ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q8IYT4 | MELSYQTLKFTHQAREACEMRTEARRKNLLILISHYLTQEGYIDTANALEQETKLGLRRFEVCDNIDLETILMEYESYYFVKFQKYPKIVKKSSDTAENNLPQRSRGKTRRMMNDSCQNLPKINQQRPRSKTTAGKTGDTKSLNKEHPNQEVVDNTRLESANFGLHISRIRKDSGEENAHPRRGQIIDFQGLLTDAIKGATSELALNTFDHNPDPSERLLKPLSAFIGMNSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDLPSREARQAMIYHWLPPVSKSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKIFDALENHQSESSDLPRIQLDIVTTADFLDVLTHTKPSAKNLAQRYSDWQREFESV | Function: Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Sequence Mass (Da): 61253
Sequence Length: 538
Subcellular Location: Cytoplasm
EC: 5.6.1.1
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Q9D3R6 | MELSYQTLKLTHQAREAYEMRTEARRKNLLILILHYLTQEGYMDAAKALEEETKLGLRRFEVCDNVDLETILMEYESYYFVKFQKYPKVVKKAPDPVENNLPSRSGGKNKRLTNDSCQNLPKICHQKSRPKTSAVKTGDTKSVKEHLKQVKESVTDTQAESTDFGLNISKIHKDQPEEKAQPRRGQIIDFRGLLSDAIKGATSEFALNTFECNPDPSERLLKPLSAFIGMNSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGMVPGGEHEGSLRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDLPSQEARQAMIYHWLPPVSKNHALELHTQLEYSVLSQETEGYSGSDIKLVCREAAMRPVRKIFSVLENNQSESNNLPGIQLDTVTTQDFLDVLAHTKPSAKNLTERYLAWQEKFESV | Function: Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Sequence Mass (Da): 61153
Sequence Length: 539
Subcellular Location: Cytoplasm
EC: 5.6.1.1
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A0JMA9 | MELSYQALRVASQNREAEELRTEARRKNLLILIMHYLLQEGYMDSANSLEQETKISLRRFDVCDNVDLETILMEYESYYYIKFQKYPKITKKALDHDSRVQSKPRSAGKLRRAGSNSTQGLPRIAQQTVLHRPVSGSYFRTHAHQKALSRENSKQENGGNSPREASEIGLNVSAISKTSGEGGQTRRRQVIDFRSMIQDTIKGASQEIALNSLNCNPDPSERLIKPVGAFIGGNSEMRELAAVISRDIYLQNPNVRWDDIIGLDAAKRLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECNTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTGPGGEHEGSRRMKTELLVQMDGLARSDDLVFVLAASNLPWELDYAMLRRLEKRILVDLPSKEARQAMIQHWLPPVSNSSGVELRTDLDYSTLGAETDGYSGSDIRLVCKEAAMRPVRKIFDALENHHSEHKNLPVISLDTVTTSDFLEVLAHTKPSAKSLAEKYAAWQKEFESV | Function: Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Sequence Mass (Da): 60918
Sequence Length: 542
Subcellular Location: Cytoplasm
EC: 5.6.1.1
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Q17CS8 | MMFLRNHNSVGGAIRTAVVLQDLQFIVSNKSSALTGAVSSVHRQQIRTMSSTSNETMHNKFDLPKRYQGSTKSVWVEYIQLAAQYKPLNLGQGFPDYHAPKYALDALAAAANSPDPLANQYTRGFGHPRLVQALSKLYSQLVDRTINPMTEVLVTVGAYEALYATIQGHVDEGDEVIIIEPFFDCYEPMVKAAGGIPRFIPLKPNKTGGTISSADWVLDNNELEALFNEKTKMIIINTPHNPLGKVMDRAELEVVANLCKKWNVLCVSDEVYEHMVFEPFEHIRICTLPGMWERTITIGSAGKTFSLTGWKIGWAYGPEALLKNLQMVHQNCVYTCATPIQEAIAVGFETELKRLKSPECYFNSISGELMAKRDYMASFLAEVGMNPTVPQGGYFMVADWSSLDSKVDLTQETDARKDYRFTKWMTKSVGLQGIPPSAFYSEPNKHLGEDFVRYCFFKKDENLQKAAEILRKWKGSS | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) . Also catalyzes the irreversible transamination of several amino acids including cysteine, tyrosine, glutamine, methionine, histidine and phenylalanine . Can use various keto-acids as the amino group acceptor .
Catalytic Activity: L-kynurenine + pyruvate = H2O + kynurenate + L-alanine
Sequence Mass (Da): 53506
Sequence Length: 477
Pathway: Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.
Subcellular Location: Mitochondrion
EC: 2.6.1.-
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B0VH76 | MAEKLKLARSMSLFEEAKQLVPGGVAGIRRPYNFVPGEYPIFFDHGKGGRVVDVDGNEYIDFLCAYGPIIIGYREDEIDDAVINQIKNKGFCFSLTQEMQNTLVKKLRELIPCCEMAALVKTGSDATTIAIRVARGYTGKTKIARYGYHGWHDWCVEVKGGIPPKLYEDIYEFHYNDLDSLKAILEANKDDMAGIIITPIGHPNGAEVQMPKPGYLEAVRELANQYHCLLIFDEIRSGFRCSLGGAQKLFGVTPDLSTFGKAMANGYAIAALVGKEEYMQVLADKVFLSSTFFPNSDGIVAAIKTIEILERDRILDVVAAKGRKFGAEVEKVVEESGVPVNFTGAPWMPYITFKKDEAGLYKKLRTEYYTQLIRHNVFMQPYHHGYICYRHTDEDLAYTVEAIRESLAEVKKML | Function: 3-aminobutyryl-CoA aminotransferase that acts specifically on coenzyme A (CoA) esters and catalyzes the conversion of 3-aminobutyryl-CoA into acetoacetyl-CoA in an alternative pathway of lysine fermentation.
Catalytic Activity: (3S)-3-aminobutanoyl-CoA + 2-oxoglutarate = acetoacetyl-CoA + L-glutamate
Sequence Mass (Da): 46481
Sequence Length: 414
Pathway: Amino-acid degradation; L-lysine degradation via acetate pathway.
EC: 2.6.1.111
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Q54KM6 | MLRNTVKRLMTYTFKPSKQTSSFGPSVWLEFSPLAIKYNAVNLGQGFPNFEPPKFVKDAMIKTIEVGGFNQYTRSPGHIRLVKALSSVYSPYFGRELNAMTEIMVGVGASESLFAAISSIVNEGDEVILIEPFFDIYIGPILMAGGIPKFVTLKEEESSQAGSSDKKRSSKHWKINKEELAAAFTDKTKLIILNNPHNPVGKVYSKEELQEIADVVAKHGPNTTVISDEVYEWMTFDGEEHHRFATLPGMWERTITIGSAGKTFSITGWKVGWCIGPSNIIGAIANTHQYVPFSVPTPTQEAVAIALEQPNIKDYFKELATMYQNKRDTLLNSLTQAGLDPVIPQGTYFIMGDTSSIHLQGDQGKDTSITGMGLHLRDWNIARYLTTEYGVTTIPPSAFYCDDHQKIPENFVRFTFCKDDLTLQKAHDNLLKLKK | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity).
Catalytic Activity: 2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate
Sequence Mass (Da): 48553
Sequence Length: 435
Pathway: Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.6.1.7
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P13487 | MKILSVLLLALIICSIVGWSEAQFTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS | Function: This toxin inhibits numerous potassium channels: shaker (Ki=227 nM), Kv1.2/KCNA2 (nanomolar range), Kv1.3/KCNA3 (nanomolar range), Kv1.5/KCNA5 (Kd>100 nM), Kv1.6/KCNA6 (Ki=22 nM), KCa1.1/KCNMA1 (IC(50)=5.9 nM). It blocks channel activity by a simple bimolecular inhibition process. It also shows a weak interaction with nicotinic acetylcholine receptors (nAChR), suggesting it may weakly inhibit it . It also exhibits pH-specific antimicrobial activities against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans .
Sequence Mass (Da): 6674
Sequence Length: 59
Domain: Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).
Subcellular Location: Secreted
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P49674 | MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGAARNPEDVDRERREHEREERMGQLRGSATRALPPGPPTGATANRLRSAAEPVASTPASRIQPAGNTSPRAISRVDRERKVSMRLHRGAPANVSSSDLTGRQEVSRIPASQTSVPFDHLGK | Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates (Probable). Participates in Wnt signaling . Phosphorylates DVL1 . Phosphorylates DVL2 . Phosphorylates NEDD9/HEF1 (By similarity). Central component of the circadian clock . In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation . Controls PER1 and PER2 nuclear transport and degradation (By similarity). Inhibits cytokine-induced granuloytic differentiation .
PTM: Autophosphorylated. Partially dephosphorylated by PPP5C. May be dephosphorylated by PP1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 47315
Sequence Length: 416
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9HCP0 | MDHPSREKDERQRTTKPMAQRSAHCSRPSGSSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLGSAGEGLPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLLSRMEYVHSKNLIYRDVKPENFLIGRQGNKKEHVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRNTPIEALCENFPEEMATYLRYVRRLDFFEKPDYEYLRTLFTDLFEKKGYTFDYAYDWVGRPIPTPVGSVHVDSGASAITRESHTHRDRPSQQQPLRNQVVSSTNGELNVDDPTGAHSNAPITAHAEVEVVEEAKCCCFFKRKRKKTAQRHK | Function: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity). Phosphorylates CLSPN.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48511
Sequence Length: 422
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q8BTH8 | MDHSNREKDDRQRTTKTMAQRNTHCSRPSGTSTSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLGSAGEGLPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLLSRMEYVHSKNLIYRDVKPENFLIGRQGNKKEHVIHIIDFGLAKEYVDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRNTPIEALCENFPEEMATYLRYVRRLDFFEKPDYEYLRTLFTDLFERKGYTFDYAYDWVGRPIPTPVGSVHVDSGASAITRESHTHRDRPSQQQPLRNQTTSSERRGEWEIQPSRQTNTSYLTSHLAADRHGGSVQVVSSTNGELNVDDPTGAHSNAPITAHAEVEVVEEAKCCCFFKRKRKKTAQRHK | Function: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CLSPN (By similarity). Regulates fast synaptic transmission mediated by glutamate.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52744
Sequence Length: 459
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P78368 | MDFDKKGGKGETEEGRRMSKAGGGRSSHGIRSSGTSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLSATEGVPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLITRMEYVHTKSLIYRDVKPENFLVGRPGTKRQHAIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEEMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRSGFVFDYEYDWAGKPLPTPIGTVHTDLPSQPQLRDKTQPHSKNQALNSTNGELNADDPTAGHSNAPITAPAEVEVADETKCCCFFKRRKRKSLQRHK | Function: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain development and vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. Regulates fast synaptic transmission mediated by glutamate. SMAD3 phosphorylation promotes its ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. Triggers PER1 proteasomal degradation probably through phosphorylation.
PTM: Autophosphorylated . Phosphorylated by aPKC which promotes dissociation from the cell cortex .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 47457
Sequence Length: 415
Domain: The phospho-regulated basic and hydrophobic (PRBH) motif is sufficient and important for interaction with phospholipids permitting cortical localization . Phosphorylation of the PRBH motif by aPKC inhibits the association of the protein with the cortical membrane .
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9Y6M4 | MENKKKDKDKSDDRMARPSGRSGHNTRGTGSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGKQLPTPVGAVQQDPALSSNREAHQHRDKMQQSKNQSADHRAAWDSQQANPHHLRAHLAADRHGGSVQVVSSTNGELNTDDPTAGRSNAPITAPTEVEVMDETKCCCFFKRRKRKTIQRHK | Function: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity).
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 51389
Sequence Length: 447
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P79197 | MEIALVPLENGGAMTVRGGGEAGTGCSQAIGGELQCPPTAGLSDGPKEPAPRARGTQRGVDPGGRPLPPLPQDPQQPRRLPPEDEEGEGDPALGMAEDQVLGAGSLHHQRVLINISGLRFETQLGTLAQFPNTLLGDPAKRLRYFDPLRNEYFFDRNRPSFDGILYYYQSGGRLRRPVNVSLDVFADEIRFYQLGDEAMERFREDEGFIKEEEKPLPRNEFQRQVWLIFEYPESSGSARGIAIVSVLVILISIITFCLETLPEFRDERELLRHPPVPHQPLGPSRGANGSGPLAPPSGPTVAPLLPRTLADPFFIVETTCVIWFTFELLVRFFACPSKAEFSRNIMNIIDVVAIFPYFITLGTELAEQPGGGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADNQETHFSSIPDAFWWAVVTMTTVGYGDMRPVTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDHEEQAALKEEQGSQSHGTGLDSGGPRKASWSKGSLCKAGVSLENADGARRGSCPLEKCNLKAKSNVDLRRSLYALCLDTSRETDL | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (By similarity). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (By similarity). Homotetrameric channels display rapid activation and slow inactivation (By similarity). May play a role in regulating the secretion of insulin in normal pancreatic islets (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65889
Sequence Length: 601
Domain: The amino terminus may be important in determining the rate of inactivation of the channel while the C-terminal PDZ-binding motif may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
Subcellular Location: Cell membrane
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P50638 | MEIALGPLENGGAMTIRGGGEETAGCSQAAPTAGLGDGSQEPAPRGRGCSARRGAEPGERPLPPQPPELPQSRRSPLEEEEGEGDPGLSVAEEQTLGAGALHHQRVLINISGLRFETQLGTLAQFPNTLLGDPAKRLRYFDPLRNEYFFDRNRPSFDGILYYYQSGGRLRRPVNVSLDVFADEIRFYQLGDEAMERFREDEGFIKDEEKPLPRNEFQRQVWLIFEYPESSGSARAIAIVSVLVILISIITFCLETLPEFKDERELLRHPPVPHQPPAAPALGANGSGAVAPASGSTVAPLLPRTLADPFFIVETTCVIWFTFELLVRFFACPSKAEFSRNIMNIIDIVAIFPYFITLGTELAEQQPGGGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADNQGTHFSSIPDAFWWAVVTMTTVGYGDMRPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDHEEQAALKEEPGSQSRGTSLDAGGQRKASWSKASLCKAGGSLETADSVRRGSCLLEKYNLKAKSNVDLRRSLYALCLDTSRETDL | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane . Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation . Homotetrameric channels display rapid activation and slow inactivation . May play a role in regulating the secretion of insulin in normal pancreatic islets (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65476
Sequence Length: 598
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.
Subcellular Location: Cell membrane
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P17658 | MRSEKSLTLAAPGEVRGPEGEQQDAGDFPEAGGGGGCCSSERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEEIRFYQLGDEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRVDGRGGNNGGVSRVSPVSRGSQEEEEDEDDSYTFHHGITPGEMGTGGSSSLSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKPAFFRNIMNIIDLVAIFPYFITLGTELVQQQEQQPASGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDDDSLFPSIPDAFWWAVVTMTTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTHVTCGQPAPDLRATDNGLGKPDFPEANRERRPSYLPTPHRAYAEKRMLTEV | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient . The channel alternates between opened and closed conformations in response to the voltage difference across the membrane . Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (By similarity). Homotetrameric channels display rapid activation and slow inactivation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58729
Sequence Length: 529
Domain: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
Subcellular Location: Cell membrane
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Q61923 | MRSEKSLTLAAPGEVRGPEGEQQDAGEFQEAEGGGGCCSSERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFMEEIRFYQLGEEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRADGRGGSNEGSGTRLSPASRSHEEEDEDEDSYAFPGSIPSGGLGTGGTSSLSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKAAFFRNIMNIIDLVAIFPYFITLGTELVQRHEQQSVSGGSGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDVDSLFPSIPDAFWWAVVTMTTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTHVTCGQPTPDLKATDNGLGKPDFAEASRERRPSYLPTPHRAYAEKRMLTEV | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (By similarity). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (By similarity). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (By similarity). Homotetrameric channels display rapid activation and slow inactivation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58674
Sequence Length: 529
Domain: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
Subcellular Location: Cell membrane
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P17659 | MRSEKSLTLAAPGEVRGPEGEQQDAGEFQEAEGGGGCCSSERLVINISGLRYETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFMEEIRFYQLGDEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRADGRGGSNEGSGTRMSPASRGSHEEEDEDEDSYAFPGSIPSGGLGTGGTSSFSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKAAFFRNIMNIIDLVAIFPYFITLGTELVQRHEQQPVSGGSGQNRQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDVDSLFPSIPDAFWWAVVTMTTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTHVTCGQPTPDLKATDNGLGKPDFAEASRERRSSYLPTPHRAYAEKRMLTEV | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KNCA5, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel . Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (Probable). Homotetrameric channels display rapid activation and slow inactivation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58884
Sequence Length: 530
Domain: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
Subcellular Location: Cell membrane
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Q96RP8 | MEPRCPPPCGCCERLVLNVAGLRFETRARTLGRFPDTLLGDPARRGRFYDDARREYFFDRHRPSFDAVLYYYQSGGRLRRPAHVPLDVFLEEVAFYGLGAAALARLREDEGCPVPPERPLPRRAFARQLWLLFEFPESSQAARVLAVVSVLVILVSIVVFCLETLPDFRDDRDGTGLAAAAAAGPFPAPLNGSSQMPGNPPRLPFNDPFFVVETLCICWFSFELLVRLLVCPSKAIFFKNVMNLIDFVAILPYFVALGTELARQRGVGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLRASMRELGLLIFFLFIGVVLFSSAVYFAEVDRVDSHFTSIPESFWWAVVTMTTVGYGDMAPVTVGGKIVGSLCAIAGVLTISLPVPVIVSNFSYFYHRETEGEEAGMFSHVDMQPCGPLEGKANGGLVDGEVPELPPPLWAPPGKHLVTEV | Function: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50559
Sequence Length: 456
Domain: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
Subcellular Location: Membrane
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Q17ST2 | MLFLPADTGHPTGVAAASGPHVRSPVARAVRAMEPRCPPPCGCCERLVLNVAGLRFETRARTLGRFPDTLLGDPVRRSRFYDGARREYFFDRHRPSFDAVLYYYQSGGRLRRPAHVPLDVFLEEVSFYGLGAAALARLREDEGCAVPPERPLPRRAFARQLWLLFEFPESSQAARVLAVVSVLVILVSIVVFCLETLPDFRDDRDDPGLAPVAAATGPFLARLNGSSPMPGAPPRQPFNDPFFVVETLCICWFSFELLVRLVACPSKAVFFKNVMNLIDFVAILPYFVALGTELARQRGVGQPAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLRASMRELGLLIFFLFIGVVLFSSAVYFAEVDRVDTHFTSIPESFWWAVVTMTTVGYGDMAPVTVGGKIVGSLCAIAGVLTISLPVPVIVSNFSYFYHRETEGEEAGMYSHVDTQPCGTLEGKANGGLVDSEVPELLPPLWPPAGKHMVTEV | Function: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Channels formed by isoform 1 inactivate faster than channels formed by isoform 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53948
Sequence Length: 489
Domain: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
Subcellular Location: Membrane
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P17970 | MVGQLQGGQAAGQQQQQQQATQQQQHSKQQQQQQQQQQQQLQLKQHQQQQQDILYQQHNEAIAIARGLQAATPADIGDNQPYYDTSGNVDWERAMGAGGAGAYGGIGIGSLPAAGGAAYHLGPANPAGLVSRHLDYGDGGHLAGPSAGLPAGAVGSGAGAGAGAGASVTGSGSGAGTGTGTGAGSGSGSGAAGKEVRYAPFPVASPTHSIPTTSQQIVGSVGGVGVGGASSQSISGGVPTHSQSNTTGALQRTHSRSMSSIPPPEPFMIAQSKAVNSRVSINVGGVRHEVLWRTLERLPHTRLGRLRECTTHEAIVELCDDYSLADNEYFFDRHPKSFSSILNFYRTGKLHIVDEMCVLAFSDDLEYWGVDELYLESCCQHKYHQRKENVHEEMRKEAESLRQRDEEEFGEGKFSEYQKYLWELLEKPNTSFAARVIAVISILFIVLSTIALTLNTLPQLQHIDNGTPQDNPQLAMVEAVCITWFTLEYILRFSASPDKWKFFKGGLNIIDLLAILPYFVSLFLLETNKNATDQFQDVRRVVQVFRIMRILRVLKLARHSTGLQSLGFTLRNSYKELGLLMLFLAMGVLIFSSLAYFAEKDEKDTKFVSIPEAFWWAGITMTTVGYGDICPTTALGKVIGTVCCICGVLVVALPIPIIVNNFAEFYKNQMRREKALKRREALDRAKREGSIVSFHHINLKDAFAKSMDLIDVIVDTGKQTNVVHPKGKRQSTPNIGRQTLDVQSAPGHNLSQTDGNSTEGESTSGRNPATTGTGCYKNYDHVANLRNSNLHNRRGSSSEQDAVPPYSFDNPNARQTSMMAMESYRREQQALLQQQQQQQQQMLQMQQIQQKAPNGNGGATGGGVANNLAMVAASSAATAVATATNASNASNTAPGSEGAEGGGDGDGGGVDDDNLSQAKGLPIQMMITPGEVAELRRQVALENLQNQRMDNLEQDVPVEFECCFCTTKGLPGCHGECIPLRANSV | Function: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 106359
Sequence Length: 985
Domain: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
Subcellular Location: Membrane
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G5EFC3 | MLDACSFNRFDSNRSSARRFSRRGSDYFGDKGISMDERIVLNVGGVRHETYQATLKKIPATRLSRLTPSLANFDPLLNEYFFDRHPAVFAMILNYYRTGKLHYPTDVCGPLFEEELQYWGLDASDTEPCCWMQLLHAKDTQETLAVLDRMDADHEDDPQLREQDTMKKFGWEEDYFQGKRTRWMKLKPQMWSLFDEPYSSQAAKLIAGISVLFIFISIFSFCLKTHQSFRLPVLIGQNITMPGGVVQPSIERVSTEPLPIFGQIEMLCNIWFTLELIIRFVFCPSKIRFFKSPLNMIDLVATLSFYADAMMVRVVEDEPKDVVEFLSMIRIFRLFKLTQHHQGLQILIHTFRASAKELILLVFFLILGIVIFAALVYYAEKMEANPNNQFQSIPLGLWWAICTMTTVGYGDMTPHTSFGRLVGSLCAVMGVLTIALPVPVIVSNFAMFYSHNQARDKLPKRRRRVLPVEQIRLQARRHAAVLEPSASQGGLGGGQAIRRRNMPILIDQNCCDEENHNHKHREKSENSDEGTNSSSTTGVDTVVKLGPSETAITTTIIS | Function: Voltage-dependent potassium channel involved in the excitation of muscles operating egg-laying and defecation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63640
Sequence Length: 558
Subcellular Location: Membrane
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P08510 | MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGYGSLPKLSSQDEEGGAGHGFGGGPQHFEPIPHDHDFCERVVINVSGLRFETQLRTLNQFPDTLLGDPARRLRYFDPLRNEYFFDRSRPSFDAILYYYQSGGRLRRPVNVPLDVFSEEIKFYELGDQAINKFREDEGFIKEEERPLPDNEKQRKVWLLFEYPESSQAARVVAIISVFVILLSIVIFCLETLPEFKHYKVFNTTTNGTKIEEDEVPDITDPFFLIETLCIIWFTFELTVRFLACPNKLNFCRDVMNVIDIIAIIPYFITLATVVAEEEDTLNLPKAPVSPQDKSSNQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGRTLKASMRELGLLIFFLFIGVVLFSSAVYFAEAGSENSFFKSIPDAFWWAVVTMTTVGYGDMTPVGVWGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDQEEMQSQNFNHVTSCPYLPGTLGQHMKKSSLSESSSDMMDLDDGVESTPGLTETHPGRSAVAPFLGAQQQQQQPVASSLSMSIDKQLQHPLQQLTQTQLYQQQQQQQQQQQNGFKQQQQQTQQQLQQQQSHTINASAAAATSGSGSSGLTMRHNNALAVSIETDV | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Forms rapidly inactivating tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient and may contribute to A-type currents . Plays a role in the regulation of sleep need or efficiency . Plays a role in sexual behavior, where it is important for male sex discrimination .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74193
Sequence Length: 655
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.
Subcellular Location: Cell membrane
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P17972 | MNLINMDSENRVVLNVGGIRHETYKATLKKIPATRLSRLTEALANYDPILNEYFFDRHPGVFAQVLNYYRTGKLHYPTDVCGPLFEEELEFWGLDSNQVEPCCWMTYTQHRDTQETLAVLDRLDLDTEKPSEEELARKFGFEEDYYKGTISWWQEMKPRIWSLFDEPYSSNAAKTIGVVSVFFICISILSFCLKTHPDMRVPIVRNITVKTANGSNGWFLDKTQTNAHIAFFYIECVCNAWFTFEILVRFISSPNKWEFIKSSVNIIDYIATLSFYIDLVLQRFASHLENADILEFFSIIRIMRLFKLTRHSSGLKILIQTFRASAKELTLLVFFLVLGIVIFASLVYYAERIQPNPHNDFNSIPLGLWWALVTMTTVGYGDMAPKTYIGMFVGALCALAGVLTIALPVPVIVSNFAMYYSHTQARAKLPKKRRRVLPVEQPRQPRLPGAPGGVSGCGTPGSGPHSGPMGSGGTGPRRMNNKTKDLVSPKSDMAFSFD | Function: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56509
Sequence Length: 498
Subcellular Location: Membrane
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Q14721 | MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLEVCDDYSLDDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTKFKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFARSIEMMDIVVEKNGENMGKKDKVQDNHLSPNKWKWTKRTLSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLEDMYNKMAKTQSQPILNTKESAAQSKPKEELEMESIPSPVAPLPTRTEGVIDMRSMSSIDSFISCATDFPEATRFSHSPLTSLPSKTGGSTAPEVGWRGALGASGGRFVEANPSPDASQHSSFFIESPKSSMKTNNPLKLRALKVNFMEGDPSPLLPVLGMYHDPLRNRGSAAAAVAGLECATLLDKAVLSPESSIYTTASAKTPPRSPEKHTAIAFNFEAGVHQYIDADTDDEGQLLYSVDSSPPKSLPGSTSPKFSTGTRSEKNHFESSPLPTSPKFLRQNCIYSTEALTGKGPSGQEKCKLENHISPDVRVLPGGGAHGSTRDQSI | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain . Plays also a role in the regulation of exocytosis independently of its electrical function (By similarity). Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization . Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes . Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells (By similarity). Channel properties are also modulated by cytoplasmic ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels (By similarity). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the slowly inactivating delayed-rectifier voltage-gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle cells. Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation. Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus (By similarity). Contributes to the regulation of glucose-induced action potential amplitude and duration in pancreatic beta cells, hence limiting calcium influx and insulin secretion . Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells. May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval. Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury. May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions (By similarity). Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits . Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose-induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner (By similarity).
PTM: Phosphorylated. Differential C-terminal phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating in hippocampal neurons. Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities. Tyr-128 can be phosphorylated by Src and dephosphorylated by cytoplasmic form of the phosphatase PTPRE. CDK5-induced Ser-607 phosphorylation increases in response to acute blockade of neuronal activity. Phosphorylated on Tyr-128 by Src and on Ser-805 by MAPK14/P38MAPK; phosphorylations are necessary and sufficient for an increase in plasma membrane insertion, apoptotic potassium current surge and completion of the neuronal cell death program. Phosphorylated on Ser-520, Ser-607, Ser-656 and Ser-805 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation. The Ser-607 phosphorylation state differs between KCNB1-containing clusters on the proximal and distal portions of the axon initial segment (AIS). Highly phosphorylated on serine residues in the C-terminal cytoplasmic tail in resting neurons. Phosphorylated in pancreatic beta cells in response to incretin hormones stimulation in a PKA- and RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell survival. Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5; levels then increase to reach adult levels by P14. Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-656 and Ser-720 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties. Dephosphorylation by phosphatase PTPRE confers neuroprotection by its inhibitory influence on the neuronal apoptotic potassium current surge in a Zn(2+)-dependent manner. Dephosphorylated at Ser-607 by protein phosphatase PPP1CA. Hypoxia-, seizure- or glutamate-induced neuronal activity promote calcium/calcineurin-dependent dephosphorylation resulting in a loss of KCNB1-containing clustering and enhanced channel activity. In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-720 are less dephosphorylated. In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced. Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein kinases and tyrosine phosphatase PTPRE in primary Schwann cells and sciatic nerve tissue (By similarity). Phosphorylation at Ser-593 of the FFAT motif activates interaction with MOSPD2, VAPA and VAPB .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95878
Sequence Length: 858
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.
Subcellular Location: Cell membrane
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P15387 | MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLQVCDDYSLEDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTKFKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFARSIEMMDIVVEKNGESIAKKDKVQDNHLSPNKWKWTKRALSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLEDMYSKMAKTQSQPILNTKEMAPQSKPPEELEMSSMPSPVAPLPARTEGVIDMRSMSSIDSFISCATDFPEATRFSHSPLASLSSKAGSSTAPEVGWRGALGASGGRLTETNPIPETSRSGFFVESPRSSMKTNNPLKLRALKVNFVEGDPTPLLPSLGLYHDPLRNRGGAAAAVAGLECASLLDKPVLSPESSIYTTASARTPPRSPEKHTAIAFNFEAGVHHYIDTDTDDEGQLLYSVDSSPPKSLHGSTSPKFSTGARTEKNHFESSPLPTSPKFLRPNCVYSSEGLTGKGPGAQEKCKLENHTPPDVHMLPGGGAHGSTRDQSI | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain . Also plays a role in the regulation of exocytosis independently of its electrical function . Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization . Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel . Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes . Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells . Channel properties are also modulated by cytoplasmic ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels . In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the slowly inactivating delayed-rectifier voltage-gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle cells . Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation . Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus (By similarity). Contributes to the regulation of glucose-induced action potential amplitude and duration in pancreatic beta cells, hence limiting calcium influx and insulin secretion . Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells . May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval (By similarity). Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury . May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions . Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits (By similarity). Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose-induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner .
PTM: Phosphorylated . Differential C-terminal phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating in hippocampal neurons . Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities . Tyr-128 can be phosphorylated by Src and dephosphorylated by cytoplasmic form of the phosphatase PTPRE isoform 2 . CDK5-induced Ser-607 phosphorylation increases in response to acute blockade of neuronal activity . Phosphorylated on Tyr-128 by Src and on Ser-804 by MAPK14/P38MAPK; phosphorylations are necessary and sufficient for an increase in plasma membrane insertion, apoptotic potassium current surge and completion of the neuronal cell death program . Phosphorylated on Ser-520, Ser-607, Ser-655 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation . The Ser-607 phosphorylation state differs between KCNB1-containing clusters on the proximal and distal portions of the axon initial segment (AIS) . Highly phosphorylated on serine residues in the C-terminal cytoplasmic tail in resting neurons . Phosphorylated in pancreatic beta cells in response to incretin hormones stimulation in a PKA- and RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell survival . Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5; levels then increase to reach adult levels by P14 . Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties . Dephosphorylation by phosphatase PTPRE isoform 2 confers neuroprotection by its inhibitory influence on the neuronal apoptotic potassium current surge in a Zn(2+)-dependent manner . Dephosphorylated at Ser-607 by protein phosphatase PPP1CA . Hypoxia-, seizure- or glutamate-induced neuronal activities promote calcium/calcineurin-dependent dephosphorylation resulting in a loss of KCNB1-containing clustering and enhanced channel activity . In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated . In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced . Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein kinases and tyrosine phosphatase PTPRE in primary Schwann cells and sciatic nerve tissue (By similarity). Phosphorylation at Ser-593 of the FFAT motif activates interaction with MOSPD2, VAPA and VAPB (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95637
Sequence Length: 857
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.
Subcellular Location: Cell membrane
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Q8L9C4 | MEICTYFKSQPTWLLILFVLGSISIFKFIFTLLRSFYIYFLRPSKNLRRYGSWAIITGPTDGIGKAFAFQLAQKGLNLILVARNPDKLKDVSDSIRSKYSQTQILTVVMDFSGDIDEGVKRIKESIEGLDVGILINNAGMSYPYAKYFHEVDEELINNLIKINVEGTTKVTQAVLPNMLKRKKGAIINMGSGAAALIPSYPFYSVYAGAKTYVDQFTKCLHVEYKKSGIDVQCQVPLYVATKMTKIRRASFLVASPEGYAKAALRFVGYEAQCTPYWPHALMGAVVSALPESVFESFNIKRCLQIRKKGLQKDSMKKE | Function: Beta-ketoacyl-coenzyme A reductase required for the elongation of fatty acids precursors of sphingolipids, triacylglycerols, cuticular waxes and suberin. Responsible for the first reduction step in very long-chain fatty acids (VLCFAs) synthesis. Decreased expression of KCR1 (RNAi) leads to plants with fused vegetative and reproductive organs, and abnormal trichome, epidermal cell and root morphology. Cannot be complemented by KCR2.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35762
Sequence Length: 318
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.330
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Q9FYL6 | MQGACISESQPWYLHFVCFIGFLFLLRVLFIPLLKWFTTRFLLTPKRLKRYGSWAMVTGATEGIGRAFAHELAKHGLNLILVSRNLSKLESVSDDFQQEFPHIKIKIIPFDFSSEGGYGAIEEGIKGLEVGILINNVGITYPRAMFFHEVDQLTWTKILRVNLEATTWVTRSLIGPMLHRRRGAIVNISSGAAVVVPSHPLYAIYAATKAYVDALSRSLHVEYKQFGIDVQCQVPLYVSTRMVSEVAAIDKPSLFVPSPEVYAKAAVAQIGIGSRCSPFWAHSLQWFLVGLVPDNLVDTWRLSIGLRRRSLS | Function: Probable reductase, but unlike KCR1, has no beta-ketoacyl-coenzyme A reductase activity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35012
Sequence Length: 312
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.-.-.-
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Q84568 | MLVFSKFLTRTEPFMIHLFILAMFVMIYKFFPGGFENNFSVANPDKKASWIDCIYFGVTTHSTVGFGDILPKTTGAKLCTIAHIVTVFFIVLTL | Function: Potassium-selective channel essential in the virus replication cycle. May be involved in preventing multiple infections (Potential).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10620
Sequence Length: 94
Subcellular Location: Membrane
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Q8VY84 | METPIDAPNKDEHECPRWKKSTVVFVLGGPGSGKGTQCANVVKHFSYTHFSAGDLLRAEIKSGSEFGAMIQSMIAEGRIVPSEITVKLLCKAMEESGNDKFLIDGFPRNEENRNVFENVARIEPAFVLFFDCPEEELERRIMSRNQGREDDNIETIKKRFKVFVESTLPIISYYESKGKLRKINAAKSSEEVFEAVRVLFASET | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 23047
Sequence Length: 204
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Cytoplasm
EC: 2.7.4.14
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O51154 | MIIAIDGPSASGKSSIARELGVRLNYKFISSGHLYRIITLIAQRSLMNSCDFISEDSLLNLILENDISFNNFAFLLNGENVENQILNDKIDFQVSFYSSYVGIRNIVNKKLREVVKFSDDNYIIEGRDITTVVFPESEFKIYLDASVKVRALRRYKQRNGNETLEELERTLKRRDDVDKKKQYGKLKLSKGVFYLDTSYKGLDDVCNIIIEKFNLKKVRER | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25602
Sequence Length: 221
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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O17622 | MYNVVFVLGPPGSGKGTICTQIHENLGYVHLSAGDLLRAERERAGSEYGALIEGHIKNGSIVPVEITCALLENAMIASKDANGFLIDGFPRNEDNWSGWNKQMGGKVNEQFVLFLSCPVDVCIDRCLHRGQGRTDDNVESLKKRVETYNQSTFPIIEHFEKVGMVREVNSERPVTEVYEDVVKVFAAANQK | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 21202
Sequence Length: 191
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and disassembling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis (By similarity).
Subcellular Location: Cytoplasm
EC: 2.7.4.14
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P43892 | MIITVDGPSGAGKGTLCYALAEKLGYALLDSGAIYRVTALAALQRKTDLTNETDLAELARHLDIQFIPQNGEVSILLAGMDVSRLIRTQEVADAASKVAVFQKVRSALLQLQQDFAKNDGLIADGRDMGTVVFPNAQVKLFLDASAEERAKRRYKQLQNKGINGNFAQILAEIKERDFRDRNREVAPLKPADDALLLDSTTLSIDEVIDQALAYIQRXGISFRFNCLFKEE | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25500
Sequence Length: 231
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q5VRN0 | MAHANKNHIESFPPPGKKITIVFVIGGPGSGKGTQCAKIVKQFGFTHLSAGDLLREEAKYDTEQGTMIKNLMNEGKLVSSDLIVKLLFKAMRESGNDKFLVDGFPRNEENRHAYENIIHIEPEFLLFIDCSKEEMERRILNRNQGRDDDNIDTIRRRFDVFQQQTLPVIQYYEKRGKLRKVDGNRQVDEVFEDVKAIFAQLNNQKIHGGQQASGLSRAQMNPLKRWFFDFFCGCFGTKEEARN | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 27947
Sequence Length: 243
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Cytoplasm
EC: 2.7.4.14
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Q6NMK6 | MWRRVALLSPMISSSSRSLKLSQAASGLKVGESFATDIISQEERVSPPKEKAPFITFVLGGPGSGKGTQCEKIVETFGLQHLSAGDLLRREIAMHTENGAMILNLIKDGKIVPSEVTVKLIQKELESSDNRKFLIDGFPRTEENRVAFERIIRADPDVVLFFDCPEEEMVKRVLNRNQGRIDDNITTMKKRLKIFNALNRPVIDYYKNKGKLYTINAVGTVDDIFQHVLPIFNSFEQLKESSHVNPQSHLGSSLVENSS | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 29045
Sequence Length: 259
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Cytoplasm
EC: 2.7.4.14
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O51759 | MKIALSGKSGCGNTTVSGMIAKHYGLEFINYTFHDIAREHNIPFSEFYEKEIIGRNDYYWDKYLDNRLSVLSRKNNTVLASRLAIWISKSADLKIYLYAKMEVRAERIMTREGGMYSDVLSSTFIRDENDKKRYLAIYNIDIDDYFSETDLVIDVTNINPNEVFELIRDEIDKRNLKKNS | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 21066
Sequence Length: 180
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q1MPW3 | MEQHTIITIDGPAGVGKSTLAKKLGTILNLPYLDTGAMFRKLALQLGNKAETLPDSILQEQCKKVTFQLQGVGKNSLLMCNGESIGHEIRSETAGILAAQLGERTIIREYLKNIEQQIGNTMSIIAEGRDLGTEVFPKAQFKFFIDANPIIRAQRRFNQLKKEGIFQDYNDILHSINYRDKLDKNRTIAPLEPAKDAILIDSSIMDIDSILKIMLNYITIPHLSQ | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25167
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q6AGF7 | MTEPATPPVVLAVDGPAGSGKSSVSKAAAGRLGWAYLDTGAAYRALGWYVVERGLDPADPAVVIDSLPDFDYRIGTDPDTYRVFVGERDVTEAIREPRVTAVVSAIARVPQVRASLTRLFREIIAGSGKAGIVVEGRDITTVVCPDALVRILLTADEAVRMNRRSAELTGHSAARVGEALRKRDAADSRVVDFMNAAEGVITVDSTELDFDQTVDAVIAVVQKETHV | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24203
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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O59845 | MPTIIDKLSDALHLHSHQSTFDSKVTVIFVLGGPGAGKGTQCARLVEDFSFSHLSAGDLLRAEQHREGSEYGQLIQTCIKEGSIVPMEVTVKLLENAMTATLAERRSGEGWTDGQGRFLIDGFPRKMDQAEKFEHDVGKATAVLFFSTTQEVMLDRLLERGKTSGREDDNVESIKKRFNTYKEQTMPVIEHYEKLGKVIEIDSSVSIEEVHQKTRSAVAKLLSGSTA | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors, but can also use AMP and dCMP to a lesser extent. May play a role during the formation of basidiospores in the gill tissue.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 25157
Sequence Length: 227
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon GTP binding. Assembling and disassembling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis (By similarity).
Subcellular Location: Cytoplasm
EC: 2.7.4.14
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Q8F6P4 | MNENVIALDGPAGSGKSTVARQIAEKIGFNYLDTGAFYRALTLYLFRLYQTSPNNRFEEWVKTSEAERSLSQIRIVCEFSAGNENRILLDGEDVSLAIRTPEITREIKHIANRRIYRDFVNKELHSLAKLHKLIMDGRDIGTEVFPDAKFKFYLTASSKVRAERRFLQLQEQGIFADRNEIEKEIILRDKSDMEREIAPLYQAKDAILIDTDILSKNSVISKILEILDQ | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 26345
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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B1MYB3 | MSHNFQIAIDGPASAGKSTIAKILATNLKYVYVDTGAMYRTMTLAAKQAGLAYEDEQGVVDLLAKTVIRFEPGVPTQRVFLNDSEVTEAIRSTEVTNNVSLIASYKAVRADLVRRQRDIANSQNVIMDGRDIGTTVLPNAQVKIFLVASVLERAERRYKENKAKGMTVDLETLKSDIETRDYKDSHRAISPLIQAKDAILVDTTGQSIQAVVSEITKIIEKKQKP | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24826
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q02CZ9 | MADTKQKRVVVAIDGPAGAGKSTIAKGLASRLGFIYIDTGAMYRAVALWALRQGVDSGDMHRMEQLAMAAQIELGPGTISLNGEDVTQAIRTPEVSNGASKIGVIPGVRRAMVAKQREIGERTSVVMEGRDIGTVVFPQADVKIFLDANPDERVRRRYQEIRTKEDPPPISQGQLAAEMKERDMRDSTRADAPLAQAPDAVYLDSTALSIAEVEEAILKIVRSRVTNGRDFS | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25177
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q8A712 | MKEIKLILTDIDGVWTDGGMFYDQTGNEWKKFNTSDSAGIFWAHNKGIPVGILTGEKTEIVRRRAEKLKVDYLFQGVVDKLSAAEELCNELGINLEQVAYIGDDLNDAKLLKRVGIAGVPASAPFYIRRLSTIFLEKRGGEGVFREFVEKVLGINLEDFIAVIQ | Cofactor: Binds 1 magnesium ion per subunit.
Function: Involved in the biosynthesis of 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid used in cell-wall polysaccharides . Catalyzes the hydrolysis of 2-keto-3-deoxy-D-glycero-D-galacto-9-phosphonononic acid (KDN-9-P) to yield 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN) . Also able to hydrolyze N-acetylneuraminate-9-phosphate (Neu5NAc-9-P), 2-keto-3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P), phosphoenolpyruvate (PEP), gluconate 6-phosphate, tyrosine phosphate ester and glucose-6-P as substrate .
Catalytic Activity: 3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate 9-phosphate + H2O = 3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate + phosphate
Sequence Mass (Da): 18340
Sequence Length: 164
EC: 3.1.3.103
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D4GSE6 | MTALVTFGETMLRLSPPRGERLETARELEVQAGGAESNVAVAAARLGRDAAWFSKLPDSPLGRRIVSELRSHSVDTDGVVWTDDADARQGVYYLEHGASPRPTNVVYDRADAAVTTLETGEFDLDAVRDAEVCFTSGITPALSETLSETTADVLDEAQNAGTTTAFDLNYRTKLWSPDEAAEVYRDLLDSVDLLFAAERDAATVLGRDGDAESVARGLADDYDIETVVVTRGEEGSLAVSDGAVSEQGVYETETYDAIGTGDAFVGGFLAKHLDGGSVTESLEWASATASFKRTVEGDIAVVTPEDVERVVAEEGDGISR | Function: Involved in the degradation of glucose via the semi-phosphorylative Entner-Doudoroff pathway. Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). Also catalyzes efficiently the phosphorylation of 2-keto-3-deoxygalactonate (KDGal) to 2-keto-3-deoxy-6-phosphogalactonate (KDPGal).
Catalytic Activity: 2-dehydro-3-deoxy-D-gluconate + ATP = 2-dehydro-3-deoxy-6-phospho-D-gluconate + ADP + H(+)
Sequence Mass (Da): 34083
Sequence Length: 320
Pathway: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 1/2.
EC: 2.7.1.178
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Q8A519 | MNTEILGVVAQVALMVILAYPLGRYIAKVYKGEKTWSDFMAPIERVIYKVCGIDPKEEMNWKQFLKALLILNAFWFVWGMVLLVSQGWLPLNPDGNGPQTPDQAFNTCISFMVNCNLQHYSGESGLTYFTQLFVIMLFQFITAATGMAAMAGIMKSMAAKTTKTIGNFWHFLVVSCTRILLPLSLIVGFILILQGTPMGFDGKMKVTTLEGQEQMVSQGPAAAIVPIKQLGTNGGGYFGVNSSHPLENPTYLTNMVECWSILIIPMAMVLALGFYTRRKKLAYSIFGVMLFAFLVGVCINVSQEMGGNPRIDELGIAQDNGAMEGKEVRLGAGATALWSIVTTVTSNGSVNGMHDSTMPLSGMMEMLNMQINTWFGGVGVGWMNYYTFIIIAVFISGLMVGRTPEFLGKKVEAREMKIATIVALLHPFVILVFTAISSYIYVYHPDFVESEGGWLNNLGFHGLSEQLYEYTSCAANNGSGFEGLGDNTYFWNWTCGIVLILSRFLPIIGQVAIAGLLAQKKFIPESAGTLKTDTLTFGIMTFVVIFIVAALSFFPVHALSTIAEHLSL | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62318
Sequence Length: 568
Subcellular Location: Cell inner membrane
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Q89FC2 | MTMIGWLQIILFCVIIVALTKPLGWYMTRVFNGERTFLSPVLRPIEAGIYWISGVDERREQHWLTYTVAMLLFHVGGFLVIYGVMRLQAVLPFNPAGQSAVAQDLSFNTAISFITNTNWQNYGGESTLSYLVQMLGLTHQNFLSAATGIALAMALIRGFSRASVRTVGNFWVDVTRCTLYVLLPICVVYTLFLVWQGIPQTLGDYVEATTLEGAKQTIAVGPVASQVAIKMLGTNGGGFFNANAAHPFENPTALSNFVQMLSIFALGAALTNVFGRMVGNQRQGWAILAVMGVLFVAGVAVTYWAEANGTSTMHALGLTGGNMEGKEVRFGLVASSLFAVITTAASCGAVNAMHDSFTALGGMIPLINMQLGEIIVGGVGAGLYGMLLFVVLAIFVAGLMVGRTPEYVGKKIEAREVKMAMLAILVLPLMYLGWTAVGVVYPAAVASMANAGPHGFTEVLYAFTSATGNNGSAFAGLTGNTLFYNLTLASAMFVGRFFMIVPAMAIAGSLAAKKSIPPSAGTFPTTGGLFVGLVVGVILIIGGLTFFPALALGPIVEHLAMNAGQVF | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60065
Sequence Length: 567
Subcellular Location: Cell inner membrane
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Q8YPE8 | MGQGLLQIGLTLCIVIAITPVLGRYIARVFLGERTILDRVMNPIERSVYVISGVRPKDEMTGWQYIRAILYTNLFMGILVYSLIYFQRLLPWNPNGLGVPSWDIVLHTVISFVTNTDQQHYAGETTLSYFSQVAALGFLMFTSAATGLAVGIAFIRGLTGRKLGNFYVDLTRGITRILLPISVIGAIALVLLGVPQTIGETLTITTLEGGTQYIARGPVASFEMIKMLGENGGGFFAANSAHPFENPNGLTNLIETIAMIAIPAAMIYTYGVFAKNIKQAWLLFWMVFIVFVILVWVAAGGELQGNPLVNGTLGIEQPNLEGKEVRFGWAETALWAVMTTATMCGAVNGMHDSLMPQGLFATLFNLFLQIIWGGQGTGTAYLFIYLILTVFLTGLMVGRTPEIFGRKIEKREIVLASLILLIHPIVVLIPSAIALAYPFSLSGISNPSFHGISQVVYEYASASANNGSGLEGLTDNSLWWNLSTSLSILTGRYVPIIAMLLLADSMSRKQTVPQTPGTLKTDSLIFTTVTAGIVLILGVLTFFPVLALGPIAEGFKLASGS | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60723
Sequence Length: 561
Subcellular Location: Cell inner membrane
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Q88FD7 | MHSYDFALLLAFFVIVLLPAPWLGRFYYKVMEGQRTWLTPVLGPVEQGCYRLAGVNASQEQNWRQYTLALLAFNLVGFLLLFAVLLLQGYLPLNPQNLPGQEWSLAFNTAVSFVTNTNWQAYSGEASVSYLSQMLGLTVQNFVSPATGLAVLVVLCRGIARRSATTLGNFWVDMTRATLYGLLPLCLLLALLLVWQGVPQTFADYAHALTLQGADQTIPLGPAASQIAIKQLGTNGGGFFGVNSAHPFENPTAWSNLFEVASIILIPVALVFTFGHYVKDLRQSRAILACMLALFLIGGSTALWSEHQPNPALESTQVQQTAPLEGKESRFGTTGSVLWAVTTTAASNGSVNAMHDSLNPLTGMVAMVNMMVGEVIFGGVGAGLYGMLLFVLIAVFLAGLMIGRTPEYLGKKLQAREVQLLVATLLVMPVGVLVLGAIAASLPGPAGAVTNPGAHGFSQLLYAYTSGSANNGSAFAGFGANTVYHNLMIGLAMLIGRFGYILPILALAGSLAAKKSAPLGQNSFPTHGPLFTGLLLVTILLVGGLTFLPTLALGPIAEHLSLGF | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59879
Sequence Length: 564
Subcellular Location: Cell inner membrane
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Q8R8I6 | MKRKREIKTWSREIVVGAIKNSFIKLNPLYMYKNPVMFVVEVGTFITLLATIFPTYFGSTPDEVGYNALVTFILFVTVLFANFAESLAEGRGKAQAETLRKTKKETMAKLVQSDGSIKIVKSSELKKGDIVICEAGDIIPADGEIIEGLAAIDESAITGESAPVIKEAGGDFSSVTGGTKVISDRIKIRVTVDEGESFLDRMIKLVEGAKRQKSPNEIALTTVLVSLTIIFIVVVMTLYPMAKFVHVRISAATMIALLVCLIPTTIGGLLSAIGIAGMDRVTRFNVIAMSGKAVEAAGDIDTILLDKTGTITFGNRLAADFIPVGGHSKEEVTYYALISSLKDLTPEGRSIVDLARKMGAKAPDDILEGAEVVEFSAETRMSGLNLKDGTIVRKGSYDKVKEYIGEKGGSIPDDLDKEVEKISLLGGTPLVVVKDNEVLGVIYLKDTIKPGMKERFKQLRAMGIKTIMITGDNPLTAKTIAEEAGVDEFIAESKPEDKINVIKREQAQGRLVAMTGDGTNDAPALAQADVGLAMNSGTMAAKEAANMVDLDSDPTKIIEVVGIGKQLLMTRGALTTFSIANDVAKYFAILPAIISETLPAIKVLDVMKLSSPTNAILSALIYNAIIIPILIPIAMRGVKYRPMSANALLMRNLLIYGLGGLIAPFVGIKLIDMIISSIFGM | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
Catalytic Activity: ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73136
Sequence Length: 681
Subcellular Location: Cell membrane
EC: 7.2.2.6
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Q9A7X7 | MSSPDIHADQGRRALAGGLSRAVLARAVKEAFLKLDPRQLTGNPVIFATWIVALLATVSAVAAVVGQQPAGFAIQIAVWLWATVVFANLAESVAEGRGKAAADSLRATRVTTKAKLIVDPNTGTWIPTPAHKLGVGEVILVEAGEVIPTDGEIIEGMASVNEAAITGESAPVIRESGGDRSAVTGGTTVVSDWIKMRVTAEAGSTFLDRMIAMVEGADRRKTPNEIALAVLLAGLTLIFLIAVVTLLGPGKFSGVALDPLVLGALFITLIPTTIGGLLSAVGIAGMDRLLKVNVLATSGRAVEAAGDVDTLLLDKTGTITFGNRMATEVIPAPGVRPDAAMKAALMASLADETPEGRSIIELARNAGLALEAPEGATAIPFTAQTRQSGLDHQGRSWRKGAVDAVYRTLGLEPQSIPTELSVAVDRIARSGGTPLAVSEDGVLVGVIHLKDVVKPGVKERFADLRRMGLRTVMITGDNPVTAAAIASEAGVDDFLAEATPEDKLRLIREEQGKGRLVAMCGDGANDAPALAQADVGVAMQTGAQAAREAGNMVDLDSDPTKVIEIVEVGKQMLITRGALTTFSIANDVAKYFAIIPAMFVVSLPALGALNVMKLHSPESAILSAVIFNALVIVALIPLALKGVKYRAVGAGKLLSRNLTLYGLGGLIAPFVGIKLIDLVVSALGLA | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
Catalytic Activity: ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71019
Sequence Length: 686
Subcellular Location: Cell inner membrane
EC: 7.2.2.6
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O32328 | MKSKKSKFITKDILKEAIIESFKKLNPKYMMKNPVMFVVEVGFFVTILLTIFPSIFGDKGHNLRVYNLIVTIILFITVLFANFAESVAEGRGKAQADALKKTRKDTIAKLIGKDGSIKTINANELKKGDVVLVENGDVIPNDGEVVDGVASVDESAITGESAPVMKEPGGDFASVTGGTKVVSDWLKVEITATPGESFLDKMINLVEGASRQKTPNEIALNTILVSLTLIFLIVLVALYPMATYTGVKIPMSTLIALLVCLIPTTIGGLLSAIGIAGMDRVTRFNVIAMSGKAVEACGDVDTMILDKTGTITYGNRLAADFITVGGADKQKLIDYSVMCSLKDDTPEGKSIVELGKQLGITIDTKKYESIEFEEFTAQTRMSGIKLENGTAVKKGAYDAIKKRVQELKGVIPKDLDEAVNKVAKLGGTPLVVCVDNKIYGVIYLKDTVKPGLVERFERLREIGIKTIMCTGDNPLTAATIAKEAGVDGFIAECKPEDKIEAIKKEQDEGKLVAMTGDGTNDAPALAQADVGLAMNSGTTAAKEAANMVDLDSDPTKVLEVVEIGKQLLITRGALTTFSIANDVAKYFAIIPAIFTIAIPKMQLMNIMHLSTPYSAILSALIFNAIIIPALIPIAMKGVKYRPMKSEALLLRNMIVFGFGGIIVPFVGIKIIDMIITPMVRILNLG | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
Catalytic Activity: ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73686
Sequence Length: 685
Subcellular Location: Cell membrane
EC: 7.2.2.6
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Q9RZP0 | MTTAPQPKQSIFSPELVRGAVRASFAKLSPRDQARNPVMFVVYLGTALTAYLTVANLVTGKPWGYELAITLLLLLTVLFANFAEGMAEARGKAQAASLRSAREDVKARRLVNGQEELVAGTALERGDLVVVEAGEMIPADGEIVEGLASVDESAITGESAPVIREAGTDHSGVTGGTKVLSDRIVIQITSGAGESFLDRMIALVEGASRQKTPNEIALSILLSGLTLIFLLAVVTLYPFTVYAGAPASAVTLIALLVCLIPTTIGGLLPAIGIAGMDRALQANVIAKSGKAVEVAGDVDVLLLDKTGTITIGNRMATKFHPLPGVTEAELAKAALLSSLADPTPEGKSIVALARQLGVDAPEPAGAEFIEFTAQTRMSGVDFPGTSIRKGAGSRISALAQERGGQLPPELAAITDEVSRQGATPLTVIENDRLLGVVALSDIIKPGIRERFEQLRRMGLRTVMITGDNPLTAEAIAKEAGVDGFLAEATPEDKMEMIKQEQASGKLVAMMGDGTNDAPALAQADVGLAMNSGTQAAKEAGNMVDLDSDPTKLLEVVEIGKGLLITRGALTTFSIANDVAKYFAILPALFVTAYPQLGVLNVMGLHSPTSAVLSAVIFNALIIPVLIPLALRGVPYQPMSAGALLNRNLLVYGGGGILVPFIAIKLIDLLIGGLMS | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
Catalytic Activity: ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70302
Sequence Length: 675
Subcellular Location: Cell membrane
EC: 7.2.2.6
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Q74AA8 | MKELKPAILMLIIFTILCGGIYPAVVTGIAQAVFPKQAKGSLITDARGREVGSTLIGQPFSGPKYFWPRPSATPEFGYNPAGSGGSNAGPANPAYLKTVGERIKALRDAGIKGSIPADLVQASASGLDPHISPEAAKVQIPRVARARGMSAGALSRLIAAHTEDRQLGFLGEPRINVLALNLALDTLMP | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19738
Sequence Length: 189
Subcellular Location: Cell inner membrane
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Q7NN39 | MSPLQEIGTAVRMTAIFWIGCGLAYPLIFTGFAQVAFPDQANGSLVRNAQNQVIGSSLIGQKFTSERYFHGRPSSIDYKAEASGASQLAPTNKVLIERVKADAAAFEAQNGTKPTIDLVTTPGSGLDPHITPAGAAVQTARVSRARNLAPEQVRKLVSQYTEGRFLGIFGEPRVNVLALNLALDGIRR | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20126
Sequence Length: 188
Subcellular Location: Cell inner membrane
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B0R9M1 | MNRQDLAVPLRLLGVSLLVFGLLYQGSLMAIGDAVFPNSSAGSPVYVDGQEQPVGSQMIGQQFRPGQPEDVQYFWSRPSANDYNAMTSASTNWGPTNPLLSERVRADLQNISQYETPDDSVPVNLVSESGSSYDAHISPAAAEYQVLRVANQTGISEQRLNEMIDEATKEPWLGIWGHERVNVLELNLMVRDALNEQNETDQNSDMNASEIANGDH | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex (By similarity). The Kdp system is essential for growth under K(+) limitation, and for survival under desiccation and salt crystal inclusion .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23768
Sequence Length: 216
Subcellular Location: Cell membrane
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A9AXV2 | MRTFFRPALAAIIIFSVLTGVIYPALVTVIAQVTFPGQANGSLIEQAGQQRGSSLIGQQFDQPEYFWGRLSATGPVPYNAAASSGSNYGPLNPALAEAVQARIDALKAADPSNQLPIPVDLVTASASGLDPEISPAAANYQVQRVAAARGLAVEQVQQLVEQHTSQRTLGVLGEPRVNVLQLNIALDQIKSLD | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20373
Sequence Length: 193
Subcellular Location: Cell membrane
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A4G5J7 | MKSTLRPALVLFAVLTLICGVIYPYAITGIGKLAFSEQAEGSLVSRNGQIVGSSLIGQAFSSPQYFWGRPSATSPMPNNAAASSGSNQGPLNLALIDSVKGRIAALKAADPANTLPVPVDLVTASASGLDPEISLAAAKYQAARIALARKMQLEEVQSIIDRHSKAQYFGFFGEPRVNVLALNLALDQHH | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20017
Sequence Length: 190
Subcellular Location: Cell inner membrane
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A6W6R7 | MSLALTNLLRQARTGLLLLLVATAGLGLVYPLAVFAVGRLVPARADGQVVAVDGQPVGSRLIGQEFPGEQWFQPRPSAAGDGYDPTASGASNLGPESTDLLKAVEERRAAVAAADGTAPVDVAPDALTASGSGLDPHVSPENARRQVARVAAARGLSEQRVAALVAEHTRGRALGFLGEPTVNVLELNLALRSAAP | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20082
Sequence Length: 196
Subcellular Location: Cell membrane
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Q72TM5 | MIFLNIISISIRLLLILTLITGILYPIVTTGFAERFFPFRSSGSRVVIQGKIVGSELIAQKFIKDEYFWPRPSAMDYAAGASNASVTNVFLKAKVEERKKFLLEKHSEQTQVPPDLLFASGSGLDPHISPDSALFQINRVAKSRKLTEGQILRLKNIVEESVEKGYIGENRINVLLLNLKLDSEFGIILK | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21280
Sequence Length: 190
Subcellular Location: Cell inner membrane
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Q8Y3Z8 | MKRFMQIWKPAVIGFLLLTLVCGVLYPGVVTVFAGVAFHDKANGSIIEEKLADGTTGKVGSAEIGQTFTEPEYLIGRAASDGVATNLNPTSEEQKQLVEKRIAWWHKLDPTNNRVIPMDLVTASASGVDPDISEAAAAYQVDRISRERGISTKEVKEIIAEHTSNRLLGFWGEPTVNVLQVNLALDRLKM | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20792
Sequence Length: 190
Subcellular Location: Cell membrane
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Q9PIB8 | MKKMILIAGPCVIESKDLIFKVAEQLKNFNENPNIEFYFKSSFDKANRTSINSFRGPGLEEGLKILQSVKDEFGMKILTDIHESNQANPVSEVADVLQIPAFLCRQTDLLVAAAKTKAKINIKKGQFLNPSDIKYSVKKVLQTRGIEDEGYEAAQRNGVFVAERGASFGYGNLVVDMRSLVIMREFAPVIFDATHSVQMPGAAGGSSGGKSEFVEPLARAAAAVGIDGFFFETHINPCEALCDGPNMLNLTRLKNCVNTLLEIQNIIKENK | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 29780
Sequence Length: 271
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.5.1.55
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Q9PLS0 | MFPNNKMLLIAGPCVIEDNSVFETARRLKEIVAPYSSSVHWIFKSSYDKANRSSLQNYRGPGLKLGLQTLAKIKETFDVEILTDVHSPDEAREAAKVCDIIQVPAFLCRQTDLLVTAGETQAIVNIKKGQFLSPWEMQGPIDKVLSTGNNKIILTERGCSFGYNNLVSDMRSIEVLRRFGFPVIFDGTHSIQLPGALQSQSGGQTEFIPVLTRSAIAAGVHGLFIETHPNPASALSDAASMLSLKDLERLLPSWVQLFTYIQEMDTVSI | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 29701
Sequence Length: 269
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.5.1.55
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Q9Z7I4 | MFNNKMILIAGPCVIEGEDITLEIAGKLQSILAPYSDRIQWFFKSSYDKANRSSLNSFRGPGLTEGLRILAKVKETFGVGILTDVHTPQDAYAAAEVCNILQVPAFLCRQTDLLVATAETGAIVNLKKGQFLSPWDMEGPINKVLSTGNNKILLTERGCSFGYNNLVSDMRSIPVLSRSGFPVIFDATHSVQLPGALSTESGGLTEFVPTLSRAALAAGAHGLFIETHTNPKIAKSDAASMLSLEEFAALLPTWDQLFTCVSSFDMVSA | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 28994
Sequence Length: 269
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.5.1.55
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C1A8V7 | MPVLAVIPARLGATRLPRKPLRLLGGEPIVVRVYQRVVQLGVADHCVVATDHPEVQEACARHGIPVVMTRADHPSGTDRVAEVAAQPEFSSFDVLLNVQGDEPFVSREALAGAVEIVTSGLAPIGTAAVPVSVDTLQRPDVVKVVCADDRRALYFSRAAIPFLRDASDAAVLAPLVRQHVGVYAYARQALQQWVSWPPHPLELIERLEQLRPLAHGLSIGVTTVAATEGGIDTEDDLVRANTHWDVLHAANSSAYRSA | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27764
Sequence Length: 258
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q74BY2 | MNITAIIPARFASTRFPGKALADIAGKPMVQHVYERTARARLVSEVVVATDDDRIAQAVRGFGGRVEMTSRDHETGTDRLAEVASRIGAEIIVNVQGDEPLIEPAMIDEAIAPLAENPAVRMGTLKSRIRTLHDFLSPNVVKVVTDLEGYALYFSRSPLPFFRDKWNDLKDESFASGRLLCYKHVGLYVYRRDFLMEFAKMPPTALELAEKLEQLRALENGCRIRVVETAHESIGVDTPNDLEKVLEKLK | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27966
Sequence Length: 250
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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P44490 | MSFTVIIPARFASSRLPGKPLADIKGKPMIQHVFEKALQSGASRVIIATDNENVADVAKSFGAEVCMTSVNHNSGTERLAEVVEKLAIPDNEIIVNIQGDEPLIPPVIVRQVADNLAKFNVNMASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSVIPYDRDQFMNLQDVQKVQLSDAYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVELAKEVPAVGVDTAEDLEKVRAILAAN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28255
Sequence Length: 254
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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A5CVZ7 | MNFSVIIPARYASSRLPAKLLRDVHGKPLIQLTYENAVNSGANRVIIATDDKRIEVVANDFGAITCMTDGHFTSGTLRIAQVLEKLDINDDEIIVNVQGDEPMLDPSVIDQVVNNLATNPMQIATLCKQITDKAQYFDPNCVKVVFNKIGKALYFSRATIPFFREARDFDLKLCYKHIGVYAYRAGVIKQYLTMNSSSYEKVEKLEQLTALNEGFDIHVAPACASVGHGVDIQRDLDEVRKELG | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27214
Sequence Length: 244
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q7MJ10 | MSFTVVIPARYQSTRLPGKPLADIAGKPMVQWVYEQAIQAGAQDVIIATDDQRVADAVAVFGGKVCMTSPNHESGTERLAEVVQLMGIADDHIVVNVQGDEPLIPPSIIRQVAENLAASSAPMATLGVAITSEEEVFNPNAVKVVTDKEGYALYFSRATIPWDRDAFARGEVLTEHSLMRHIGIYAYRAGFINTYVNWQPSSLEKIECLEQLRVLWYGEKIHVELAKEAPPAGVDTPEDLELVRKIIAAKS | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27514
Sequence Length: 251
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q8D2V1 | MEFIVIIPARFFSKRFPKKPLININGKPMIIHTIENAKKSGASRVIVVTDNNEIYSLVNKNGIEVLLTKKEYNSGTERLIEAIEKFKIKDNQIIVNLQVDEPFLNSDNIFNVAKKLKEKNLIVSTLAIPILNKKEIFDKNIVKVVIDINGYALYFSRSVIPWCENYNSYYIKNNFLKHVGIYAYYAKFVRLYSNYNSSKLEKMENLEQLRILWYGKRIYVSVENIKNCFSINTPSDMLNIKSF | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28341
Sequence Length: 243
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q3BTC6 | MTPTTPADFVVAIPARYASTRLPGKPLQRIGDRPMIQHVTERALLAGAREVWVATDDARIAAAIEHLPGVHVAMTGAAHLSGTDRLAECARIAGWDDQTCVVNLQGDEPFAPAAGIRAVADLLQHSGAQMATLAAPVDNAHDLFDPNVVKLVRTAGGDALYFSRAPIPWHRDSFASQRDSVPAEGQWLRHIGIYAYRAGFLQRFAAMPPGMLERIESLEQLRVMEAGYRIAVAVTPEPFPPGIDTPDDLVRAQVRVASP | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27977
Sequence Length: 259
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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A6TEY9 | MAGSDLLLAGVLFLFAAVIAVPLASRLGIGAVLGYLLAGIAIGPWGLGFISDVDEILHFSELGVVFLMFIIGLELNPAKLWRLRSSIFGVGAAQVMLSAAILGGLLMTTGFSWQAAVVGGIGLAMSSTAMALQLMREKGMSRSEAGQLGFSVLLFQDLAVIPALALVPLLAGSADEHVNWLTVGMKVLAFAGMLIGGRYLLRPVFRFIASSGVREVFTAATLLLVLGSALFMEALGLSMALGTFIAGVLLAESEYRHELEIAIDPFKGLLLGLFFISVGMALNLGVLYTHLLWVAVSVAVLVAVKMLVLYLLARLYGLRSSERMQFAGVLSQGGEFAFVLFSLPASQRLFLHDQMALLLVAVTLSMMTTPLLMKGIDKLLSRRLNPADDTGEAPWVEDDKPQVIIVGFGRFGQVIGRLLMANKMRITVLERDISAVNLMRNYGYKVYFGDATQLELLRSAGAEEAQSIVITCNEPEDTMRLVEMCQQHFPHLHILARARGRVEAHELLQAGVTQFSRETFSSALELGRKALITLGMHPHQAQRAQLHFRRLDMRMLRELMPVHTDTVQISRVREARRELEEIFQREMQKESRQLDGWDEFE | Function: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65945
Sequence Length: 601
Subcellular Location: Cell inner membrane
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P44933 | MSQLANPELMKVVILLASSVTIVPLFKRLGLGSVLGYLVAGCLIGPSVFGIVQEPTAVVHLAELGVVMFLFIIGLEMYPERLWAMRKAIFGRGLLQVGLCGCLLTFSGIYLLGLTKEVSFIAGMGFTLSSTAIVMQSLEERGLTSTSKGQRVISTLIFEDIAIVPLLASVAFLAPHSKEATPHTDWVSIGIALSAVVGLIVTGKWLMNPLFRLISKARIREMMTAGALLVVLGAALAMEIGGLSMAMGAFVAGVMMSESAFRHQLEADIEPFRGLLLGLFFMGVGMSLDLHLVFNHWILLLGIVFLYILGKASAVYIIARITRLDHREAIGRMSLMAHGGEFAFVLFSAAATAEVISNEEQATFTAAVIISMLFSPIIAQIARKLIQRTEPKHLDQLDENDLDTIVDLEDNVLVIGFGRFSQIVCQTLLIRGISVSVIDRNIENIRAAAKFGFKVYYGDGIRLDVLRAAGIEKAKCVVLGINDTQRIEHIVSQMKEAYPNLPILTRTYDRKTTVSLIKQDVDFIVRETFESAITLSRATLMKLGIDKIEAEEIIKEVRTLDQERLNEEVLHGFSNEIVKKYWTPRPFIKPHLDTKALNKETEEILSEKIEEEISNDHS | Function: Transport system that facilitate potassium-efflux, possibly by potassium-proton antiport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68077
Sequence Length: 618
Subcellular Location: Cell inner membrane
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Q9Z2Y0 | MFYIQSSEALQILKNSLRKHLPESLKVYGTVFHMNQGNPFKLKAVVDKWPDFNTVVIRPQEQDMTDDLDHYNNTYLIYSKDPKHCQEFLGSSDVINWKQHLQIQSSQADLGKVIENLGATNLGKVKHKQCFLYMVSHTAKKLTPSLVDAKHLVVSSEKPTPFDHQLFKFARLDVKHAALVNSIWYFGGNEKSQKFIERCIFTFPSVCIMGPEGTPVSWALMDHTGELRMAGTLPKYRHQNLIYHVAFHQVHTLEKLGFPMYLHVDKVNLTIQRMSAVLGHVPMPCTWNQWNWVPL | Function: Acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines (By similarity).
Catalytic Activity: an acyl-CoA + glycine = an N-acylglycine + CoA + H(+)
Sequence Mass (Da): 34016
Sequence Length: 295
Subcellular Location: Cytoplasm
EC: 2.3.1.13
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P43614 | MAGIKLTHKLYQYYQLATSFLYAALLIRWLILMPLVGSRFLPGGIHEFLIYLMFYSSIMEVIWLLRFHGFKYGLLSRTFLKDLNFIYLVSVIHFYDDYEHALILKNASYSSFIISLSLSQAYCHWCKLFKRKGVKERTLVWKVNTFVTLPILYLSEFALLLLNIQVKNYHSTPTLDIINRVVLLAYFPVLLTAYKKLLTK | Function: Involved in the biosynthesis of (1->6)-beta-D-glucan polymers of the cell wall. Required for viability. Involved in maintaining chromosome stability.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23555
Sequence Length: 200
Subcellular Location: Endoplasmic reticulum membrane
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O13994 | MALFRRPNWSALFEKIFIQKSFLGFCSLRVGCEIIIWFAIINKVSGLYGIVSLFQNSDASPWQVLMYVSSVLMLILFSWLAIHIPKSSVPHALILFYVYLIDFLLNVLFTVLFALSWFSKLVQSDSSSTEESADSDPSPSLLYLFFQAESIPSLLLLIFFASLKFYFVLITLSYSNKLIVDSGIRPQNLPPNFSGRVTRLLMKPYIMAANRSYLRNHTKRFTDSIELEQRLMDEVV | Function: Regulatory component of the inositol phosphorylceramide (ICP) synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis. Helps the medial Golgi localization of IPC synthase in a COPI vesicle-dependent manner (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27112
Sequence Length: 236
Subcellular Location: Golgi apparatus membrane
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Q06346 | MRSSLLTLPKSFLGFMPLYLAVEIVLGISILNKCSGAYGILALFTGHPLDFMQWIAYLWSVFTLIVFSQGLYLIHKPNLLVFSQICVLYTIDTISTCFFTLWFTTQWFTLEDTANIDGNNALQSNPISTGKLTERGIDISKQSATESYEYTMTILITLVSLIFRFYFNFILASFVQELLHHPKYLVDRDDVEQNLKNKPIWKRLWAKSQKGCYKLCKNLLE | Function: Regulatory component of the inositol phosphorylceramide (ICP) synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis. Helps the medial Golgi localization of IPC synthase in a COPI vesicle-dependent manner.
PTM: The precursor protein is cleaved into two polypeptide chains, KEI1N and KEI1C. The cleavage is performed in the Golgi apparatus by the KEX2 protease which recognizes residue Arg-135. Generation of KEX2 cleavage site may have been an accidental event in evolution without specific advantages or disadvantages in IPC synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25484
Sequence Length: 221
Subcellular Location: Golgi apparatus membrane
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P23276 | MEGGDQSEEEPRERSQAGGMGTLWSQESTPEERLPVEGSRPWAVARRVLTAILILGLLLCFSVLLFYNFQNCGPRPCETSVCLDLRDHYLASGNTSVAPCTDFFSFACGRAKETNNSFQELATKNKNRLRRILEVQNSWHPGSGEEKAFQFYNSCMDTLAIEAAGTGPLRQVIEELGGWRISGKWTSLNFNRTLRLLMSQYGHFPFFRAYLGPHPASPHTPVIQIDQPEFDVPLKQDQEQKIYAQIFREYLTYLNQLGTLLGGDPSKVQEHSSLSISITSRLFQFLRPLEQRRAQGKLFQMVTIDQLKEMAPAIDWLSCLQATFTPMSLSPSQSLVVHDVEYLKNMSQLVEEMLLKQRDFLQSHMILGLVVTLSPALDSQFQEARRKLSQKLRELTEQPPMPARPRWMKCVEETGTFFEPTLAALFVREAFGPSTRSAAMKLFTAIRDALITRLRNLPWMNEETQNMAQDKVAQLQVEMGASEWALKPELARQEYNDIQLGSSFLQSVLSCVRSLRARIVQSFLQPHPQHRWKVSPWDVNAYYSVSDHVVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCLACDNHALQEAHLCLKRHYAAFPLPSRTSFNDSLTFLENAADVGGLAIALQAYSKRLLRHHGETVLPSLDLSPQQIFFRSYAQVMCRKPSPQDSHDTHSPPHLRVHGPLSSTPAFARYFRCARGALLNPSSRCQLW | Cofactor: Binds 1 zinc ion per subunit.
Function: Zinc endopeptidase with endothelin-3-converting enzyme activity. Cleaves EDN1, EDN2 and EDN3, with a marked preference for EDN3.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 82824
Sequence Length: 732
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q9EQF2 | MGPPWSQESSPEERLPTEWSRQLTRARWVLLAVLLCGLLLGSSMLWFYIFRNCGPCPCETPVCMELLDHYLASGNRSVAPCTDFFSFACEKANGTSDSFQALTEENKSRLWRLLEAPGSWHLGSGEEKAFQFYNSCMDTDAIEASGSGPLIQIIEELGGWNITGNWTSLDFNQNLRLLMSQYGHFPFFRAYLRPHPAPPHTPIIQIDQPEFDILLQQEQEQKVYAQILREYVTYLNRLGTLLGSNPQEAQQHASWSIVFTSRLFQFLRPQQQQQAQDKLFHVVTIDELQEMAPAIDWLSCLQAIFTPMSLNSSQTLVVHDLDYLRNMSQLVEEGLLNHRESIQSYMILGLVDTLSPALDTKFQEARRELIQELRKLKERPPLPAYPRWMKCVEQTGAFFEPTLAALFVREAFGPSIQSAAMELFAEIKDAVIIRLKKLSWISEETQKEALNKLAQLQVEMGAPKRAVKPDIATQEYNDIQLGPSFLQSFLSCVRSLRARNVQSFLQPFPYHRWQKSPWEVNAYYSISDHMVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCPACDTHVLQEALLCLERHYAAFPLPSISSFNGSHTLLENAADIGGVAIAFQAYSKRIVEHTGELTLPNLDLSPYQLFFRSYAQVMCRGLSSQDPQDPHSPPSLRVHGPLSNTPDFAKHFHCPRGTLLNPSARCKLW | Cofactor: Binds 1 zinc ion per subunit.
Function: Zinc endopeptidase with endothelin-3-converting enzyme activity. Cleaves EDN1, EDN2 and EDN3 (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 80866
Sequence Length: 713
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q8RHI9 | MSLGALYVVSGPSGAGKSTVCKLVRERLGINLSISATSRKPRNGEQEGVDYFFITAEEFERKIKNDDFLEYANVHGNYYGTLKSEVEERLKRGEKVLLEIDVQGGVQVKNKFPEANLIFFKTANKEELEKRLRGRNTDSEEVIQARLKNSLKELEYESKYDRVIINNEIEQACNDLISIIENGVK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 21025
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q5L0S8 | MKNERGLLIVMSGPSGVGKGTVRKALFSQPDINLHYSVSVTTRKPREGEVEGVDYFFRTREQFEQMIRENKLLEWAEYVGNYYGTPIDYVEKTLAEGKDVFLEIEVQGAMKVRRAFPEALFIFLAPPSLTELEKRIMGRGTESKELIENRLRAAKEELEMMDEYDYVVENDEVELACERIKAIVIAEHCRRERVAERYKRMLGVE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23793
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q39T72 | MKREGVLYIISAPSGAGKTTLCKEIIDIFPHLRHSVSYTTRQPRAGEVHGKDYYFISMDEFRSMVDKGEFAEWAEVHGNCYGTSIRTLEECRITGIDLILDIDIQGARQLKERYEGGVYIFILPPSYEELRRRLNGRSSDSDDVISRRIDAAAGEIRESRWYDYIIVNDQFSRAVEELKSVVVAERCRTFRVLETVTERFDMG | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23403
Sequence Length: 203
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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P60551 | MKREGVLYILSAPSGAGKTTLCREIIDIFPQLRHSVSYTTRTPRPGEIHGKDYFFVSMDEFHRMIDADEFAEWAEVHGNCYGTSIRTLEENRAAGVDLILDIDIQGARQLQERFAGGVYIFILPPSFEELRRRLNGRSSDSDEVISRRINAAAGEIRESRWYDYIIVNDQFSRAVEELKSVIIAEQCRTARVLDAVSEIFSMD | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23171
Sequence Length: 203
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q5FS85 | MTQLPRRGVCLVISAPSGAGKSTIANALRASEPTLRHSVSVTTRSPRPGEVEGVHYHFRDIAEFRRMAADGELLEWAEVFGRGYGTPRAPVEEALDAGHDMVFDIDWQGHRLLRAALPDDVVSLFVLPPSLEELERRLNKRASDHPEEIARRMKAALDEISHWSEFDHTIINSDLDTAISQARSVLTAARLATRRQRNLLDMVASFSR | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23244
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q0BPZ9 | MMRPLPETGRRGLCLVVAAPSGAGKSSITRALLAEDPGLRLSVSVTTRAPRAGEQEGVHYYFRTQEEFDAMAAEGQLLEYARVFGRSYGTPRGPVQKALSEGSDVLFDVDWQGYHQLRSALPGDVVGIFVLPPSLDDLASRLEGRGDAPDIIAQRMAAARDEIAHVGEFPYVVVNTHLPEAIDQVRTILHAARTETKRQGWLRHWLGGLGLSE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23271
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
P44310 | MSQGNLYILSAPSGAGKSSLISALLASDSSTQKMVSVSHTTRAPRPGEVEGVHYYFVSKEEFESLIEQDLFLEYAKVFGGNYYGTSLPAIEENLAKGIDVFLDIDWQGAQQIRKKVPSVKSIFILPPSLPELERRLIGRGQDSEEVIAERMSKAMSEISHYDEYDYVIVNDDFEKTLKDLQSILQSERLTKDYQQKQNAMLIQQLLAK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23419
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q9K9Y2 | MEKEKGLLIVLSGPAGVGKGTVCSALRKHDTNIQYSVSATTRAPRKGEVDGVNYFFKSREQFEAMIEKEELLEWAEYVGNYYGTPIQYVRETIDSGKDIILEIEVQGALKVRERFPEGVFIFLMPPSLAELRSRIVGRGTETEEVINKRMNVAKEEIEMMKKYDYVVENDEVELAVDRIKAIVTAEHCKRERLIEKYHQLVEVE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23407
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
P56103 | MHNDFNLLILSGPSGAGKSTLTKYLQEKIPKTHFSLSTTTRKPREGEVDGLHYNFVSEEEFKQGIEKGQFLEWAIVHNHYYGTSKIPVEKALKEGKIVIFDIDVQGHEILKKHYPNACSVFISTKNQEILKERLLLRGTDSKETIEKRLINAYKEMQCLESFDYLIINEDLEKSKEIILSIAKTLVHRLKAFNFEKICKAWKNETL | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23830
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q9KXS0 | MAATPRGTSPVPPDARPRLTVLSGPSGVGKSTVVAHMRKEHPEVWLSVSATTRRPRPGEQHGVHYFFVSDEEMDKLIANGELLEWAEFAGNRYGTPRTAVLERLEAGEPVLLEIDLQGARQVRESMPEARLVFLAPPSWDELVRRLTGRGTEPPEVIERRLAAAKVELAAEPEFDQTLVNTSVEDVARELLALTNVV | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 21734
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q3JK86 | MAVFTAVSNADLALWMRHYDLGDVVAFRGIPSGIENSNFFLTTTRGEYVLTIFENLTAGQLPFYVDLMSHLAKHGVPVPAPVARDDGTLFGELHGKPAAIVTKLEGAAQLAPGVEHCVEVGQMLARMHLAGRDYPRHQPNLRSLPWWRDTVPAIAPFVTGEQRALLEGELAHQAAFFASDDYAALPEGPCHCDLFRDNALFAHAEPDTGHSVRLGGFFDFYFAGCDKWLFDVAVTVNDWCVDLPTGALDAARADALLRAYQTVRPFTAGERRHWGDMLRAGAYRFWVSRLYDFHLPRAAQMLKPHDPGHFERILRERIAHAGALPETHACN | Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 36759
Sequence Length: 331
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
EC: 2.7.1.39
|
Q8R711 | MDSDMSGGMVKVMVPASTANLGPGFDVLGVALNLYTEISMEFIKDGLEIFVEGEGVEDIENDQNNLIYKSAEVIFKKIGVFNKGLRIKIKNEIPLGRGLGSSAAAIVGGLLAANELTGRVLKREEILNLAALIEGHADNVTAALNGGLNVSIFDKNKVYYARKALEDDIDFLAFVPQEMVRTEIARKVLPEKVDFNDAVFNTGRTAFLVSVLIEKKYELLKIATQDMLHQKYRAKLVPFMEECFEKALLAGAYAAFLSGAGPTIMAISSPENSERVLKEVGKVYEERGLSYRAYRLKCENNGAQVLKTPSFV | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 34212
Sequence Length: 312
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
A4XI71 | MISVKVPASSANLGAGFDCMGVALKLYNIIEVEEIEKGLEITSSPDDPSIAKDENNLVFKAMKVVFNEVGWYPKGLRINLINEIPLTRGLGSSAACISGGIYAANLLCGGKLSEEEMIFLAAKMEGHPDNSTPAMIGGLVFAVLEENKVNYIKFVVPNRLKFAVFIPDFQLSTEYARNILPKYIEFKDAVFNVGRAALFASAITTGNYDLLPAATQDRLHQPYRKNLIPDFDKIVNLSLEFGAKGAFLSGAGPSIIALIDENYDSFEQNVKLALSSLELKSKWDLMILEADNSGATVFSVQSSSSFKR | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 33565
Sequence Length: 308
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
A0RQZ6 | MKILTPATSANLGPGFDSLGLSLKLYNEVTITKQNFTSVCISGEGSDKIGLKKNNTFVNIFNETMLYLTGKTPNFRFNFINNIPFSRGLGSSSSVIVGAIASAYHMAGFKVDRALVLNQALKYESHPDNISPAVWGGFTSNIVHKGTVYTQKADISSDLRAVVVIPDKPTSTKQSRGKLPKTYPMADVISNVSHAAFLTACFIKQDYENLRLASIDKMHEIRRMHGLKELFRVREIAYLSGALMSNLSGSGSSFLNLAHKDRAQTLRDILQLEFPEFKVEIYELDNNGFILQS | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 32381
Sequence Length: 293
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
A0R219 | MTQTLPVGLSATSVVAASSANLGPGFDSLGIALSLYDEIVVETVESGLTVHVEGEGAGQVPLDQTHLVVRAINKGLQAAGFSAPGLVVRCRNDIPHSRGLGSSAAAVVGGLAAVNGLVTQAGSEPMDDARLIQLSSEFEGHPDNAAAAVLGGAVVSWTEQAGAFGGEPRYSAVPVRLHPDIRLFPAVPQQRSSTAETRVLLPEQVSHVDARFNLSRAALLVVALSERPDLLMAATEDVLHQPQRAAAMPASAEYLAILRRCGIAAVLSGAGPSVLGLSAQSGLPAEALEYGTAHGFTVTEMSVGAGVRWTAGAVVRN | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 32443
Sequence Length: 317
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
B2A8C9 | MEEKNLVKVQVPGTSANLGAGFDSMGIALNIYNYVSLRQLEPGSGVIIEVKGEGADFISRDKDNLVYQAIAGVYREIYGSDVLIPDLEITLENNIPLARGLGSSAAAIVGGAVAANEMFNGELTRDELLKHVLELEGHLDNIAPAMYGGLTCSLITRENELMFRTVDVVEDWNFIIIVPGQELSTQKAREALPERIAFQDGLFNLSRANMLILAFQQRDYELLWHSMDDELHEPYRAKLIPGLDRLLQEVRGAGIPAAISGAGPSIACVLSEIEEEKIVRELGKEKFSAHGIESNFFKLKPDNSGAKSILH | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 34093
Sequence Length: 311
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
Q9JWE5 | MSVYTSVSDDEMRGFLSGYDLGEFVSLQGIAQGITNSNYFLTTTSGRYVLTVFEVLKQEELPFFLELNRHLSMKGVAVAAPVARKDGRLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPLEMENPRYDAWWTEACARLLPVLSQDDAALLRAEIDALKDNLGNHLPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLDEALKKAFIGGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFHFPQAGEMTFIKDPNAFRNLLLSLG | Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 33657
Sequence Length: 305
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
EC: 2.7.1.39
|
Q82UL3 | MSVFTPVTKEQLAVWLKNYSLGSLIDLQGISSGIENTNYLVTTTQDKFILTLFEKLTSTELPFYLNLMAHLSEQSIPCPRPVESQNHRLLGQLNGKPACIVTFLPGRSMVQVAEKQCAQVGEMLARMHLAGRNYSGWNQNPRGLNWWQTTAETVMPFLSSSEQNLLDEELQFQAAQMTANLPQSVIHADLFRDNVLFTSDGIGGVIDFYFACNDTLLYDLAITANDWCTLTDGIMDKTRMHALVTAYHAVRPLTADEHSAWPAMLRAGALRFWLSRLYDYYLPRPGELTHKKDPGHFKRILEHHLSNPGVLPSFQA | Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 35633
Sequence Length: 316
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
EC: 2.7.1.39
|
Q5SIH5 | MDLPRLYVPATLANLGSGFDALGVALDLYLEVEAHPAPEDAFLYEGEGHVEGTDNLIHEGYRAGMRALGLEPFPLRVRAFNPIPLARGMGSSSAALVAGVALADRLSGGRLGREGVFRVAAGLEGHPDNVAPAVYGGFVAALSDPPLAIPLPRPEGVRFVLAVPPYEVPTPLAREALPREVPLEDAIYNLARSALWPAALSSGRLEALREACRDRLHQPHRAHLMPGVLEAIEGALEAGALAAFVGGAGPTLAALARAGEEAPVIRALSAYRGPEGRTLVLGIGEGYFWKET | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 30690
Sequence Length: 292
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
Q979X5 | MPSMELSVISPCSSANLGPGYDVLAIAFDAFYDQVNVMLSDKLRILADEIPVQPDKNTAGLTALKMIEDFGIKDGIKISIKKGIPYGLGLGSSGSSAAAAAYAINNLFALGLERKDLIKYAAVGELASSGSPHPDNVSASILGGLVIVSPEGISAKRIEVSDQFKFLLVIADLKIRDKTKYARSLVPSGVSMGDHKRNTSRVASLIAGLMSGDRELVSTGMNDDIVEAAREPIFPYYRRVKDTAIESGAVGAVVSGAGPSILVVYDNKTETKQMIRKISRIYEGMGISVNFATPNVADGVREVANPLAD | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 32698
Sequence Length: 309
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
Q9KPK4 | MSVVVYAPASIGNVSVGFDVLGAAVSPIDGTLLGDRVKVEAGAEAFTLKTAGRFVDKLPANPQENIVYDCWQVFARELEKKSVVLKPLTMTLEKNMPIGSGLGSSACSIVAALDALNQFHASPLDETELLALMGEMEGKISGSIHYDNVAPCYLGGVQLMLEELGIISQSVPSFDDWYWVMAYPGIKVSTAEARAILPAQYRRQDIVAHGRYLAGFIHACHTQQPELAAKMIKDVIAEPYREKLLPGFAKARNYAASAGALATGISGSGPTLFSVCKEQAVAERVARWLEQNYVQNEEGFVHICRLDKQGSKVTGSEL | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 34295
Sequence Length: 318
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
Q8P9Q0 | MNQMVDMSHAVPTARGLREARAFAPASVANVAVGFDLLGYPLDGVGDTVTVRRIDAPVVRIAAIRGTTVALPLEAERNTAGAALMSLRAALALPFGFELEIDKGIALSSGMGGSAASCVAALVAANALLDTPISTDQLYQHALDGEAVASGSRHGDNLGPLFLGGLVLCTLERLVPIAVPEAWHSLVVHPEAVLETRRAREALAGDYRLSEFVAQSTNLALVLAGCHAGDADLVRAGLRDVLVEPRRAPLIAGFAQAKQAALAHAALGASISGAGPSVFAWFETRAAAAAAAPAVQAAFAGVGLDSQAWVTPINSPAARLLA | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 32925
Sequence Length: 322
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
|
O60282 | MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKTLKNVIQHLEMELNRWRNGEAVPEDEQISAKDQKNLEPCDNTPIIDNIAPVVAGISTEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAIRGGGGSSSNSTHYQK | Function: Microtubule-associated force-producing protein that may play a role in organelle transport. Has ATPase activity (By similarity). Involved in synaptic transmission . Mediates dendritic trafficking of mRNAs (By similarity). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 109495
Sequence Length: 957
Domain: Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
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