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stringlengths 6
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stringlengths 11
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stringlengths 108
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P32190 | MFPSLFRLVVFSKRYIFRSSQRLYTSLKQEQSRMSKIMEDLRSDYVPLIASIDVGTTSSRCILFNRWGQDVSKHQIEYSTSASKGKIGVSGLRRPSTAPARETPNAGDIKTSGKPIFSAEGYAIQETKFLKIEELDLDFHNEPTLKFPKPGWVECHPQKLLVNVVQCLASSLLSLQTINSERVANGLPPYKVICMGIANMRETTILWSRRTGKPIVNYGIVWNDTRTIKIVRDKWQNTSVDRQLQLRQKTGLPLLSTYFSCSKLRWFLDNEPLCTKAYEENDLMFGTVDTWLIYQLTKQKAFVSDVTNASRTGFMNLSTLKYDNELLEFWGIDKNLIHMPEIVSSSQYYGDFGIPDWIMEKLHDSPKTVLRDLVKRNLPIQGCLGDQSASMVGQLAYKPGAAKCTYGTGCFLLYNTGTKKLISQHGALTTLAFWFPHLQEYGGQKPELSKPHFALEGSVAVAGAVVQWLRDNLRLIDKSEDVGPIASTVPDSGGVVFVPAFSGLFAPYWDPDARATIMGMSQFTTASHIARAAVEGVCFQARAILKAMSSDAFGEGSKDRDFLEEISDVTYEKSPLSVLAVDGGMSRSNEVMQIQADILGPCVKVRRSPTAECTALGAAIAANMAFKDVNERPLWKDLHDVKKWVFYNGMEKNEQISPEAHPNLKIFRSESDDAERRKHWKYWEVAVERSKGWLKDIEGEHEQVLENFQ | 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): 79824
Sequence Length: 709
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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P52112 | MFKALIGAAVVVLLAVLSKTRNYYIAGLVPLFPTFALIAHYIVGKGRSLDDLKTTIVFGMWSIIPYFVYLAALYLLVERFRLETSLALAALAWLVAASVLVGLWVRLHA | Function: Could play a role in alginate biosynthesis. Overexpression may be lethal.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12041
Sequence Length: 109
Subcellular Location: Cell inner membrane
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O86963 | MTFSQKDRKETIQETAKTTYDVLIIGGGITGAGVAVQTAAAGMKTVLLEMQDFAEGTSSRSTKLVHGGIRYLKTFDVEVVADTVRERAIVQQIAPHIPKPDPMLLPIYDEPGATFSLFSVKVAMDLYDRLANVTGSKYENYLLTKEEVLAREPQLQAENLVGGGVYLDFRNNDARLVIENIKRAQADGAAMISKAKVVGILHDEQGIINGVEVEDQLTNERFEVHAKVVINTTGPWSDIVRQLDKNDELPPQMRPTKGVHLVVDREKLKVPQPTYFDTGKNDGRMVFVVPRENKTYFGTTDTDYTGDFAHPTVTQEDVDYLLTIVNERFPHAQITLDDIEASWAGLRPLITNNGGSDYNGGGKGKLSDESFEQIVESVKEYLADERQRPVVEKAVKQAQERVEASKVDPSQVSRGSSLERSKDGLLTLAGGKITDYRLMAEGAVKRINELLQESGASFELVDSTTYPVSGGELDAANVEEELAKLADQAQTAGFNEAAATYLAHLYGSNLPQVLNYKTKFEGLDEKESTALNYSLHEEMVLTPVDYLLRRTNHILFMRDTLDDVKAGVVAAMTDFFGWSEEEKAAHVLELNQVIAESDLTALKGGKKDE | Catalytic Activity: O2 + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H2O2
Sequence Mass (Da): 67216
Sequence Length: 609
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.3.21
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Q6X1C0 | MLNGNKCHILLLPCPAQGHINPILQFGKRLASHNLLTTLVNTRFLSNSTKSEPGPVNIQCISDGFDPGGMNAAPSRRAYFDRPQSRSGQKHVGLIESLRSRGRPGACFGLRPVPLWAMNVAERSGLRSVAFFTQPCAVDTIYRHVWEGRIKVPVAEPVRLPGLPPLEPSDLPCVRNGFGRVVNPDLLPLRVNQHKNLDKADMMGRNSIYELEADLLDGSRLPLPVKSIGPTVPSTYLDNRIPSDSHYGFNLYTPDTTPYLDWLDSKAPNSVIYVSFGSLSSLSPDQTNEIASGLIATNKSFIWVVRTSELAKLPANFTQENASRGLVVTWCDQLDLLAHVATGCFVTHCGWNSTMEGVALGVPMVGVPQWSDQPMNAKYVEDVWKVGVRAKTYGKDFVRGEEFKRCVEEVMDGERSGKIRENAARWCKLAKDSVSEGGSSDKCIKEFIHQCCNDSKISLV | Function: Crocetin glucosyltransferase involved in the synthesis of crocin, one of the apocarotenoids responsible for the color and bitter taste of saffron.
Catalytic Activity: crocetin + UDP-alpha-D-glucose = beta-D-glucosyl crocetin + UDP
Sequence Mass (Da): 50722
Sequence Length: 460
EC: 2.4.1.271
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Q8MVS5 | MMQIKRLLCKSCGLGTLLVAVVWLLALLFYSHSLRSSIRSAGWRIDEGNATPRAELSYQARVTVGCTPNASITTGESPAAPKPPSDPEQLELLGVVRNKQDKYIRDIGYKHHAFNALVSNNIGLFRAIPDTRHKVCDRQETTEAENLPQASIVMCFYNEHKMTLMRSIKTVLERTPSYLLREIILVDDHSDLPELEFHLHGDLRARLKYDNLRYIKNEQREGLIRSRVIGAREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAVPVIDLINADTFEYTPSPLVRGGFNWGLHFRWENLPEGTLKVPEDFRGPFRSPTMAGGLFAVNRKYFQHLGEYDMAMDIWGGENIEISFRAWQCGGAIKIVPCSRVGHIFRKRRPYTSPDGANTMLKNSLRLAHVWMDQYKDYYLKHEKVPKTYDYGDISDRLKLRERLQCRDFAWYLKNVYPELHVPGEESKKSAAAPIFQPWHSRKRNYVDTFQLRLTGTELCAAVVAPKVKGFWKKGSSLQLQTCRRTPNQLWYETEKAEIVLDKLLCLEASGDAQVTVNKCHEMLGDQQWRHTRNANSPVYNMAKGTCLRAAAPTTGALISLDLCSKSNGAGGSWDIVQLKKPTEAEGRAKEARNSDKAL | Function: Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor . Displays the same enzyme activity toward MUC1, MUC4, and EA2 . Not involved in glycosylation of erythropoietin (EPO) . It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties . Protein modification by this enzyme might be important for cytokinesis and tube formation during embryogenesis . Together with Pgant3, regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles .
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 71828
Sequence Length: 632
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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Q6WFW1 | MAKEHIVLFPFMSQGHIIPFLSLAKLISERHPTYTITLLNTPLNILNLQSTLPPNSNIHLKSLPYRSSDFGLPPDRENTDSLPFPLVLSFYQSGESLATHFTHFVSDLTRQNHDTPPLLIVADVFFGWTAEIAKRLNTHVSFSTCGAYGTAAYFSVWLHLPHAETDLPDFTAPGFPETFKLQRNQLSTYLKKADGSDRWSKFFQRQISLSLTSDAMICNTVEEMEAEGLRLLRKNTGLRVWSIGPLLPSLPPNSSLGRSGRKSGMEVSYIMKWLDSHPPGSVVYVSFGSIHDTAAQMTSLAVGLAVELATRSCGHSGRRFGGNRNRNSNPNGVPDEFEARMRGSGRGILIHGWAPQLEILEHESTGAFVSHCGWNSTLESLSRGVCMIGWPLAAEQFYNSKMVEEDWEWGGTCEGSGGGVRSEEVERLVRLVTEDEKGSDEENEQYDEMIGGYEEKGGEGSLSGQLIKFIGMESQ | Function: Crocetin glucosyltransferase involved in the synthesis of crocin, one of the apocarotenoids responsible for the color and bitter taste of saffron.
Catalytic Activity: crocetin + UDP-alpha-D-glucose = beta-D-glucosyl crocetin + UDP
Sequence Mass (Da): 52650
Sequence Length: 475
EC: 2.4.1.271
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G5EBR3 | MATWIVGKLIIASLILGIQAQQARTKSQDIFEDDNDNGTTTLESLARLTSPIHIPIEQPQTSDSKILAHLFTSGYDFRVRPPTDNGGPVVVSVNMLLRTISKIDVVNMEYSAQLTLRESWIDKRLSYGVKGDGQPDFVILTVGHQIWMPDTFFPNEKQAYKHTIDKPNVLIRIHNDGTVLYSVRISLVLSCPMYLQYYPMDVQQCSIDLASYAYTTKDIEYLWKEHSPLQLKVGLSSSLPSFQLTNTSTTYCTSVTNTGIYSCLRTTIQLKREFSFYLLQLYIPSCMLVIVSWVSFWFDRTAIPARVTLGVTTLLTMTAQSAGINSQLPPVSYIKAIDVWIGACMTFIFCALLEFALVNHIANKQGVERKARTEREKAEIPLLQNLHNDVPTKVFNQEEKVRTVPLNRRQMNSFLNLLETKTEWNDISKRVDLISRALFPVLFFVFNILYWSRFGQQNVLF | Function: Glutamate-gated chloride channel subunit; channel properties depend on the subunit composition. Glutamate binding triggers a rapidly reversible current in heteromeric channels formed by glc-1 and glc-2, while the anti-helmintic drug ivermectin and other avermectins trigger a permanently open channel configuration. Channels containing only glc-1 are activated by ivermectin, but not by glutamate alone (in vitro). The heteromeric channel formed by glc-1 and glc-2 is also activated by ibotenate, and it is blocked by picrotoxin and flufenamic acid . Plays a role in the regulation of locomotor behavior .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52553
Sequence Length: 461
Domain: Glutamate binding is mediated by the extracellular domain. In contrast, the allosteric modulator ivermectin binds between subunits at the periphery of the transmembrane domain, proximal to the extracellular side.
Subcellular Location: Postsynaptic cell membrane
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Q94900 | MGSGHYFWAILYFASLCSASLANNAKINFREKEKKVLDQILGAGKYDARIRPSGINGTDGPAIVRINLFVRSIMTISDIKMEYSVQLTFREQWTDERLKFDDIQGRLKYLTLTEANRVWMPDLFFSNEKEGHFHNIIMPNVYIRIFPNGSVLYSIRISLTLACPMNLKLYPLDRQICSLRMASYGWTTNDLVFLWKEGDPVQVVKNLHLPRFTLEKFLTDYCNSKTNTGEYSCLKVDLLFKREFSYYLIQIYIPCCMLVIVSWVSFWLDQGAVPARVSLGVTTLLTMATQTSGINASLPPVSYTKAIDVWTGVCLTFVFGALLEFALVNYASRSGSNKANMHKESMKKKRRDLEQASLDAASDLLDTDSNATFAMKPLVRHPGDPLALEKRLQCEVHMQAPKRPNCCKTWLSKFPTRQCSRSKRIDVISRITFPLVFALFNLVYWSTYLFREEEDE | Function: Glutamate-gated chloride channel subunit . Together with Gamma-aminobutyric acid receptor Rdl, plays an important role in the visual response by regulating the activity of ON/OFF-selective neurons .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52307
Sequence Length: 456
Subcellular Location: Postsynaptic cell membrane
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Q7Z3D6 | MPFTLHLRSRLPSAIRSLILQKKPNIRNTSSMAGELRPASLVVLPRSLAPAFERFCQVNTGPLPLLGQSEPEKWMLPPQGAISETRMGHPQFWKYEFGACTGSLASLEQYSEQLKDMVAFFLGCSFSLEEALEKAGLPRRDPAGHSQTTVPCVTHAGFCCPLVVTMRPIPKDKLEGLVRACCSLGGEQGQPVHMGDPELLGIKELSKPAYGDAMVCPPGEVPVFWPSPLTSLGAVSSCETPLAFASIPGCTVMTDLKDAKAPPGCLTPERIPEVHHISQDPLHYSIASVSASQKIRELESMIGIDPGNRGIGHLLCKDELLKASLSLSHARSVLITTGFPTHFNHEPPEETDGPPGAVALVAFLQALEKEVAIIVDQRAWNLHQKIVEDAVEQGVLKTQIPILTYQGGSVEAAQAFLCKNGDPQTPRFDHLVAIERAGRAADGNYYNARKMNIKHLVDPIDDLFLAAKKIPGISSTGVGDGGNELGMGKVKEAVRRHIRHGDVIACDVEADFAVIAGVSNWGGYALACALYILYSCAVHSQYLRKAVGPSRAPGDQAWTQALPSVIKEEKMLGILVQHKVRSGVSGIVGMEVDGLPFHNTHAEMIQKLVDVTTAQV | Function: D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline.
Catalytic Activity: D-glutamate = 5-oxo-D-proline + H2O
Sequence Mass (Da): 66437
Sequence Length: 616
Subcellular Location: Mitochondrion matrix
EC: 4.2.1.48
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Q8BH86 | MTISFLLRSCLRSAVRSLPKAALIRNTSSMTEGLQPASVVVLPRSLAPAFESFCQGNRGPLPLLGQSEAVKTLPQLSAVSDIRTICPQLQKYKFGTCTGILTSLEEHSEQLKEMVTFIIDCSFSIEEALEQAGIPRRDLTGPSHAGAYKTTVPCATIAGFCCPLVVTMRPIPKDKLERLLQATHAIRGQQGQPIHIGDPGLLGIEALSKPDYGSYVECRPEDVPVFWPSPLTSLEAVISCKAPLAFASPPGCMVMVPKDTASSASCLTPEMVPEVHAISKDPLHYSIVSAPAAQKVRELESTIAVDPGNRGIGHLLLKDELLQAALSLSHARSVLVTTGFPTHFNHEPPEETDGPPGAIALAAFLQALGKETAMVVDQRALNLHMRIVEDAIRQGVLKTPIPILTYQGRSMEDARAFLCKDGDPKSPRFDHLVAIERAGRAADGNYYNARKMNIKHLVDPIDDIFLAAQKIPGISSTGVGDGGNELGMGKVKAAVKKHIRNGDVIACDVEADFAVIAGVSNWGGYALACALYILNSCQVHERYLRRATGPSRRAGEQSWIQALPSVAKEEKMLGILVENQVRSGVSGIVGMEVDGLPFHDVHAEMIRKLVGATTVHM | Function: D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline.
Catalytic Activity: D-glutamate = 5-oxo-D-proline + H2O
Sequence Mass (Da): 66366
Sequence Length: 617
Subcellular Location: Mitochondrion matrix
EC: 4.2.1.48
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P48244 | MSTLWADLGPSLLPAFWVTIKLTIYSAIGAMIFGTILTTMRVSPVKILRTLSTAYINTVRNTPLTLVVLFCSFGLYQNLGLTLAGRESSTFLVDNNFRLAVLGFILYTSTFVAESLRSGINTVHFGQAEAARSLGLGFGATFRSIIFPQAVRAAIVPLGNTLIALTKNTTIASVIGVGEASLLMKATIENHANMLFVVFAIFAVGFMILTLPMGLGLGKLSERLAVKK | Function: Part of the ABC transporter complex GluABCD involved in glutamate uptake. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24469
Sequence Length: 228
Subcellular Location: Cell membrane
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P9WGI9 | MTAAPDARTTAVMSAPLAEVDPDIAELLAKELGRQRDTLEMIASENFVPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAKALFGAEFANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNFSGKLYENGFYGVDPATHLIDMDAVRATALEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSGLIVGKQQYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLMAPDVAKAGVSVVSGGTDVHLVLVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPMVTSGLRIGTPALATRGFGDTEFTEVADIIATALATGSSVDVSALKDRATRLARAFPLYDGLEEWSLVGR | Cofactor: Binds 1 pyridoxal phosphate per homodimer. This is unusual in the SHMT family, that normally contains 1 pyridoxal phosphate per subunit.
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-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 46216
Sequence Length: 438
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
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Q88R12 | MFSKQDQIQGYDDALLAAMNAEEQRQEDHIELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEALAIERAKQLFGADYANVQPHSGSSANGAVYLALLQAGDTILGMSLAHGGHLTHGAKVSSSGKLYNAVQYGIDTNTGLIDYDEVERLAVEHKPKMIVAGFSAYSKTLDFPRFRAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKSNEEIEKKLNAAVFPGAQGGPLMHVIAAKAVCFKEALEPGFKAYQQQVIENAQAMAQVFIDRGYDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAHITVNKNAVPNDPQSPFVTSGLRIGTPAVTTRGFKVAQCVALAGWICDILDNLGDADVEADVAKNVAALCADFPVYR | 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-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 44556
Sequence Length: 417
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
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Q9Z831 | MVSLLHKFLENASGKKGQSLASTAYLAALDHLLNAFPSIGERIIDELKSQRSHLKMIASENYSSLSVQLAMGNLLTDKYCEGSPFKRFYSCCENVDAIEWECVETAKELFAADCACVQPHSGADANLLAVMAILTHKVQGPAVSKLGYKTVNELTEEEYTLLKAEMSSCVCLGPSLNSGGHLTHGNVRLNVMSKLMRCFPYDVNPDTECFDYAEISRLAKEYKPKVLIAGYSSYSRRLNFAVLKQIAEDCGSVLWVDMAHFAGLVAGGVFVDEENPIPYADIVTTTTHKTLRGPRGGLVLATREYESTLNKACPLMMGGPLPHVIAAKTVALKEALSVDFKKYAHQVVNNARRLAERFLSHGLRLLTGGTDNHMMVIDLGSLGISGKIAEDILSSVGIAVNRNSLPSDAIGKWDTSGIRLGTPALTTLGMGIDEMEEVADIIVKVLRNIRLSCHVEGSSKKNKGELPEAIAQEARDRVRNLLLRFPLYPEIDLEALV | 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-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 54263
Sequence Length: 497
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
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Q8TK94 | MSYIEKIDPDMFEAIQKEADRQEHKLNLIASENYASRAVMEAQGSIMTNKYAEGYSGKRYYGGCDFVDIAENLAIARAKEIFGAKYVNVQPHSGSGANMAVYFSVLQPGDTIMSMDLSHGGHLSHGSPVSFSGKLYNIVPYGVSKETEALDYDELMKMAKECKPKMIVCGASAYPRVIDFKKFREIADEVGAYLLADIAHIAGLVVSGVHPSPVPYADFVTTTTHKTLRGPRGGMIISKTEELAMGVNKAVFPGIQGGPLMHVIAAKAVAFKEAMDEKFRQDQAQTVKNAKVLCACLKEKGFDIVSGGTDNHLMLVNLNNMNITGKDAEAAMSKAGIIANKNTVPFETRSPFITSGVRLGTPACTTRGMKEKEMELIADYIETAIKNAGNDALLSEVSAKVRDLCSRFPVYS | 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-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 44740
Sequence Length: 412
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
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Q2FLH5 | MSYLETTDPEIAAIIDKETNRQINGLELIASENVVSRAVLEASGSIMTNKYAEGYPGKRYYGGCEFHDMAENLARDRVCSLFGAEHANVQPHSGSQANMAVYFTVLKPSDKILSMNLSQGGHLSHGSPVNFSGIIYESHQYGVDLKTERMDYGTIAEMARTIKPKIIVCGASAYPREIDFKAFAEISEEVGAYCVADIAHIAGLCATGIHPSPVGLTTFTTSTTHKTLRGPRGGFILCDKEFAAPIDKAVFPGMQGGPLMHIIAAKAVCFKEASTKEFKKYSEQVVKNARTMAETLSANGVRLVSGGTDNHLCLLDLTNFGITGLEAEQALGNAGITVNKNTIPNETKSPFVTSGLRVGTPAVTSRGMKESEMKQIGEWIAAIIRDSKNTRLQETIREEVKSLASQYPLYPDLT | 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-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 44828
Sequence Length: 414
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
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Q9UWT5 | MSLPKELEKVLEITKAQNVWRRTQTLNLIASENVMSPLAESVYMSDFMSRYAEGKPYKRYYQGTKYTDEIETLTMELMNEITNSKDCDLRPTSGTIANAAVFRVLAEPGDKALIAPVQAGAHVSHTKFGTLGALGIQHIEMPFDEENINVDVDKAIKMIEEVKPKFVVLGGSLYLFPHPTKELAQHVHAVGAKLVYDAAHVYGLIEGKVWSNPLKDGADIMTVSTHKTFPGPQGGAIFSDGSEVFKQVSKTIFPWFVSNHHLHRLPATAVTAIEMKYFGESYANQILRNSKALAEALAERGFKVIGENLGYTKSHQVAVDVRQFGGGNKIAKLLEDANIIVNKNLLPYDKPEDVSDPSGLRIGVQEMTRYGMKEGEMEEIAELFKKVIIDKKDVNEVKKEVIEMRRNFLEVKYTFDDMKDLEKYSSKSLKLII | Function: Catalyzes the reversible interconversion of serine and glycine with the modified folate sulfopterin serving as the one-carbon carrier. Cannot use tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of both allo-threonine and beta-phenylserine.
Catalytic Activity: 5,10-methylenetetrahydrosulfopterin + glycine + H2O = L-serine + tetrahydrosulfopterin
Sequence Mass (Da): 48509
Sequence Length: 433
Pathway: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.2.-
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A8M1D3 | MSRNAESTAYRSALEVISAVEPRVADAIRSELTDQRESLKLIASENYASPATLLAMGNWFSDKYAEGTIGRRFYAGCQNVDTIEALAAEHARELFGATHAYVQPHSGIDANLVAFWAVLADRVESPTLERARARHVNDLTEADWFALRRELGNQRMLGMSLDAGGHLTHGFRPNISGKMFDQRSYGTDPETGLIDYDQVAEAAREFRPLILVAGYSAYPRKVNFRIMREIADSVGATFMVDMAHFAGLVAGKVFTGDFDPVPHAHIVTSTTHKSLRGPRGGLVLCGPELAEQVDRGCPMVLGGPLPHVMAAKAVALAEARRPDFADYAERIVANAQALADGLLRRGAKLVTGGTDNHLALIDVTGYGLTGRQAEQALLDSGIVTNRNAVPQDPNGAWYTSGIRVGTPALTTRGLGTAELEATAELIHTVLSLTSPGANADGTPSKAKYVLDPAVADRVNKQASELLAGFPLYPAIDLG | 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-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 51274
Sequence Length: 478
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
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A4X6P4 | MSGNAESTAYRSALEVIGAVEPRVANAIRAELTDQRESLKLIASENYASPATLLAMGNWFSDKYAEGTVGRRFYAGCQNVDTVEALAAEHARELFGAPYAYVQPHSGIDANLVAFWAVLADRIESPALRRAQARHVNDLTEADWFALRRELGNQRMLGMSLDAGGHLTHGFRPNISGKMFDQRSYGTDPETGLIDYDGVAEAAREFKPLILLGGYSAYPRKVNFRILREIADSVGATFMVDMAHFAGLVAGKAFTGDFDPVPHAHIVTSTTHKSLRGPRGGLVLCGPELAEQVDRGCPMVLGGPLPQVMAAKAVALAEARRPDFVDYAGRIVANAQALADGLQRRGAQLVTGGTDNHLALIDVTGYGLTGRQAEHALLDSGIVTNRNAIPQDPNGAWYTSGIRVGTPALTTRGLGTAELDATAELIHTVLSHTAPGTNADGTSSKAKYVLDPAVADRVGKQASDLLTGFPLYPAIDLG | 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-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 50917
Sequence Length: 478
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
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Q9LM59 | MDRIAQSDLSLGFGSSHALPLPHPPRIPIADDSITLQIDSSFRPSSNPMPPVPLQLLEQRFDVTGSCSRVVEEDDEVVGDNDDDDQREEEQFILLGHPMKLKRGRGGNSYSLASSSPCKRFVVDSGIESRRAVVRAWGNQSIEEADPEIHEFMEKEKQRQFRGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIEILCQERALAAFGLNHEKWGVNVQPYSCTSANFAVFTGLLMPGERIMGLDSPSGGHMSHGYYTPGGKKVSGASIFFESFPYKVDPRTGYIDYDKLEEKALDYRPKILICGGSSYPRDWEFPRFRHIADKCGAVLMFDMAQISGLVAAKESPNPFDYCDIVTSTTHKSLRGPRGGIIFYKRGLKPKKQSINLNHCESNIQYDFEEKINFSVFPSLQGGPHNNHIAALAIALKQAASPEYKLYMRQVKKNAKALASALISRKCKLITGGTDNHLLLWDLTPLGLTGKVYEKVCEMCHITVNKVAIFSENGVISPGGVRIGSPAMTSRGCLEPEFETMADFLYRAAQIASAAQREHGKLQKEPLKSIYHCKEIADLRNQVEAFATQFAMPAFDM | Function: Catalyzes the 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): 66647
Sequence Length: 599
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
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Q84WV0 | MDLSRSQTNFQLGFGCSHASMTPTPTPRAPIADDSINLQVDQSFRSLPTTFSPIPLQLLEQKAEKTTTVDEPKKDGGGGGDQKEDEHFRILGHHMCLKRQRDCPLLLTQSKHPKRSSIGDSDLESRRAAVRAWGDQPIHLADPDIHELMEKEKQRQVRGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIENLCIERALTAFGLESDKWGVNVQPYSCTSANFAVYTGLLLPGERIMGLDSPSGGHMSHGYCTPGGKKISAASIFFESFPYKVNPQTGYIDYDKLEDKALDYRPKILICGGSSYPRDWDFARVRQIADKCGAVLMCDMAHISGLVATKECSNPFDHCDIVTSTTHKGLRGPRGGIIFYRRGPKIRKQGHHSSHCDTSTHYDLEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYIQQMKKNAQALAAALLRRKCRLVTGGTDNHLLLWDLTPMGLTGKVYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTTRGCIESDFETMADFLIKAAQITSALQREHGKSHKEFVKSLCTNKDIAELRNRVEAFALQYEMPASLIRIE | Function: Catalyzes the 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): 66294
Sequence Length: 598
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
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Q89669 | MATFKVLVLMILWITSIFNVRCEKFVTIPVNCSGEVDIDKMDVMCPNRYNLLSTNHLMEGEEVETFCRPSLRENDLLDGYLCRKQKWEVTCTETWYFVTDVKYQIIEVIPTENECMEERERKLKGEYIPPYYPPTNCVWNAIDTQERTFITLIEHPVIEDPVTMTLMDSKFTKPCNPKHNEVTICDTYNPLIKWISKETSGLNLHCQIKSWECIPVKLHHSHRNMMEALYLESPDFGIVDASKICNLTFCGYNGILLDNGEWWSIYRSGFTHGFLDNHILKNRRIEECKEKKPGYKLAKLDTTYIDLEFEIELEHEKCLGTLEKLQNGEYVTPLDLSYLSPSNPGKHYAYRLEYINTTEHKCVQLGFTYEGGDCRKMLDERDDHGAYYNWTTIKLQRVIRAVCYYHTFSMNLDESKHKYYDQDNRSIQIDEKFISEVLKSTPLIDRHEKYEGNLSWNGIIIESKNGHEKNVIVPSASQYNHVMINKILKRLDTVMYDSYKFDSESGSISYNKIVPIVREDNLQNAHRVDVIQYIKDKGSYIINGFTGWFSSLGKLMRWTIWGVGLFFSIFTLYKIIMILRKHSNDNVRKEFKETAGKVMIGQPIDTKSMSRTSIKANNKGKFDKVKDLFTPRSKTISHLTTDTLKEHTDGTYEELHFFNV | Function: Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity).
PTM: Glycosylated by host. Glycosylation is crucial for glycoprotein export at the cell surface (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 77206
Sequence Length: 660
Subcellular Location: Virion membrane
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P32595 | MFKVLIITLLVNKIHLEKIYNVPVNCGELHPVKAHEIKCPQRLNELSLQAHHNLAKDEHYNKICRPQLKDDAHLEGFICRKQRWITKCSETWYFSTSIEYQILEVIPEYSGCTDAVKKLDQGALIPPYYPPAGCFWNTEMNQEIEFYVLIQHKPFLNPYDNLIYDSRFLTPCTINDSKTKGCPLKDITGTWIPDVRVEEISEHCNNKHWECITVKSFRSELNDKERLWEAPDIGLVHVNKGCLSTFCGKNGIIFEDGEWWSIENQTESDFQNFKIEKCKGKKPGFRMHTDRTEFEELDIKAELEHERCLNTISKILNKENINTLDMSYLAPTRPGRDYAYLFEQTSWQEKLCLSLPDSGRVSKDCNIDWRTSTRGGMVKKNHYGIGSYKRAWCEYRPFVDKNEDGYIDIQELNGHNMSGNHAILETAPAGGSSGNRLNVTLNGMIFVEPTKLYLHTKSLYEGIEDYQKLIKFEVMEYDNVEENLIRYEEDEKFKPVNLNPHEKSQINRTDIVREIQKGGKKVLSAVVGWFTSTAKAVRWTIWAVGAIVTTYAIYKLYKMVKSNSSHSKHREADLEGLQSTTKENMRVEKNDKNYQDLELGLYEEIRSIKGGSKQTGDDRFFDH | Function: Attaches the virus to host cellular receptors, inducing endocytosis of the virion. The acidic pH of the endosome induces conformational changes in the glycoprotein trimer which trigger fusion between the virus and the cell membrane (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72284
Sequence Length: 623
Subcellular Location: Virion membrane
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P13180 | MTSSVTISVVLLISFITPLYSYLSIAFPENTKLDWKPVTKNTRYCPMGGEWFLEPGLQEESFLSSTPIGATPSKSDGFLCHAAKWVTTCDFRWYGPKYITHSIHNIKPTRSDCDTALASYKSGTLVSLGFPPESCGYASVTDSEFLVIMITPHHVGVDDYRGHWVDPLFVGGECDQSYCDTIHNSSVWIPADQTKKNICGQSFTPLTVTVAYDKTKEIAAGGIVFKSKYHSHMEGARTCRLSYCGRNGIKFPNGEWVSLDVKTRIQEKHLLPLFKECPAGTEVRSTLQSDGAQVLTSEIQRILDYSLCQNTWDKVERKEPLSPLDLSYLASKSPGKGLAYTVINGTLSFAHTRYVRMWIDGPVLKEPKGKRESPSGISSDIWTQWFKYGDMEIGPNGLLKTAGGYKFPWHLIGMGIVDNELHELSEANPLDHPQLPHAQSIADDSEEIFFGDTGVSKNPVELVTGWFTSWKESLAAGVVLILVVVLIYGVLRCFPVLCTTCRKPKWKKGVERSDSFEMRIFKPNNMRARV | Function: Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity).
PTM: Glycosylated by host. Palmitoylated by host on Cys-498 (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 59185
Sequence Length: 530
Subcellular Location: Virion membrane
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A7WNB3 | MAHYELHVLFVHSWMLALILITTLVWLAASQKAFTPDLVFPEMNRNSSWSVANYGEILCPTSFQSYDPKKHQILTRVLVERPSLNTDTKVEGYTCHKVKYETICDMPWYFSPTISHSISPLRVKESECKDAIAEHQLGTHVPLSFPPEDCSWNSVNTKEYEDIIVKEHPVMLDPYTNNYVDAIFPGGISSPGMGGTIHDDMMWVSKDLAVSPECSGWQRSMGLIYSSRLYGEREPMLEVGSIHIEGHRDKNLTLACRISFCGEIGVRFHDGEWMKVSVNLDHPNSVTFQVTDFPPCPPGTTIQTAVVENINPEIQELTVNMMYRLKCQETISKMVSGLPTSALDLSYLIQVQEGPGIVYKREKGILYQSVGMYQYIDTVTLNKEENQLGENSRGQKVFWTEWSDSPTRPGLQEGINGIVKYEGQVRVPLGMSLRLEAATELMWGHPVHTVSHPILHVISNHTEQSVTTWNRGVNSTNLIGLATRSISGFYDNLKLYLILALIFVSLIALVVLDVIPFKYILFVLCPPLLLCRFIKCSRRKPETRDRYHVEYNRPGQVSSAF | Function: Attaches the virus to host receptors, inducing clathrin-dependent endocytosis of the virion.
PTM: Glycosylated by host.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63553
Sequence Length: 561
Subcellular Location: Virion membrane
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Q77SK0 | MDPRIMYYTVLLTTAARVYGQTIKPGVDSVSDQPTWANPLFTYPVDCPAAKLSKVSPSQLRCPRIFDDENRGLVAYPAVIRSLSVGNNLGDIHTQGEYVHKVLYRTTCSTGFFGGQTIEKALVEMKLAPREVGVYDTTTASALYFPAPRCQWYTDNVHNDLTFYYTTAKSVLRDPYTLGFLDSDFIEGKCSKSPCQTHWSNVVWKGDSGVAACDTGSEIKGHIFVDKTSHHVVKATSYGHHPWGLHRACMITFCGKPWIRTDLGDLIAIEYNGGATLLAFPACKDTTVGMRGSLDDFAYLDDLVKSSESREECLEAHAEIIATNSVTPYLLSKFRSPHPGINDVYAMHDGSIYHGKCMTVAIDEVSKDRRTYRAHQTSAFVAWGHPFGDEWGGFHGLHGNDTPVIPDLEKYVAQYKVSMMDKMDIRPVPHPSVQILYNDTDTADITIRKIDSFDLQSLNWSFWPSLSALGGVPILLALVFFLYCCMNRRPSMPAAPQEIPMYHLASRG | Function: Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity).
PTM: Glycosylated by host. Glycosylation is crucial for glycoprotein export at the cell surface (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 56602
Sequence Length: 508
Subcellular Location: Virion membrane
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P28278 | MGFVCLFGLVVMGAWGAWGGSQATEYVLRSVIAKEVGDILRVPCMRTPADDVSWRYEAPSVIDYARIDGIFLRYHCPGLDTFLWDRHAQRAYLVNPFLFAAGFLEDLSHSVFPADTQETTTRRALYKEIRDALGSRKQAVSHAPVRAGCVNFDYSRTRRCVGRRDLRPANTTSTWEPPVSSDDEASSQSKPLATQPPVLALSNAPPRRVSPTRGRRRHTRLRRN | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25193
Sequence Length: 224
Subcellular Location: Virion membrane
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P52526 | MELLLFVMSLILLTFSKAMPLFDHNSFYFEKLDDCIAAVINCTRSEVPLLLEPIYQPPVYNEDVMSILLKPPTKKKPFSRIMVTNEFLSDFLLLQDNPEQLRTLFALIGDPESRDNWLNFFNGFQTCSPSVGITTCISDNCRKYLPERITYVNNFFVDNIAGLEFNISENTDSFYSNIGFLLYLENPATGITKIIRFPFNSLTLFDTILNCLKYFHLKTGVEFDLLKQMEAYNSKLPFRSSRPTILIRNT | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28904
Sequence Length: 250
Subcellular Location: Virion membrane
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P52509 | MKTNIFFIFLISILNQIYALFNNSYYSNLEQECIKNILNCTQSKTLSLLEPIDQAPIPKSDIISRLLYHTPYISRRDQVLIDEDFLETFYLLYNNPNQLHTLLSLIKDSESGHNWLGFLNNFERCLSDNTLLTCRDNVCKSYSYEKLKFTGNIFVENIIGFEFNIPSNMINFNMSILIYLENEETRTQRIVRIDHHGINVFDALLNCLRYFSRYYNFSFPLIQEMEKYNEVLPFRSEFSNLLIRTY | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29259
Sequence Length: 246
Subcellular Location: Virion membrane
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F5HDB7 | MGIFALFAVLWTTLLVTSHAYVALPCCAIQASAASTLPLFFAVHSIHFADPNHCNGVCIAKLRSKTGDITVETCVNGFNLRSFLVAVVRRLGSWASQENLRLLWYLQRSLTAYTVGFNATTADSSIHNVNIIIISVGKAMNRTGSVSGSQTRAKSSSRRAHAGQKGK | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH. Targets heparan sulfate proteoglycans of the syndecan family as well as host EPHA2 to promote viral entry.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17999
Sequence Length: 167
Subcellular Location: Virion membrane
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P52514 | MMPLLLLILLSTRNLLGAAQSQESPVAGERRALDLTTVYVLPRSEPINATVEHKCREALASCYNGSEFQPLHDDGPIRPDPYRFSTMIRFKRSYGELPLPIELNDEFLEQLSLLHNNTDQLRVLLTLMRTSRASDWMSFLGGYTQCDAPKSVVFTCVESVCYEHDLMRLNYTTDLFTENVLGLDVSPPVLSVLVLLRNNHTKAESVVRVPTSSMSLLDGTYNLLRTILGHMSLDTDLIGVLRSYRDRFPAVFSVSDQIKITRQHYRPQYQRKRP | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31221
Sequence Length: 274
Subcellular Location: Virion membrane
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Q6UDG5 | MRRSAARGRAVSSTQTAMGAGAAIAVWAAALIALYSSCAAQTAPKTSSLRAANASDTIGRLIDGAEQLVSMRCMTSFEHEAAVTLYGPEYTPGGSMFEDLLTIIFKPQCSPPEAILWYKSGTAVRVNPYYLCRILVLALQGNPRGEVKFVVSRLIAEHAGGPLVRWPTTNVLRPEKTAPGGV | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH.
PTM: O-glycosylated, and sialylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19354
Sequence Length: 182
Subcellular Location: Virion membrane
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Q01031 | MKWLLGAYVCLCLANILNALIPNPCCNVFALNETLIPSIYDINWIYITDPQTCKGVSVAQVFQRRTAQHMSTRYVCSNGFNVISFLLAVLRKLPLNTEEYNFKNRLITLQNSFLSKLGPDTTSAIKFKSKYGQLAKTRNLE | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16000
Sequence Length: 141
Subcellular Location: Virion membrane
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P52511 | MSPLVAVLVFFSAALGVPGPGVAGNPRGLDAIFEAPVTPAPPTRHPRREELEWDDEDHPLLDLEPPVGSRCHPYIAYSLPPDMNAVTSVVVKPYCSPPEVILWASGTAYLVNPFVAIQALAVGEPLNEAALKELGEVAVHKDSLPPLRYNGGPPAE | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH.
PTM: O-glycosylated, and sialylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16588
Sequence Length: 156
Subcellular Location: Virion membrane
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Q9J3N1 | MASHKWLLQMIVFLKTITIAYCLHLQDDTPLFFGAKPLSDVSLIITEPCVSSVYEAWDYAAPPVSNLSEALSGIVVKTKCPVPEVILWFKDKQMAYWTNPYVTLKGLTQSVGEEHKSGDIRDALLDALSGVWVDSTPSSTNIPENGCVWGADRLFQRVCQ | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17779
Sequence Length: 160
Subcellular Location: Virion membrane
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Q9JRN5 | MKTAIVTGASGQDGAYLSQLLLDKGYKVYATYRRSSSVNLWRIDELNIRNHPNLHLFEFDLTDMSSCISLVTKAQPGEVYNLAAQSFVGVSFSQPVTTAEITAIGVLNLLEAIRIINPKIKFYQASTSEMFGKVQQIPQTEKTPFYPRSPYGVAKLYGHWITLNYRESYDIFGCSGILFNHESPLRGREFVTRKITDTVAKIALNKQSCLELGNLDAKRDWGFAKEYVEGMWRMLQEDQPDTYVLATNRTETVRDFVAMAFQAVNIPLEFNGKGENEIGVNTDTGDVLVRVNKEYYRPAEVDLLIGDYSKAKRILGWEPKTSLEELCKMMIEADIERNKLGFSF | Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Catalytic Activity: GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O
Sequence Mass (Da): 38986
Sequence Length: 344
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
EC: 4.2.1.47
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P0AC90 | MSKVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVQPDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQQEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVEEKGIVVSVTGHDAPGVKPGDVIIAVDPRYFRPAEVETLLGDPTKAHEKLGWKPEITLREMVSEMVANDLEAAKKHSLLKSHGYDVAIALES | Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Catalytic Activity: GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O
Sequence Mass (Da): 42047
Sequence Length: 373
Pathway: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.
EC: 4.2.1.47
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Q51366 | MTRSALVTGITGQDGAYLAKLLLEKGYRVHGLVARRSSDTRWRLRELGIEGDIQYEDGDMADACSVQRAVIKAQPQEVYNLAAQSFVGASWNQPVTTGVVDGLGVTHLLEAIRQFSPETRFYQASTSEMFGLIQAERQDENTPFYPRSPYGVAKLYGHWITVNYRESFGLHASSGILFNHESPLRGIEFVTRKVTDAVARIKLGKQQELRLGNVDAKRDWGFAGDYVEAMWLMLQQDKADDYVVATGVTTTVRDMCQIAFEHVGLDYRDFLKIDPAFFRPAEVDVLLGNPAKAQRVLGWKPRTSLDELIRMMVEADLRRVSRE | Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Catalytic Activity: GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O
Sequence Mass (Da): 36399
Sequence Length: 323
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
EC: 4.2.1.47
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B2UNE0 | MSEYIRNQILGIADNFKALASMAGDIEQVARICTDTLKAGNKIMFCGNGGSAADSQHLAAELVGRYKLNRPAMNALALTVDTSILTAVGNDYGYETVFSRQLEGVGRPGDLLVGLSTSGNSRNIVLAMELARRMGVRTVALTGRGGGEMKEVAEFCIAVPSDATNNIQEMHIAVGHLVCELVEREIYGG | 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): 20109
Sequence Length: 189
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.28
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A8EVR5 | MKSAIIKEFLAHQETIAKVIETMQEPLEKASKIAVETLKNGNKILLCGNGGSAADAQHFAAELTGRYKTERRGLPGIALTTDTSALTAIGNDYGYDRVFDRQVEALASKGDLLIGISTSGNSTNVINALKVARDLGCKTIGLTGRDGGKMNELCDINLVVPSNDTPRIQEMHILFEHTICQIIDNELSH | 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): 20409
Sequence Length: 189
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.28
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O67054 | MLEKVKKIFRESAEVKLAFVELYAQQIVDVAGIIATALKDGNKVLLFGNGGSAADAQHIAAELVGRFKKERRPLPAIALTTDTSILTALGNDYGFETIFERQVEALCMPGDVAIGITTSGNSENVIRGLKKAHDLGATTIAFTGRNGGKVAQIAHYTFIVPSYETQRIQECHITLGHVLCELVEEMVCERS | 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): 20706
Sequence Length: 191
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.28
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C1DQ86 | MDMHARISQLFQASIETKQQAMEVILPHIVQASELMVQALLNEGKILSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTLTSIANDYSYNEVFSKQIRALGQPGDVLLAISTSGNSANVIQAIQAAHDREMQVVALTGRDGGGMAALLLPEDIEIRIPAKVTARIQEVHLLVIHCLCDLIDNQLFGSEE | 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): 21306
Sequence Length: 197
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.28
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A5EN81 | MNRAADDLIASHLARSHAAMARAAQDTALLASAGRIAAKIVTALRSGRKLLIVGNGGSAADAQHIAAEIVGRYKQERPAFAAIALTTDTSALTAIGNDYGFDHVFARQVEGLGTSGDVLLAISTSGRSPSILNALRKARERGLTTIGFTGANGLAMGELCDELLVAPSDDTPLIQQIHLATAHGICETIEAALMQDLS | 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): 20498
Sequence Length: 198
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.28
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Q9AGY5 | MKNKALFLDRDGVINVEKNYVHKIEDFEFMDGIFETLRYFQEKGYLLIIITNQAGIGRGYYTEEQFHILNDWMLSEFEKEGIYITKVYYCPYHPEHGIGKYKRDSFDRKPNPGMILKSQKEFNIDLSKSILVGDKESDIQAGKRAGVNVNIIFSNNKNGDELDCCKKINSLSELVSLIL | Function: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 20764
Sequence Length: 179
Pathway: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.3.83
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Q8AAI7 | MRLQDIDVTGFETLLLDRDGVVNRLRPDDYVKKWEEFEFLPGVLEILKAWNTHFKYIFIVTNQRGVGKEIMSEEDLKHIHERMISEVKNYGGRIDRIYYCTALTDSDINRKPGIGMFLQILRDYPDIDKAKCLMIGDSDSDIKFAKNCGIVGIKVI | Function: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate (alpha-HBP) intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 18105
Sequence Length: 156
Pathway: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.3.83
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Q9AI34 | MKNRALFLDRDGVINRDDGYVFEIEKFVFLDGIFELAGAAKALGYLSIVVTNQAGIGRGYYSEDDFFRLSDWMKGVFATEGAPIDGVYFCPTHPEHGIGRYKVESRFRKPNPGMILAAQHDFDLDLGASLLVGDKESDIQAGSTAGVGTTLLICDRDASRVATAASAVVRNPRDVIPFLTGPGPDAGSF | Function: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 20428
Sequence Length: 189
Pathway: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.3.83
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Q6TG07 | MKTKALFLDRDGVINIDKKYVYKIEDFEFCDGIFELCRYFLARNYLLFIATNQSGIARGYYKESDFFKLCDYMLKEFAKQDIKIDKIYHCPHLEGCECRKPKAGMLLKAKDEFDLDMKNSIFIGDNLSDMQAGLNADIGTLILVNEEKKEGDFFRQFKNLKEILNFFKEKDI | Function: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 20246
Sequence Length: 172
Pathway: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.3.83
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Q97EQ5 | MNKAVFLDRDGTINVEKNYLYKIEDFEFTEGAVEAIKLLNQNEYKVIVISNQAGVARGYYTEEAVDKLHEYIQKQLKKYDAHIDAFYYCPHHPIHGVGKYKLQCKCRKPEDGLYKRAIKDFNIDVEKSYAVGDKLSDLIPAVDNNIKSFLVMTGYGKEEVKNIKTDMRITKNLYSFVTEII | Function: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 20962
Sequence Length: 181
Pathway: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.3.83
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Q7U2U1 | MVAERAGHQWCLFLDRDGVINRQVVGDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDGVLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLRRHPDSEPLLSIVVGDSLSDLELAHNVAAAAGACASVQIGGASSGGVADASFDSLWEFAVAVGHARGERG | Function: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 20611
Sequence Length: 190
Pathway: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.3.83
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P9WMV2 | MVAERAGHQWCLFLDRDGVINRQVVGDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDGVLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLGRHPDSEPLLSIVVGDSLSDLELAHNVAAAAGACASVQIGGASSGGVADASFDSLWEFAVAVGHARGERG | Function: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 20511
Sequence Length: 190
Pathway: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.3.83
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Q7MY63 | MQHNKIKVAFLDRDGVINKEVNYLHKIEDFEYTSKCIVGLKKIRDLGYEIIIITNQAGIARGYYSEKQYQLLTDWYRNDLKEKGVDILDIFHCPHYPDGIVPELSKDCYCRKPSPGMIEQARKKYSIDIKSSILVGDKNSDIHAGERAGIPRCFLVKTGHPTSEPTENAILSNNLFTISKLIE | Function: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 20934
Sequence Length: 183
Pathway: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.3.83
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Q7WG29 | MKLIILDRDGVVNQDSDAFVKSPDEWIALPGSLQAIARLTQADWTVVLATNQSGLARGLFDTATLNAIHDKMHRALAQMGGVVDAIFMCPHGPDDGCACRKPLPGMYRDIARRYDVDLAGVPAVGDSLRDLQAAAQAGCAPWLVQTGNGRKTLAQGGLPEGTRVCEDLAAVAEQLLQEA | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 19035
Sequence Length: 179
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4.
Subcellular Location: Cytoplasm
EC: 3.1.3.82
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Q7VL21 | MGKKAVFLDRDGTLNIDHGYVHQIDDFQFIEGVGKALKQLQDKGYLLVLVTNQSGIARGYFSEQQFQQLTEWMDWSLDEDYGVVLDGIYYCPHYPEGQGEYQQKCDCRKPKAGMFQQAIKDLNIDPAQSYMVGDKLEDLLAAETAGVKTKVLVRTGKAITAEGEKKADLVLNSLVDLVPYVN | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 20432
Sequence Length: 182
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4.
Subcellular Location: Cytoplasm
EC: 3.1.3.82
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P46452 | MNKAIFLDRDGTLNIDYGYVHEIDNFKFIDGVIDALRELKKMGYMLVLVTNQSGIARGYFSEDQFLQLTEWMDWSLAEQDVDLDGIYYCPHHSEGKGEYKEDCDCRKPKSGMLLQAIKELKIDPTQSIMVGDKVEDLKAGIGAKVKMNVLVRTGKPVTGEGEGIADYVLDSIVDLPRILKRLKK | Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position in vitro. Also catalyzes the dephosphorylation of D-glycero-alpha-D-manno-heptose 1,7-bisphosphate, phosphoserine and fructose-1,6-biphosphate in vitro.
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
Sequence Mass (Da): 20810
Sequence Length: 184
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4.
Subcellular Location: Cytoplasm
EC: 3.1.3.82
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Q9LFU9 | MAETFKIRKLEISDKRKGFIELLGQLTVTGSVTDEEFDRRFEEIRSYGDDHVICVIEEETSGKIAATGSVMIEKKFLRNCGKAGHIEDVVVDSRFRGKQLGKKVVEFLMDHCKSMGCYKVILDCSVENKVFYEKCGMSNKSIQMSKYFD | Function: Acetyltransferase involved in UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthesis. UDP-GlcNAc is an essential metabolite that serves as an initial sugar donor for N-glycan synthesis and thus plays an important role in protein and lipid glycosylation.
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17028
Sequence Length: 149
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.4
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Q17427 | MSHIFDASVLAPHIPSNLPDNFKVRPLAKDDFSKGYVDLLSQLTSVGNLDQEAFEKRFEAMRTSVPNYHIVVIEDSNSQKVVASASLVVEMKFIHGAGSRGRVEDVVVDTEMRRQKLGAVLLKTLVSLGKSLGVYKISLECVPELLPFYSQFGFQDDCNFMTQRF | Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 18459
Sequence Length: 165
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
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O93806 | MMLPQGYTFRKLKLTDYDNQYLETLKVLTTVGEISKEDFTELYNHWSSLPSIYHPYVITNASGIVVATGMLFVEKKLIHECGKVGHIEDISVAKSEQGKKLGYYLVTSLTKVAQENDCYKVILDCSPENVGFYEKCGYKDGGVEMVCRF | Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 16898
Sequence Length: 149
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
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Q54WR8 | MSSIVDDGISFRPLDIDDFDKGYSECLQQLTEAKFTKEQFIERFNQIKKQSDTYFLIVAVDVKLNKIIACGSLFVEKKFIRNCGKCGHIEDIVVNNNYRGKNLGLRIIEQLKCIGSQAGCYKIILDCSEANVKFYEKCKFERKGVQMSIYLPTPPKL | Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 17994
Sequence Length: 157
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
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Q9VAI0 | MVQLTEETYLYDPNLLLKLDFHRSPANFKPFISAANPGEPWMKVRPLKDTDYDRGFLQLLSQLTHVGNVNRTQFLTRFSQMKASGDYFVTVIEDTRKNEIIGAASLVIERKFIHNCAVRGRLEDVVVNDTYRGKQLGKLIVVTVSLLAEELGCYKMSLDCKDKLIKFYESLGYVAIPGNSNSMTIRYDEGPTLKRNATSAGSSGTVGDSCQTVSLDFAS | Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 24492
Sequence Length: 219
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
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Q96EK6 | MKPDETPMFDPSLLKEVDWSQNTATFSPAISPTHPGEGLVLRPLCTADLNRGFFKVLGQLTETGVVSPEQFMKSFEHMKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVEDVVVSDECRGKQLGKLLLSTLTLLSKKLNCYKITLECLPQNVGFYKKFGYTVSEENYMCRRFLK | Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20749
Sequence Length: 184
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.4
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Q5UPZ9 | MQISINELNFDDDSYQYMELLKQLTYIDPSIITNEMFEKQLSIIKNNPFHKIIVAKIDGKIVGSTTVLIEPKFIHNLSSVGHIEDVVVDQNYRLHGIGKLLIVKAIDICRQERCYKIILDCSDKVCGFYCKLGFTPKEKQMALYLNGK | Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 17017
Sequence Length: 148
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
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Q9JK38 | MKPDETPMFDPSLLKEVDWSQNTAIFSPAISPTHPGEGLVLRPLCTADLNKGFFKVLGQLTETGVVSPEQFMKSFEHMKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVEDVVVSDECRGKQLGKLLLSTLTLLSKKLNCYKITLECLPQNVGFYKKFDYTVSEENYMCRRFLK | Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20791
Sequence Length: 184
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.4
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Q5U9F2 | MEQPLPTAAAEAAAAGGDGEAYRIRPLELADISRGFLGLLNQLSPSPPLTEEAFRARFEELAALGADHLVLVAEDAATGRLAAAGAVLVERKFIRRCGRVGHVEDVVVDAAARGRGLGERVVRRLVEHARGRGCYKVIINCTPELTGFYAKCGFVEKNVQMGLYF | Function: Acetyltransferase involved in de novo biosynthesis of UDP-N-acetylglucosamine (UDP-GlcNAc) in roots and is required for maintaining normal root cell shape. UDP-GlcNAc is an essential metabolite that serves as an initial sugar donor for N-glycan synthesis and thus plays an important role in protein and lipid glycosylation.
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17720
Sequence Length: 165
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.4
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O13738 | MKKDFHSTYYIIVVEDLESHHVIGTATLFLERKFLRGKGICGHIEEVIVHPDHQRKAIGKLMVLTLIKLAFSLNSYKVILDCSDSNVGFYEKCGLSRAGIEMKKYASHSII | Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 12596
Sequence Length: 111
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
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E3Q1H1 | MTDIVDLELRVLEESDLSSHLELLGHLTEAPPLSGVELANIADMRRRAGIVTKVFCHQPTGRIVGSASLMIQPKFTRGGRAVGHIEDVVVDPSYRGAGLGKALIMDLCEISRSKGCYKVILDSSEKSLPFYEKLGFRAHERQMRLDL | Function: Involved in the biosynthesis of UDP-N-acetyl-alpha-D-glucosamine. Catalyzes the formation of N-acetyl-D-glucosamine 6-phosphate from acetyl-coenzyme A (acetyl-CoA) and D-glucosamine 6-phosphate.
PTM: Contains poly-N-acetyllactosamines.
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 16247
Sequence Length: 147
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
Subcellular Location: Glycosome
EC: 2.3.1.4
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P43577 | MSLPDGFYIRRMEEGDLEQVTETLKVLTTVGTITPESFSKLIKYWNEATVWNDNEDKKIMQYNPMVIVDKRTETVAATGNIIIERKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEMQIRK | Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 18135
Sequence Length: 159
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
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C7IZ16 | MASTSPEPSTAAAVAETGCSVQIRRLEATDHEKGFVALLSQLSACPDLTASEFAACFADLAALGDDHVILVAEDPAAPESRILATGCLFVERKFLRGGGKVGHVEDVVVDAAARGRGLGLRVVRRLVEIAKEAGCYKVILDCTPELRAYYAKCGFVEKGVQMAIYF | Function: Acetyltransferase involved in UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthesis. UDP-GlcNAc is an essential metabolite that serves as an initial sugar donor of N-glycan synthesis and thus plays an important role in protein and lipid glycosylation (By similarity).
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17619
Sequence Length: 166
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.4
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Q9NVN8 | MMKLRHKNKKPGEGSKGHKKISWPYPQPAKQNGKKATSKVPSAPHFVHPNDHANREAELKKKWVEEMREKQQAAREQERQKRRTIESYCQDVLRRQEEFEHKEEVLQELNMFPQLDDEATRKAYYKEFRKVVEYSDVILEVLDARDPLGCRCFQMEEAVLRAQGNKKLVLVLNKIDLVPKEVVEKWLDYLRNELPTVAFKASTQHQVKNLNRCSVPVDQASESLLKSKACFGAENLMRVLGNYCRLGEVRTHIRVGVVGLPNVGKSSLINSLKRSRACSVGAVPGITKFMQEVYLDKFIRLLDAPGIVPGPNSEVGTILRNCVHVQKLADPVTPVETILQRCNLEEISNYYGVSGFQTTEHFLTAVAHRLGKKKKGGLYSQEQAAKAVLADWVSGKISFYIPPPATHTLPTHLSAEIVKEMTEVFDIEDTEQANEDTMECLATGESDELLGDTDPLEMEIKLLHSPMTKIADAIENKTTVYKIGDLTGYCTNPNRHQMGWAKRNVDHRPKSNSMVDVCSVDRRSVLQRIMETDPLQQGQALASALKNKKKMQKRADKIASKLSDSMMSALDLSGNADDGVGD | Function: Stabilizes TERF1 telomeric association by preventing TERF1 recruitment by PML. Stabilizes TERF1 protein by preventing its ubiquitination and hence proteasomal degradation. Does so by interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase. Required for cell proliferation. By stabilizing TRF1 protein during mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2 protein by preventing its ubiquitination, and hence proteasomal degradation. By acting on MDM2, may affect TP53 activity. Required for normal processing of ribosomal pre-rRNA. Binds GTP.
Sequence Mass (Da): 65573
Sequence Length: 582
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Nucleus
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Q21086 | MAKYCLKKTSKRVSCAKRYKIEKKVRDHNRKVKKEAKKNGTTNKKEKTISVPNSCPFKEEILVQAEQEREKIKVRQEAAKEAAKIHRIEKRKNNLPANFESMVAKASKQGTEFDKKVASAAEHEKFNTLDDKTIKAYASEVRKTVEIADVIIQVLDARDPLGSRSKSVEDQVLKGGKRLVLLLNKIDLVPRENVQKWLEYLRGQFPTIAFKASTQEQKSNIGRFNSAILNNTETSKCVGADIVMKILANYCRNKDIKTSIRVGVVGFPNVGKSSVINSLKRRKACNVGNLPGITKEIQEVELDKNIRLIDSPGVILVSQKDLDPIEVALKNAIRVDNLLDPIAPVHAILRRCSKETIMLHYNLADFNSVDQFLAQLARRIGKLRRGARPDVNAAAKRVLNDWNTGKLRYYTHPPEQGTAKEDIVVPAEVVSQFSKEFDIDAIAEEQNQIVEGLPMESDIIAPHNSDEEEDDDDEMETDVNEKKQTVTSGRKVKGPTKDDDKPVLPESLALEGNVQLNKLIKTAIKKQKKKSKKTANRADKLSDSLGNMLGGDAMEM | Function: May play a role in regulating cellular proliferation in both germline and somatic tissues.
Sequence Mass (Da): 62339
Sequence Length: 556
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Nucleus
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Q6DRP2 | MKRPKLKKASKRLSCAKRYKIQKKVREHNRKLKKAAKKQGISRKAKKDIGVPNSAPFKEEVLREAEQRKQELETLKEQNKIVKQQEKAAKRKKEKDAASSVKEPAAKKAKKAAKIKEARAAIVKVKSAKTFKCQELNKVIEASDVIVEVLDARDPLGCRCPQLEEMVLKHEGKKKLLFILNKIDLVPKDNLEKWLHFLEAECPTFLFKSSMQLKDRTVQQKRQQRGTNAVLDHSRAASCFGKDFLLQTLNDLANKKEGETMLKVGVVGFPNVGKSSIINSLKEMRACNAGVQRGLTRCMQEVHITKKVKMIDSPGILAALSNPGSAMALRSLQVEEKEESPQEAVRNLLKQCNQQHVMLQYNVPDYRSSLEFLTTFAMKHGLLQKGGVADTELAATTFLNDWTGAKLSYYSRVPERQGLPSYLSDAIVTELQSDVDMDAVKKGNENVKRSVRFPNLASCISFDSSGPTAGVLDVSELPKEILTKAATTTDAEEEKMDTTTNTDEPEAESHISSTVEPIQEPTEKRKDKPAKEVKFVPVNTDLTSMQNKNNEDAYDFNTDFV | Function: May play a role in regulating cellular proliferation.
Sequence Mass (Da): 62901
Sequence Length: 561
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Nucleus
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Q8MT06 | MALKRLKTKKSKRLTGRLKHKIEKKVRDHNKKERRAAKKNPKKGSKKQKLIQIPNICPFKDDILKEVEEAKQRQEAERLARREAFKAEREQNKFKTLESMVEDADMRSTVHGIMHENDAQDQDEKKYKNAVTKEQSLKQYFKEFRKVIENADVVLEVVDARDPLGTRCNEVERAVRGAPGNKRLVLVLNKADLVPRENLNNWIKYFRRSGPVTAFKASTQDQANRLGRRKLREMKTEKAMQGSVCIGAELLMSMLGNYCRNKGIKTSIRVGVVGIPNVGKSSIINSLTRGRSCMVGSTPGVTKSMQEVELDSKIKLIDCPGIVFTSGGENSHAVLKNAQRVGDVKDPFTIAESVLKRASKEYFCTMYDITNYDTFEEFFAKKAARMGKFLKKGVPDVVAAARSVLNDWNTGKIKYCTQPPEVQEGQSVHISASIVHSEAREFDVENFESMETEILEHCAVKTDDIMEITSTGPLEIRQPREEAEPADKITASLVIDEKEKPAKGRKRKLDEEKEKVDPSLLLEENQSLNKGIKQMQKLKKKQNVRNEKKISKITDVLDSFSLGPSSSKAEKYDFDEDYVIE | Function: May play a role in regulating cellular proliferation.
Sequence Mass (Da): 65985
Sequence Length: 581
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Nucleus
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Q9BVP2 | MKRPKLKKASKRMTCHKRYKIQKKVREHHRKLRKEAKKRGHKKPRKDPGVPNSAPFKEALLREAELRKQRLEELKQQQKLDRQKELEKKRKLETNPDIKPSNVEPMEKEFGLCKTENKAKSGKQNSKKLYCQELKKVIEASDVVLEVLDARDPLGCRCPQVEEAIVQSGQKKLVLILNKSDLVPKENLESWLNYLKKELPTVVFRASTKPKDKGKITKRVKAKKNAAPFRSEVCFGKEGLWKLLGGFQETCSKAIRVGVIGFPNVGKSSIINSLKQEQMCNVGVSMGLTRSMQVVPLDKQITIIDSPSFIVSPLNSSSALALRSPASIEVVKPMEAASAILSQADARQVVLKYTVPGYRNSLEFFTVLAQRRGMHQKGGIPNVEGAAKLLWSEWTGASLAYYCHPPTSWTPPPYFNESIVVDMKSGFNLEELEKNNAQSIRAIKGPHLANSILFQSSGLTNGIIEEKDIHEELPKRKERKQEEREDDKDSDQETVDEEVDENSSGMFAAEETGEALSEETTAGEQSTRSFILDKIIEEDDAYDFSTDYV | Function: May be required to maintain the proliferative capacity of stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation (By similarity).
Sequence Mass (Da): 61993
Sequence Length: 549
Domain: The basic domain (B) allows nucleolar localization in the absence of GTP. The intermediate domain (I) inhibits nucleolar localization by the B domain and is required for exit from the nucleolus. Exit from the nucleolus to the nucleoplasm requires both the I and the acidic (A) domains, and may be triggered by GTP hydrolysis (By similarity).
Subcellular Location: Nucleus
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Q6UDL9 | MWLLRPAGSNFIVALIVLACAGPLTCSAQLDAGILNPWGSAGHNDAVMPGMFANSESDERFYSPHCSSRGLPLVNESMASVIFFLSLAMVCVAIVAILYNCCFNSFKNSVINSRW | Function: Envelope glycoprotein necessary for proper maturation of gM and modulation of its membrane fusion activity. Also plays a critical role in virion morphogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 12391
Sequence Length: 115
Subcellular Location: Virion membrane
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Q01049 | MTWKLFICFLSFGVIFLRVSSLTEKSHTTSYTILHNNNFYSNSCSADTYVPSIKTFSSVWAILNVIIFFCASLFYLRHLCIVKFISNLTK | Function: Envelope glycoprotein necessary for proper maturation of gM and modulation of its membrane fusion activity. Also plays a critical role in virion morphogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 10405
Sequence Length: 90
Subcellular Location: Virion membrane
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Q87088 | MVSSAGLSLTLVAALCALVAPALSSIVSTEGPLPLLREESRINFWNAACAARGVPVDQPTAAAVTFYICLLAVLVVALGYATRTCTRMLHASPAGRRV | Function: Envelope glycoprotein necessary for proper maturation of gM and modulation of its membrane fusion activity. Also plays a critical role in virion morphogenesis.
PTM: O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 10155
Sequence Length: 98
Subcellular Location: Virion membrane
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Q65ZG0 | MGSITASFILITMQILFFCEDSSGEPNFAERNFWHASCSARGVYIDGSMITTLFFYASLLGVCVALISLAYHACFRLFTRSVLRSTW | Function: Envelope glycoprotein necessary for proper maturation of gM and modulation of its membrane fusion activity. Also plays a critical role in virion morphogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9762
Sequence Length: 87
Subcellular Location: Virion membrane
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Q9H2G9 | MTTKNLETKVTVTSSPIRGAGDGMETEEPPKSVEVTSGVQSRKHHSLQSPWKKAVPSESPGVLQLGKMLTEKAMEVKAVRILVPKAAITHDIPNKNTKVKSLGHHKGEFLGQSEGVIEPNKELSEVKNVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDLQYHFERLAREKNQLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNSRAALQRQNRDAHGAIQDLLSEREQFRQEMIATQKLLEELLVSLQWGREQTYSPSVQPHSTAELALTNHKLAKAVNSHLLGNVGINNQKKIPSTVEFCSTPAEKMAETVLRILDPVTCKESSPDNPFFESSPTTLLATKKNIGRFHPYTRYENITFNCCNHCRGELIAL | Function: Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface.
PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.
Sequence Mass (Da): 44910
Sequence Length: 400
Domain: The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2.
Subcellular Location: Golgi apparatus membrane
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A8NS89 | MTETVTDQGKQRSSKLQKNEAAKDEQVEGKGKETLESGTDKSAEQNSSLLVGQPDVIDNDNVQTVDDFKNLMYKMQETRRAIVFALLNEKDLTKDDVEILKRAYEKLTDNQTHSFQREMCTLTTKLSVNIGDETRGLEKDLKYLDALMNIRREEPNLLWPIIMSRVDLFSILANYHPKGKETFLKEYEDTVKFLKTFISSEAITGKKPIFITDWDGTMKDYCSQYATNLQPVYSAVGMTRFAASFTRISAVLTAGPLRGPGILDLTAMPIDGPVMFSGSWGREWWLSGKRVVHQDGITDEGFNALQRLDDEMKDLLHTSDYAPFALVGSGVQRKVDRLTLGVQTVCHHVTSELSNRYQMAVKERMHRVDPNSQILVFDPSTELEVEVVAHNSGIIWNKGNGVERLIKSLGDSLQSPGKILICGDTLSDIPMVRQAVKQNPDGVLAIFVGAKMSLREEVKQVIGDESRCCFVSCPDVIHAAMSQILNEHCIGK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of trehalose 6-phosphate to trehalose and phosphate; prevents the accumulation of toxic levels of trehalose 6-phosphate.
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 55119
Sequence Length: 492
EC: 3.1.3.12
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A8X485 | MTVASQSIEEFKECLYHMQETRKLLTMQLLATGKITSAEIQILKRTLEEMQDERTTDFYIRHIHSRGATFAINIRDEILGLKKDFLFLENFASECESEESFTNRLKLCDLPGLLSNNQIDIRLMNGFAEEVAKCKEFLMDLITIESDGIKPLFITDWDGTMKDYCSQYATNLQPAYSAIVMGVFARNFTRAFAVLTAGPLRHPGILDLTSLPIDGPVMFSGSWGREWWLGGRRVVHDDGIPEEGSVAIGQLYEQLEEILHEGEFVQFALVGSGVQKKVDRLTLGVQTVFGQVPKELSAKYIDAVKERIHRVDPNSQYLILENCSPLEIEVCVHSSGAIWNKGDGVAALVEFNKDSLKLGKVCVAGDTTSDLPMLQKAAQENPTQVRALFVNVNKEIQSTINKIVGDSSRTCFISCPDVAHAAFAQIIIELTQNA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of trehalose 6-phosphate to trehalose and phosphate; prevents the accumulation of toxic levels of trehalose 6-phosphate.
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 48434
Sequence Length: 434
EC: 3.1.3.12
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Q9XTQ5 | MNCEKESQMTIASQSIEDFKECLYQMQEARKSVTNEILETGHIKADQVQIFKSTLEEMNDERTSKNHIRDIHSRGTTFGINIQDEIKGLQKDHHFLDAFAVESDKENNSFANVLKLCDLPGLLSKFVDDEIRFEKEVAECKAFLMDLIDTSTTGGIKPLFITDWDGTMKDYCSQYATNLQPAYSAIVMGVFSRLFTRAFAVLTAGPLRHPGILDLTALPINGPVLFSGSWGREWWLGGRRIVHDDGIPEEGSVAIGQLCEQLDEILHEGEFVQFALVGSGVQRKVDRLTLGVQTVFKQVPEDLSARYIDAVRERIHRVDPNSQYLVLENCSPLEIEVCVHSSGAVWNKGDGVAALVESLHDSLKVGKVCVAGDTASDVPMLKKAADENPENVRALFVNINKQLQENITNIVGDAKRVCFISSPDVAHAAFAQIISEFSG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of trehalose 6-phosphate to trehalose and phosphate; prevents the accumulation of toxic levels of trehalose 6-phosphate.
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 48721
Sequence Length: 439
EC: 3.1.3.12
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Q9XZ14 | MAINQGKYKPSICAIDEVDDRSFKLHNSQDEIGGKQQLQQIEGSETAPLTTNQQKLHMDDGSHLTPKDLEAARQDALNEVAAGGAGGRTPAAITPNSTHPSANGLRALLLPGRRSFDALMSLSRKRRILYVTTACLCALLLLIIILLLAFWPEVPFYLRAPLCLDKECVESSRQLLLWANTSKSPCHETYEWACGNFASDYANHEYFVIKRGEWNYETYNEYQELNELNRFIAMLPNSQEGSVESTVSSLYRSCRETDVLDKSQSDLLLKRAINAVYGWQAFRDSNRLQSWEYKRVLVVLQAKHGIFPYYRVTVENGFSNPHDYVITLDEGELGLPDKYFYGNDADEEVVRGYKLLLRDFAINMGIVSREADLFADDIFHYERRIVNHIEDAKADANRPINKLMRLADLKIKAPSLPILESLQAIFPKTKITEDTEVLVRDPEVMHALSVLLSTSDKKPINNFIVWSLARKMLPHLSKEYRTLAETFDHALYGRTASYPRWLICSKVVRDWLPFAVDALQQQPPRQQFETMTSKSRGLNKTQGNEELLKLMFFSLRNQLKDSLEQAKWLEPAARQFIQKKLNEMRLQFGIPDEVLQQPTYLAQYYNELILNNVFFVEHLEWIWTFRRSQMEKKLGPLAILDVIVSEMYTRDNPQAIAYSNKLNMLLVSKVLISSNYYDYRYPVAVNFARIGTDILEALIDNFSTFLLQFNTQSTDISDAAPEIRYAQPDVNCLAAGQPPRLVHELNELSSNALKSFHVTLSAARTAARALSNFVNAIDAGSAIQGSGIDQANTYEALGLTRRLRIPGLRSFNENELFTLSYMQQHCSTTIADKDYARIKPLVESQLAESYLFNATWQHIQFLPRSTNCAAAEATCSNLL | Function: Plays a role in the ovary in limiting the number of primordial germ cells (PGCs) that develop directly into gametes, allowing them instead to enter the developmental pathway that produces germline stem cells (GSCs) from PGCs and ensuring lifelong production of gametes from these GSCs. Negatively regulates epidermal growth factor receptor (Egfr) signaling. Probably down-regulates EGFR signaling on intermingled cells, a type of somatic stromal cell which contacts PGCs, and the resultant low level of signaling limits the proportion of PGCs which start gametogenesis, maintaining them in an undifferentiated proliferative state.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 100068
Sequence Length: 879
Subcellular Location: Cell membrane
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Q2TAP0 | MATEVHNLQELRRSASLATKVFIQRDYSDGTICQFQTKFPPELDSRIERQLFEETVKTLNGFYAEAEKIGGSSYLEGCLACATAYFIFLCMETHYEKVLKKISRYIQEQNEKIFAPRGLLLTDPVERGMRVIEISIYEDRCSSGSSSSGSSSGSGSSSGGGGGAGAR | Function: Play a role in cell adhesion by regulating the plasma membrane localization of the palmitoyltransferase ZDHHC5 . May be involved in protein transport from Golgi to cell surface.
PTM: Palmitoylated by ZDHHC5. Palmitoylation is required for the maintenance of ZDHHC5 at the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 18335
Sequence Length: 167
Subcellular Location: Cell membrane
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Q94A76 | MGRLRRRQEIIDHEEEESNDDVSSRRGKLSLAETFRWLDSSEHRRIETDGHNDYKYIIHPKNRWYKAWEMFILVWAIYSSLFTPMEFGFFRGLPERLFVLDIVGQIAFLVDIVLQFFVAYRDTQTYRTVYKPTRIAFRYLKSHFLMDFIGCFPWDLIYKASGKHELVRYLLWIRLFRVRKVVEFFQRLEKDTRINYLFTRILKLLFVEVYCTHTAACIFYYLATTLPPENEGYTWIGSLKLGDYSYENFREIDLWKRYTTALYFAIVTMATVGYGDIHAVNLREMIFVMIYVSFDMVLGAYLIGNITALIVKGSNTERFRDKMNDLISFMNRKKLGRDLRSQITGHVRLQYDSHYTDTVMLQDIPASIRAKIAQLLYLPYIKKVPLFKGCSTEFINQIVIRLHEEYFLPGEVITEQGNVVDHLYFVCEGLLEALVTKTDGSEESVTLLGPHTSFGDISIICNISQPFTVRVCELCHLLRLDKQSFSNILEIYFHDGRTILNNIMEEKESNDRIKKLESDIVIHIGKQEAELALKVNSAAFQGDFYQLKSLIRSGADPNKTDYDGRSPLHLAACRGYEDITLFLIQEGVDVNLKDKFGHTPLFEAVKAGQEGVIGLLVKEGASFNLEDSGNFLCTTVAKGDSDFLKRLLSSGMNPNSEDYDHRTPLHVAASEGLFLMAKMLVEAGASVISKDRWGNSPLDEARLCGNKKLIKLLEDVKNAQSSIYPSSLRELQEERIERRKCTVFPFHPQEAKEERSRKHGVVVWIPSNLEKLIVTAAKELGLSDGASFVLLSEDQGRITDIDMISDGHKLYMISDTTDQT | Function: Major selective outward-rectifying potassium channel of the guard cell membrane. Involved in regulation of stomatal movements according to the water status. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by depolarization. Conductance of the channel is modulated in a potassium-dependent fashion. May interact with the cytoskeleton or with regulatory proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 94461
Sequence Length: 820
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity.
Subcellular Location: Membrane
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Q9BQQ3 | MGLGVSAEQPAGGAEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSDQILQESEDFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPPSYHKKPPGTPPPSALPLGAPPPDALPPGPTPEDSPSLETGSRQSDYMEALLQAPGSSMEDPLPGPGSPSHSAPDPDGLPHFMETPLQPPPPVQRVMDPGFLDVSGISLLDNSNASVWPSLPSSTELTTTAVSTSGPEDICSSSSSHERGGEATWSGSEFEVSFLDSPGAQAQADHLPQLTLPDSLTSAASPEDGLSAELLEAQAEEEPASTEGLDTGTEAEGLDSQAQISTTE | Function: Key structural protein of the Golgi apparatus . The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon . Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks . However, other studies suggest that GORASP1 plays an important role in assembly and membrane stacking of the cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis (By similarity). Caspase-mediated cleavage of GORASP1 is required for fragmentation of the Golgi during apoptosis (By similarity). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes . Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane .
PTM: Phosphorylated by CDC2/B1 and PLK kinases during mitosis. Phosphorylation cycle correlates with the cisternal stacking cycle. Phosphorylation of the homodimer prevents the association of dimers into higher-order oligomers, leading to cisternal unstacking.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 46482
Sequence Length: 440
Subcellular Location: Golgi apparatus
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Q9H8Y8 | MGSSQSVEIPGGGTEGYHVLRVQENSPGHRAGLEPFFDFIVSINGSRLNKDNDTLKDLLKANVEKPVKMLIYSSKTLELRETSVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGADTVMNESEDLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPTRPFEEGKKISLPGQMAGTPITPLKDGFTEVQLSSVNPPSLSPPGTTGIEQSLTGLSISSTPPAVSSVLSTGVPTVPLLPPQVNQSLTSVPPMNPATTLPGLMPLPAGLPNLPNLNLNLPAPHIMPGVGLPELVNPGLPPLPSMPPRNLPGIAPLPLPSEFLPSFPLVPESSSAASSGELLSSLPPTSNAPSDPATTTAKADAASSLTVDVTPPTAKAPTTVEDRVGDSTPVSEKPVSAAVDANASESP | Function: Key structural protein of the Golgi apparatus . The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon . Acting in concert with GORASP1/GRASP65, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks . However, other studies suggest that GORASP2 plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after breakdown during mitosis and meiosis . May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA . Required for normal acrosome formation during spermiogenesis and normal male fertility, probably by promoting colocalization of JAM2 and JAM3 at contact sites between germ cells and Sertoli cells (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane .
PTM: Myristoylated . Myristoylation is essential for the Golgi targeting (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 47145
Sequence Length: 452
Subcellular Location: Golgi apparatus membrane
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Q9R064 | MGSSQSVEIPGGGTEGYHVLRVQENSPGHRAGLEPFFDFIVSISGSRLNKDNDTLKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGADTVMNESEDLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPTRPFEEGKKISLPGQMTGTPITPLKDGFTQVQLSSVSPPSLSPPGTAGVEQSLSGLSISSAPPAVSNVLSTGVPTVPLLPPQVNQSLASVPPMNPAATLPSLMPLSAGLPNLPNLPSLSNFNLPAPHIMPGVGLPELGKPGLPPLPSLPPRNVPGIAPLPMPSDFLPSFPLVPEGSSAASAGEPLSSLPAMGPPSDPVMTTAKADTSSLTVDVMSPASKVPTTVEDRVSDCTPAMEKPVSAVTDANASGAS | Function: Key structural protein of the Golgi apparatus (By similarity). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (By similarity). Acting in concert with GORASP1/GRASP65, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (By similarity). However, other studies suggest that GORASP2 plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after breakdown during mitosis and meiosis . May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA (By similarity). Required for normal acrosome formation during spermiogenesis and normal male fertility, probably by promoting colocalization of JAM2 and JAM3 at contact sites between germ cells and Sertoli cells (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity).
PTM: Myristoylated (By similarity). Myristoylation is essential for the Golgi targeting .
Location Topology: Lipid-anchor
Sequence Mass (Da): 47221
Sequence Length: 454
Subcellular Location: Golgi apparatus membrane
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Q9LMP7 | MDVPSSWDALRKQARKIEAQLDEQMHSYRRLVSTKALSKSDGNESDLEAGIDLLLRQLQQVNAQMQAWVSSGGSEMVSHTLTRHQEILQDLTQEFYRHRSSLRAKQEHASLLEDFREFDRTRLDLEDGYGSEQALIKEHMGINRNTAQMDGVISQAQATLGTLVFQRSTFGGINSKLSNVASRLPTVNTILAAIKRKKSMDTIILSLVAAVCTFLIFIYWITK | Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 25214
Sequence Length: 223
Subcellular Location: Golgi apparatus membrane
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O22151 | MTESSLDLQESGWEELRREARKIEGDLDVKLSSYAKLGARFTQGDTDLVMNYEKVLKCVLVSGYVDTGSPTVGSGRSWKSMEMEIQSLLEKLLDINDSMSRCAASAAPTTSVTQKLARHRDILHEYTQEFRRIKGNINSLREHAELLSSVRDDISEYKASGSMSPGVQVLRERASIHGSISHIDDVIGQAQATRAVLGSQRSLFSDVQGKVKNLGDKFPVIRGLLGSIKRKRSRDTLILSAVIAACTLFLIIYWLSK | Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 28522
Sequence Length: 257
Subcellular Location: Golgi apparatus membrane
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Q09835 | MKSMLLRDSVKKASQFQRSLHSDPNQAKILLEERRKLLEEANSSADENDSHSMATIKSHFERLKRDEQLLNGVLKKYDAKQEVLSPEELRDAQNFLEMQEANSLDNSIRGTNELLERAYATREDFDYQNSVLGNVTNRINGAAMSIPFINQILRKTSIRRRRDSIILALLISVLMLLFLFFH | Function: Nonessential SNARE involved in retrograde transport within the Golgi complex.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 21067
Sequence Length: 182
Subcellular Location: Golgi apparatus membrane
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Q2TBU3 | MAAGTSNYWEDLRKQARQLENELDLKLVSFSKLCTSYSHSSARDGRRDRYSSDTTPLLNGSSQDRMFETMAIEIEQLLARLTGINDKMAEYTSSAGVPSLNAALMHTLQRHRDILQDYTHEFHKTKANFVAIRERENLMGSVRKDIESYKSGSGVNNRRTELFLKEHDHLRNSDRLIEETISIAMATKENMTSQRGMLKSIQSKMNTLANRFPAVNSLIQRINLRKRRDSLILGGVIGVCTILLLLYAFH | Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 28542
Sequence Length: 250
Subcellular Location: Golgi apparatus membrane
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Q95ZW1 | MSETWEALRKKARSTENSIDVKLVSLNKLTASSHGGFDIDEKTVSSRQTSFKTVTTEIEGLIEQLTNINDDMNDVAGAQSSASWANNPAIQHTLRRHREILRDYGSEYRRARDNVDQVLQRELLLSSSNENRNNPILNNRARGYDMYLKENDHINACDRLLDEQLEMAMSTKENMARQGINLRGISTRLHHISKKYPAINNLMQKIKTKKQKNTLILAAVISSCLIFTIFWIIN | Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. Cooperates with ykt-6 for proper expression of Golgi-resident proteins. Required along with ykt-6 for normal embryonic development, seam cell division or differentiation, and ray formation.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 26776
Sequence Length: 234
Subcellular Location: Golgi apparatus membrane
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Q52085 | MNKFITLFVLLASVSVAMSATCLTCVKEGAVCDATANICEEGTVCIKPNSTAANTICFVLPTLNEDCSGPLACADSYYCNTTSKICVEAYYLGVGESCSSENQCSTSLVCTGGKCVNEVYPLCGASNSRVGCKAGEGCAFNGTALVCSPFIANGAACNTSTSGLCHPVSSCSNGVCTAPLTGALNSNCTSNTDCNIANGLYCSSGKCTAVPEALNNCTTTPTVDNCLGYSACMCPSNDDTAKTGSCKDTIEYSDVTSDAYNKYDSCVVSCPAVTIVQKQSCLSKCTNPLAGAANNVCSSATTIAFNAFVVFAIVLSVLLF | Function: Cell-cell adhesion during development.
PTM: Contains 18 disulfide bonds.
Location Topology: Lipid-anchor
Sequence Mass (Da): 32724
Sequence Length: 320
Subcellular Location: Cell membrane
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A5PLE7 | METTSANFTQNDSNVCTNLYNHRGWAQYFLPAMYSLICIVGLLGNVLALHVIWPNLKKINSTTLYSANLVVSDILFSLALPLRVVYYARGFDWPMGEGLCKAVALLFYINMYAGVNFMTCLSVDRFIAVVLPLRFSRFRKVQKVRYICGVVWVVVLMQTLPLLSMPMTNIEQSGHITCMEYPNFEKIDNLPVMLIGAVVLGFGIPVITILVCYTALCLKLRHLAKSNKLTEKSGRSSKAIGVICTVILVFVVCYSPYHVDLLQYMIKKLRYDPDCSELHKFQISLHITVCFMNLNSCLDPFIYFFACKGYKKKVLKLLKKQVSMSFSSVVRTSPEGSSKDVFGNDKIQMNSRSFQKERSSVLLNSLEQ | Function: G-protein coupled receptor expressed in lymphocytes that acts as a chemotactic receptor for B-cells, T-cells, splenic dendritic cells, monocytes/macrophages and astrocytes (By similarity). Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols (By similarity). Mediates cell positioning and movement of a number of cells by binding the 7-alpha,25-OHC ligand that forms a chemotactic gradient (By similarity). Binding of 7-alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41705
Sequence Length: 368
Subcellular Location: Cell membrane
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P78333 | MDAQTWPVGFRCLLLLALVGSARSEGVQTCEEVRKLFQWRLLGAVRGLPDSPRAGPDLQVCISKKPTCCTRKMEERYQIAARQDMQQFLQTSSSTLKFLISRNAAAFQETLETLIKQAENYTSILFCSTYRNMALEAAASVQEFFTDVGLYLFGADVNPEEFVNRFFDSLFPLVYNHLINPGVTDSSLEYSECIRMARRDVSPFGNIPQRVMGQMGRSLLPSRTFLQALNLGIEVINTTDYLHFSKECSRALLKMQYCPHCQGLALTKPCMGYCLNVMRGCLAHMAELNPHWHAYIRSLEELSDAMHGTYDIGHVLLNFHLLVNDAVLQAHLNGQKLLEQVNRICGRPVRTPTQSPRCSFDQSKEKHGMKTTTRNSEETLANRRKEFINSLRLYRSFYGGLADQLCANELAAADGLPCWNGEDIVKSYTQRVVGNGIKAQSGNPEVKVKGIDPVINQIIDKLKHVVQLLQGRSPKPDKWELLQLGSGGGMVEQVSGDCDDEDGCGGSGSGEVKRTLKITDWMPDDMNFSDVKQIHQTDTGSTLDTTGAGCAVATESMTFTLISVVMLLPGIW | Function: Cell surface proteoglycan that bears heparan sulfate.
Location Topology: Lipid-anchor
Sequence Mass (Da): 63707
Sequence Length: 572
Subcellular Location: Cell membrane
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Q8CAL5 | MDARTWRLGWRCLLLLALLGSTRSEGVESCEEVRKLFQWRLGGAVKGLPEAPRAGPDLQVCLSKNPTCCTRKMEERYQIAARQDLQQVLQTSSSTLKLLISRNAAAFQETLETLIRQAENYTSILFCNTYRNMALEAAASIQEFFTDVGLYLFGADVNPEEFVNRFFDSLFPLVYNHLINPGVTDSSLQYSECIRMARQDVSPFGNIPKRVMGQMGRSLLPGRTFLQALNLGIEVINTTDHIHFSKECSRALLKMQYCPHCQSLMLSKPCMGYCLNVIRGCLAHMTELNPHWHAYIRSLEELSDAMHGTYDVEHVLLNFHLLVNDAVLQAHLNGQKLLDQVNTICGHPVRTPTQSPRCTFDPSKEKHGMKISARNGEETLANRRKEFINSLRLHGSFYGGLADQLCVNELAAPEGRPCWNGEEIVKSYAQRVVGNGIKAQSANPEVRVRGTDPVVNQIIDKLKHVIQLLRGRSPKPNKWELLQPGSGGGMLENSSGDCDDEDGCGGSGSGEVKRTLKITNWMPDSMNFSDVKQVHRADHGSTLDTTSTGCASGTESMALPLMGTLMFLPWLW | Function: Cell surface proteoglycan that bears heparan sulfate.
Location Topology: Lipid-anchor
Sequence Mass (Da): 63792
Sequence Length: 572
Subcellular Location: Cell membrane
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Q9PW88 | MAGLDLSLVLMLSVLAGVREVSLTQVNQQGVIAPGDIIIGGLFPIHEAAEAVNFTGLNSFSSFQHPVCNRYYTKGLNQALAMIHAVEMANQSPMLSSLNLTLGYRIYDTCSDVTTALWAVQDLTRPYSYCDSQTNSSQPVQPIMAVIGPSSSEISIAVARELNLLMIPQISYASTATILSDKSRFPAFMRTVPNDEYQTHAMVQLLKDNKWTWVGIIITDGDYGRSAMESFVKHTEREGICVAFKVILPDSLADEQKLNIHINETVDIIEKNTKVNVVVSFAKSSQMKLLYEGLRSRNVPKNKVWVASDNWSTSKNILKDVNLSDIGNILGFTFKSGNVTAFLQYLKDLKFGSEAKMNNSFLEEFLKLPEIGNAANAVQEQIKNTHLDMVFSVQMAVSAIAKAVVELCVERQCKTPSAIQPWELLKQLRNVTFEKEGVMYNFDANGDINLGYDVCLWDDDESEKNDIIAEYYPSNSSFTFTRKNLSNIENVLSKCSDSCQPGEYKKTAEGQHTCCYECLACAENQYSNHTDADTCSKCDTESLWSNANSSKCYPKFYEYFEWNSGFAIALLTLAALGILLLISMSALFFWQRNSLVVKAAGGPLCHLILFSLLGSFISVIFFVGEPSNESCRVRQVIFGLSFTLCVSCILVKSLKILLAFQMNLELKELLRKLYKPYVIVCMCMGLQVTICTLWLTLHRPFIEKVVQPKSILLECNEGSDLMFGLMLGYIVLLALICFTFAYKGRKLPQKYNEAKFITFGMLIYLMAWVIFIPVHVTTSGKYVPAVEVVVILISNYGILSCHFLPKCYIIIFKKEYNTKDAFLKNVFEYARKSSENIRGLSGTDPHSKTDNSVYVISNPSLVPEEKQVSVPEIDNVL | Function: Olfactory receptor that is activated by amino acids that act as potent odorants in fish. Most highly activated by basic amino acids such as L-lysine and L-arginine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 98120
Sequence Length: 877
Subcellular Location: Cell membrane
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Q5T6X5 | MAFLIILITCFVIILATSQPCQTPDDFVAATSPGHIIIGGLFAIHEKMLSSEDSPRRPQIQECVGFEISVFLQTLAMIHSIEMINNSTLLPGVKLGYEIYDTCTEVTVAMAATLRFLSKFNCSRETVEFKCDYSSYMPRVKAVIGSGYSEITMAVSRMLNLQLMPQVGYESTAEILSDKIRFPSFLRTVPSDFHQIKAMAHLIQKSGWNWIGIITTDDDYGRLALNTFIIQAEANNVCIAFKEVLPAFLSDNTIEVRINRTLKKIILEAQVNVIVVFLRQFHVFDLFNKAIEMNINKMWIASDNWSTATKITTIPNVKKIGKVVGFAFRRGNISSFHSFLQNLHLLPSDSHKLLHEYAMHLSACAYVKDTDLSQCIFNHSQRTLAYKANKAIERNFVMRNDFLWDYAEPGLIHSIQLAVFALGYAIRDLCQARDCQNPNAFQPWELLGVLKNVTFTDGWNSFHFDAHGDLNTGYDVVLWKEINGHMTVTKMAEYDLQNDVFIIPDQETKNEFRNLKQIQSKCSKECSPGQMKKTTRSQHICCYECQNCPENHYTNQTDMPHCLLCNNKTHWAPVRSTMCFEKEVEYLNWNDSLAILLLILSLLGIIFVLVVGIIFTRNLNTPVVKSSGGLRVCYVILLCHFLNFASTSFFIGEPQDFTCKTRQTMFGVSFTLCISCILTKSLKILLAFSFDPKLQKFLKCLYRPILIIFTCTGIQVVICTLWLIFAAPTVEVNVSLPRVIILECEEGSILAFGTMLGYIAILAFICFIFAFKGKYENYNEAKFITFGMLIYFIAWITFIPIYATTFGKYVPAVEIIVILISNYGILYCTFIPKCYVIICKQEINTKSAFLKMIYSYSSHSVSSIALSPASLDSMSGNVTMTNPSSSGKSATWQKSKDLQAQAFAHICRENATSVSKTLPRKRMSSI | Function: Receptor activated by multiple ligands, including osteocalcin (BGLAP), basic amino acids, and various cations . Activated by amino acids with a preference for basic amino acids such as L-Lys, L-Arg and L-ornithine but also by small and polar amino acids . The L-alpha amino acids respond is augmented by divalent cations Ca(2+) and Mg(2+) (By similarity). Seems to act through a G(q)/G(11) and G(i)-coupled pathway (By similarity). Regulates testosterone production by acting as a ligand for uncarboxylated osteocalcin hormone: osteocalcin-binding at the surface of Leydig cells initiates a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner (By similarity). Mediates the non-genomic effects of androgens in multiple tissue (By similarity). May coordinate nutritional and hormonal anabolic signals through the sensing of extracellular amino acids, osteocalcin, divalent ions and its responsiveness to anabolic steroids .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 104753
Sequence Length: 926
Subcellular Location: Cell membrane
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Q9Y625 | MPSWIGAVILPLLGLLLSLPAGADVKARSCGEVRQAYGAKGFSLADIPYQEIAGEHLRICPQEYTCCTTEMEDKLSQQSKLEFENLVEETSHFVRTTFVSRHKKFDEFFRELLENAEKSLNDMFVRTYGMLYMQNSEVFQDLFTELKRYYTGGNVNLEEMLNDFWARLLERMFQLINPQYHFSEDYLECVSKYTDQLKPFGDVPRKLKIQVTRAFIAARTFVQGLTVGREVANRVSKVSPTPGCIRALMKMLYCPYCRGLPTVRPCNNYCLNVMKGCLANQADLDTEWNLFIDAMLLVAERLEGPFNIESVMDPIDVKISEAIMNMQENSMQVSAKVFQGCGQPKPAPALRSARSAPENFNTRFRPYNPEERPTTAAGTSLDRLVTDIKEKLKLSKKVWSALPYTICKDESVTAGTSNEEECWNGHSKARYLPEIMNDGLTNQINNPEVDVDITRPDTFIRQQIMALRVMTNKLKNAYNGNDVNFQDTSDESSGSGSGSGCMDDVCPTEFEFVTTEAPAVDPDRREVDSSAAQRGHSLLSWSLTCIVLALQRLCR | Function: Cell surface proteoglycan that bears heparan sulfate. Putative cell surface coreceptor for growth factors, extracellular matrix proteins, proteases and anti-proteases (By similarity). Enhances migration and invasion of cancer cells through WNT5A signaling.
Location Topology: Lipid-anchor
Sequence Mass (Da): 62736
Sequence Length: 555
Subcellular Location: Cell membrane
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Q8C0L9 | MTPSQVTFEIRGTLLPGEVFAICGSCDALGNWNPQNAVALINENETGDSVLWKAVIALNRGVSVKYRYFRGCFLEPKTIGGPCQVIVHKWETHLQPRSITPLESEIIIDDGQFGIHNGVETLDSGWLTCQTEIRLRLHFSEKPPVSISKKKFKKSRFRVKLTLEGLEEDEDDDDDKVSPTVLHKMSNSLEISLISDNEFKCRHSQPECGYGLQPDRWTEYSIQTMEPDNLELIFDFFEEDLSEHVVQGDVLPGHVGTACLLSSTIAESGRSAGILTLPIMSRNSRKTIGKVRVDFIIIKPLPGYSCSMQSSFSKYWKPRIPLDVGHRGAGNSTTTAKLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKYEADPVELFEIPVKELTFDQLQLLKLSHVTALKTKDRKQSLYEEENFFSENQPFPSLKMVLESLPENVGFNIEIKWICQHRDGVWDGNLSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPELMDLRSRTTPIAMSFAQFENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRIYDWMPEQPNIFQVEQLERLKQELPELKNCLCPTVSHFIPSSFCVEPDIHVDANGIDSVENA | Function: May be involved in the negative regulation of skeletal muscle differentiation, independently of its glycerophosphocholine phosphodiesterase activity.
Catalytic Activity: H2O + sn-glycerol 3-phosphocholine = choline + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 76579
Sequence Length: 675
Subcellular Location: Cytoplasm
EC: 3.1.4.2
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Q4FS72 | MTSANDKSTDTNVDSTQAEQKMAEKQNKLLSGIIERATKSGIGRKKLNPSAVESAVAKNMAEIHNNPTKLRLVVLGGGSFGTAMANLAARNGCDTTLWVRNKRTVKAMAKSQMNKKYLPGYKLDDRLKYSHELQAAVKDTDIIFIAVPGLAFRETLKSIAPFISGQSIVSLTKGMEKDTFALMSDIIKEELPEVNFGVMSGPNLAIEIMKNMPSATVIASESEPLRHAVQAALHSAFFRVFASDDIRGVELGGALKNIYAIAMGMAAAYEVGENTKAMILTRGLAEMSRFGVHAGANPLTFLGLSGVGDLYATCSSELSRNYRIGNMLGRGMTIDAAVKKLGQTAEGVNTIQQVHEKATKEGIYMPITHALHAVIYEDKAALGVALHLMEAGFRSDVEFVMEHDHSNASLTAQMQTANNQAKNEKTKPDNK | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 46567
Sequence Length: 431
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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