4VS12 | MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAAMSLLQQLEAIESTLLEKEADRNSRQKRCLGENVPCGDFPCCGKLVCQKTFGYGWLYKSPYCVKPSNG | Function: Ion channel inhibitor.
Sequence Mass (Da): 12891
Sequence Length: 114
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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W4VSC0 | MKTLVLVAVLGLASLYLLSYASEVQQISRDEEDFRALMASFGGIFDTEERGVDKEGCRKMFGDCWGDGDCCLHLGCKTRKLPPWTDKPYCAWDWTFGRK | Function: Ion channel inhibitor.
Sequence Mass (Da): 11235
Sequence Length: 99
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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W4VRV3 | MKTMIAWLVLLTFAAALCFADEGLKQEHMNERKKSRFREDIPDEISEDLLLQEMEAMEAELLEKEMRMEENRNSREKRCLGEDISCGEKPGDLVRMPCCAKYECKETAGYWWYQKRFCVKKKSG | Function: Ion channel inhibitor.
Sequence Mass (Da): 14626
Sequence Length: 124
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P13199 | MEDIIEGGISSDDDFDSSDSSSDEEESDTSPQIMKSDVTMASPPSTPEPSPDVSASTSNLKRERQRSPITWEHQSPLSRVYRSPSPMRFGKRPRISSNSTSRSCKTSWADRVREAAAQRRPSRPFRKPYSHPRNGPLRNGPPRAPPLLKLFDISILPKSGEPKLFLPVPSLPCQEAEKTNDKYVLAMAQRAMHDVPISSKQLTANLLPVKFKPLLSIVRYTPNYYYWVSMRKETIASANLCTVAAFLDESLCWGQQYLKNDFIFSENGKDIILDTSSALLSQLVHKIKMLPFCHCLMQTTPQDHIVKQVCYLIASNNRILDAVRYLQTSVIKSPIVLLLAYAVCLPAAIICTKNETQLYSHCMRILKEYRPGDVMNILHESLTQHLNKCPSSTCAYTTRAIVGTKANTTGLFFLPTQ | Function: Probably acts as a viral splicing factor that regulates viral RNA splicing. Functions as a multifunctional regulator of the expression of viral lytic genes (By similarity). Early protein that promotes the accumulation and nuclear export of viral intronless RNA transcripts by interacting with mRNAs and cellular export proteins.
Sequence Mass (Da): 46816
Sequence Length: 417
Domain: Binds viral intronless RNAs; the RNA binding site overlaps partially with the binding site for host ALYREF or ALYREF2.
Subcellular Location: Host cytoplasm
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Q85232 | MEDSGNSSGSEASRSGSEERRPVRERLGSRPPERRPVRARLGAIRRRRGGRGGRAARQALRQRRRQQQQQQRQQQHQRRRQEADRPDGGPDAPPDRLSESARAAVSATHARVGATRVNELFASARHDLSRPVFNDGFRAAGSSPWAAVLEFGAEQFTPDGRRVTWETLMFHGADLHRLFEVRPHATEAARVLREMVLLNEGLTESLASADETLTWVKLILTKGLTLRTLDPIVATAGAVLQNLRLKLGPFLRCYLRDTPVDELVRRRRLRDVRCIVTYTLVMLARIARVVERGSSCVLPEDLGDSPVPLEEYVPGACLGGIMDALDSHKTGCDAPTCRLTCSYTLVPVYMHGKYFYCNHLF | Function: Multifunctional regulator of the expression of viral genes that mediates nuclear export of viral intronless mRNAs. This immediate early (EI) protein promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP (By similarity).
Sequence Mass (Da): 40451
Sequence Length: 361
Domain: Binds viral intronless RNAs and SR proteins through the Arg-rich region.
Subcellular Location: Host cytoplasm
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P09269 | MASASIPTDPDVSTICEDFMNLLPDEPSDDFALEVTDWANDEAIGSTPGEDSTTSRTVYVERTADTAYNPRYSKRRHGRRESYHHNRPKTLVVVLPDSNHHGGRDVETGYARIERGHRRSSRSYNTQSSRKHRDRSLSNRRRRPTTPPAMTTGERNDQTHDESYRLRFSKRDARRERIRKEYDIPVDRITGRAIEVVSTAGASVTIDSVRHLDETIEKLVVRYATIQEGDSWASGGCFPGIKQNTSWPELMLYGHELYRTFESYKMDSRIARALRERVIRGESLIEALESADELLTWIKMLAAKNLPIYTNNPIVATSKSLLENLKLKLGPFVRCLLLNRDNDLGSRTLPELLRQQRFSDITCITTYMFVMIARIANIVVRGSKFVEYDDISCNVQVLQEYTPGSCLAGVLEALITHQRECGRVECTLSTWAGHLSDARPYGKYFKCSTFNC | Function: Multifunctional regulator of the expression of viral genes that mediates nuclear export of viral intronless mRNAs. This immediate early (EI) protein promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP (By similarity).
PTM: Phosphorylated in vitro by SRPK1.
Sequence Mass (Da): 51543
Sequence Length: 452
Domain: Binds viral intronless RNAs and SR proteins through the Arg-rich region.
Subcellular Location: Host cytoplasm
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Q4GZL2 | MKQFIFFALLCTSTYAAIHILTEKEDHATLHISFNDLIKIQLRTNPSTGYAWNIEYPTDTFSLSQDTIKAEPHPSGMVGFPSIREIQLKPLKVGTTTIKLGYSRPWEKGKEPLRSLTYSVVIR | Function: Cysteine protease inhibitor . Inhibits cysteine proteases CP1, CP2 and to a lesser extent CP5 .
Sequence Mass (Da): 14000
Sequence Length: 123
Domain: The BC, DE and FG loops form a tripartite wedge that blocks the substrate-binding site of target cysteine proteases . The BC loop interacts with the catalytically active cysteine and histidine residues of the protease catalytic center (Probable).
Subcellular Location: Cytoplasmic vesicle
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P08353 | MARRRRHRGPRRPRPPGPTGAVPTAQSQVTSTPNSEPAVRSAPAAAPPPPPASGPPPSCSLLLRQWLHVPESASDDDDDDDWPDSPPPEPAPEARPTAAAPRPRSPPPGAGPGGGANPSHPPSRPFRLPPRLALRLRVTAEHLARLRLRRAGGEGAPEPPATPATPATPATPATPATPATPATPATPATPARVRFSPHVRVRHLVVWASAARLARRGSWARERADRARFRRRVAEAEAVIGPCLGPEARARALARGAGPANSV | Function: Inhibits the establishment of the immune response and of the integrated stress response (ISR) in the infected cell . Plays essential roles in viral nuclear egress to mediate capsid transit across the nuclear membrane (By similarity). Facilitates nuclear egress cooperatively with host C1QBP and protein kinase C/PKC to induce lamin A/C phosphorylation and subsequent reorganization (By similarity). In turn, lamina disassembles and nuclear egress occurs (By similarity). Recruits the serine/threonine protein phosphatase PPP1CA/PP1-alpha to dephosphorylate the translation initiation factor EIF2S1/eIF-2alpha, thereby couteracting the host shutoff of protein synthesis involving double-stranded RNA-dependent protein kinase EIF2AK2/PKR . In turn, controls host IRF3 activation and subsequently inhibits host interferon response (By similarity). Controls the DNA sensing pathway by interacting with and inhibiting host STING/TMEM173 (By similarity). Also down-modulates the host MHC class II proteins cell surface expression . Acts as a neurovirulence factor that has a profound effect on the growth of the virus in central nervous system tissue, by interacting with host BECN1 and thereby antagonizing the host autophagy response (By similarity).
Sequence Mass (Da): 27533
Sequence Length: 263
Domain: The triplet repeats region may play a role in modulating virus egress.
Subcellular Location: Host cytoplasm
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Q7TLC4 | MSSLYLAEVDAFLQSPRTRHRTCADLRRELDAYADEERREAAKAIAHPDRPLLAPPSAPPDRSRPAPRGTAHPPAASP | Function: Plays a role in the inhibition of host immune response. Binds specifically to transporters associated with antigen processing (TAP), thereby blocking peptide-binding and translocation by TAP as well as subsequent loading of peptides onto MHC class I molecules. Empty MHC I molecules are retained in the endoplasmic reticulum and ultimately directed to proteasomal degradation. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes.
Sequence Mass (Da): 8567
Sequence Length: 78
Domain: The N-terminal active domain blocks peptide binding to and peptide transport by TAP.
Subcellular Location: Host cytoplasm
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P03170 | MSWALEMADTFLDTMRVGPRTYADVRDEINKRGREDREAARTAVHDPERPLLRSPGLLPEIAPNASLGVAHRRTGGTVTDSPRNPVTR | Function: Plays a role in the inhibition of host immune response. Binds specifically to transporters associated with antigen processing (TAP), thereby blocking peptide-binding and translocation by TAP as well as subsequent loading of peptides onto MHC class I molecules. Empty MHC I molecules are retained in the endoplasmic reticulum and ultimately directed to proteasomal degradation. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes.
Sequence Mass (Da): 9793
Sequence Length: 88
Domain: The N-terminal active domain blocks peptide binding to and peptide transport by TAP.
Subcellular Location: Host cytoplasm
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P14345 | MSWALKTTDMFLDSSRCTHRTYGDVCAEIHKREREDREAARTAVTDPELPLLCPPDVRSDPASRNPTQQTRGCARSNERQDRVLAP | Function: Plays a role in the inhibition of host immune response. Binds specifically to transporters associated with antigen processing (TAP), thereby blocking peptide-binding and translocation by TAP as well as subsequent loading of peptides onto MHC class I molecules. Empty MHC I molecules are retained in the endoplasmic reticulum and ultimately directed to proteasomal degradation. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes.
Sequence Mass (Da): 9785
Sequence Length: 86
Domain: The N-terminal active domain blocks peptide binding to and peptide transport by TAP.
Subcellular Location: Host cytoplasm
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Q9W303 | MKLYALFSLLVGSLAIGQISAAGSHHLLCYYDGNSFVREGLSKLILTDLEPALQYCTHLVYGYAGINPSSNKLVSNNEKLDLDLGSSLFRQVTGLKRKYPALKVLLSVGGDKDTVDPENNKYLTLLESSNARIPFINSAHSLVKTYGFDGLDLGWQFPKNKPKKVHGSIGKFWKGFKKIFSGDHVVDEKAEEHKEAFTALVRELKNAFRPDGYILGLSVLPNVNSSLFFDVPAIINNLDYVNLHTYDFQTPERNNEVADFPAPIYELNERNPEFNVNYQVKYWTGNRAPAAKINVGIATYGRAWKLTKDSGLTGLPPVAEADGVAPAGTQTQIPGLLSWPEVCAKLPNPANQHLKGADGPLRKVGDPTKRFGSYAYRSADDSGENGVWVGYEDPDTAAIKAEYVKREGLGGIAVVDLSFDDFRGGCTGHDKFPILRQVKSKL | Function: Cooperates with insulin-like peptides to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex.
PTM: Glycosylated.
Sequence Mass (Da): 48604
Sequence Length: 442
Subcellular Location: Secreted
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Q8T0R7 | MMWIQKNPFLGLLLCSFLAFFQSTYAEVGKLVCFYDAQSFVREGPAQMSLAELEPALQFCNFLVYGYAGIDAVTYKIKSLDPSLTNDRQHYRHITALRKKYPHVRFLLSVGGDRDVNSEGVADSDKYLRLLEQSEHRKSFQASVLAELNNNGFDGIDLAWQFPKNRPKLQQGVFKRVWGSLRGWFSSSSVDEKSEEHREQFATLLEELQSDLRRGGQLLTVSMLPHVSAELFIDVPKVLSNVDFVNLGTYDFQTPERDPKVADLPTPLYAMYDRDPSHNVQYQVQYWMNQTSEISVHKLHVGVTSYGRAWNMTRNSGITGYPPIPAANGAAPPGRQTVTPGLLSWPEICDLLQQQPQDREVPHLRKVGDPTKRFGIYAYRAADDQGENGLWVGYEDPLTAAIKAGFVHAQGLGGVAFHDLSMDDFRGQCAGEKFPILRSIKFKL | Function: Probably required to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex (By similarity).
PTM: Glycosylated.
Sequence Mass (Da): 50108
Sequence Length: 444
Subcellular Location: Secreted
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Q2PQM6 | MRNKMIYFNFHLFVIIFANLQIFQVQAANIFCYYDTQRITDVNAAINYLEPALQFCNFLIYGYAGIDGETYQVKSLDYGLNYDIYQAITSLKLKHNRLKVLLSIGGDRDQTEDLAEDNKYLKLLENLSSRNAFINSIQSVIRTYGFDGLDMAWQFPKNPPKHEHSGFRKYLDKLMNLFRRSPVIDENSAFHKEQFVSLLTELRQSLNPMGAIMTMTVLPHVSAELFLDVKPIVNHVDFIILATFDYLTPYRDPTIAHYTAPIYAVSEHDPSHNINYDVQYWLNHTTATSKLVLGVPAYGRSWTMIKKSGITGHPPITAGGPGRAGHRTLTAGLLSWPEICVKIHQNKELEGDAARFRKVSDPTKRFGTYAYRSVDENNEYGIWVSYEEPKTAANKAEYAHARNLSGVALFDLSMDDVTGECGDGTYSILKSIHNAFKKFK | Function: Cooperates with insulin-like peptides to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex (By similarity).
PTM: Glycosylated.
Sequence Mass (Da): 50108
Sequence Length: 440
Subcellular Location: Secreted
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P86357 | VLLSVGGDADTESPEKKNLGGVSIVDLSMDDFRGLLT | Function: Cooperates with insulin-like peptides to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex (By similarity).
PTM: Glycosylated.
Sequence Mass (Da): 3849
Sequence Length: 37
Subcellular Location: Secreted
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O13302 | MFSLRTAQPAQSLFRAATNTYSTSLPRSAIAARSFATVQSDIFKPTKYGGKYTVTLIPGDGIGTEVAESVKTIFKADNVPIEWEQVDVSGLDAGNKHSEDLFKESIASLKRNKLGLKGILHTPVERSGHQSFNVALRQELDIYASIVLIKNIPGYKTRHDNVDLCIIRENTEGEYSGLEHQSVSGVVESLKIITRAKSERIAKFAFSFALANNRKKVTCIHKANIMKLADGLFRSTFHKVAESYPTLETNDMIVDNASMQAVARPQQFDVMVMPNLYGGILSNVGAALVGGPGIVPGCNMGRDVAVFEPGCRHVGLDIKGKDQANPTALILSGSMLLRHLGLDEHANRISKAVYDVIGEGVTRTRDMGGQASTHEFTRAVLDKMESAL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the citric acid cycle.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 42222
Sequence Length: 388
Subcellular Location: Mitochondrion
EC: 1.1.1.41
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O13285 | MIRASAIQRTAMLLRQLRGFSTSATLADKIKVKNPIVELDGDEMTRIIWQKIKDQLILPYLDVDLKYYDLGIESRDATDDQITIDAANAIKEYGVGVKCATITPDEARVKEFHLKKMWLSPNGTIRNILGGTVFRESIIIPCIPRLIPGWEKPIVIGRHAFGDQYKATDLVINEPGRLELRFTPASGGEAQTQKVYDYTGPGVGLAMYNTDESITGFAHASFKMALAKGLPLYMSTKNTILKKYDGRFKDIFQQIYEQDYAAEFEKQGLWYEHRLIDDMVAQMIKSKGGFVMALKNYDGDVQSDIVAQGFGSLGLMTSALMTPDGKAYEAEAAHGTVTRHYRQHQQGKETSTNSIASIFAWTRGLAQRGKLDETPDVVDFASKLEQATIDTVEVDRIMTKDLALAMGKTDRSAYVTTTEFLDAVADRLKK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Mitochondrial IDP1 may regulate flux through the tricarboxylic acid cycle and respiration. Its probably critical function is the production of NADPH.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 48009
Sequence Length: 430
Subcellular Location: Mitochondrion
EC: 1.1.1.42
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P41560 | MTNKIIIPTTGDKITFIDGKLSVPNNPIIPYIEGDGIGVDVTPPMLKVVNAAVAKAYGGDRKIEWLEVYAGEKATKMYDSETWLPEETLNILQEYKVSIKGPLTTPVGGGMSSLNVAIRQMLDLYVCQRPVQWFTGVPSPVKRPSEVDMVIFRENTEDIYAGIEYKAGSDKAKSVIKFLIEEMGASNIRFTENCGIGIKPVSKEGSQRLVRQAIQYAIDNNKDSVTLVHKGNIMKFTEGAFKDWGYELAIEEFGASLLHGGPWCSLKNPNTGKEIIIKDVIADAMLQQVLLRPAEYSVIATLNLNGDYLSDALAAQVGGIGIAPGANLGDEVAVFEATHGTAPKYAGKNKVNPGSVILSAEMMLRHMGWLEADLLLKGMSGAIQAKTVTYDFERLMDDATLVSCSAFGDCIIDHM | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 45145
Sequence Length: 415
EC: 1.1.1.42
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O94229 | MLRQGIAAQKKSFATLAAEQLLPKKYGGRYTVTLIPGDGVGKEVTDSVVKIFENENIPIDWETIDISGLENTENVQRAVESLKRNKVGLKGIWHTPADQTGHGSLNVALRKQLDIFANVALFKSIPGVKTRLNNIDMVIIRENTEGEYSGLEHESVPGVVESLKIMTRAKSERIARFAFDFALKNNRKSVCAVHKANIMKLGDGLFRNTVNEIGANEYPELDVKNIIVDNASMQAVAKPHQFDVLVTPNLYGSILGNIGSALIGGPGLVPGANFGREYAVFEPGSRHVGLDIKGQNVANPTAMILSSTLMLRHLGLNAYADRISKATYDVISEGKSTTRDIGGSASTSEFTNAVIEKLAKL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the citric acid cycle.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 39158
Sequence Length: 361
Subcellular Location: Mitochondrion
EC: 1.1.1.41
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B7G620 | MSSLSTLRILHSTAGRRWASYYGIYPKSAACSSSSVAIARFFSTAADRPPKHAMLSVENKVVAPPMVYIAGEEMTRYACDLVVKSWLEPYFDLSQWEYFDLSCVNRDNTNDQVLRDAVTAGQRIGAIFKEPTITPSAIQKKAFGLKNSLGSPNGAMRAGWNGITISRDTIHIDGIELGYKRPVFFERHAVGGEYGAGWSKVGRGTLLTTYLPSDGRDPFVVDKRDLTDQHNVVVTYHNPYDNVEPLAHLFFQRCLDANITPYVVTKKTVFKWQEGFWAVMKDVFDEHYKSRFEEKGLLQACGGDLQHLISDAATMQLIRWTDGGFGMAAHNYDGDMLTDQIAQVHRSPGFITSNLVGKAPDGSLIKEFEASHGTVSDLWNDHLAGKETSLNPLGLVEAIVGALQHAAVLDAEKNPDDEHKVKARDQIFNFTTTLRTAMHNTFRYGQGTRDMSGPSGYTTEDFVRKVAWRLQRYLDAQYDEAPPPQLGEPSRKLRRNYDIDEEAINGLFQKYDKNGDGFIDFEEFTRMLVKMNLAPLLTKKEKEKKPDV | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (By similarity). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production. No activity with NADP(+) .
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 61537
Sequence Length: 548
Domain: The C-terminal EF-hand domain is required for homodimerization.
Subcellular Location: Mitochondrion
EC: 1.1.1.41
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O13696 | MFKSLVRKSSAFQPLKYGGKYTVTLIPGDGIGRETSNAVTEIFKTANVPIEFEEIDVTGMEKNNKSSGDALHEAIQSLKRNKVGLKGILFTPFEKGGHTSFNVALRKELDIYASLVLIKNIPGFKTRHDNVDFAIIRENTEGEYSGLEHQSVPGVVESLKIITEYKSKRIAQFAFDFALQNGRKSVTCIHKANIMKLADGLFRRTFYDVANGYDAITPKDLIVDNASMQAVSRPQQFDVLVMPNLYGSILSNIGSALVGGPGVIPGANFGRDYALFEPGCRHVGLSITGRGEANPTAAILSACLMLRHLGLKDYADLINAATYSVIEEGKTLTKDLGGSASTGDFTHAILERMESL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 38758
Sequence Length: 356
Subcellular Location: Mitochondrion
EC: 1.1.1.41
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P28834 | MLNRTIAKRTLATAAQAERTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETINIKQTDHKEGVYEAVESLKRNKIGLKGLWHTPADQTGHGSLNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIVIRENTEGEFSGLEHESVPGVVESLKVMTRPKTERIARFAFDFAKKYNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPDIDVSSIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGAALIGGPGLVAGANFGRDYAVFEPGSRHVGLDIKGQNVANPTAMILSSTLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGGSSSTTDFTNEIINKLSTM | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 39324
Sequence Length: 360
Subcellular Location: Mitochondrion
EC: 1.1.1.41
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Q81FS0 | MVRAKRKLDHIEYALSTGQSRTHGFHDIDFVHQSLPNSNYDTITCETKIGELSLSSPIFINAMTGGGGEKTLHINEQLAYVAKHHNLAMAVGSQMAALKDESEAASYKVIRKVNPNGIFFANLGSEATIEQAERAVDMIEANALQIHLNVIQELTMPEGDRDFTGVLQRIEKIVLNSKVPIIVKEVGFGMSKETMQQLVNVGVTAIDIGGQGGTNFAAVENERRQRMLSYFNNWGIQTATSIIEATSTNNNLSFIASGGIQTALDVAKAIALGANTTAFAGYFLRILMQDGIEKLVDEIELLHTDLKFIMTALGAKTIEELQSVPLVVKGETYHWLMQRGIDTAHYSRR | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 38339
Sequence Length: 349
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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P50740 | MTRAERKRQHINHALSIGQKRETGLDDITFVHVSLPDLALEQVDISTKIGELSSSSPIFINAMTGGGGKLTYEINKSLARAASQAGIPLAVGSQMSALKDPSERLSYEIVRKENPNGLIFANLGSEATAAQAKEAVEMIGANALQIHLNVIQEIVMPEGDRSFSGALKRIEQICSRVSVPVIVKEVGFGMSKASAGKLYEAGAAAVDIGGYGGTNFSKIENLRRQRQISFFNSWGISTAASLAEIRSEFPASTMIASGGLQDALDVAKAIALGASCTGMAGHFLKALTDSGEEGLLEEIQLILEELKLIMTVLGARTIADLQKAPLVIKGETHHWLTERGVNTSSYSVR | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 37221
Sequence Length: 349
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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Q6MMK2 | MDESNSQFEKRKRDHIRIALDPRSQTDGQNGLDSITLIHEALPDLNFKEVDISTSFFFSGESIPLSSPIFISSMTAGHEKGREINEALARLSDRRQILMGVGSQRRELEDSNAAEEWARVRKQAPKARLLGNIGIAQLIKSPIDKIRRLIDSTEAVALFVHLNPLQEALQPEGTTDFKNGLAAIENLVKLAGVPVIVKETGCGFSVDTLKRLSSTGIYGVDVSGKGGTHWGRVEGYRSEESDMLYHVAQTFANWGISTKQSMLNAIDARVEYQLWASGGVRNGLEIGKLMALGASKVGVAKPFLEAALQGDEALEKLLTQLETELKVTMFCTGSRNLKDLQSKKVIQ | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 38122
Sequence Length: 347
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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Q0RBQ7 | MSPQGPGTAVDVDDEVVLLDPDRRPCGTAPRLAVHGLDTPLHLAFSSYLFDAAGRLLVTRRALGKRTWPGVWTNSCCGHPRPGEDIALAVERRVDQELRLALTDLHCALPDFAYRATAADGLVENEVCPVYVARAVGDPDPDPAEVVEWRWVDWESYRQAALAAPWALSPWSVDQMTAFGQAAHPLTAALRAVG | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 21089
Sequence Length: 194
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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A1WXH5 | MEHVVIVDPEGQRVGTEEKIRAHADGGTLHLAFCVFVFNPRGELLLQRRADSKYHFSGLWSNTCCGHPRPGEGVTEAAERRLGEEFGFVTRLHPVAQFTYHAEDHHTGLAEYEYAHVLIGRAPTDQPAPDPLEIGAWEWAAPLRIQADTQQYPLRYTPWFRRLIQEQPVADWATG | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 19853
Sequence Length: 175
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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Q9HP40 | MRDSMSEADRSSPGSGKTDREDETAENATQDVIAVTPDDERTGLANRLDAHTGDGVRHRAFTCLLFDEDGRVLLAQRADRKRLWDTHWDGTVASHPIEGQSQVDATRQRLAEELGIEPHQYDKLEITDRFEYKRRYLDEGLEWEVCAVLQATLHDTSFDRDPEEVGGAMWVDYEDLYENPRYYRQLRLCPWFEIAMRRDFEGDADPVPDGTRA | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 24567
Sequence Length: 213
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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B2GFH1 | MSENSTPERVVLLDEQHQPTGTALKSEVHTEATPLHLAFSCHVLNPDGRVLVTRRALSKRTWPGVWSNSFCGHPGPHESFEDAIARRARQELGLEIRNLTVVVPEFQYRATDATGVVENEFCPVFVAVTDTDPQPAESEVAEYAWTAPRDLIAAVESAPYAFSPWLGDQVREPALREALG | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 19902
Sequence Length: 180
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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Q6AC73 | MTPPREEVVLLAEDGAPIGTADKATVHSESTPLHLAFSCHLFDGDGRILVTRRALGKATWPGVWTNSFCGHPALGESLEEAIARRAHEELGTSVDALALALALPDFRYRAVDATGVVEHEMCPVYTATIAWELRPSADEVAEWEWADPRALLSSVAATPWAFSPWLTLQLPALYAASGDQPSGQL | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 19942
Sequence Length: 185
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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Q9Z0N1 | MAGGEGGVTLGQPHLSRQDLATLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD | Function: Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 51065
Sequence Length: 472
EC: 3.6.5.3
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Q8U082 | MGEKRKTRQAEVNIGMVGHVDHGKTTLTKALTGVWTDTHSEELRRGITIKIGFADAEIRRCSNCGRYSTSPICPYCGHETEFIRRVSFIDSPGHEALMTTMLAGASLMDGAILVIAANEPCPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALENYRQIKEFIKGTVAENAPIIPISALHGANIDVLVKAIEEFIPTPKRDSNKPPKMLVLRSFDVNKPGTPPEKLVGGVLGGSIVQGKLKVGDEIEIRPGVPYEEHGRIKYEPITTEIVSLQAGGQFVEEAYPGGLVGIGTKLDPYLTKGDLMAGNVVGKPGKLPPVWTDLRLEVHLLERVVGTEQELNVEPIKRKEVLLLNVGTARTMGLVTALGKDEIELKLQIPVCAEPGERVAISRQIGSRWRLIGYGIIKE | Function: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 45038
Sequence Length: 411
EC: 3.6.5.3
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Q980A5 | MAWPKVQPEVNIGVVGHVDHGKTTLVQAITGIWTSKHSEELKRGMTIKLGYAETNIGVCESCKKPEAYVTEPSCKSCGSDDEPKFLRRISFIDAPGHEVLMATMLSGAALMDGAILVVAANEPFPQPQTREHFVALGIIGVKNLIIVQNKVDVVSKEEALSQYRQIKQFTKGTWAENVPIIPVSALHKINIDSLIEGIEEYIKTPYRDLSQKPVMLVIRSFDVNKPGTQFNELKGGVIGGSIIQGLFKVDQEIKVLPGLRVEKQGKVSYEPIFTKISSIRFGDEEFKEAKPGGLVAIGTYLDPSLTKADNLLGSIITLADAEVPVLWNIRIKYNLLERVVGAKEMLKVDPIRAKETLMLSVGSSTTLGIVTSVKKDEIEVELRRPVAVWSNNIRTVISRQIAGRWRMIGWGLVEI | Function: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 45792
Sequence Length: 415
EC: 3.6.5.3
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Q09130 | MAENLDISELSPIHPAIISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKCSNEECPRPGCYRSYSSNKEDHPPCEICNSPMNLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMQLKHIIILQNKVDLIRESAAEEHYQSILKFIKGTVAENSPIVPISAQLKYNIDAILEYIVKKIPIPVRDFTTAPRLIVIRSFDVNKPGAEVDDLKGGVAGGSILTGVLRLNDEIEIRPGIVTKDDDGRIRCQPIFSRIISLFAEHNDLKIAVPGGLIGVGTTVDPTLCRADRLVGQVLGSKGNLPEVYTELEINYFLLRRLLGVKSGDKNTTKVQKLAKNEVLMVNIGSTSTGGRVMMVKADMAKILLTAPACTEIGEKVALSRRIEKHWRLIGWAKVVEGKTLKV | Function: As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 48781
Sequence Length: 446
EC: 3.6.5.3
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O36041 | IGHVAHGKSTLCKVLTGVDPIKFAAEKVNNITIKLGFANAKIFECKDCAAPKNYFSQKSSSPDQPPCPTCKGTHTQLLRHISIIDCPGHHDYMTTMLSGVAAMDGTLLLISAEQRCPQEQTREHFQAIQATGQKKIIIAQNKIDLVTEQQAQNNYQEIQAFVHGISDINVVPISAIQNLNIDYILKHLVETITPPRRNLKAHPRFTIIRS | Function: As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 23288
Sequence Length: 210
EC: 3.6.5.3
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P01575 | MNNRWILHAAFLLCFSTTALSINYKQLQLQERTNIRKCQELLEQLNGKINLTYRADFKIPMEMTEKMQKSYTAFAIQEMLQNVFLVFRNNFSSTGWNETIVVRLLDELHQQTVFLKTVLEEKQEERLTWEMSSTALHLKSYYWRVQRYLKLMKYNSYAWMVVRAEIFRNFLIIRRLTRNFQN | Function: Type I interferon cytokine that plays a key role in the innate immune response to infection, developing tumors and other inflammatory stimuli . Signals via binding to high-affinity (IFNAR2) and low-affinity (IFNAR1) heterodimeric receptor, activating the canonical Jak-STAT signaling pathway resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response, such as antiviral proteins, regulators of cell proliferation and differentiation, and immunoregulatory proteins (By similarity). Signals mostly via binding to a IFNAR1-IFNAR2 heterodimeric receptor, but can also function with IFNAR1 alone and independently of Jak-STAT pathways . Elicits a wide variety of responses, including antiviral and antibacterial activities, and can regulate the development of B-cells, myelopoiesis and lipopolysaccharide (LPS)-inducible production of tumor necrosis factor . Plays a role in neuronal homeostasis by regulating dopamine turnover and protecting dopaminergic neurons: acts by promoting neuronal autophagy and alpha-synuclein clearance, thereby preventing dopaminergic neuron loss . IFNB1 is more potent than interferon-alpha (IFN-alpha) in inducing the apoptotic and antiproliferative pathways required for control of tumor cell growth .
PTM: This beta interferon does not have a disulfide bond.
Sequence Mass (Da): 22127
Sequence Length: 182
Subcellular Location: Secreted
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Q969P0 | MGALRPTLLPPSLPLLLLLMLGMGCWAREVLVPEGPLYRVAGTAVSISCNVTGYEGPAQQNFEWFLYRPEAPDTALGIVSTKDTQFSYAVFKSRVVAGEVQVQRLQGDAVVLKIARLQAQDAGIYECHTPSTDTRYLGSYSGKVELRVLPDVLQVSAAPPGPRGRQAPTSPPRMTVHEGQELALGCLARTSTQKHTHLAVSFGRSVPEAPVGRSTLQEVVGIRSDLAVEAGAPYAERLAAGELRLGKEGTDRYRMVVGGAQAGDAGTYHCTAAEWIQDPDGSWAQIAEKRAVLAHVDVQTLSSQLAVTVGPGERRIGPGEPLELLCNVSGALPPAGRHAAYSVGWEMAPAGAPGPGRLVAQLDTEGVGSLGPGYEGRHIAMEKVASRTYRLRLEAARPGDAGTYRCLAKAYVRGSGTRLREAASARSRPLPVHVREEGVVLEAVAWLAGGTVYRGETASLLCNISVRGGPPGLRLAASWWVERPEDGELSSVPAQLVGGVGQDGVAELGVRPGGGPVSVELVGPRSHRLRLHSLGPEDEGVYHCAPSAWVQHADYSWYQAGSARSGPVTVYPYMHALDTLFVPLLVGTGVALVTGATVLGTITCCFMKRLRKR | Function: May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin-dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65034
Sequence Length: 613
Domain: The Ig-like C2-type domains 3 and 4 are required for interaction with CD81.
Subcellular Location: Cell membrane
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Q8R366 | MGVPSPTPLSSLLLLLLILGTRCYARQVHVPRGPLYRVAGTAVSISCNVSDYEGPAQQDFEWFMYRPEAPATSLGIVSTKDSQFSYAVFGPRVASGDLQVQRLKGDSVVLKIARLQAQDSGFYECYTPSTDTQYLGNYSAKVELRVLPDELQVSAAPPGPRGRQAATSPSRLTVHEGQELALGCLAQTKTKKHTHLSVSFGRAIPEAPVGRATLQEVVGLRSDMAVEAGAPYAERLASGELRLSKEGTDRYRMVVGGAQAGDSGTYHCTAAEWIQDPDGSWVQVAEKRAVLAHVDVQTLSSQLAVTVGPGERRIGPGEPLELLCNVSGALPPPGRHAAYSVGWEMAPAGAPGPGRLVAQLDTEGIGSLGPGYEDRHIAMEKVASRTYRLRLEAARPADAGTYRCLAKAYVRGSGTRLREAASARSRPLPVHVREEGVVLEAVAWLAGGTVYRGETASLLCNISVRGGPPGLRLAASWWVERPEEGELSSGPAQLVGGVGQDGVAELGVRPGGGPVSVELVGPRSHRLRLHGLGPEDEGIYHCAPSAWVQHADYSWYQAGSARSGPVTVYPYTHAVDTLFVPLLVGTGVALVTGASVLATITCCFMKRMRKR | Function: May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin-dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65011
Sequence Length: 611
Domain: The Ig-like C2-type domains 3 and 4 are required for interaction with CD81.
Subcellular Location: Cell membrane
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Q767C8 | MAKQHFLVITIGAQGHINPARRLAARLIEAGGARVTLTVPILAYRRMFPSAAAELEPREEKDDGLLTYMPYSDGVEDGLDPAANPAEFKRRIAESLRCIAAGFVARGRPITCIVYALLLSMAAAVARDLGVPSVLFWIQSATSFAVNYHYFAGGYDKLFSEAAADPSFLVELPGLPAFRRKDLPTLLTGPRPEGTFYSFLHTLYGEVFETLRREVSAGEEKPRVILNTFRALEEDVVAGFEASIDMVTVGPLVPPSLIMTSPEETATNDLYEHDTSNYMEWLDGKEEGSVVYVSFGSYATLKEEEREEVKKGLSASGRPYIWAMAKGGSGDDGGGLGVKVEWCEQARVLSHRSVGCFVTHCGWNSVAEAMACGVPMVMLPQWTDQVTNAKLAEEEWGVGVRAEAVAGEELRRCLDVVMGGGEADDGGIVMRRRAKAWSEKAREAAGDGGSSARNLAAFVVGGN | Function: Catalyzes the transfer of the glucosyl moiety from UDP-glucose to the 5-hydroxyl group of anthocyanin. Anthocyanins are ubiquitous colored pigments that are responsible for variations in petal color. Also acts on the 3-O-rutinosides of pelargonidin, delphinidin and malvidin, but not the corresponding glucosides or 6-acylglucosides. Does not catalyze the glucosylation of the 5-hydroxy group of cyanidin 3-glucoside.
Catalytic Activity: cyanidin 3-O-rutinoside + UDP-alpha-D-glucose = cyanidin 3-O-rutinoside 5-O-beta-D-glucoside + H(+) + UDP
Sequence Mass (Da): 50129
Sequence Length: 463
Pathway: Pigment biosynthesis; anthocyanin biosynthesis.
EC: 2.4.1.116
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Q5A8I8 | MRPTPLFFALLQIALAAKRADQICNDHCSNAYQKQQSCGGTDDVSSQSATLKCLCADESYWSELASCDCSSYDSNVSAQDLRAYYCNVGVTGGSQGQSTSGDANAATNSNDATGTATDAAAATNGNDGASGTADANNANNTDGSGATDASNTNNNGSTDTVNTNTAGSGSSETTAAAGAAAGTAAGTNSASDQANETGSDATNAATGSDASGTAATNTASTASGATSGSGSDAAKKTGTNTDSDSDTATKGSDATAGSMTTAASGLGATNGTSNSTGSHSGSMTSITTGSGFTNGTSSRSGSGSGSSTRSGSNSDSSSSGSGSRSSSSADSSDSDSGSGSSSTESGSGSGSGSSTSSGSGSGSGSSTRSGGFAATIPTVTFGSLVALALNLL | Function: GPI-anchored cell wall protein that may be involved in cell wall organization, hyphal growth, as well as in virulence.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36945
Sequence Length: 392
Subcellular Location: Secreted
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P01584 | MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS | Function: Potent pro-inflammatory cytokine . Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production . Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells . Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6 . Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore . Acts as a sensor of S.pyogenes infection in skin: cleaved and activated by pyogenes SpeB protease, leading to an inflammatory response that prevents bacterial growth during invasive skin infection .
PTM: Activation of the IL1B precursor involves a CASP1-catalyzed proteolytic cleavage. Processing and secretion are temporarily associated.
Sequence Mass (Da): 30748
Sequence Length: 269
Subcellular Location: Cytoplasm
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P24394 | MGWLCSGLLFPVSCLVLLQVASSGNMKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWAGQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLRIAASTLKSGISYRARVRAWAQCYNTTWSEWSPSTKWHNSYREPFEQHLLLGVSVSCIVILAVCLLCYVSITKIKKEWWDQIPNPARSRLVAIIIQDAQGSQWEKRSRGQEPAKCPHWKNCLTKLLPCFLEHNMKRDEDPHKAAKEMPFQGSGKSAWCPVEISKTVLWPESISVVRCVELFEAPVECEEEEEVEEEKGSFCASPESSRDDFQEGREGIVARLTESLFLDLLGEENGGFCQQDMGESCLLPPSGSTSAHMPWDEFPSAGPKEAPPWGKEQPLHLEPSPPASPTQSPDNLTCTETPLVIAGNPAYRSFSNSLSQSPCPRELGPDPLLARHLEEVEPEMPCVPQLSEPTTVPQPEPETWEQILRRNVLQHGAAAAPVSAPTSGYQEFVHAVEQGGTQASAVVGLGPPGEAGYKAFSSLLASSAVSPEKCGFGASSGEEGYKPFQDLIPGCPGDPAPVPVPLFTFGLDREPPRSPQSSHLPSSSPEHLGLEPGEKVEDMPKPPLPQEQATDPLVDSLGSGIVYSALTCHLCGHLKQCHGQEDGGQTPVMASPCCGCCCGDRSSPPTTPLRAPDPSPGGVPLEASLCPASLAPSGISEKSKSSSSFHPAPGNAQSSSQTPKIVNFVSVGPTYMRVS | Function: Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2.
PTM: On IL4 binding, phosphorylated on C-terminal tyrosine residues. Phosphorylation on any one of tyrosine residues, Tyr-575, Tyr-603 or Tyr-631, is required for STAT6-induced gene induction.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 89658
Sequence Length: 825
Domain: The extracellular domain represents the IL4 binding protein (IL4BP).
Subcellular Location: Cell membrane
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P16382 | MGRLCTKFLTSVGCLILLLVTGSGSIKVLGEPTCFSDYIRTSTCEWFLDSAVDCSSQLCLHYRLMFFEFSENLTCIPRNSASTVCVCHMEMNRPVQSDRYQMELWAEHRQLWQGSFSPSGNVKPLAPDNLTLHTNVSDEWLLTWNNLYPSNNLLYKDLISMVNISREDNPAEFIVYNVTYKEPRLSFPINILMSGVYYTARVRVRSQILTGTWSEWSPSITWYNHFQLPLIQRLPLGVTISCLCIPLFCLFCYFSITKIKKIWWDQIPTPARSPLVAIIIQDAQVPLWDKQTRSQESTKYPHWKTCLDKLLPCLLKHRVKKKTDFPKAAPTKSLQSPGKAGWCPMEVSRTVLWPENVSVSVVRCMELFEAPVQNVEEEEDEIVKEDLSMSPENSGGCGFQESQADIMARLTENLFSDLLEAENGGLGQSALAESCSPLPSGSGQASVSWACLPMGPSEEATCQVTEQPSHPGPLSGSPAQSAPTLACTQVPLVLADNPAYRSFSDCCSPAPNPGELAPEQQQADHLEEEEPPSPADPHSSGPPMQPVESWEQILHMSVLQHGAAAGSTPAPAGGYQEFVQAVKQGAAQDPGVPGVRPSGDPGYKAFSSLLSSNGIRGDTAAAGTDDGHGGYKPFQNPVPNQSPSSVPLFTFGLDTELSPSPLNSDPPKSPPECLGLELGLKGGDWVKAPPPADQVPKPFGDDLGFGIVYSSLTCHLCGHLKQHHSQEEGGQSPIVASPGCGCCYDDRSPSLGSLSGALESCPEGIPPEANLMSAPKTPSNLSGEGKGPGHSPVPSQTTEVPVGALGIAVS | Function: Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2.
PTM: On IL4 binding, phosphorylated on C-terminal tyrosine residues.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 87627
Sequence Length: 810
Domain: The extracellular domain represents the IL4 binding protein (IL4BP).
Subcellular Location: Cell membrane
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P9WEU0 | MSSTQTTAAEPIMTDNVALRAYYESWDSRVVYQIIMGGTQHFGYWDKDTYWPFPLGSKLRRSMEQKLMEILALPKGSRVLDAGCGVGHVARYMAQHGMRVFGIDIIDWAIEDARKAAKDAGLSKEMMSVEKMDYHHLDSLASESFDGVYTMQAFGHAVDPQKAMAGFFRVVRPGGRIAMVEVERKTAAKHDDPNDRLTQELKMVNDYTVMPTNEAASEDYFKNLLEEAGFVDVVVRDWQPNILPILRLFYSLVMIPYLFFRLFGNEKSFINMICARSGYAGRSRWRFVAITATKAGEKLEDHKSK | Function: S-adenosyl-l-methionine-dependent Diels-Alderase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain . IliD catalyzes the Diels-Alder reaction that converts the acyclic 2-pyridone intermediate to 8-epi-ilicicolin H . The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).
Catalytic Activity: 3-[(2E,4E,8S,10E,12Z)-4,8-dimethyltetradeca-2,4,10,12-tetraenoyl]-4-hydroxy-5-(4-hydroxyphenyl)-1,2-dihydropyridin-2-one = ilicicolin H
Sequence Mass (Da): 34700
Sequence Length: 305
Pathway: Mycotoxin biosynthesis.
EC: 2.1.-.-
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P0DO33 | MTSTEAAGTGKAPAIRANPALQTYYESQESYLVYEVVLRGSHHFGFYEKDTYWPFPVGRSLERMEAKLLSALALPSGSQILDAGCGFGPVAISMAKKGMRVTAIDIIDHHVTKARRNVEKAGLPKGQVTVEKMDYQHLESIASESHDDAKAAATGFFRILKPGGRIAFFEAQRSRTSGDYDEGDELAGHLKLVNEYTAMPTNELSREDYFKDLLEDAGFVDVEFTLPPGTREPREHWSYSALKA | Function: S-adenosyl-l-methionine-dependent Diels-Alderase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain . IliD catalyzes the Diels-Alder reaction that converts the acyclic 2-pyridone intermediate to 8-epi-ilicicolin H . The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).
Catalytic Activity: 3-[(2E,4E,8S,10E,12Z)-4,8-dimethyltetradeca-2,4,10,12-tetraenoyl]-4-hydroxy-5-(4-hydroxyphenyl)-1,2-dihydropyridin-2-one = ilicicolin H
Sequence Mass (Da): 27012
Sequence Length: 244
Pathway: Mycotoxin biosynthesis.
EC: 2.1.-.-
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P0DO34 | MSEQLGSHITTPSSHDDASKDKRPAAEVVNGSGIFIMADLHTGKPITLKCGLTLPNRLVKAATAESMAPNNTLPDEKFQNLYRHWAEGGWGMVLAGNVQVDANHICTATDLSVDHSLSDSKIVEAWRPWAAACNGNGTVTVMQLCHPGRQSPAGAGKRGLFAKSIAPSAVALQMGSGLVAKAVTALLFGTPREMSVSDIETVVSQFARSARLAAESGFAGVEVHAGHGFLLEQFLSTKSNRRTDAYGGTPAKRARIVVEVLTAIRAVVPAGFCVGLSLNSVDLQSQTELKDCVEQVKLITDAGVDFIEVSGGTFENPTMFLGPEKSRKQAQLGQPLAHEPFFLDFAKAIRPHVPGVPLIVTGGFRSCQGIEETIAGGDADLVGLARPAVVNPLLPKTTVLSPKTTEFGPEIEDGDVTLYAKKTEAPWILKQIGIRAVEVHIDNSVYHNRRHAAKQVRRASVLLQFPSRPSLSVAAVDIDNVISRLSTARPFVFIFLAITVEVNIDTDIAALLLALRPSPELYHLAAAMPPRRSDGSADHDVPDWPKTPHPTPYDILAMRKDDPYTKHRFFQLVKIYHPDRHGHTPAVHRLPHATRLERYRLIVAANDLLSNPSKRSLYDTQGVGWTGDRPPTLNESVRHAEKSWRHQPGNASRNATWEDWERWYDARDGKTRDPMYMSNGVFATLVVMMCMIGAFAQMSRAEQSGTEYLETRDQSNLAIGQQISRTTLVSAGRSKDERVDSFLRERENVAYEFTPSKYDDRTRTEA | Function: NADH-dependent flavin oxidoreductase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain . The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 83902
Sequence Length: 766
Subcellular Location: Membrane
EC: 1.-.-.-
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F4IS56 | MENITAQLKRGISRQFSTGSIRRTLSRQFTRQSSLDPRRTNMRFSFGRQSSLDPIRRSPDSSKSDDEPHMSVPENLDSTMQLLFMASKGDVRGIEELLDEGIDVNSIDLDGRTALHIAACEGHLGVVKALLSRRANIDARDRWGSTAAADAKYYGNLDVYNLLKARGAKVPKTRKTPMTVSNPREVPEYELNPLEVQVRKSDGISKGAYQVAKWNGTRVSVKILDKDSYSDPERINAFRHELTLLEKVRHPNVIQFVGAVTQNIPMMIVVEYNPKGDLSVYLQKKGRLSPSKALRFALDIARGMNYLHECKPDPIIHCDLKPKNILLDRGGQLKISGFGMIRLSKISQDKAKVANHKAHIDLSNYYIAPEVYKDEIFDLRVDAHSFGVILYEITEGVPVFHPRPPEEVARMMCLEGKRPVFKTKSRSYPPDIKELIEKCWHPEAGIRPTFSEIIIRLDKIVANCSKQGWWKDTFKFPWK | Function: Functions as a link between plant defense pathways, stress responses and potassium homeostasis. Promotes osmotic stress sensitivity, responses to the bacterial-derived pathogen-associated molecular pattern (PAMP) flg22, and resistance to bacterial pathogens. Promotes the accumulation of POT5/HAK5, a potassium transporter that mediates high-affinity uptake during potassium deficiency.
PTM: Autophosphorylated at Ser-17 and Ser-26.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54415
Sequence Length: 479
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9H0C8 | MDLFGDLPEPERSPRPAAGKEAQKGPLLFDDLPPASSTDSGSGGPLLFDDLPPASSGDSGSLATSISQMVKTEGKGAKRKTSEEEKNGSEELVEKKVCKASSVIFGLKGYVAERKGEREEMQDAHVILNDITEECRPPSSLITRVSYFAVFDGHGGIRASKFAAQNLHQNLIRKFPKGDVISVEKTVKRCLLDTFKHTDEEFLKQASSQKPAWKDGSTATCVLAVDNILYIANLGDSRAILCRYNEESQKHAALSLSKEHNPTQYEERMRIQKAGGNVRDGRVLGVLEVSRSIGDGQYKRCGVTSVPDIRRCQLTPNDRFILLACDGLFKVFTPEEAVNFILSCLEDEKIQTREGKSAADARYEAACNRLANKAVQRGSADNVTVMVVRIGH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase that may play a role in regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. Selectively associates with integrin linked kinase (ILK), to modulate cell adhesion and growth factor signaling. Inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 42907
Sequence Length: 392
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q8R0F6 | MDLFGDLPEPERAPRPSAGKEAQGRPVLFEDLPPASSTDSGSGGPLLFDDLPPAASGNSGSLATSGSQVVKTEGKGAKRKAPEEEKNGGEELVEKKVCKASSVIFGLKGYVAERKGEREEMQDAHVILNDITQECNPPSSLITRVSYFAVFDGHGGIRASKFAAQNLHQNLIRKFPKGDIISVEKTVKRCLLDTFKHTDEEFLKQASSQKPAWKDGSTATCVLAVDNILYIANLGDSRAILCRYNEESQKHAALSLSKEHNPTQYEERMRIQKAGGNVRDGRVLGVLEVSRSIGDGQYKRCGVTSVPDIRRCQLTPNDRFILLACDGLFKVFTPEEAVNFILSCLEDDKIQTREGKPAVDARYEAACNRLANKAVQRGSADNVTVMVVRIGH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase that may play a role in regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. Selectively associates with integrin linked kinase (ILK), to modulate cell adhesion and growth factor signaling. Inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 42774
Sequence Length: 392
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q9Z1Z6 | MDLFGDLPEPERPPRPSAGKEAQEGPVLFEDLPPTSSTDSGSGGPLLFDGLPPAGSGNSGSLATSGSQVVKNEGKGAKRKAPEEEKNGGEELVEKKVCKASSVIFGLKGYVAERKGEREEMQDAHVILNDITQECNPPSSLITRVSYFAVFDGHGGIRASKFAAQNLHQNLIRKFPKGDVISVEKTVKRCLLDTFKHTDEEFLKQASSQKPAWKDGSTATCVLAVDNILYIANLGDSRAILCRYNEESQKHAALSLSKEHNPTQYEERMRIQKAGGNVRDGRVLGVLEVSRSIGDGQYKRCGVTSVPDIRRCQLTPNDRFILLACDGLFKVFTPEEAVNFILSCLEDEKIQTREGKPAVDARYEAACNRLANKAVQRGSADNVTVMVVRIGH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase that may play a role in regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. Selectively associates with integrin linked kinase (ILK), to modulate cell adhesion and growth factor signaling. Inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 42744
Sequence Length: 392
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q9TZC4 | MSLSTHYHAHKPNVPIIMEDVFGWVREGNAFQVRVWLDDHEHDLNVGDDHAFSLLHWAAKGGHVAIAEMLLSRGARVNSTNMGDDTSLHLAAAHGHRQIVVKLLSRKADVNATNEHGMTPLHYACFWGYEQIAEDLISCGAAVNVCNKKGMTPLDVCQPMCKNTILEIAQEHGQSPNDRVPFKDTTWKGTKSRTRDATLSRYTGVDVSSLNLITKIAESHSGELWRGKWQGNDIVARILNVQEVTARISRDFQTEFPALRIFAHPNICAVLAAANQPPNLVIISQYMPFGSLYNVLHEQSSVVIDHGQAVRFALDIARGMSYLHSLDPMLLRFYLSSKHVVVDEELTAKLSMADTKFSFQEVGKAYSPAWMSPEALSRAPEDLNIRAADMWSFAILLWELNTREVPFSDLPPMECGMKIALEGLRVHIPPGIARNMNRLMNICMNEDPGRRPNFDQIIPILERMIL | Function: Probable pseudokinase that acts as an adapter protein . Component of an integrin containing attachment complex, which is required for muscle development and maintenance . Involved in the assembly of dense bodies and M lines during body wall muscle development by recruiting several of their components including integrin pat-3, cpna-1, unc-89 and unc-112 to integrin-mediated attachment sites . Plays a role in distal tip cell (DTC) migration and in oocyte development probably by regulating the actin cytoskeleton . During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles . May be involved in thermotolerance and lifespan .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52260
Sequence Length: 466
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cytoplasm
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Q9DF58 | MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSNVVDMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLIQFKADINAVNEHGNTPLHYACFWGHDTVAEDLVGNGALVSIANKYSETPIDKAKMPLREILKERAEKLGQNLTKIPYKDTFWKGTTRTRPRNGTLNKLAGIDFKQLSLSQKLNENQSGELWKGRWQGNDIVIKMLKIRDWTTRKSRDFNEEYPKLRIFSHPNVLPVLGACQSPPAPHPIVISHWMPYGSLYNVLHEGTNFVVDQMQAVKFAFDIARGMAFLHTLEPLIPRHHLNSRSIMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEEINRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHICKLMKICMNEDPAKRPKFDMIVPILEKMQDK | Function: Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling.
PTM: Autophosphorylated on serine residues.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 51518
Sequence Length: 452
Subcellular Location: Cell junction
EC: 2.7.11.1
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O55222 | MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLAKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQAPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK | Function: Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Regulates cell motility by forming a complex with PARVB. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.
PTM: Autophosphorylated on serine residues.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 51373
Sequence Length: 452
Domain: A PH-like domain is involved in phosphatidylinositol phosphate binding.
Subcellular Location: Cell junction
EC: 2.7.11.1
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O25097 | MALPVYYDKDIDLGVIQSLQVGIIGYGAQGEAQALNLRDSKVKARIGLYQGSLSVSKAKKEGFEVLEVKELVQNSDVIMALLPDELHKEVLEKEVIPFLKEGQIVGFAHGFSVHFNQVVLPKGVGAILVAPKGPGSALREEYLKNRGLYHLIAIEQESSIHNAKAVALSYAKAMGGGRMGVLETSFKEECESDLFGEQAVLCGGLEAIVRMGFETLIKAGYPEELAYFECVHEVKLVADLLHYKGVEGLRKHISNTAEFGAIKAREPMGKLLKKRMQKILKKIQNGSFAKDFLLEKSLNYPRLNTERKALKETKIEQIGEILRAPFNHKK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
Sequence Mass (Da): 36534
Sequence Length: 330
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.86
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E0SRA9 | MAKIYKDEDISLEPIKNKTIAILGYGSQGRAWALNLRDSGLNVVVGLERQGDSWRRAIDDGFKPMYTKDAVAIADIIVFLVPDMVQKSLWLNSVKDFMKKGADLVFAHGFNIHFKIIEPPKDSDVYMIAPKSPGPIVRRSYEMGGGVPALVAVYQNVSGEALQKALAIAKGIGCARAGVIESTFKEETETDLFGEQVILVGGIMELIKASFETLVEEGYQPEVAYFETVNELKLIVDLIYEKGLTGMLRAVSDTAKYGGITVGKFIIDKSVRDKMKIVLERIRSGEFAREWIKEYERGMPTVFKELSELEGSTIETVGRKLREMMFRGMKQISSH | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH or NADH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NAD(+) = (2S)-2-acetolactate + H(+) + NADH
Sequence Mass (Da): 37346
Sequence Length: 335
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.383
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D0WGK0 | MSVKTKEKEMAVTILYEQDVDPKVIQGLKVGIIGYGSQGHAHALNLMDSGVDVRVGLREGSSSWKTAEEAGLKVTDMDTAAEEADVIMVLVPDEIQPKVYQEHIAAHLKAGNTLAFAHGFNIHYGYIVPPEDVNVIMCAPKGPGHIVRRQFTEGSGVPDLACVQQDATGNAWDIVLSYCWGVGGARSGIIKATFAEETEEDLFGEQAVLCGGLVELVKAGFETLTEAGYPPELAYFECYHEMKMIVDLMYESGIHFMNYSISNTAEYGEYYAGPKVINEQSREAMKEILKRIQDGSFAQEFVDDCNNGHKRLLEQREAINTHPIETTGAQIRSMFSWIKKED | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
Sequence Mass (Da): 37779
Sequence Length: 342
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.86
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P51785 | MAELRSNMITQGIDRAPHRSLLRAAGVKEEDFGKPFIAVCNSYIDIVPGHVHLQEFGKIVKEAIREAGGVPFEFNTIGVDDGIAMGHIGMRYSLPSREIIADSVETVVSAHWFDGMVCIPNCDKITPGMLMAAMRINIPTIFVSGGPMAAGRTSDGRKISLSSVFEGVGAYQAGKINENELQELEQFGCPTCGSCSGMFTANSMNCLSEALGLALPGNGTILATSPERKEFVRKSAAQLMETIRKDIKPRDIVTVKAIDNAFALDMALGGSTNTVLHTLALANEAGVEYSLERINEVAERVPHLAKLAPASDVFIEDLHEAGGVSAALNELSKKEGALHLDALTVTGKTLGETIAGHEVKDYDVIHPLDQPFTEKGGLAVLFGNLAPDGAIIKTGGVQNGITRHEGPAVVFDSQDEALDGIINRKVKEGDVVIIRYEGPKGGPGMPEMLAPTSQIVGMGLGPKVALITDGRFSGASRGLSIGHVSPEAAEGGPLAFVENGDHIIVDIEKRILDVQVPEEEWEKRKANWKGFEPKVKTGYLARYSKLVTSANTGGIMKI | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 59500
Sequence Length: 558
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
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Q73TT7 | MPTTDSARAADIKQPDIKPRSRDVTDGLEKAAARGMLRAVGMGDEDFAKPQIGVASSWNEITPCNLSLDRLAKAVKEGVFAAGGYPLEFGTISVSDGISMGHEGMHFSLVSREVIADSVETVMQAERLDGSVLLAGCDKSLPGMLMAAARLDLASVFLYAGSILPGVAKLSDGSEREVTIIDAFEAVGACARGLMPREDVDAIERAICPGEGACGGMYTANTMASAAEALGMSLPGSAAPPATDRRRDGFARRSGQAVVELLRRGITARDILTKEAFENAIAVVMAFGGSTNAVLHLLAIAHEADVALSLDDFSRIGSKVPHLADVKPFGRHVMTDVDHIGGVPVMMKALLDAGLLNGDCLTVTGATVAQNLAAIAPPDPDGKVLRALSDPLHPTGGITILRGSLAPEGAVVKSAGFDSDVFEGTARVFDGERAALDALEDGTITKGDAVVIRYEGPKGGPGMREMLAITGAIKGAGLGKDVLLLTDGRFSGGTTGLCVGHIAPEAVDAGPIAFLRDGDRIRLDVANRVLDVLVDPAEFDSRRTGFTPPPPRYKTGVLAKYVKLVGSAAIGAVCG | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 59561
Sequence Length: 575
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
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Q3IMV2 | MSQQTEPDDDAALDGDEPGAYGKDERLRSREVTEGPERAPHRAMFRAMGYDDEDLSSPLIGVPNPAADITPCNVHLDDVAESALEGIDEAGGMPIEFGTITISDAISMGTEGMKASLISREVIADSVELVSFGERMDALVTVAGCDKNLPGMMMAAIRTDLPSVFLYGGSIMPGQHEGRDVTIVQVFEGVGAYAQGEMSGDELDDLERNACPGAGSCGGMFTANTMASLSEALGLAPLGSASPPAENHERYAVARRAGELAVEVVEEDRHPSDILTRTSFENAIALQTAMGGSTNAVLHLLALAAEAGIDLDIEDFDAISRRTPKIADLQPGGDRVMNDLHEIGGVPVVIRRLMEADLFDGSQLTVTGRTIEEELAHLESEHGLPTDDEIDADFLYPVDDPKEAEGAIKILTGNLAPDGAVLKVTGDDEFYHEGPARVFENEEDAMKYVQEGHIESGDVIVIRNEGPEGGPGMREMLGVTAAVVGAGHEDDVALLTDGRFSGGTRGPMIGHIAPEAFVGGPIGALEDGDHITVDIPDRTIEVDLSDSELERRLDERDDPEPAYTNGVVAKYGSLFGSAANGAVTNPGLHNDQH | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 62779
Sequence Length: 593
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
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Q9JS61 | MPEYRSKTSTHGRNMAGARALWRATGVMETDFGKPIIAVANSFTQFVPGHVHLHNMGQLVAREIEKAGAIAKEFNTIAIDDGIAMGHSGMLYSLPSRDLIADSIEYMVNAHCADALVCISNCDKITPGMLIAAMRLNIPTIFVSGGPMEAGKVIGVANIQPERRLDLIDAMIESADDNVSNRQVEEVEQNACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSYLATHAGRKELFLEAGRMIVEITKRYYEQNDETVLPRSIATKKAFENAMTMDIAMGGSTNTILHLLAVANEAGVDFKMADIDRLSRVVPCICKTAPNNHDYYMEDVHRAGGIFAILKELDKAGKLHTDVHTIHAPTLKDAIEQWDVTNPENTRAIERFKAAPGGVRTTQAFSQNRMWKTLDLDREKGCIRDVAHAYSQDGGLAVLFGNIAERGCVVKTAGVDESILKFTGRARVFESQEDAVEGILGNQIVAGDIVIIRYEGPKGGPGMQEMLYPTSYLKSKGLGKACALLTDGRFSGGTSGLSIGHASPEAAEGGAIGLVHEGDTVEIDIPNRSIHLAISDEELAARRAEMEARGSKAWKPKNRDRYVSAALRAYGAMATSADKGAVRDVAQIER | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 66786
Sequence Length: 619
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
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Q9WZ21 | MRSDVIKKGLERVPHRSLLKALGITDDEMRRPFIGIVSSWNEIIPGHVHLDKVVEAVKAGVRMAGGVPFVFPTIGICDGIAMDHRGMKFSLPSRELIADSIEIVASGFPFDGLVFVPNCDKITPGMMMAMGRLNIPSVLISGGPMLAGRYNGRDIDLITVFEAVGGYKVGKVDEETLKAIEDLACPGAGSCAGLFTANTMNSLAEALGIAPRGNGTVPAVHAKRLRMAKEAGMLVVELVKRDVKPRDIVTLDSFMNAVMVDLATGGSTNTVLHLKAIAESFGIDFDIKLFDELSRKIPHICNISPVGPYHIQDLDDAGGIYAVMKRLQENGLLKEDVMTIYLRKIGDLVREAKILNEDVIRPFDNPYHKEGGLGILFGNLAPEGAVAKLSGVPEKMMHHVGPAVVFEDGEEATKAILSGKIKKGDVVVIRYEGPKGGPGMREMLSPTSAIVGMGLAEDVALITDGRFSGGSHGAVIGHVSPEAAEGGPIGIVKDGDLIEIDFEKRTLNLLISDEEFERRMKEFTPLVKEVDSDYLRRYAFFVQSASKGAIFRKP | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 59781
Sequence Length: 554
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
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Q5SIY0 | MRSDQIKKGLKQAPARAMLRAVGVGDEDFGRPFVGVVNTFTDGMPCNFHLRELAQHLKAGLKEAGLFPFEFGAPAISDGISMGTPGMRASLVSREVIADSVELIAQGYLYDGMVGLSACDKTIPGTAMGVIRSGVPGMILYGGTIAPGEWQGRKLTIVEVFEAVGQRAAGKISEEELLEIERRAIPGPGACGGQYTANTMAMALEALGLSPVGYNAIPAVHPEKERATKEAGKILAWAIAHDWKPKDFLTRKSFLNAIAAVAATGGSTNAVLHLLALAKEAGVELSLDDFDQISRKTPVIADLRPWGTYTAWELYEAGGTALVFKRLLEAGLLFGEEKTLTGRTLAEEVERAYREQEGQKVVFPVEKALKPHGGLVVLKGNLAPKGAVLKLAGTERTYFEGPARVFDSEEAAMEKVLKGEIRPGDVVVIRYVGPKGAPGMPEMLSVTSAIVGEGLGPEVALLTDGRFSGGTRGLMIGHIAPEAFVGGPIALLEEGDRIRIDVEGRRLEVLLPEEELERRRARWRPRPPAFTHGLFARYAALVRQADEGAVLEDPL | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 59491
Sequence Length: 555
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
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Q6L5F5 | MQPASPVSGDAGPVAEAVPPRGAPQVLVRRRSVPFSPDSPLAPGSRGGGERRSTFREDVSHAAAETYLVTRLAFILLRYLGVGYRWISQLAALIIYAILLMPGFIRVGYYYFFSRQVLRSVIYGDQPRNRLDLYIPRDPKKPSPVVAFVTGGAWIIGYKAWGALLGRRLAERGIIVACIDYRNFPQGTISDMVSDASDGISFVCETVGAYGGDPNQIYLMGQSAGAHIAACALLEQAAKESRGEQISWSVTQIKAYFGLSGGYNIENLVDHFHERGLYRSIFLSIMEGKKSLPHFSPETVAKKLCPETIALLPQIVLLHGTDDYSIPFSASETFAGVLKQAGAKAKLLLYEGKTHTDVFLQDPLRGGRDKLVEDVISVIHADDADAREKDALAPIPGRLVSEWQIKLAHRISPF | Function: Catalyzes the demethylation of isoprenylcysteine methylesters.
Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + H2O = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + H(+) + methanol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45334
Sequence Length: 414
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.1.n2
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Q747K6 | MTLRKTAGYLWNPISLIGFLLAVVATGLIIAFIAMEMITGIDHPYIGLLVYFAFPGMLILGLILVPIGAWRVRNQRRTEVPEEVPPYPRVDFNDPHKRRLFIFFVLASVIFVLIVSVASILGFEFTESTTFCGELCHVVMEPEHKAWQGSPHARVKCVECHVGPGAEWYVKAKLSGLRQVWAVLTHSYHFPIATPIENLRPARDTCEQCHWPEKFYSGRQRVFYHYAPNKENTPREINMLIKIGGTPKSPHAMGIHWHIGTEVTYIARDRKRLDIPYVAVKQKDGSIVEYMDTEKPLTREEIAKAEKRRMDCIDCHNRPTHIYRSPAREMDEHIVSGQIDAGLPYIKKVAVEILEQPYKSKEEAHAAIEAKLPEYYAKNFPEVAKVKAAAINQAVAHVKDIYSRNFFPRMKVTWSTYPNHIGHFYTPGCFRCHDGKHKTSTGKIISKDCNMCHEMIGQKGENIPEGKVVKEFVHPADIGDALYNVNCSDCHMAAAEDSAGGEGPGKH | Function: Redox protein involved in a high-potential metal respiratory pathway. Is required only for electron transfer to terminal extracellular electron acceptors with redox potentials higher than -0.1 V. ImcH likely transfers electrons from the quinone pool to a periplasmic acceptor.
PTM: Binds 4 heme c groups covalently per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57386
Sequence Length: 507
Subcellular Location: Cell inner membrane
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Q5Z9I2 | MQVELADRAAARPSETGEAPPSSPAAAAAASAAAEDAPLLPGGGGGVRRRVVVSERFRQRSGSFRREVRRAAEETYLLTRLTLILLRYLGIGYRWIRQFLALCCYTFLLMPGFIQVVYYYFFSSQVCRSVVYGEQPRNRLDLYIPTDRTGLKPVVAFVTGGAWIIGYKGWGALLGRRLAERGILVACIDYRNFPQGTIGDMVEDASQGIAFVCNNIASYGGDPERIYLVGQSAGAHIAACTLLHQAIKESGEGDASTWSIAQLKAYFGISGGYNLLNLVDHFHKRGLYRSIFLSIMEGEESLQKFSPLVMVKDPAARSAVSLLPRIFLFHGTSDYSIPSAESEAFFDALQQNGAKADLFLYDGKTHTDLFLQDPLRGGRDKLLEEIVTVIHNDNPDTSAQHLAVPVARRLVPEFMLMLAGRVSPF | Function: Catalyzes the demethylation of isoprenylcysteine methylesters.
Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + H2O = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + H(+) + methanol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46758
Sequence Length: 425
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.1.n2
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Q5VNW5 | MRPVSSAEEVGALLSRSDSSGRRRRSSPVQSASPRPAGCGCGGPRRQSSFRDDVGHAASETYLVTRLTFSLLQYLGLGYRWMSQLLALTIYAILLMPGFLQVGYYYFFSSQVRRSIVYGEQPRNRLDLYIPKDINRPCPVVAFVTGGAWIIGYKAWGSLLGRRLAERGIIVACIDYRNFPQGTIGDMVSDASQGISYVCNNIASYGGDPNRIYLVGQSAGAHIAACALIEQAVKESSGQSISWSVTQIKAYFGLSGGYNMHSLVDHFHERGLNRSIFFSIMEGEESLSRYSPEIVVKQSSSQTIALLPPIVLMHGTEDYSIPSSARFLLMPSADVHLR | Function: Catalyzes the demethylation of isoprenylcysteine methylesters.
Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + H2O = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + H(+) + methanol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37159
Sequence Length: 338
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.1.n2
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A0JNA3 | MADYLISGGTGYVPEDGLTAQQLFANADGLTYNDFLILPGFIDFTADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKIRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRNELVVAPAGVTLKEANEILQRSKKGKLPIVNDRDELVAIIARTDLKKNRDYPLASKDSHKQLLCGAAVGTREDDKYRLDLLTQAGADVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPVIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 55424
Sequence Length: 514
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.205
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P20839 | MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 55406
Sequence Length: 514
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.205
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F6S675 | MADYLISGGTGYVPEDGLTAQHLFANSDGLTYNDFLILPGFIDFTADEVDLTSALTRKITLKTPLISSPMDTVTESDMAIAMALMGGIGIIHHNCTPEFQANEVRKKFEQGFITDPVVMSLNHTVGDVFEAKNRHGFSGIPVTETGKMGSKLVGIVTSRDIDFLTEKDYSTYLSEVMTKRDELVVAPAGVTLKEANEILQRSKKGKLPIVNDSDELVAIIARTDLKKNRDYPLASKDCRKQLLCGAAIGTREDDKYRLDLLTQAGVDVVVLDSSQGNSVYQINMIHYIKQKYPELQVVGGNVVTAAQAKNLIDAGVDALRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPVIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKNTSSQKRYFSEGDKVKVAQGVSGSIQDKGSIHKFVPYLIAGIQHGCQDIGAKSLSILRSMMYSGELKLEKRTMSAQVEGGVHGLHSYEKRLY | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 55454
Sequence Length: 512
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.205
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P39567 | MAAIRDYKTALDLTKSLPRPDGLSVQELMDSKIRGGLAYNDFLILPGLVDFASSEVSLQTKLTRNITLNIPLVSSPMDTVTESEMATFMALLDGIGFIHHNCTPEDQADMVRRVKNYENGFINNPIVISPTTTVGEAKSMKEKYGFAGFPVTADGKRNAKLVGAITSRDIQFVEDNSLLVQDVMTKNPVTGAQGITLSEGNEILKKIKKGRLLVVDEKGNLVSMLSRTDLMKNQKYPLASKSANTKQLLWGASIGTMDADKERLRLLVKAGLDVVILDSSQGNSIFQLNMIKWIKETFPDLEIIAGNVVTKEQAANLIAAGADGLRIGMGTGSICITQKVMACGRPQGTAVYNVCEFANQFGVPCMADGGVQKHWSYYYQSFGSWFFYCYDGWYVGRYYRITR | Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 44386
Sequence Length: 403
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.205
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Q9SA34 | MSGFEDGFSAEKLFSQGYSYTYDDVIFLPHFIDFSTDAVSLSTRLSKRVPLSIPCVASPMDTVSESHMAAAMAALGGIGIVHYNCDIDTQASVIRHAKSLQVPIASDAVFKCPEHQIGSVDDFGPSSFVFVSQTGTLTPKLLGYVSKSEWSSMKDDQKEVKIYDYMKSCENKDYYVPWDIDLDKIEAVLEDKQKGFVVLEKEGETVNVVTKDDVERVKGYPKLGSGTVGADKKWMVGAAIGTRESDKERLEHLVKAGANVVVLDSSQGNSIYQLEMIKYVKNTYPELDVVGGNVVTMYQAENLIKAGVDGLRVGMGSGSICTTQEVCAVGRGQATAVYKVSTLAAQHGVPVIADGGISNSGHIVKALVLGASTVMMGSFLAGSTEAPGAYEYRNGRRVKKYRGMGSLEAMTKGSDQRYLGDTAKLKIAQGVVGAVADKGSVLKFIPYTMHAVKQGFQDLGASSLQSAHELLRDNTLRLEARTGAAQIEGGIHGLVSYEKKSF | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 54051
Sequence Length: 502
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.205
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B0UXP9 | MADYLISGQTGYVPDDGLTGQQLFNSGDGLTYNDFLILPGYIDFTADQVDLTSALTKQITMKTPLISSPMDTVTESGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKRYEQGFITDPVVMSPNERVRDVFQAKARHGFCGIPITDNGQMGGRLVGIISSRDIDFLKESEHDLPLSEVMTKREDLVVAPAGVTLKEANEILQRSKKGKLPIVNEEGCLVAIIARTDLKKNRDFPLASKDSRKQLLCGAAIGTHNDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKEKYPNVQVIGGNVVTAAQAKNLIDAGADALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQTVGHIAKALALGASTVMMGSLLAATSEAPGEYFFSDGIRLKKYRGMGSLDAMDKNLGSQTRYFSESDKIKVAQGVSGAVQDKGSIHKFVPYLLVGIQHSCQDIGAKSLTQLRAMMYSGELRFEKRTMSAQMEGGVHSLHSYEKRLF | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 55696
Sequence Length: 514
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.205
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P12268 | MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth . Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism . It may also have a role in the development of malignancy and the growth progression of some tumors.
PTM: Ubiquitinated leading to its degradation by the proteasome.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 55805
Sequence Length: 514
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.205
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D5RAW5 | MDNHIKGALLVCLAATMWGFDGIALTPRLFSLHVPFVVFILHLLPLILMSILFGKEEVKNIKKLQKNDLFFFFCVALFGGCLGTLCIVKALFLVNFKHLTVVTLLQKLQPIFAIILARLLLKEKLKRAYLFWGFLALLGGYLLTFEFHLPEFVSSDNLLPASLYSLLAAFSFGSATVFGKRILKSASFRTALYLRYLMTSCIMFVIVTFTSGFGDFLVATAGNWLIFVIIALTTGSGAILLYYFGLRYITAKVATMCELCFPISSVVFDYLINGNVLSPVQIASAILMIISIIKISKLN | Function: Transports riboflavin into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33263
Sequence Length: 299
Subcellular Location: Cell membrane
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