ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5ZUS2 | MKNDNRIIKNTIKQFKEKLCKDFSQKTNITSITRKLAVFIDTILIQLFIKNKLHFGDNFCLLALGSYGRRELQLHSDIDLLILHTEKVSNIQLQRAQKFIQDCWDVGLEVSHQITTVSSCANLASQDLSVISTIMDMFLLCGHGALMEELIYQTHTLHMWPSHQYFFAKLQEQQNRYAKYGETAYNLEPNIKNGPGGLRDLQILLSISKRHFKIKKLAEGIGYGFITDKEYEELKYCQNFLWRVRFALHMLAGKPEERLSFDYQVKLAQFFGYQDQSHILAIEQFMKDYFKVIKRNRELNEMLLQWFNETIVYHQKQKII... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
Q60BB2 | MDGPNSDRAHDRHAFDRVAACKARIQHNTAELAERFRTGTPVADLIRERTAFIDHLLSEAWDRRIGRGATDVALVAVGGYGRGELLLHSDVDLLILLDEAAPSSRKQDLSDFLRLLWDIGLKPGHSVRSPAECAEAARTDQTIITNLLEGRLLVGSAALWEAVRSETAPERMWSSAAFFEAKMAEQRIRYSKYHNTAYNLEPNVKEGPGGLRDIQLIGWIIRRHSDARGLQDLVAHGWLTDAEYRELKEAQAFLWRIRFALHALTGRCEDRLLFDYQRELAGLFGYRGETSNEVVEGFMQDYFRTVTGVERLNELLLQLF... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
A5U6S3 | MEAESPCAASDLAVARRELLSGNHRELDPVGLRQTWLDLHESWLIDKADEIGIADASGFAIVGVGGLGRRELLPYSDLDVLLLHDGKPADILRPVADRLWYPLWDANIRLDHSVRTVSEALTIANSDLMAALGMLEARHIAGDQQLSFALIDGVRRQWRNGIRSRMGELVEMTYARWRRCGRIAQRAEPDLKLGRGGLRDVQLLDALALAQLIDRHGIGHTDLPAGSLDGAYRTLLDVRTELHRVSGRGRDHLLAQFADEISAALGFGDRFDLARTLSSAGRTIGYHAEAGLRTAANALPRRGISALVRRPKRRPLDEGV... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
O34563 | MKKIFSLALISLFAVILLAACGSKGSNGEASKESKKDTLAAIKDNDKIVFGVKTDTRLFGLKNPSSGEIEGFDIDIAKQIAKDILGDEKKAQFKEVTSKTRIPMLQNGDIDAIVATMTITEERKKEVDFSDVYFEAGQSLLVKKGSKIKSVENLGKGSKVLAVKGSTSSQNIREKAPEASVLEFENYAEAFTALKSGQGDALTTDNAILYGMADENKNYQLTGKPFTDEPYGIAVKKGQSALAKEINASLKKMKSDGRYDEIYKKWIKEDPAE | Function: Part of the ABC transporter complex GlnHMPQ involved in glutamine transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 29756
Sequence Length: 273
Subcellular Location: Cell membrane
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B8ZYW0 | MSETETGNDGIKLVMAIIRPDKLADVKTALAEVGAPSLTVTNVSGRGSQPAKKGQWRGEEYTVDLHQKVKIECVVADIPAGDVVDAIAEAAHTGEKGDGKIFILPVEGAVQVRTGKEGSPAV | Function: Involved in the regulation of nitrogen metabolism . Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell . Increases the activity of the glutamine synthetase 3 in the presence of 2-oxoglutarate . May regulate the activity of the ammonia channel Am... |
Q7VM19 | MLKITAIPALQDNYIWAIQQGQEVMIVDPAQADPVFHFLAKNKLNLTTILITHYHQDHIGGIAGLQATYPDLTIYGSHEVAQYVNHIVQAGDHLHLLNSDVEVINSAGHTAQHISFLFAQQYLFCGDALFSAGCGRVFTGDYQAQFNTLQRFKTLPESTLVFPAHEYTLTNLKFAASVLPNNNDIREAQARAETLRAQQQPTLPSTIKQELRINPFLQADNLAEFITLRQQKDQY | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 26403
Sequence Length: 235
Pathw... |
P71374 | MLFALPALNDNYIWLYQRENLPLIIVDLPETDKLFAWLEKQNATIEAVLLTHEHDDHTQGVSAFKKRYPTVPIYGPQECEKKGATQIVNEGKILTANYQIDVIPTGGHTKQHVSFLVDNHLFCGDALFSAGCGRVFTGNYALMFEGLQRLNTLPDETIVCPAHEYTLGNLAFAETVLVDKSAVEKSAVEKQRIFVETQRAENKPSLPTTLKLEREINPFLQAKTLEEFTALRKAKDIF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 26850
Sequence Length: 238
Pathw... |
Q2SJ47 | MTEILPIPAFNDNYIWSIQSDQGDAWVVDPGDAQPVLRHLAENHLTLRGILITHHHHDHTGGVNELLANHPVPVYGFMRSAIKAITVPLQEGDRVDLGDFSLEVLETPGHTLDHISYFGDIAGAPRLFCGDTLFSAGCGRLFEGDPAMMRQSLDKLKRLPGDTYIYCAHEYTLSNLRFAQAVMPESDEVNKRKLQCESLRARGVPTLPAVLGEEIAYNPFLMAEHPVVRRMAQEVSGSPCATATDTFAAIRAWKDRF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28532
Sequence Length: 257
Pathw... |
Q16775 | MVVGRGLLGRRSLAALGAACARRGLGPALLGVFCHTDLRKNLTVDEGTMKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 33806
Sequence Length: 308
Pathw... |
Q31H51 | MKIVGLPTLSDNYTWVIQSENADDKRAWIVDPGESQKVIHYFEENQLQLDGILLTHHHYDHTDGIMGVMDALGEVAIVSNAQGPFKPVTHPVKEGDQVQVLNETFQVIETPGHTDEHICFYHPEALFSGDTLFTGGCGKIWQNPPEQMAESLLKLRALNDDCMVYCGHEYTYANLNFAKIAEPNTPAILDRLAEVKTNTQRNIPCVPARLGLEKQTNPFLRFDHPPLMQTLMERQAQPNESVSTLFATLRAWKDELDQTNILEAGLND | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 30195
Sequence Length: 268
Pathw... |
Q0BWR4 | MSVLIEIHQFPCLNDNYGYLVHEPGSGRTIAIDTPDAAVYLAEAEKMSWTISEIWNTHWHPDHAGGNLKIKEATGCKIIGPAGEADKIPGIDRRVKGGDTVELGGATATVIDVPGHTLGHIAFHFPDQEAAFVGDAVFALGCGRVFEGTMEMMWESLKRIKKLPKKTQLYCAHEYTASNAKFAVTIEPENKALKEYVAWIEKRRAEDKPTVPALLERELETNPFLRADLPEMQLAMGHAGNAAATFGEIRGRKDRF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28240
Sequence Length: 256
Pathw... |
Q5QZL0 | MRVHAIEAFDDNYIWAIETNDKDKVIIVDPGEAQPVQQWLEQNSKSIETILVTHHHYDHTGGIAELIEQSPCPVIGPENPEIKTLTKTVTEGDELTVGGIQWQVLTTPGHTLDHISFYTPGFLFCGDTLFSGGCGRMFEGTPEQFTQSLLKLRKLPGETRVFCAHEYTQANVNFALKVEPENAVLQSYAEKVRMLREQEQITLPSTLQLELAINPFLRFDQKSVIAAANKHAESVKNSPEDVFYTIRQWKDNA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28539
Sequence Length: 253
Pathw... |
Q5ZVZ3 | MTILPISAFSDNYIWTFIDKIAGVLDCVDPGEAAPIIRFAQSNQLTLRTILLTHHHYDHIGGVDSLIKQWPSCKVYGPIDERINNVTHPIKQGQSVQVGSLHFHILFNPGHTSTHISYYEPQQGWLFCGDTLFSAGCGRVFDGTIEELHESLLLFKKLPRNTKVFCAHEYTFQNLKFAHTVEPCNSSVINYMQQILKQPSSCTLPSNIDLELSINPFLRTDKEQVKQYALSHGANSSDSLDVFKVLRNQKNSFK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28736
Sequence Length: 254
Pathw... |
S3DB70 | MYKISFAGLLRGNDKDVEALAEAATTQGFLELELDCMEAKALQKDVKFLESFAESILDSPEDVKAAYHFHKTGRFRTTGFKPLGSEEGAKAGNPDGFEFFFLPQKEILLSEFREQLNCPPLAMSNIDTLTDCFKHYERTAQMLLQRLTEGLKLGNELLNAHNTSLPCVTNMGLIRYPPQPKESGNFGHIAHTDVGSLTILAATQRGLQTLDNITQKWIWVDPSDECLFVQLGDSLKFLSRGKILPSLHRVLPSDVAPEATKYTIAYFLRPNEEAEITSDDGKVWLYKDYHCRKFDAFARPLGYRPDGEESLISLRDYTGV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-di... |
S3E7P4 | MDQNPILIQRHHHRQNFAQKAPPAPLFLIHDGGGTVFSYFLLESLGRTVYGISNPNFETESTWENGIASMAEYYVNLIKATYPSGHILLGGWSLGGLIAIQAAHILSNDPELKVVGIVMIDSTFPVEGQFNKARRLAFMAETSTSPDMKEKTRKCMDEARIQSREWKAPSWRSSATETLDNHSQTINVQIHDHVTPTCPPTVLIRALDDGSNNSRDLNETSPTETSNDSETQALGFDRYQNFNLRYVVNTPGDHFSIFNKENVKELSKKVKEACDKLVMKS | Function: Probable thioesterase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthesized by the reducing... |
S3D775 | MIAALFTTNLQLGAVGVFIFALLAFAFNKLTTWEYSIPKEVQWVDRRTQPFSYLRAKARALARSKENTLEAYFRFNKLGKAAALAVPFGRPLLLLPQTFVRWIVDQPESIISLDPIHDDFHVFVGGDLTGDHTVQELLRRELTLNLDKLISVINDEIVCALDDVLGNSPEWKSTSLADDLKTIVARTSNRVFVGKDLCRNKHYISTVKGLALVIMPETVLQDLIPQFLKGPLSRITKAFNNIYGMKKFSSLLLGVVRQRYIDVKDVLEGSGDKTRLPDDLLTWMVQKSIRKGESSANIDKLLVARIAMANLAAIETTTAA... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthesized by the ... |
S3DQN8 | MLSEVIARVELLIGEQTLSGGILTFLFIVVIAHFVLTRFTVHSRFWNSQAWTGVREEWFPKMRAKVRTIGNIRQMLSDGYEGFSKQNKAFALPVIAEKPWLVLPHSCIPELLAKSDSEIDMKIIHEEQLMHEYTTGSLGRHVVDVPIQYDILLRQVNRKLPLLISAFNEELDKSFCHYWGTDTSYSEVNLSETCEKIVTQALNRIFAGKEICRDEGFLEHSRLYSEGVGRNAIMVRMLPPLLRPLLAPFITYSNRKHRDICLRVCLPVIRERVQHTAAKRADAEHKWEPPLDVLQWIIEESFARNDPKELDPRMITQRLL... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthesized by the ... |
Q9FYG4 | MKKSTRLLWLLSIIVLVAAVSKAVAEVDNDDDDDNTSLEGMTTAKRETLEVEDHTSLEGMVKREALEVKPPKAGKGKGKGKGRGTVAAGPEMNWPGQWELFMKNSGVSAMHAILMPLINKVQFYDATIWRISQIKLPPGVPCHVFDAKKNKVDCWAHSVLVDINTGDIKPLALTTDTWCSSGGLTVNGTLVSTGGFQGGANTARYLSTCENCVWIEYPKALAARRWYSTQATLPDGTFIVVGGRDALNYEYILPEGQNNKKLYDSQLLRQTDDPEENNLYPFVWLNTDGNLFIFANNRSILLSPKTNKVLKEFPQLPGGA... | Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylate by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include glyoxal and other aldehydes (By similarity). May be regulated by the transcription factor MYB80 during anther development and play a role in tape... |
A0A2H4HHY6 | MASSIKTVILFLLPLLLAYSVLAAPDITDGGDKPGPEIDDGGGDKPVPGNNDGASDYAKPAFEPEFMGAWVIDNPNAGVAAMQLQLMPNDQIVWFDTTSLGASGYKLPEGTPCPINPDANNQPDCYAHGIAYDWKTSKYRPLTLQGDAWCSSGNLWPNGNLMATGGTFSGDKAIRVIANDDPKGDFTTKIGALADTRWYSSNQVLPDGSSVVLGGRDSYSYEIVPPQMEFKPKRFDLPFMQQTTEPPLGPGRPVENNLYPFLFLLPDGNIFLFANNRAITFEPATGKTVKEFPVLPGGSRNYPPSGSAALFPLKLTADNA... | Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylate by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include glyoxal and other aldehydes (Probable). Does not have enzymatic activity on D-galactose .
PTM: The N-terminus is blocked.
Catalytic Activity: an ... |
Q01772 | MLSLLAVVSLAAATLAAPAASDAPGWRFDLKPNLSGIVALEAIVVNSSLVVIFDRATGDQPLKINGESTWGALWDLDTSTVRPLSVLTDSFCASGALLSNGTMVSMGGTPGGTGGDVAAPPGNQAIRIFEPCASPSGDGCTLFEDPATVHLLEERWYPSSVRIFDGSLMIIGGSHVLTPFYNVDPANSFEFFPSKEQTPRPSAFLERSLPANLFPRAFALPDGTVFIVANNQSIIYDIEKNTETILPDIPNGVRVTNPIDGSAILLPLSPPDFIPEVLVCGGSTADTSLPSTSLSSQHPATSQCSRIKLTPEGIKAGWQV... | Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylic acids by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include, methylglyoxal, glycolaldehyde, acetaldehyde, formaldehyde and glyoxal. May act as a source of extracellular hydrogen peroxide required for ... |
Q3HRQ2 | MILDAAIVALADLPGTWELIVPNAGIASMHTAVTRYGTVVLLDRTNIGPSRKMLPKGHCRYDPKDEVLKRDCYAHSVILDLNTNKIRPLKILTDTWCSSGQFLPDGSLLQTGGDLDGVKKIRKFVPCGPHGFCDWEELKDVELETGRWYATNQILPDGSVIIVGGRAANSVEYYPPRKGGAVQLPFLSDVEDKQMDNLYPYVHLLPNGHLFIFANNKAVMYDYTSNKVMLEYPPLDGGPRNYPSAGSSVMLALEGDYSMAIIVVCGGAQFGAFIQKSTDTPAHGSCGRIVATSPHPVWEMEDMPFGRIMGDMVMLPTGDV... | Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylate by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include glyoxal and other aldehydes (By similarity). Involved in disease resistance against the grapevine powdery mildew E.necator. Is sufficient to conf... |
P43220 | MAGAPGPLRLALLLLGMVGRAGPRPQGATVSLWETVQKWREYRRQCQRSLTEDPPPATDLFCNRTFDEYACWPDGEPGSFVNVSCPWYLPWASSVPQGHVYRFCTAEGLWLQKDNSSLPWRDLSECEESKRGERSSPEEQLLFLYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVLSEQWIFRLYVSIGWGVPLLFVVPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVN... | Function: G-protein coupled receptor for glucagon-like peptide 1 (GLP-1) . Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels . Plays a role in regulating insulin secretion in response to GLP-1 (By similarity).
PTM: N-glycos... |
P32301 | MAVTPSLLRLALLLLGAVGRAGPRPQGATVSLSETVQKWREYRHQCQRFLTEAPLLATGLFCNRTFDDYACWPDGPPGSFVNVSCPWYLPWASSVLQGHVYRFCTAEGIWLHKDNSSLPWRDLSECEESKQGERNSPEEQLLSLYIIYTVGYALSFSALVIASAILVSFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLGCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVFSEQRIFKLYLSIGWGVPLLFVIPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVN... | Function: G-protein coupled receptor for glucagon-like peptide 1 (GLP-1) . Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels . Plays a role in regulating insulin secretion in response to GLP-1 (By similarity).
PTM: N-glycos... |
P84159 | TDPGHLQDVXVAINDPKXGVFVNRK | Function: May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved.
PTM: The three different mass spectrometry results appear to arise from different glycosylation variants.
Sequence Mass (Da): 2743
Sequence Length: 25
Subcellular Location: Secreted
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Q87KM5 | MDQFQHIDVQGAQALLEQGEAKLVDIRDPQSFAVAHAESAYHLTNDTIVAFMEDVEFEQPILVMCYHGISSQGAAQYLVNQGFEQVYSVDGGFEAWQRAQLPIVRS | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 11845
Sequence Length: 106
Subcellular Location: Cytoplasm
EC: 2.8.1.1
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Q8ZJI3 | MEQFEATSVEQAYLRWKEGKTALVDIRDPQSYEAGHAPGAFHLTNSSLHTFMQQTDFDQPVMVMCYHGNSSKGAAQYLLQQGFDVVYSIDGGFEAWARSYPQDITSESR | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 12304
Sequence Length: 109
Subcellular Location: Cytoplasm
EC: 2.8.1.1
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F9USY3 | MHGFLGEFLGTMVLIVFGVGSGAAMNLKGNYARHQNWTFICLAWGLAVTFGVYVAGQFGSDGHLNPAVTVGFALFGYLPMANVWPYLLGQFLGAFIGAVIVIIQYYPHFQAAKTAADGNQVGIFATGPAISNPVFNFLSETIATFFFIFVLLNLGNFTQGLKPLMVGLLIVVVGQTLGGTTGFAINPARDWAPRLAYTILPVPNKGLANWGYAWVPMFGPLLGGILAAGLETIIS | Function: Transporter that facilitates the transmembrane diffusion of water, dihydroxyacetone, glycerol and H(2)O(2). Is not permeable to urea and D/L-lactic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24998
Sequence Length: 235
Subcellular Location: Cell membrane
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F9UTW9 | MMKDPLALQLLGEFLGTFILILLGDGVVAGVTLNKSKAQNAGWVAITLGWGFAVTMGVYASSFMSPAHLNPAVSLGMAVAGKFPWAYVIPYSAAQIAGGVIGGLVVWLHYYPHWQATKDAGAILGIFATGPGIRRYFWNFISEVIGTFVLVFGLLAFTKGQFTAGLNPIVVGILIIAIGLSLGGTTGYAINPARDLGPRIAHAVLPIANKGTSDWAYSWVPIAGPLVGGALGALLFNVLP | Function: Transporter that facilitates the transmembrane diffusion of water, dihydroxyacetone, glycerol and H(2)O(2). Is not permeable to urea and D/L-lactic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25054
Sequence Length: 240
Subcellular Location: Cell membrane
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F9UUB3 | MTGSWEARYAAEFFGTLILVLLGNGAVANAFLKNTTGNDDPGLANGGWLLVASGYGLGVMLPAMMFGSISGNHLNPAITIGQAVIGIFPWAHVAPYLIWQFLGAIAGQCLILALYWPHYRQTTDNEAVLGTFATSDHANSQLNGFVTEMVGTAVLIFGAMGLYRGMFFHQNIDIANIGVGLLIAAMVISLGGPTGPALNPARDLGPRLVHALFPVPNKGSSHWEYSWVPVVAPIVGAVIGIWIYKIFFGL | Function: Probable transporter that facilitates the transmembrane diffusion of an unknown substrate. Is not permeable to water, dihydroxyacetone, glycerol, urea, H(2)O(2) and D/L-lactic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26557
Sequence Length: 250
Subcellular Location: Cell membran... |
F9UUD2 | MRKYLAEFLGTFMLVFLGTATVVIAKGDVLAIGLAFGLAITVSAYAFGGISGGHFNPAVTTAMLINRRIDAADAIGYIIAQIIGAIVASAAVKSFVSALGLSATLLGQTDFPKIGSGMAFFVEALVTFLFLMVILNVTSNDHGNADFAGLTIGVTLAFLIIVALNLTGGSLNPARSIGPAIFAGGSALSHLWVYILAPEVGAILAAFCARVMGSED | Function: Probable transporter that facilitates the transmembrane diffusion of an unknown substrate. Is not permeable to water, dihydroxyacetone, glycerol, urea, H(2)O(2) and D/L-lactic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22133
Sequence Length: 216
Subcellular Location: Cell membran... |
P18156 | MTAFWGEVIGTMLLIIFGAGVCAGVNLKKSLSFQSGWIVVVFGWGLGVAMAAYAVGGISGAHLNPALTIALAFVGDFPWKEVPVYIAAQMIGAIIGAVIIYLHYLPHWKSTDDPAAKLGVFSTGPSIPHTFANVLSEVIGTFVLVLGILAIGANQFTEGLNPLIVGFLIVAIGISLGGTTGYAINPARDLGPRIAHAFLPIPGKGSSNWKYAWVPVVGPILGGSFGGVFYNAAFKGHITSSFWIVSVILVVVLLGLYVYTKSHSAKTLSNSKYI | Function: Mediates glycerol diffusion across the cytoplasmic membrane via a pore-type mechanism.
Catalytic Activity: glycerol(in) = glycerol(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28735
Sequence Length: 274
Domain: Aquaporins contain two tandem repeats each containing three membrane-spa... |
P57392 | MNIYRKKNIIKKCFMEFFGTGLVMFFGIGCLAASKLTNANFTQFEISCIWGFGVSIAIYFSSSISGAHLNPAVTIFFWLSSKLNKRKVLPYIISQTLGSFFFTMLTYYLYNNLLISFERNNNVVRGTQESLNLASIFCVYPNYNNSFIYDFIIEIFSTALFILIVLEFNNRNSNYFLYNRSVAPILTGFLVCMINLVINPLNNISLNPARDLGPKILLSLTGWGLFSFTGGNDNILYCFIPIMGPILGANLGGWIHKTLINNS | Function: Mediates glycerol diffusion across the cytoplasmic membrane via a pore-type mechanism.
Catalytic Activity: glycerol(in) = glycerol(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29720
Sequence Length: 263
Domain: Aquaporins contain two tandem repeats each containing three membrane-spa... |
Q21944 | MVLLAAIDQGTSSSRFLVFEADTGELVTSHQIEVRQLFPHGGWVEMDPMELYDTVVSCISKTIEKLENLGISADEIKSVGVANQRETSIVWDKETGKPLYNAIVWLDTRTSSLADEAISRTASKSKDEFRAKTGLPIHPYFSALKLKWLFQNVPEVKKAYADGNLMFGTVDTWLIWKLTGAYVTDVSNASRTLLLDLHKRKWSTQLCEFFDLPIEILPEIRSSAEVYGHFDKGPLEGVPLSGCLGDQQAAMVGHQCLNAGQTKNTYGTGTFMLCNIGTRPIISKNGLLTTVGFQFGADSPVVYALEGSGSIGGNVVRFLR... | Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 55165
Sequence Length: 502
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
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Q3AB25 | MTKKYVLALDQGTTSCRAILFDRDSNIVGVAQKEFTQHYPKPGWVEHDPEEIWSTQYGVIAELMARYNVNPEEIAAIGITNQRETTVVWDRNTGKPVYNAIVWQCRRTAGICDELKAKGLEEKVRYKTGLVIDAYFSGTKIKWILDNVEGAREKAERGELLFGTIDTWLVWKLTGGKVHVTDYSNASRTMIYNIRELKWDEELLAELGIPASMLPEVKPSSYVYGETDPNVFFGHAIPISGIAGDQQAALFGQTCFEPGMAKNTYGTGCFMLMNTGDKVYESKNGLLTTIAWGIDGKVEYALEGSIFIAGAVIQWLRDGL... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 55606
Sequence Length: 500
Pathway: Polyol metabolism; glycerol degradation ... |
A9WJ21 | MAKYAAAIDQGTTSTRCMIFDHSGNVICYDQKEHEQIYPRPGWVEHSPDEIWERTQSVIRGALSKGGLSASDIVAVGITNQRETTVVWNRKTGRPVYNAIVWQDTRTDQICNELAADGGQDRFRPKVGLPLATYFSGPKIRWILDNVPGAREAAEAGDVVFGNIDTFLTWWLTGGPNGGVHVTDVTNASRTMLMNLETLDWDDEILGIMGIPRQMLPKIVPSSMVYGTATGELAGVPVAGILGDQQAAMVGQTCFDVGEAKNTYGTGSFMLLNTGTKLVPSKSGLLTTVCYKFGDQPAVYALEGSIAITGALVQWLRDNL... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 54383
Sequence Length: 498
Pathway: Polyol metabolism; glycerol degradation ... |
A5CS23 | MSEKYIVAIDQGTTSTRAIVFDHSGSIVSTGQLEHEQIFPRAGWVEHDPMEIWRNTREVIGQALSKADITRHDVEAVGITNQRETAVVWDRTTGKPVYNAIVWQDTRTQKIVDRLAADGGVERFKPTVGLPLATYFSGTKIVWILENVDGAREKAEAGELMFGTTDTWVLWNLTGGTDGGVHVTDVTNASRTLFMDLETLQWDDEILKAFDVPRSMLPEIKSSSEVYGQVESSSLLREVPIAGILGDQQAATFGQAAFDQGESKNTYGTGNFLIFNTGTDIIHSQNGLLTTLGYKLGDQEPHYALEGSIAVTGSLVQWMR... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 55485
Sequence Length: 505
Pathway: Polyol metabolism; glycerol degradation ... |
Q01V13 | MSNYIGAIDQGTTSTRFIVFDHGGRIVSVAQKEHEQIFPQPGWVEHDANEIWRRTREVIAEALEKRALSASDLAAIGITNQRETTVVWDRLSGEPVYNALVWQDTRTAAAVAELARDGGADRFRAQTGLPLATYFSALKIGWILDNVPAVRARAEAGDILFGNIDTFLLWNLTGGLHLTDCTNASRTHLMNLQTLDWDDELLAAFRIPRAMLPRIVSSSEVYGNATLASVAGVPIAGILGDQQAALVGQTCFHAGEAKNTYGTGCFLLMNTGTKPTPSKHGMLTTVAYRFATQPAVYALEGSVAITGALVQWVRDNFGLI... | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 54310
Sequence Length: 494
Pathway: Polyol metabolism; glycerol degradation ... |
P17695 | METNFSFDSNLIVIIIITLFATRIIAKRFLSTPKMVSQETVAHVKDLIGQKEVFVAAKTYCPYCKATLSTLFQELNVPKSKALVLELDEMSNGSEIQDALEEISGQKTVPNVYINGKHIGGNSDLETLKKNGKLAEILKPVFQ | Function: Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity . The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the en... |
Q5XJ54 | MANFTDAASLQQFDELLKNNSKSLTVVHFHAPWAPQCSQMNDVMAELAKEHKHTMFVKLEAEAVPEVSEKYEITSVPTFLFFKGGEKIDRLDGAHAPELTNKVQRLGSGGGGAVGAGDVPKEDLNQRLKRLINAAPCMLFMKGSPQEPRCGFSRQIIQILKDHNVQYSSFDILSDEEVRQGLKTYSNWPTYPQVYVSGELIGGLDIVKELVESGELENTFPKTVSLENRLKSLINKSPVMLFMKGNKEAAKCGFSRQILEIMNNTGVEYDTFDILEDEEVRQGLKTYSNWPTFPQLYVKGDLIGGLDIVKELLEGGELVS... | Function: Together with bola2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins (By similarity). Required for hemoglobin maturation . Does not possess any thyoredoxin activity since it lacks the conserved motif that is essenti... |
G3XCY6 | MSANGRSILLVDDDQEIRELLETYLSRAGFQVRSVSRGADFRQALCEEEASLAILDVMLPDEDGFSLCRWIRSHQRLACMPIIMLTASSDEADRVIGLELGADDYLGKPFSPRELLARIKALLRRAQFTQVRGGDVLAFEDWRLDTVSHRLFHEDGEEFFLSGADFALLKLFLDHPQQILDRDTIANATRGREVLPLERIVDMAVSRLRQRLRDTGKAPRLIQTVRGSGYLLAAQVRPHLQP | Function: Member of the two-component regulatory system GtrS/GltR involved in the regulation of glucose metabolism and transport, as well as regulation of the exotoxin A gene expression . GltR controls the transcription of genes involved in glucose metabolism (glk and edd/gap-1) and transport (oprB) as well as the expr... |
P0AER8 | MFHLDTLATLVAATLTLLLGRKLVHSVSFLKKYTIPEPVAGGLLVALALLVLKKSMGWEVNFDMSLRDPLMLAFFATIGLNANIASLRAGGRVVGIFLIVVVGLLVMQNAIGIGMASLLGLDPLMGLLAGSITLSGGHGTGAAWSKLFIERYGFTNATEVAMACATFGLVLGGLIGGPVARYLVKHSTTPNGIPDDQEVPTAFEKPDVGRMITSLVLIETIALIAICLTVGKIVAQLLAGTAFELPTFVCVLFVGVILSNGLSIMGFYRVFERAVSVLGNVSLSLFLAMALMGLKLWELASLALPMLAILVVQTIFMALY... | Function: Catalyzes the sodium-dependent, binding-protein-independent transport of glutamate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42425
Sequence Length: 401
Subcellular Location: Cell inner membrane
|
O07605 | MKRIKFGLATQIFVGLILGVIVGVIWYGNPALPTYLQPIGDLFLRLIKMIVIPIVVSSLIIGVAGAGNGKQVGKLGFRTILYFEIITTFAIILGLALANIFHPGTGVNIHEAQKSDISQYVETEKEQSNKSVAETFLHIVPTNFFQSLVEGDLLAIICFTVLFALGISAIGERGKPVLAFFEGVSHAMFHVVNLVMKVAPFGVFALIGVTVSKFGLGSLISLGKLVGLVYVALAFFLIVIFGIVAKIAGISIFKFLAYMKDEILLAFSTSSSETVLPRIMEKMEKIGCPKGIVSFVIPIGYTFNLDGSVLYQSIAALFLA... | Function: This carrier protein is part of the Na(+)-dependent, binding-protein-independent glutamate-aspartate transport system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45920
Sequence Length: 429
Subcellular Location: Cell membrane
|
O59010 | MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYADAVKTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPKQAPPLVKILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVKVVGELAKVTAAVYVGLTLQILLVYFVLLKIYGIDPISFIKKAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGV... | Function: Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake (PubMed:17435767, PubMed:19380583, PubMed:17230192, Ref.11). Has only very low glutamate transport activity . Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions, resulting ... |
B9F676 | MDPPPRPRPHRVAVLLLLLLASSPAARAWKKDEFRNCNQTPFCKRARTRAPHSLDAPLSLDAASLAVATDGSLTASLSHPSRLRPLLLRLSALPPHALRLQIDEDYSSNTPPHRRFQVPDVLLPDVEARTLHLPQPKTSAAGVSTFALSSDVDVVVKHDPFELTVRRAGSGAPVLSFNSHGLFDFEPLQESKQEGETWEEQFRSHTDTRPRGPQSITFDVSFYGADFVYGLPEHGSTSLALRPTRGPGAEESEPYRLFNLDVFEYLHESPFGLYGSIPFMIAHGDGPSSGFFWLNAAEMQIDVLAPGWDGASSTENGRID... | Function: Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. May be required for defense response elicited by pathogen-associated molecular patterns (PAMPs).
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D... |
Q9US55 | MRYHGICWFIFQAAIIFAIFGSCQGAFRHQFKTAEQDGFARRNRDLAKFQKENLNWNGLFQLNSISYNSGVVSGVFEQQSENGENQHLFPFSISFLKNDVVRFQMDEKSRLEGTVEYEKNILTKRRFDASTELGFNERAEVYGKDAHLLEQTSTSLTIRYGSHGRFTVIVTFSPFKVEFQRDGEPQVVLNERHLLNMEYYRPKSSRTPEQEANGMWDETFDNFHDSKPKGPESVGLDIKFVDYGNVYGVPEHTSSLSLKETNNSDAGYTEPYRLYNVDLFEYEVDSPMSQYGAIPFMQAHKPNSDVAVFWSNAAATWIDV... | Function: Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins.
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alph... |
P38138 | MVLLKWLVCQLVFFTAFSHAFTDYLLKKCAQSGFCHRNRVYAENIAKSHHCYYKVDAESIAHDPLENVLHATIIKTIPRLEGDDIAVQFPFSLSFLQDHSVRFTINEKERMPTNSSGLLISSQRFNETWKYAFDKKFQEEANRTSIPQFHFLKQKQTVNSFWSKISSFLSLSNSTADTFHLRNGDVSVEIFAEPFQLKVYWQNALKLIVNEQNFLNIEHHRTKQENFAHVLPEETTFNMFKDNFLYSKHDSMPLGPESVALDFSFMGSTNVYGIPEHATSLRLMDTSGGKEPYRLFNVDVFEYNIGTSQPMYGSIPFMFS... | Function: Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins.
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alph... |
Q28034 | MLLLLLLLPMCWAVEVRRPRGVSLTNHHFYDESKPFTCLDGSASIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKALYISSRWVNDGVCDCCDGTDEYNSGIVCENTCKEKGRKERETLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEVLRTLKEEAEKPEEAAKDQHRRLWEEQQAISKEQRERELAASAFQELDDDMDGAVSVAELQTHPELDTDGDGALSEGEAQTLLGGDAQMDAAFFYDRVWAAIRDKYRSEVLPTEYPPSPPAPDVMEPKEEQPPMPSPPTEEEDEDEE... | Function: Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (By similarity). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the... |
P14314 | MLLPLLLLLPMCWAVEVKRPRGVSLTNHHFYDESKPFTCLDGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVCDCCDGTDEYNSGVICENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLWEEQLAAAKAQQEQELAADAFKELDDDMDGTVSVTELQTHPELDTDGDGALSEAEAQALLSGDTQTDATSFYDRVWAAIRDKYRSEALPTDLPAPSAPDLTEPKEEQPPVPSSPTEEEEEEEE... | Function: Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins . Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia ... |
Q88Q27 | MFSRDLTIAKYDAELFEAMQQEALRQEEHIELIASENYTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGADYANVQPHAGSQANAAVYLALLSAGDTILGMSLAHGGHLTHGASVSSSGKLYNAIQYGIDGNGLIDYDEVERLAVEHKPKMIVAGFSAYSQVLDFARFRAIADKVGAYLFVDMAHVAGLVAAGVYPNPVPFADVVTTTTHKTLRGPRGGLILARANADIEKKLNSAVFPGAQGGPLEHVIAAKAICFKEALQPEFKAYQQQVVKNAQAMASVFIERGFDVVSGGTQNHLFLL... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q98A81 | MAEPGTYGRSSLVQVDCRVHELLLRQRRQERTMLKLIASENFASSAVLEATGSIFANKYAEGYPGARYYAGNEIVDELETLAIERLKALFGSEHANVQPYSGSPANQAVYRALLSPRDKVMGLPLPEGGHLTHGWSVNFSGTDYQRVPYGLHDKTQQIDYDRLRETARRERPKLIWVGGTSYPRVFDYAAMAEIALEANSYLVADIAHISGLIVAGAHPNPVVHCDVVTSTSHKSIRGPRGGFILSKNEDRYQALYHSTSKHNLAKRIDRAVFPQLQGGPHMNTIAALAVALQEAATPSFRTYGHQIVKNAKALAEALLG... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q9KMP4 | MNANLNKAYPNVSLENFFSTPLAATNDAVFAAIQAEYTRQNEQIELIASENIVSKAVMQAQGTCLTNKYAEGYPGRRYYGGCEHVDSVEQIAIERAKMLFQCQYANVQPHSGAQANGAVMLALLQPGDTIMGMSLDAGGHLTHGARPALSGKWFNAVQYGVDRQTLEINYDSVRALALEHKPKMIIAGGSAIPRTIDFAQFRSIVDEVGALLMVDMAHIAGLVATGAHPSPLPHAHVVTTTTHKTLRGPRGGMILTNSEEIHKKINSAVFPGLQGGPLMHVIAAKAVAFGEALGPEFRTYIDSVIDNAKVLAEVLQTRGC... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q7MEH7 | MNSHYQNHSLENFFSTNLSATDDAVFAGIQAEFTRQNEQIELIASENIVSKAVMQAQGTCLTNKYAEGYPGRRYYGGCEHVDTVEAIAIERAKKLFNCEYANVQPHSGAQANGAVKLALLQPGDTIMGMSLDAGGHLTHGARPALSGKWFNAVQYGVDKETLEINYDDVRALAVEHKPKMIIAGGSAIPRVIDFAKFREIADEVGAILMVDMAHIAGLIATGAHPSPLPHAHVVTTTTHKTLRGPRGGMILTNHEEIIKKINSAVFPGLQGGPLMHVIAAKAVAFGEALGPEFKTYIDSVINNAKVLAEVLQTRGCDIVT... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
P50434 | IVAGWSAYPRQLDFVRFREIADKVGAYLFVDMAHFAGLVATGLHPSPVPHAHVVTSTTHKTLAGPRGGIILSNDAEIAKKLNSAVFPGQQGGPLEHVIAGKAVAFKIAASAEFKERQQRTLAGSRILAQRLTQADVAAKGISVLTGGTDVHLVLVDLRHSELDGQQAEDLLAKVEITVNRNSVPFDPRPPMTTSGLRIGTPALATRGFSEEAFAEVAEIIAQTLIAGAEGNTGVLPELKARILELAAAHPLYPNLKKIGE | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
A7MGY5 | MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNFSGKLYNIIPYGIDESGKIDYEDMAKQAKEHKPKMIIGGFSAYSGIVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGSEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFL... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q6AAU3 | MSDPRAVDPTARDIAEKLAPAYRTMLDAIAQVEPRIAEATRAELTDQRHSLKLIASENYASLPVLATMGTWFSDKYAEGTAGHRFYAGCQNVDTVETIAAEHACALFGAEHAYVQPHSGIDANLTAYWTILAHHIETPALSEFGARTVNDLTQVDWDTLRHRFNDQRAIGMSLDAGGHLTHGFRPNISGKMFDQRSYGTDPQTGLLDYDKVAELAREFKPLVIVAGYSAYPRRVNFAKMREIADEVGAVLMVDMAHFAGLVAGKVFTGDENPIPHAQVVTTTTHKSLRGPRGGMVLTTKDYADDVDRGCPMVLGGPLSHV... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q6MS85 | MNTKISPLIKESLNKELKRQQSHIELIASENYVSKAVLELNGSVLTNKYAEGYPGKRYYGGCEFIDEIESLGIQTAKELFHAEHANIQPHSGSQANDAAYKALLEPKDRVVAMSLDAGGHLTHGYPINFSGYTYDFRFYGVNKDTEQLDYQEIEKIVLEHKPKLIVAGASAYSRIIDFKKFKEIADKVGAYLMVDMAHIAGLVAAGVHPNPLEYADIVTTTTHKTLRGARGGLILCKQEFAKKVDLAVFPGSQGGPLENLIAGKTQALLEASTDEFKEYGKQIVKNTKALANVLQENGLRLVAGGSDNHLINVDVKSTLR... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
A0R2V7 | MAADPSSNSSSVPAANGADYADTASAAYQAALQVIESVEPRVAAATRKELADQRDSLKLIASENYASPAVLLTMGTWFSDKYAEGTIGHRFYAGCQNVDTVESVAAEHARELFGAPYAYVQPHSGIDANLVAFWAILATRVEAPELANFGAKHINDLSEADWETLRNKLGNQRLLGMSLDAGGHLTHGFRPNISGKMFHQRSYGTNPETGFLDYDAVAAAAREFKPLVLVAGYSAYPRRVNFAKMREIADEVGATLMVDMAHFAGLVAGKVFTGDEDPVPHAHVTTTTTHKSLRGPRGGMVLATEEYAPAVDKGCPMVLG... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q3IRX5 | MNYEQVREADPAIAAALADERDRQEDTLAMIASENHVSEAVLQAQSSELTNKYAEGYPGERYYAGCGPADDVEELAIERAEELWGAEHINVQPHSGTQANMAVYLAMLEPGDRILSLELEHGGHLSHGHPANFTGQTYEVEQYEVDPETGYIDYDELHEQAEAFEPDIIVSGYSAYPREVEFERIQEAADAVDAYHLADIAHITGLVAAGVHQSPVGVADFVTGSTHKTIRAGRGGIVMCDEEYADDIDAAVFPGAQGGPLMHNVAGKAVGFKEALQPEFEQYAQQVIDNAEALGERLQEHGFSLVSGGTDNHLVLVDLR... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,... |
Q5XC65 | MIFDKGNVEDFDKELWDAIHAEEERQEHHIELIASENMVSKAVMAAQGSVLTNKYAEGYPGNRYYGGTECVDIVETLAIERAKKLFGAAFANVQAHSGSQANAAAYMALIEAGDTVLGMDLAAGGHLTHGSPVNFSGKTYHFVGYSVDADTEMLNYEAILEQAKAVQPKLIVAGASAYSRSIDFEKFRAIADHVGAYLMVDMAHIAGLVAAGVHPSPVPYAHIVTSTTHKTLRGPRGGLILTNDEALAKKINSAVFPGLQGGPLEHVIAAKAVAFKEALDPAFKDYAQAIIDNTAAMAAVFAQDDRFRLISGGTDNHVFL... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q97R16 | MIFDKDDFKAYDADLWNAIAKEEERQQNNIELIASENVVSKAVMAAQGSILTNKYAEGYPGRRYYGGTDVVDVVETLAIERAKEIFGAKFANVQPHSGSQANCAAYMSLIEPGDTVMGMDLASGGHLTHGAPVSFSGQTYNFVSYSVDPKTELLDFDAILKQAQEVKPKLIVAGASAYSQIIDFSKFREIADAVGAKLMVDMAHIAGLVAAGLHPSPVPYAHITTTTTHKTLRGPRGGLILTNDEELAKKINSAIFPGIQGGPLEHVVAAKAVSFKEVLDPAFKEYAANVIKNSKAMADVFLQDPDFRIISGGTENHLFL... | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-ind... |
Q8B121 | MGQVIGFFQSLPEIINEALNIALICVALLATIKGMVNIWKSGLIQLLFFLTLAGRSCSHSFTIGRFHEFQSVTVNFTQFMSYAPSSCSVNNTHHYFKGPQNTTWGLELTLTNESMINITNSMRVFTNIHHNVTNCVQNISEHEGVLKWLLETMHLSISKPGKHIAPVMCERQKGLLIEYNLTMTKDHHPNYWNQVLYGLAKLLGSSKRLWFGACNKADCQMQSDHQHIKCNYSNCKGYTSFKYLIIQNTTWENHCEYNHLNTIHLLMSPIGQSFITRRLQAFLTWTLSDALGNDLPGGYCLEQWAVVWFGIKCFDNTAMA... | Function: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the... |
P09991 | MGQIVTMFEALPHIIDEVINIVIIVLIVITGIKAVYNFATCGIFALISFLLLAGRSCGMYGLKGPDIYKGVYQFKSVEFDMSHLNLTMPNACSANNSHHYISMGTSGLELTFTNDSIISHNFCNLTSAFNKKTFDHTLMSIVSSLHLSIRGNSNYKAVSCDFNNGITIQYNLTFSDAQSAQSQCRTFRGRVLDMFRTAFGGKYMRSGWGWTGSDGKTTWCSQTSYQYLIIQNRTWENHCTYAGPFGMSRILLSQEKTKFFTRRLAGTFTWTLSDSSGVENPGGYCLTKWMILAAELKCFGNTAVAKCNVNHDAEFCDMLR... | Function: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the... |
P34898 | MSTYSLSETHKAMLEHSLVESDPQVAEIMKKEVQRQRESIILIASENVTSRAVFDALGSPMSNKYSEGLPGARYYGGNQHIDEIEVLCQNRALEAFHLDPKQWGVNVQCLSGSPANLQVYQAIMPVHGRLMGLDLPHGGHLSHGYQTPQRKISAVSTYFETMPYRVNIDTGLIDYDTLEKNAQLFRPKVLVAGTSAYCRLIDYERMRKIADSVGAYLVVDMAHISGLIASEVIPSPFLYADVVTTTTHKSLRGPRGAMIFFRRGVRSVDAKTGKETLYDLEDKINFSVFPGHQGGPHNHTITALAVALKQAASPEFKEYQ... | Function: Interconversion of serine and glycine.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 52978
Sequence Length: 480
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC... |
P03540 | MGQIVTLIQSIPEVLQEVFNVALIIVSVLCIVKGFVNLMRCGLFQLVTFLILSGRSCDSMMIDRRHNLTHVEFNLTRMFDNLPQSCSKNNTHHYYKGPSNTTWGIELTLTNTSIANETSGNFSNIGSLGYGNISNCDRTREAGHTLKWLLNELHFNVLHVTRHIGARCKTVEGAGVLIQYNLTVGDRGGEVGRHLIASLAQIIGDPKIAWVGKCFNNCSGDTCRLTNCEGGTHYNFLIIQNTTWENHCTYTPMATIRMALQRTAYSSVSRKLLGFFTWDLSDSSGQHVPGGYCLEQWAIIWAGIKCFDNTVMAKCNKDHN... | Function: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the... |
P35623 | MAAPVNKAPRDADLWSLHEKMLAQPLKDNDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELEVLCQKRALQVYGLDPECWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQLEENARLFHPRLIIAGTSCYSRNLDYARLRKIADDNGAYLMADMAHISGLVAAGVVPSPFEHCHVVSTTTHKTLRGCRAGMIFYRKGVRSVDPKTGKETRYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAM... | Function: Interconversion of serine and glycine.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 53025
Sequence Length: 484
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC... |
Q1I5A5 | MDMQSRIRRLFQASIDTKQQAMDILAPHIEQASLVMVNALLSDGKMLACGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTLTSIANDYSYNEVFSKQIRALGQPGDVLLAISTSGNSANVIQAIQAAHDREMIVVALTGRDGGGMASLLLPEDVEIRVPSTVTARIQEVHLLAIHCLCDLIDSQLFGSEE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
Catalytic Activity: 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
Sequence Mass (Da): 21208
Sequ... |
Q4ZNX7 | MDMQSRIRRLFQASIETKQQAMEVLAPFIEQASQVMVNALLNEGKMLACGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLLLPEDVEIRVPANVTARIQEVHLLAIHCLCDLIDSQLFGSEE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
Catalytic Activity: 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
Sequence Mass (Da): 21313
Sequ... |
A1SUJ5 | MNLSIIKAELLEAEKVLQAFLADEQNLKNIEKAASLLADSFKNDGKVLSCGNGGSHCDAMHFAEELTGRYREHRPAYPAIAISDPSHISCVGNDYGYDAIFARYLEGVGRKGDVLFCLSTSGNSKNILNAIEVAKAKGISVIALTGKDGGKMSGLADVEIRVPHFGFADRIQEVHIKIIHILIYLIEKKMA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
Catalytic Activity: 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
Sequence Mass (Da): 20761
Sequ... |
Q85041 | MCGPRNAEAVSWRSWLIEVCGFALAALTLVLTLIFASLPEMGFPCFYATVADYDTLNDTSGGVWTRQPLVAPALFLETPTVTSFFGFTATVLLAHALYAVAGAVVLRREAGRLAFQPSVVLYAASTVAAPGTLMLGALCAWTLQAVVLLMAHKQAGLAAAAYITHFVFLALFGACHACKGTGDVRAALAASPPLRRVAVHARAVVTNVVLGAVGLGAAVVGLMLGVLLANSFHISLWKTAEAALAVFTLLALALMVFVEVVVSGYVQVLPTPAFCVLVASAAFGVSAHRYFAKFSEALGETHGVVIGTRAVLAVLSLIAL... | Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41546
Sequence Length: 393
Subcellular Lo... |
P09298 | MGTQKKGPRSEKVSPYDTTTPEVEALDHQMDTLNWRIWIIQVMMFTLGAVMLLATLIAASSEYTGIPCFYAAVVDYELFNATLDGGVWSGNRGGYSAPVLFLEPHSVVAFTYYTALTAMAMAVYTLITAAIIHRETKNQRVRQSSGVAWLVVDPTTLFWGLLSLWLLNAVVLLLAYKQIGVAATLYLGHFATSVIFTTYFCGRGKLDETNIKAVANLRQQSVFLYRLAGPTRAVFVNLMAALMAICILFVSLMLELVVANHLHTGLWSSVSVAMSTFSTLSVVYLIVSELILAHYIHVLIGPSLGTLVACATLGTAAHSY... | Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48672
Sequence Length: 435
Subcellular Lo... |
P52206 | LLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHRYVHAIKTLWDDPGIQECYDRRREYQLSDSAKYYLADVDRIATSGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDHVLVE | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity). Together with GNAQ, required... |
P29992 | MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHQYVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDS... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems . Acts as an activator of phospholipase C . Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) . Together with GNAQ, required for heart development (By si... |
P45645 | MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSEEDKKGFTKLVYQNIFTAMQSMIRAMETLKILYKYEQNKANAVLIREVDVEKVMTFEQPYVSAIKTLWNDPGIQECYDRRREYQLSDSAKYYLSDVDRIATPGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDS... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42058
Sequence Length: 359
Subcellular Location: Cell membrane
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P27600 | MSGVVRTLSRCLLPAEAGARERRAGAARDAEREARRRSRDIDALLARERRAVRRLVKILLLGAGESGKSTFLKQMRIIHGREFDQKALLEFRDTIFDNILKGSRVLVDARDKLGIPWQHSENEKHGMFLMAFENKAGLPVEPATFQLYVPALSALWRDSGIREAFSRRSEFQLGESVKYFLDNLDRIGQLNYFPSKQDILLARKATKGIVEHDFVIKKIPFKMVDVGGQRSQRQKWFQCFDGITSILFMVSSSEYDQVLMEDRRTNRLVESMNIFETIVNNKLFFNVSIILFLNKMDLLVEKVKSVSIKKHFPDFKGDPH... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems . Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF12/LARG) (By similarity). GNA12-dependent Rho signaling subsequently regulates transcription factor ... |
Q63210 | MSGVVRTLSRCLLPAEAGARERRAGAARDAEREARRRSRDIDALLARERRAVRRLVKILLLGAGESGKSTFLKQMRIIHGREFDQKALLEFRDTIFDNILKGSRVLVDARDKLGIPWQHSENEKHGMFLMAFENKAGLPVEPATFQLYVPALSALWRDSGIREAFSRRSEFQLGESVKYFLDNLDRIGQLNYFPSKQDILLARKATKGIVEHDFVIKKIPFKMVDVGGQRSQRQKWFQCFDGITSILFMVSSSEYDQVLMEDRRTNRLVESMNIFETIVNNKLFFNVSIILFLNKMDLLVEKVKSVSIKKHFPDFKGDPH... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems . Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF12/LARG) (By similarity). GNA12-dependent Rho signaling subsequently regulates transcription factor ... |
Q14344 | MADFLPSRSVLSVCFPGCLLTSGEAEQQRKSKEIDKCLSREKTYVKRLVKILLLGAGESGKSTFLKQMRIIHGQDFDQRAREEFRPTIYSNVIKGMRVLVDAREKLHIPWGDNSNQQHGDKMMSFDTRAPMAAQGMVETRVFLQYLPAIRALWADSGIQNAYDRRREFQLGESVKYFLDNLDKLGEPDYIPSQQDILLARRPTKGIHEYDFEIKNVPFKMVDVGGQRSERKRWFECFDSVTSILFLVSSSEFDQVLMEDRLTNRLTESLNIFETIVNNRVFSNVSIILFLNKTDLLEEKVQIVSIKDYFLEFEGDPHCLR... | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems . Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG) . GNA13-dependent Rho signaling subsequently re... |
Q96P88 | MSAGNGTPWDATWNITVQWLAVDIACRTLMFLKLMATYSAAFLPVVIGLDRQAAVLNPLGSRSGVRKLLGAAWGLSFLLAFPQLFLFHTVHCAGPVPFTQCVTKGSFKAQWQETTYNLFTFCCLFLLPLTAMAICYSRIVLSVSRPQTRKGSHAPAGEFALPRSFDNCPRVRLRALRLALLILLTFILCWTPYYLLGMWYWFSPTMLTEVPPSLSHILFLLGLLNAPLDPLLYGAFTLGCRRGHQELSIDSSKEGSGRMLQEEIHAFRQLEVQKTVTSRRAGETKGISITSI | Function: Putative receptor for gonadotropin releasing hormone II (GnRH II) which is most probably non-functional.
PTM: Phosphorylated on the C-terminal cytoplasmic tail.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32537
Sequence Length: 292
Subcellular Location: Cell membrane
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Q95JG1 | MSAGNGTPWGSAAGEESWAASGVAVEGSELPTFSAAAKVRVGVTIVLFVSSAGGNLAVLWSVTRPQPSQLRPSPVRTLFAHLAAADLLVTFVVMPLDATWNITVQWLAEDIACRTLMFLKLMAMYSAAFLPVVIGLDRQAAVLNPLGSRSGVRKLLGAAWGLSFLLALPQLFLFHTVHRAGPVPFTQCVTKGSFKARWQETTYNLFTFRCLFLLPLTAMAICYSHIVLSVSSPQTRKGSHAPAGEFALCRSFDNCPRVRLWALRLALLILLTFILCWTPYYLLGLWYWFSPTMLTEVPPSLSHILFLFGLLNAPLDPLLY... | Function: Receptor for gonadotropin releasing hormone II (GnRH II). This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
PTM: Phosphorylated on the C-terminal cytoplasmic tail.
Location Topology: Multi-pass membrane protein
Sequence Mass ... |
P15586 | MRLLPLAPGRLRRGSPRHLPSCSPALLLLVLGGCLGVFGVAAGTRRPNVVLLLTDDQDEVLGGMTPLKKTKALIGEMGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKSWQKIQEPNTFPAILRSMCGYQTFFAGKYLNEYGAPDAGGLEHVPLGWSYWYALEKNSKYYNYTLSINGKARKHGENYSVDYLTDVLANVSLDFLDYKSNFEPFFMMIATPAPHSPWTAAPQYQKAFQNVFAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIQFLDNAFRKRWQTLLSVDDLVEKLVKRLEFTGELNNTY... | Cofactor: Binds 1 Ca(2+) ion per subunit.
PTM: The form A (78 kDa) is processed by internal peptidase cleavage to a 32 kDa N-terminal species (form B) and a 48 kDa C-terminal species.
Catalytic Activity: Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulf... |
Q9C7G6 | MGHLPQSLYSAAGPKFPYPGSSGLGVDQRKLTWSRFPVFLRCASTESLTSLTQNNAAEIELKYLVSQHGWDVRRLNRDDEDEIRRVSLVQAEAFHIPLALFDDFFFMFFQAEVLSALLYKLKNSPPDRYACLVAEQTSETETLSSSSVVGVVDVTAQTESSVLRYFPGVEEYLYVSGLAVSKSQRRKKMASTLLKACDVLCYLWGFKLLALRAYEDDAAARNLYSNAGYSVVETDPLWTSTWIGRKRRVLMSKRFS | Function: Protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA), with a preference for leucine, methionine, serine, valine and to a lower extent threonine and alanine as substrates (can also use glycine), and epsilon-lysine acetylation (KA) of several plastid proteins.
PTM: Autoacety... |
Q555X4 | MSNFYNNNPRRNTFRLTERIKKKPYQTLIVFILIFLFLYVFGPFGEKKSNNNNNNHPVSKTSSFTESLYTKFQTETFAYRANGDLKKYDISIITQFTVDRFDRIAMMADKWRAPISAAVYITSFKDIDEVFKLVRNSFAVTEFVDLHFLFANKTRYPVNNLRNLALRNARTEWCLLLDVDFISPLGMYDYLHSTLEKLDTSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNENNDNDNGNNNNNNDNEKNFKKKQEDLKIDPNDFEGDLKAIEKLKRNGEKLYVKNLKKVLDGSENNLGKNINFNNNNNDNNNKDDGGG... | Function: May have a role in modulating cell adhesion and glycosylation. Essential for development.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 59898
Sequence Length: 516
Subcellular Location: Membrane
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Q9Y761 | MAFGSRRKIKAILVAASAMVFISLLGTFGSDSVYEKIKTFDVSWGSNVSGGLSSMLQKKKTVLYDPENIKQIPYSTIQKLYDHELESVTNIDWSQYAYVNYVADKNYVCSSMIHFNRLHESGTQAKLVMLVAKELTELPEDDSVTRMLAQFKEISDNCIVKPVENIVLSQGSAQWMTSMTKLRVFGMVEYKRIVYFDSDSIITRNMDELFFLPDYIQFAAPATYWFLNDNDLPQLIEDNKQIALANNQTAELTEIEDILQQKIDDSEDIYNFLPNLPKRLYPKSDNARIDSTDNTYFKYAATLMVIKPEQEMFERLEQEV... | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 53169
Sequence Length: 460
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q6CT96 | MLKRKVRYLLLIVVVFTGIILSVEAIMRFQLNKNVDYYLKFFDKHKDNIENMYDPLNIKQIPYSTIDQLYTKRQSEAEPIDWDKFAYVNYITDFEYLCNTLIQFRKLNDSGSKAKLLALVTDTLVNKSKENKEVEALLNKIKSVSDRVAVTEVGSVIQPNDHTPWSKSLTKLAIFNLTDYERIIYMDNDAIIHDKMDELFFLPSYVKFAAPISYWFVTADDLRTVSTDTKKLFKTNKLDPIEKKLASRVKNSLEIYNHLPNLPQHFYSKSMNFIIDIDGFQKSDNKVNFATHLMVIKPDVTMANDIRDNILPRYLKAKEE... | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 53508
Sequence Length: 453
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q4WBL2 | MGNKKATLLPYRRDSASSEADFFDIPDEPCLAIAKRQLRRIRTWIFFAVFIILILWFRREAPSPAPVSHIDYNKVDWSRYAYSQYATSSAYLCNAVMVFEALERLGSRADRVLFYPEDWDLFVADDHDRDSQLLVLAKEKYKALLVPISAEMIKAGGGSGESWDKSIAKLLAFGETEYDRVIHIDSDVTVLQSMDELFFLPPAKVAMPRAYWALPDTKTLSSLLIVIEPSYREFKALMESAQPALHGQVEVDSNETQRYDMELLNNRYADSALVLPHRQYGLVTGEFRKKDHRSFFGNDYETWDPDKVLAEAKLVHFSDW... | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 44512
Sequence Length: 384
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q59ZI3 | MTSKSSSWKALLKNWEFKVAAFIGIYFLISHVVLETTDVVNEKGLKSHLKVLPEEVIDYYGKQPFSNVDKYAYMQYATNYDYLNLAIINFIHLRKANTKIPNLVIIYDEVLHYYASDKWSELYQVANQYKITLKAAPLIKASYQDDSNWAASFTKFHIFNQVEYDRIVFFDSDSMLVDIPNEIDFDNMESRFNHIDELFKIPQELSFASPQAYWLNNVVEGKSPRPRKNVEIPNKKRYSLRMKKLVNDLSIYQDFNLLPSLIYENHYFDNANHFFANHIMVITPSKNTFQELMRYIHNPWWWSITNRGSLRKPNDYDMEI... | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 55312
Sequence Length: 462
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q54CL4 | MFTDQQKIGAMLSAMGLFFGFLGVLLFLDRNLLALGNLLLVSGIVLILGLQKTTKFFAQKKKIKGTILFFFGIVVLLVTRWTFVGMVIEIFGFVNLFGDAFPIVISILRKLPIIGNILNHPLVNRLLQKADSGNELPF | Function: May be involved in fusion of ER-derived transport vesicles with the Golgi complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15343
Sequence Length: 138
Subcellular Location: Golgi apparatus membrane
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Q9USJ2 | MWLSDLQKIGVGTTALGFLFMIMGIFMFFDGPLLSLGNLLLVFGFFMIAGFSKSVSFFLRKDRMLGSISFFSGLLLTLFHFPIIGFFVECLGFFNLFKVFYPLIISFLRTVPYIGPYIDRLTSYQQSPV | Function: Nonessential protein required for the fusion of ER-derived transport vesicles with the Golgi complex. Can be replaced by sft2 (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14707
Sequence Length: 129
Subcellular Location: Golgi apparatus membrane
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Q03554 | MWLTEAQKFGVAFTFGGFLFFLFGIFTFFDRALLALGNILFLIGVFLIIGSQKTYIFFTRPNKRRGSLFFLVGAFLILLKWTFLGFIIESLGIIGLFGDFFGVIVQFLRSMPIIGPILSHPAIAPIVDKLAGVRVLPV | Function: Nonessential protein required for the fusion of ER-derived transport vesicles with the Golgi complex. Can be replaced by SFT2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15431
Sequence Length: 138
Subcellular Location: Golgi apparatus membrane
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A0A3L6E0R4 | MGEITNVMEYQAIAKQKLPKMAYDYYASGAEDEWTLQENREAFSRILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAAAAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRKVVEQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPHLTLKNFEGLDLGKMDQAADSGLASYVAGQVDRTLSWKDVKWLQTITTLPILVKGVLTAEDTRLAVANGAAGIIVSNHGARQLDYVPATISALEEVVKAARGQLPVFVDGGVRRGTDVFKALALGAAGVFVGRPVVFSLAAAG... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2 . Is an essential enzyme in photorespiration in plants . Photorespiration plays a vital role in C4 photosynthesis in Z.mays and is essential for maize seedling development and maintaining low ... |
P13006 | MQTLLVSSLVVSLAAALPHYIRSNGIEASLLTDPKDVSGRTVDYIIAGGGLTGLTTAARLTENPNISVLVIESGSYESDRGPIIEDLNAYGDIFGSSVDHAYETVELATNNQTALIRSGNGLGGSTLVNGGTWTRPHKAQVDSWETVFGNEGWNWDNVAAYSLQAERARAPNAKQIAAGHYFNASCHGVNGTVHAGPRDTGDDYSPIVKALMSAVEDRGVPTKKDFGCGDPHGVSMFPNTLHEDQVRSDAAREWLLPNYQRPNLQVLTGQYVGKVLLSQNGTTPRAVGVEFGTHKGNTHNVYAKHEVLLAAGSAVSPTIL... | Catalytic Activity: beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
Sequence Mass (Da): 65638
Sequence Length: 605
Subcellular Location: Secreted
EC: 1.1.3.4
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P05414 | MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPRILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGKMDKANDSGLSSYVAGQIDRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSLAAEGE... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2 . Is a key enzyme in photorespiration in green plants (Probable). To a lesser extent, is also able to use L-lactate and 2-hydroxbyutanoate as substrate in vitro, but shows almost no activity w... |
F5HGP1 | MGKKEMIMVKGIPKIMLLISITFLLLSLINCNVLVNSRGTRRSWPYTVLSYRGKEILKKQKEDILKRLMSTSSDGYRFLMYPSQQKFHAIVISMDKFPQDYILAGPIRNDSITHMWFDFYSTQLRKPAKYVYSEYNHTAHKITLRPPPCGTVPSMNCLSEMLNVSKRNDTGEKGCGNFTTFNPMFFNVPRWNTKLYIGSNKVNVDSQTIYFLGLTALLLRYAQRNCTRSFYLVNAMSRNLFRVPKYINGTKLKNTMRKLKRKQALVKEQPQKKNKKSQSTTTPYLSYTTSTAFNVTTNVTYSATAAVTRVATSTTGYRPD... | Function: Plays a role in viral entry into host cells. Forms a trimeric complex at the surface of the viral envelope together with gH and gL. This complex is required for entry in host fibroblasts . Mechanistically, engages host receptor(s) including PDGFRA to mediate infection .
PTM: N-glycosylated.
Sequence Mass (Da)... |
Q96P66 | MTSTCTNSTRESNSSHTCMPLSKMPISLAHGIIRSTVLVIFLAASFVGNIVLALVLQRKPQLLQVTNRFIFNLLVTDLLQISLVAPWVVATSVPLFWPLNSHFCTALVSLTHLFAFASVNTIVVVSVDRYLSIIHPLSYPSKMTQRRGYLLLYGTWIVAILQSTPPLYGWGQAAFDERNALCSMIWGASPSYTILSVVSFIVIPLIVMIACYSVVFCAARRQHALLYNVKRHSLEVRVKDCVENEDEEGAEKKEEFQDESEFRRQHEGEVKAKEGRMEAKDGSLKAKEGSTGTSESSVEARGSEEVRESSTVASDGSMEG... | Function: Orphan receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56716
Sequence Length: 508
Subcellular Location: Cell membrane
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A0MD30 | MQWGHCGVKSASCSWMPSLSFLSVWLILSFSLPYCLGSPSQDGYWSFFSEWFAPRFSVRALPFTLPNYRRSYESLLPNCRPDVPQFAFKHPLGILWHMRVSHLIDEMVSRRIYQTMEHSGQAAWKYVVGEATLTKLSKLDIVTHFQHLAAVEADSCRFLSSRLVMLKNLAVGNVSLQYNTTLDRVELIFPTPGTRPKLTDFRQWLISVHASIFSSVASSVTLFIVLWLRIPALRYVFGFHWPTATHHSS | Function: Minor envelope protein. Along with GP4, serves as the viral attachment protein responsible for mediating interactions with CD163 thereby playing a role in virus entry into susceptible host cells.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 28561
Sequence Length: 249
Subcellular ... |
P28992 | MQRFSFSCYLHWLLLLCFFSGSLLPSAAAWWRGVHEVRVTDLFKDLQCDNLRAKDAFPSLGYALSIGQSRLSYMLQDWLLAAHRKEVMPSNIMPMPGLTPDCFDHLESSSYAPFINAYRQAILSQYPQELQLEAINCKLLAVVAPALYHNYHLANLTGPATWVVPTVGQLHYYASSSIFASSVEVLAAIILLFACIPLVTRVYISFTRLMSPSRRTSSGTLPRRKIL | Function: Minor envelope protein. Part of the glycoproteins heterotrimer GP2b-GP3-GP4 which is probably responsible for the attachment to target host cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis.
Location Topology: Single-pass type I membrane protein
Sequence... |
P28968 | MGFIYARKLLLCMAVSIYAIGSTTTTETTTSSSSTSGSGQSTSSGTTNSSSSPTTSPPTTSSSPPTSTHTSSPSSTSTQSSSTAATSSSAPSTASSTTSIPTSTSTETTTTTPTASTTTPTTTTAAPTTAATTTAVTTAASTSAETTTATATATSTPTTTTPTSTTTTTATTTVPTTASTTTDTTTAATTTAATTTAATTTAATTTAATTTAATTTAATTTAATTSSATTAATTTAATTTAATTTAATTTAATTTAATTTGSPTSGSTSTTGASTSTPSASTATSATPTSTSTSAAATTSTPTPTSAATSAESTTEAPTS... | Function: Virulence factor.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 80343
Sequence Length: 797
Subcellular Location: Virion membrane
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P25088 | RRGSPQGGSHTTPHPDRLTPSPDDTYDDDTNHPNGRNNSIEIVPQLPPDRPLIELGVATLRKNFMEASCTVETNSGLAIFWKIGKPSVDAFNRGTTHTRLMRNGVPVYALVSTLRVPWLNVIPLTKITCAACPTNLVAGDGEDLNSCTTKSTTIPCPGQQRTHIFFSAKGHRAVCITSELVSQPTITWSVGSDRLRNDGFSQTWYGIQPGVCGILRSRFAFTAPPGALDQHQRTISVRSAHRTQRRAITKCYPTPTQLPTSL | Function: Virulence factor.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28695
Sequence Length: 262
Subcellular Location: Virion membrane
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O43292 | MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMVEEQFAGGDRARAFARDFAAHRKKSGALPVAWLERTMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRAASTESLVLTVPCGSDSTNSQAVGLLLALAAHFRGQIYWAKDIVFLVTEHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASGRPHGSHGLFLRYRVEALTLR... | Function: Component of the GPI transamidase complex, necessary for transfer of GPI to proteins . Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67623
Sequence Le... |
Q8G7C3 | MGKNITVLGAGAWGTAFGQVLADAGNTVTMWAKEQQIVEGIRDHHHNAVRLPSVEKLPDNMTATGDRAEAVKNADIVVVAIAAQFARVALVEFKGLIPDHAIVVSLMKGIERGTNKRMDEVVRESLDLPADRFAAISGPNLSKEIADRHPAATVVACTNLDNATKVAEACTTSYFKPFVTTDVIGLEMCGSLKNVTALAVGMARGAGYGENTAAMIETRGLAELTALGVAAGADPKTFFGLAGVGDLIATCGSSLSRNYTFGANLGKGLTVEEATKVSNGVAEGVPTTDAVVALGDQLDVPTPLAYQMSRVLNEGISCSE... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 34616
Sequence Length: 333
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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Q7VS47 | MSQARPATLRVAVLGAGSWGTALAAAASRRHPTVLWARDGAQAQAMAARHENTRYLPGVALPHALQVSADLAQALAHLAHDPAHALIILGVPVAGMTPLCTELAARLPALGLQAVPLVWTCKGFEEQTARLPHETVQAALGAMPGLAAGVLSGPSFAREVAQGLPVALTVASGSSAVRDAVTTALHGAAVRIYASTDVVGVEVGGALKNVIAVACGICDGLALGTNARAALITRGLAEMARFGAALGAQQETFAGLTGLGDLVLTATGELSRNRRVGLEIGAGRKLADILASGMTAEGVRCARAARDRARALNIELPITE... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 35664
Sequence Length: 351
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
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