ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q76M72 | MSFQELLNQVGSLGRFQILQIVFLLLLNAIVVPHIAMENFTAAIPNHRCWVPILDNDTASDNGSRILSQDDLLRISIPLDSNLRPEKCRRFAQPQWHLLHLNGTFSNVSEPDTEPCVDGWVYDRSNFLSTIVTEWDLVCESQALNSVTKFSFMIGLFIGGIICGHLSDRLGRKFILTCALLQFAITETCVAFAPSFFIYCSLRFLAGLSVEPILVNSHLLMLEWTSPKFLTMMAALLSCAPNIGYMISAGLAFLFRIWHHLQLTMSVPIFFFLILTRWLSESARWLIVTNKPQKGLKELRKVAHMNGMKNSGDLTMEIVR... | Function: Does not appear to have transporter activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62045
Sequence Length: 551
Subcellular Location: Cell membrane
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A6NKX4 | MEQEARVLRAAGGFGRARRLLASASWVPCIVLGLVLSSEELLTAQPAPHCRPDPTLLPPALRALRGPALLDAAIPRLGPTRAPAEALGVLSPSYLAPLTRAPRPSSWASCSGAAAGPTWNLVCGDGWKVPLEQVSHLLGWLLGCVILGAGCDRFGRRAVFVASLVLTTGLGASEALAASFPTLLVLRLLHGGTLAGALLALYLARLELCDPPHRLAFSMGAGLFSVVGTLLLPGLAALVQDWRLLQGLGALMSGLLLLFWGFPALFPESPCWLLATGQVARARKILWRFAEASGVGPGDSSLEENSLATELTMLSARSPQ... | Function: Organic anion transporter that mediates the uptake of ions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58815
Sequence Length: 556
Subcellular Location: Membrane
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Q7SXP0 | MVLLTMIARLADGLPLAASMQEDEQMGRDLQQYQSQAKQLFRKLNEQSPNRCTLEAGSMSFHYVIEKGVCYLVLCEAGFPKKLAFAYLEDLQAEFHEQHGKKVPTVSRPYSFIEFDTYIQKTKKSYIDSRARRNLSNINTELQDVQRIMVANIEEVLQRGEALSALDSKASNLSSLSKKYRSDAKYLNTRSTYAKLAAGGVFFIMLIVYIRFWWL | Function: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 24689
Sequence Length: 215
Subcellular Location: Endoplasmic reticulum ... |
Q28ES4 | MDLDEAFLYIGEFGCCQKRLTAFLTLLQVYVACQSMLIVLVGAVPEYLIDNEDISASKEEYTKHLHDTNNFTSIVSEWHLIKNEAYKVNLASSLFFAGLLIGNILFGPLSDKLGRRPVYLSGLFFDITFGYCTALAPSYEVFAVSRFFVGIMNGGMALVSFVLTQEYVGKSYWALTGSLTNLIFAVGIAFYALLGFYIRNWRTLAFVANSPGIFFFLLSFLLPESPRWLYSHGYTTEAEGVLQSMAVGNGVERPVVKLKSCPGTSSKSAHSVFDLVKYGVLRWRTILLMYIWYVCSLVYYGLTLNAGELKGNLYLNVALY... | Function: Probably transports organic cations.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53644
Sequence Length: 487
Subcellular Location: Membrane
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Q9UHI7 | MRAQEDLEGRTQHETTRDPSTPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTIAVPFLLAEALCVGHDQHMVSQLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKAILALERWKCPPEEEIYGNWSLPLNTSHIWHPRIREVQGAIMVSSVVEVVIGLLGLPGALLNYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIILFSQYLRNLTFLLPVYRWGKGLTLLRIQIFKMFPIMLAIMTVWLLCYVLTLTDVLPTDPKAYGFQARTDARGDIMAIAPWIRIPYPCQWGLPTVTAAA... | Function: Sodium:ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate . Has retained some ancestral activity toward nucleobases such as urate, an oxidized purine. Low-affinity high-capacity sodium:urate cotransporter, may regulate serum urate levels by s... |
Q9Z2J0 | MKTPEDPGSPKQHEVVDSAGTSTRDRQAPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTIAVPFLLAEALCVGRDQHMVSQLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKSILALERWKCPSEEEIYGNWSMPLNTSHIWHPRIREVQGAIMVSSMVEVVIGLMGLPGALLSYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIVLFSQYLRNLTFLLPVYRWGKGLTLFRVQIFKMFPIVLAIMTVWLLCYVLTLTDVLPADPTVYGFQARTDARGDIMAISPWIRIPYPCQWGL... | Function: Sodium:L-ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each L-ascorbate . Has retained some ancestral activity toward nucleobases such as urate, an oxidized purine. Low-affinity high-capacity sodium:urate cotransporter, may regulate serum urate levels ... |
Q9UGH3 | MMGIGKNTTSKSMEAGSSTEGKYEDEAKHPAFFTLPVVINGGATSSGEQDNEDTELMAIYTTENGIAEKSSLAETLDSTGSLDPQRSDMIYTIEDVPPWYLCIFLGLQHYLTCFSGTIAVPFLLADAMCVGYDQWATSQLIGTIFFCVGITTLLQTTFGCRLPLFQASAFAFLAPARAILSLDKWKCNTTDVSVANGTAELLHTEHIWYPRIREIQGAIIMSSLIEVVIGLLGLPGALLKYIGPLTITPTVALIGLSGFQAAGERAGKHWGIAMLTIFLVLLFSQYARNVKFPLPIYKSKKGWTAYKLQLFKMFPIILAI... | Function: Sodium/ascorbate cotransporter . Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate .
PTM: Phosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: L-ascorbate(out) + 2 Na(+)(out) = L-ascorbate(in) + 2 Na(+)(in)
Sequence Mass (Da): 70337
Seq... |
O35488 | MLPVLYTGLAGLLLLPLLLTCCCPYLLQDVRYFLRLANMARRVRSYRQRRPVRTILRAFLEQARKTPHKPFLLFRDETLTYAQVDRRSNQVARALHDQLGLRQGDCVALFMGNEPAYVWIWLGLLKLGCPMACLNYNIRAKSLLHCFQCCGAKVLLASPDLQEAVEEVLPTLKKDAVSVFYVSRTSNTNGVDTILDKVDGVSAEPTPESWRSEVTFTTPAVYIYTSGTTGLPKAATINHHRLWYGTGLAMSSGITAQDVIYTTMPLYHSAALMIGLHGCIVVGATLALRSKFSASQFWDDCRKYNVTVIQYIGELLRYLC... | Function: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport across cell membranes, playing an important role in hepatic fatty acid uptake . Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty ... |
Q5K4L6 | MAALLLLPLLLLLPLLLLKLHLWPQLRWLPADLAFAVRALCCKRALRARALAAAAADPEGPEGGCSLAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAFLRALGWDWGPDGGDSGEGSAGEGERAAPGAGDAAAGSGAEFAGGDGAARGGGAAAPLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGLHLWAAGPGTHPAGISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQLCGVHQE... | Function: Mainly functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates . Can mediate the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across membranes (By similarity).
Catalytic Act... |
O88561 | MAALLLLLPLLLLLPLLLKLDVWPQLRWLPADLAFTVRALRCKRALRARALAAAAADPESSESGCSLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLRARGWTGGRRGSGRGSTEEGARVAPPAGDAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSL... | Function: Mainly functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates . Can mediate the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across membranes .
Catalytic Activity: a fatty ... |
Q6P1M0 | MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLLKVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFW... | Function: Mediates the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across cell membranes . Appears to be the principal fatty acid transporter in small intestinal enterocytes . Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA... |
Q91VE0 | MLLGASLVGALLFSKLVLKLPWTQVGFSLLLLYLGSGGWRFIRVFIKTVRRDIFGGMVLLKVKTKVRRYLQERKTVPLLFASMVQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLPSHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFW... | Function: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport across cell membranes . Appears to be the principal fatty acid transporter in small intestinal enterocytes . Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LC... |
Q9Y2P5 | MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWVPHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAFERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLS... | Function: May mediate the import of long-chain fatty acids (LCFA) by facilitating their transport across cell membranes . Also catalyzes the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates . Mainly functions as a bile acyl-CoA synthetase catalyzing the activati... |
Q9Y2P4 | MLLSWLTVLGAGMVVLHFLQKLLFPYFWDDFWFVLKVVLIIIRLKKYEKRGELVTVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLSENISVWGMKDSVPQGVISLKEKLSTSPDEPVPRSHHVVSLLKSTCLYIFTSGTTGLPKAAVISQLQVLRGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCK... | Function: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport at the plasma membrane . Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (By similarity). Plays a pi... |
E9Q9W4 | MLLSWLTGLGAGLLSLHFLQKLLFPYFWDDFWYLLKVVRYGIQMEMYKLRGELVTVLDKFLSHTRKQPRKAFIIYEGDVYTYEDVDKRSNRIAHALLNHSSLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFDSLLHCINTCEPTAVVVGGDLLGSIEEILPSLPKHVRVWGMKDSVPEGIDSLQEKLSLASDEPVPPSHHVTSSLKSTCLYIFTSGTTGLPKAAVISQLQVLKGSVGLWAFGCTADDIIYITLPLYHSSGSLLGIGGCVELGATCVLKKKFSASQFWNDCKKYNVTVFQYIGELCRYLCK... | Function: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport at the plasma membrane (By similarity). Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates . Plays a pi... |
O00337 | MENDPSRRRESISLTPVAKGLENMGADFLESLEEGQLPRSDLSPAEIRSSWSEAAPKPFSRWRNLQPALRARSFCREHMQLFRWIGTGLLCTGLSAFLLVACLLDFQRALALFVLTCVVLTFLGHRLLKRLLGPKLRRFLKPQGHPRLLLWFKRGLALAAFLGLVLWLSLDTSQRPEQLVSFAGICVFVALLFACSKHHCAVSWRAVSWGLGLQFVLGLLVIRTEPGFIAFEWLGEQIRIFLSYTKAGSSFVFGEALVKDVFAFQVLPIIVFFSCVISVLYHVGLMQWVILKIAWLMQVTMGTTATETLSVAGNIFVSQT... | Function: Sodium and pyrimidine nucleoside symporter of the plasma membrane that imports uridine, thymidine and cytidine into cells by coupling their transport to the transmembrane sodium electrochemical gradient. Also transports adenosine, an atypical substrate transported with high apparent affinity, but low maximum ... |
Q62674 | MADNTQRQRESISLTPMAHGLENMGAEFLESMEEGRLPHSHSSLPEGEGGLNKAERKAFSRWRSLQPTVQARSFCREHRQLFGWICKGLLSTACLGFLMVACLLDLQRALALLIITCVVLVFLAYDLLKRLLGSKLRRCVKFQGHSCLSLWLKRGLALAAGVGLILWLSLDTAQRPEQLVSFAGICVFLVLLFAGSKHHRAVSWRAVSWGLGLQFVLGLFVIRTEPGFIAFQWLGDQIQVFLSYTEAGSSFVFGEALVKDVFAFQVLPIIIFFSCVMSVLYYLGLMQWVILKIAWLMQVTMGTSATETLSVAGNIFVSQT... | Function: Sodium and pyrimidine nucleoside symporter of the plasma membrane that imports uridine, thymidine and cytidine into cells by coupling their transport to the transmembrane sodium electrochemical gradient. Also transports adenosine, an atypical substrate transported with high apparent affinity, but low maximum ... |
O43868 | MEKASGRQSIALSTVETGTVNPGLELMEKEVEPEGSKRTDAQGHSLGDGLGPSTYQRRSRWPFSKARSFCKTHASLFKKILLGLLCLAYAAYLLAACILNFQRALALFVITCLVIFVLVHSFLKKLLGKKLTRCLKPFENSRLRLWTKWVFAGVSLVGLILWLALDTAQRPEQLIPFAGICMFILILFACSKHHSAVSWRTVFSGLGLQFVFGILVIRTDLGYTVFQWLGEQVQIFLNYTVAGSSFVFGDTLVKDVFAFQALPIIIFFGCVVSILYYLGLVQWVVQKVAWFLQITMGTTATETLAVAGNIFVGMTEAPLL... | Function: Sodium-dependent and purine-selective transporter . Exhibits the transport characteristics of the nucleoside transport system cif or N1 subtype (N1/cif) (selective for purine nucleosides and uridine) . Plays a critical role in specific uptake and salvage of purine nucleosides in kidney and other tissues . May... |
Q5M7S0 | MDSDQTPLINPSLFEECAQNHFAATDPRSRRPFHIEPSYITSINDDDPQRITSVASAMNKRIHYYSKLSNPSDKGLIAPDHVLPAPEEIYVYSPLGTALKIDGSDGTGKNSSIVTIFMIWNTMMGTSILSIPWGIKQAGFTTGVCILFLMGILTLYCCYRVVKSRGTIPLTDTSNWEFPDVCQYYFGSFGRWSSLLFSLVSLIGAMIVYWVLMSNFLFNTGKFIYNYVNDVNVTDDVLSNNGSDKVICPNPDSTRPLNKSMDTYFGNGTNYEQFETWWSKTNTVPFYLVVLLLPLLSFRSPSFFAKFNILGTVSIIYLVS... | Function: Lysosomal amino acid transporter involved in the activation of mTORC1 in response to amino acid levels. Probably acts as an amino acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response t... |
Q08AI6 | MKQAGFPLGILLLFWVSYVTDFSLVLLIKGGALSGTDTYQSLVNKTFGFPGYLLLSVLQFLYPFIAMISYNIIAGDTLSKVFQRIPGVDPENVFIGRHFIIGLSTVTFTLPLSLYRNIAKLGKVSLISTGLTTLILGIVMARAISLGPHIPKTEDAWVFAKPNAIQAVGVMSFAFICHHNSFLVYSSLEEPTVAKWSRLIHMSIVISVFICIFFATCGYLTFTGFTQGDLFENYCRNDDLVTFGRFCYGVTVILTYPMECFVTREVIANVFFGGNLSSVFHIVVTVMVITVATLVSLLIDCLGIVLELNGVLCATPLIFI... | Function: Putative sodium-dependent amino acid/proton antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44825
Sequence Length: 406
Subcellular Location: Membrane
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P59889 | MDYLLQVKVGALVGLLLLTLFFGFIPARMKWFHVTGGTELHKAVLSFVSCFAGGVFLSACLLDIIPDYLSDIHGELQKRDLDDGFPLPEFIMACGFFTVLILEKMVLSCTEGHRNEETAPLLAPAAPNGHAHGHPSVNDLEGSGHHVHVDFHAHSSFRSFMLFLSLSLHSVFEGLAIGLQTTNAKVLEICIAILVHKSIIVFSLSVKLVQSAVKPLWVVLYVTVFAIMSPLGIGIGIVVIETERQAGGLIQAVLEGLAAGTFIYITFLEILPHELNSSERPLLKVLFLLCGFSIMAALCFLG | Function: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space.
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32822
Sequence Length: 302
Subcellular Location: Cell membrane
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Q9NY26 | MGPWGEPELLVWRPEAVASEPPVPVGLEVKLGALVLLLVLTLLCSLVPICVLRRPGANHEGSASRQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALAALHVTLQFPLQEFILAMGFFLVLVMEQITLAYKEQSGPSPLEETRALLGTVNGGPQHWHDGPGVPQASGAPATPSALRACVLVFSLALHSVFEGLAVGLQRDRARAMELCLALLLHKGILAVSLSLRLLQSHLRAQVVAGCGILFSCMTPLGIGLGAALAESAGPLHQLAQSVLEGMAAGTFLYITFLEILPQELASSEQRILKVILLLAGFALLTGLL... | Function: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space . Functions as the major importer of zinc from circulating blood plasma into prostate cells .
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass ... |
Q9QZ03 | MGPWGEPELLVWRPEAVASEPSVPVGLEVKLGALVLLLLLTLICSLVPVCVLRRSGANHEASASGQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALEALHVTLQFPLQEFILAMGFFLVLVMEQITLAYKEQTSPPHPEETRALLGTVNGGPQHWHDGPGIPQAGGTPAAPSALRACVLVFSLALHSVFEGLAVGLQRDRARAMELCLALLLHKGILAVSLSLRLLQSHLRVQVVAGCGILFSCMTPLGIGLGAALAESAGPLHQLAQSVLEGMAAGTFLYITFLEILPQELATSEQRILKVILLLAGFALLTGLL... | Function: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space.
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34293
Sequence Length: 324
Subcellular Location: Cell membrane
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Q5BKX6 | MKMAPQNADPESMQVQELSVPLPDPQKAGGAEAENCETISEGSIDRIPMRLWVMHGAVMFGREFCYAMETALVTPILLQIGLPEQYYSLTWFLSPILGLIFTPLIGSASDRCTLSWGRRRPFILALCVGVLFGVALFLNGSAIGLALGDVPNRQPIGIVLTVLGVVVLDFSADATEGPIRAYLLDVVDSEEQDMALNIHAFSAGLGGAIGYVLGGLDWTQTFLGSWFRTQNQVLFFFAAIIFTVSVALHLFSIDEEQYSPQQERSAEEPGALDGGEPHGVPAFPDEVQSEHELALDYPDVDIMRSKSDSALHVPDTALDL... | Function: Proton-associated sucrose transporter. May be able to transport also glucose and fructose.
Catalytic Activity: H(+)(out) + sucrose(out) = H(+)(in) + sucrose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83878
Sequence Length: 768
Subcellular Location: Membrane
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Q0P5V9 | MKMAPQNADSESMQVQELPVPLPDPQKPRDPEAETQEETTSEGSIDRIPTRLWVMHGAVMFGREFCYAMETALVTPILLQIGLPEKYYSLTWFLSPVLGLIFTPLIGSASDRCTLSWGRRRPFILALCVGVLIGVALFLNGSAIGLALGDVPSRQPIGIVLTVLGVVVLDFSADATEGPIRAYLLDVVDSEEQDMALNIHAFSAGLGGAIGYVLGGLDWTQTFLGDWFQTQNQVLFFFAAVIFSVSVALHLFSIEEEQYSPQQDRGPEDPTLPGTSVQPGAPAPASRLSSLGGGMQDGSPPFPDEVQSEHELSLDYLDVD... | Function: Proton-associated sucrose transporter. May be able to transport also glucose and fructose.
Catalytic Activity: H(+)(out) + sucrose(out) = H(+)(in) + sucrose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85765
Sequence Length: 785
Subcellular Location: Membrane
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Q8CA03 | MGPGGTCPWSSRLSGFRVRTWIEPVVASTQVAGSLYDAGLLLVVKESFKSEAGGSSNYSANQSLVEYQEDQQQKAISNFNIIYNLVLGLTPLLSAYGLGWLSDRYHRKISICTAMLGFLLSRIGLLLKVMLDWPVEVMYGAAALNGLCGSFSAYWSGVMALGSLGCSEGRRSVRLILIDLVLGLAGFSGSMASGHLFKQIVGHSAQGLLLTACSVGCAAFALFYSLFVLKVPESKPNKVHPTVDTVSGMMGTYRTLDPDQQDKQNVPRNPRTPGKGKSSQREVVALLFVGAIIYDLAAVGTVDVMALFVLKEPLHWNQVQ... | Function: Proton-coupled transporter that delivers pathogen-associated or danger-associated molecular patterns to cytosolic pattern recognition receptors as part of the innate immune response to microbes or tissue injury . Has selectivity toward muropeptides that contain the amino acid diaminopimelic acid (DAP-type pep... |
Q5F4B8 | MRKVLLVEPVIFIYIFASSLTSPVVQQFIYRKLWEEEYNSTAISSDNSSHCERNKSSPTYVMEKAIQEKTSFFNMQLDLTGAVPSLIVAFIIVANGDHQGRKKSLVLPSIGALIADIFLTIVSYFSWPTSVLFLATFISGLFGSMATFLGGGFAYIADQCHDEKQKTTRIAVIDLIFGVVSGLAGLSSGYFLREMGFTWTFATASLLHVVNIIYITFFLQDTVHISEFQQQAPLSYKEHLKETFSGVYMLFKTAPSKKRILIIVLLFIFMTYLFTMFGGSSLFTLYELDEPLCWTEVYIGYGAAAFTSISLTSFLGVYLF... | Function: Lysosomal proton-coupled steroid conjugate and bile acid transporter. Preferentially recognizes lipophilic steroid conjugates or bile acis as endogenous substrates and seems to mediate escape from lysosomes to the cytoplasm (By similarity). Modulates hepatic cytosolic copper homeostasis, maybe acting as a lys... |
Q7Z3Q1 | MKILFVEPAIFLSAFAMTLTGPLTTQYVYRRIWEETGNYTFSSDSNISECEKNKSSPIFAFQEEVQKKVSRFNLQMDISGLIPGLVSTFILLSISDHYGRKFPMILSSVGALATSVWLCLLCYFAFPFQLLIASTFIGAFCGNYTTFWGACFAYIVDQCKEHKQKTIRIAIIDFLLGLVTGLTGLSSGYFIRELGFEWSFLIIAVSLAVNLIYILFFLGDPVKECSSQNVTMSCSEGFKNLFYRTYMLFKNASGKRRFLLCLLLFTVITYFFVVIGIAPIFILYELDSPLCWNEVFIGYGSALGSASFLTSFLGIWLFSY... | Function: Lysosomal proton-coupled steroid conjugate and bile acid transporter. Preferentially recognizes lipophilic steroid conjugates or bile acis as endogenous substrates and seems to mediate escape from lysosomes to the cytoplasm . Modulates hepatic cytosolic copper homeostasis, maybe acting as a lysosomal copper t... |
Q9DC26 | MKISFIEPAILLNAFAMTLTIPLTAQYVYRRIWEETGNYTFASNSNGSECDQNKSSSIFAFREEVQKKASLFNLQVEMSALIPGLVSTFMLLASSDNHGRKLPMVLSSLGSLGTNTWLCMMSYFDLPLQLLIASTFIGALFGNYTTFWGACFAYIVDQQKEYKHRIIRIAILDFMLGVVTGLTGLSSGYFIRELGFVWSYFITAMVLIVNLAYILFFLNDPIKESSSQIVTMSCIESLKDLFYRTYMLFKNGSSKRQALLCLLIFTLVIYFFVIIGISPIFTLYELGPPLCWNEVYIGYGSALGSVSFLSSFLGIWLFSY... | Function: Lysosomal proton-coupled steroid conjugate and bile acid transporter. Preferentially recognizes lipophilic steroid conjugates or bile acis as endogenous substrates and seems to mediate escape from lysosomes to the cytoplasm (By similarity). Modulates hepatic cytosolic copper homeostasis, maybe acting as a lys... |
A1Z7R6 | MNEEPHAHENLVAKAQRSGDADPEVASTASEKQRSSGASAIAVGTEFPGNPQASRPQSLGMYLLEPFILILLFAYNFSSTVLKNEVIYQSCTAGFGYPDSVCQLLGTKNITNETKRIEEQVQPYAAQVTLAMRLVECFIPAFCGLFAGSWADHYGRKPLLMCSFLGYGLQYLISAAIAYCAMYTQGLVSPWWYVLSIVPLSCLGSSVTYSVAAVCFIADVSGGKVRSYRMIAYELAIYVGLLLGSLGSGYAYEATDAYIVFSISAVCIFTALFLMALLLPESLPARNRTLSTPTTDTSVVSMLKSLWSTCSKPREHQNRF... | Function: Putative proton-coupled transporter that delivers pathogen-associated molecular patterns to cytosolic pattern recognition receptors as part of the innate immune response to microbes. Likely transports anhydro-muropeptides that contain the amino acid diaminopimelic acid (DAP-type peptidoglycan muropeptides) su... |
A1L1P9 | MDSITSYNVTQMNGDTKQEKCDDVLSTSSTQKFCGGCRKKLRSLLPVNYKTEIVELLKLAGPVFISQLMIFLISFVSTVFCGHLGKTELAGVALAIAVINVTGISIGSGLASACDTLISQTFGSNNLKRVGVILQRGILILLLACFPCWALLINTEPILLAVRQSPNVASLSQLYVKIFMPALPAAFMYQLQGRYLQNQGIIWPQVITGAAGNILNALINYVFLHLLELGVAGSAAANTISQYSLAVFLYVYIRWKNLHKATWDGWSRDCLQEWGAFIRLALPSMLMLCVEWWTYEIGGFLAGLISETELGAQSVVYELA... | Function: Solute transporter for tetraethylammonium (TEA), cimetidine, metformin, guanidine, N-methylnicotinamide (NMN) and also the zwitterionic cephalosporin cephalexin. Responsible for the secretion of cationic drugs across the brush border membranes (By similarity).
Location Topology: Multi-pass membrane protein
Se... |
Q96FL8 | MEAPEEPAPVRGGPEATLEVRGSRCLRLSAFREELRALLVLAGPAFLVQLMVFLISFISSVFCGHLGKLELDAVTLAIAVINVTGVSVGFGLSSACDTLISQTYGSQNLKHVGVILQRSALVLLLCCFPCWALFLNTQHILLLFRQDPDVSRLTQTYVTIFIPALPATFLYMLQVKYLLNQGIVLPQIVTGVAANLVNALANYLFLHQLHLGVIGSALANLISQYTLALLLFLYILGKKLHQATWGGWSLECLQDWASFLRLAIPSMLMLCMEWWAYEVGSFLSGILGMVELGAQSIVYELAIIVYMVPAGFSVAASVRV... | Function: Multidrug efflux pump that functions as a H(+)/organic cation antiporter . Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively . Mediates the efflux of endogenous compounds such as crea... |
Q5I0E9 | MEVLEEPAPGPGGADAAERRGLRRLLLSGFQEELRALLVLAGPAFLAQLMMFLISFISSVFCGHLGKLELDAVTLAIAVINVTGISVGHGLSSACDTLISQTYGSQNLKHVGVILQRGTLILLLCCFPCWALFINTEQILLLFRQDPDVSRLTQTYVMVFIPALPAAFLYTLQVKYLLNQGIVLPQVITGIAANLVNALANYLFLHQLHLGVMGSALANTISQFALAIFLFLYILWRKLHHATWGGWSWECLQDWASFLQLAIPSMLMLCIEWWAYEVGSFLSGILGMVELGAQSITYELAIIVYMIPAGFSVAANVRVG... | Function: Multidrug efflux pump that functions as a H(+)/organic cation antiporter . Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively . Mediates the efflux of endogenous compounds such as crea... |
Q86VL8 | MDSLQDTVALDHGGCCPALSRLVPRGFGTEMWTLFALSGPLFLFQVLTFMIYIVSTVFCGHLGKVELASVTLAVAFVNVCGVSVGVGLSSACDTLMSQSFGSPNKKHVGVILQRGALVLLLCCLPCWALFLNTQHILLLFRQDPDVSRLTQDYVMIFIPGLPVIFLYNLLAKYLQNQGWLKGQEEESPFQTPGLSILHPSHSHLSRASFHLFQKITWPQVLSGVVGNCVNGVANYALVSVLNLGVRGSAYANIISQFAQTVFLLLYIVLKKLHLETWAGWSSQCLQDWGPFFSLAVPSMLMICVEWWAYEIGSFLMGLLS... | Function: Multidrug efflux pump that functions as a H(+)/organic cation antiporter. Mediates the efflux of cationic compounds, such as the model cations, tetraethylammonium (TEA) and 1-methyl-4-phenylpyridinium (MPP+), the platinum-based drug oxaliplatin or weak bases that are positively charged at physiological pH, ci... |
P31662 | MPKNSKVTQREHSNEHVTESVADLLALEEPVDYKQSVLNVAGETGGKQKVAEEELDAEDRPAWNSKLQYILAQIGFSVGLGNIWRFPYLCQKNGGGAYLVPYLVLLIIIGIPLFFLELAVGQRIRRGSIGVWHYVCPRLGGIGFSSCIVCLFVGLYYNVIIGWSVFYFFKSFQYPLPWSECPVIRNGTVAVVEPECEKSSATTYFWYREALDISNSISESGGLNWKMTVCLLVAWSIVGMAVVKGIQSSGKVMYFSSLFPYVVLACFLVRGLLLRGAVDGILHMFTPKLDKMLDPQVWREAATQVFFALGLGFGGVIAFS... | Function: Functions as a sodium-dependent vesicular transporter selective for proline, glycine, leucine and alanine. In contrast to other members of this neurotransmitter transporter family, does not appear to be chloride-dependent.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81055
Sequence Lengt... |
Q96N87 | MAHAPEPDPAACDLGDERPKWDNKAQYLLSCTGFAVGLGNIWRFPYLCQTYGGGAFLIPYVIALVFEGIPIFHVELAIGQRLRKGSVGVWTAISPYLSGVGLGCVTLSFLISLYYNTIVAWVLWYLLNSFQHPLPWSSCPPDLNRTGFVEECQGSSAVSYFWYRQTLNITADINDSGSIQWWLLICLAASWAVVYMCVIRGIETTGKVIYFTALFPYLVLTIFLIRGLTLPGATKGLIYLFTPNMHILQNPRVWLDAATQIFFSLSLAFGGHIAFASYNSPRNDCQKDAVVIALVNRMTSLYASIAVFSVLGFKATNDYE... | Function: Does not show neutral amino acid transporter activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70897
Sequence Length: 628
Subcellular Location: Membrane
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O88576 | MAQASGMDPLVDIEDERPKWDNKLQYLLSCIGFAVGLGNIWRFPYLCQTHGGGAFLIPYFIALVFEGIPLFYIELAIGQRLRRGSIGVWKTISPYLGGVGLGCFSVSFLVSLYYNTVLLWVLWFFLNSFQHPLPWSTCPLDLNRTGFVQECQSSGTVSYFWYRQTLNITSDISNTGTIQWKLFLCLVACWSTVYLCVIRGIESTGKVIYFTALFPYLVLTIFLIRGLTLPGATEGLIYLFTPNMKTLQNPRVWLDAATQIFFSLSLAFGGHIAFASYNPPRNNCEKDAVIIALVNSMTSLYASIAIFSVMGFKASNDYGR... | Function: Symporter that transports one amino acid molecule together with two sodium and one chloride ions in kidneys and plays a role in the neutral amino acids reabsorption . Preferentially transports neutral amino acids such as L-glycine and L-alanine but also other neutral amino acids . Required CLTRN for cell surf... |
Q695T7 | MVRLVLPNPGLDARIPSLAELETIEQEEASSRPKWDNKAQYMLTCLGFCVGLGNVWRFPYLCQSHGGGAFMIPFLILLVLEGIPLLYLEFAIGQRLRRGSLGVWSSIHPALKGLGLASMLTSFMVGLYYNTIISWIMWYLFNSFQEPLPWSDCPLNENQTGYVDECARSSPVDYFWYRETLNISTSISDSGSIQWWMLLCLACAWSVLYMCTIRGIETTGKAVYITSTLPYVVLTIFLIRGLTLKGATNGIVFLFTPNVTELAQPDTWLDAGAQVFFSFSLAFGGLISFSSYNSVHNNCEKDSVIVSIINGFTSVYVAIV... | Function: Transporter that mediates resorption of neutral amino acids across the apical membrane of renal and intestinal epithelial cells . This uptake is sodium-dependent and chloride-independent . Requires CLTRN in kidney or ACE2 in intestine for cell surface expression and amino acid transporter activity .
Catalytic... |
Q9NP91 | MEKARPLWANSLQFVFACISYAVGLGNVWRFPYLCQMYGGGSFLVPYIIMLIVEGMPLLYLELAVGQRMRQGSIGAWRTISPYLSGVGVASVVVSFFLSMYYNVINAWAFWYLFHSFQDPLPWSVCPLNGNHTGYDEECEKASSTQYFWYRKTLNISPSLQENGGVQWEPALCLLLAWLVVYLCILRGTESTGKVVYFTASLPYCVLIIYLIRGLTLHGATNGLMYMFTPKIEQLANPKAWINAATQIFFSLGLGFGSLIAFASYNEPSNNCQKHAIIVSLINSFTSIFASIVTFSIYGFKATFNYENCLKKVSLLLTNT... | Function: Mediates the Na(+)- and Cl(-)-dependent uptake of imino acids such as L-proline, N-methyl-L-proline and pipecolate as well as N-methylated amino acids . Also transports glycine, regulates proline and glycine homeostasis in the brain playing a role in the modulation of NMDAR currents .
Catalytic Activity: chlo... |
Q9VWQ2 | MGNSQPRNASRSRRTSQWPQGAAELGASASDHHYHQEELYQEQQQQQQQPQQEQPSSRRIQFQAHTNQPTQSHPPGDEEQPVQSQQQQLSTWSLGSLSGGRLNWSFSGARNSFRHRNKATRKSLTSLHGSRRGKTQWHRPLTNSIFNSHFKETSKNDLYRIDHLVAKGAFGVVFKVSSKSDISQCYALKVLKKSKLIEDNSVRQIKDEADIQKVCGHHPFIVKQIDLWQNRHNLHILSEYVPNGELFSKITHFSIDLVRLYIGEIALALDFLHNAGIIYRDAKPENILLTEQFHIKLTDFGLSKWLKLGANTRTMCGTFK... | Function: Displays kinase activity. Inhibits neuromuscular junction (NMJ) growth by interacting with and promoting the proteasome-mediated degradation of the receptor tkv which inhibits bone morphogenetic protein (BMP) signaling.
Sequence Mass (Da): 55372
Sequence Length: 483
Subcellular Location: Cytoplasm
EC: 2.7.11.... |
P28475 | MSTVTLSSGYEMPVIGLGLWRLEKDELKEVILNAIKIGYRHFDCAAHYKSEADVGEALAEAFKTGLVKREELFITTKIWNSDHGHVVEACKNSLEKLQIDYLDLYLVHYPMPTKHNAIGKTASLLGEDKVLDIDVTISLQQTWEGMEKTVSLGLVRSIGLSNYELFLTRDCLAYSKIKPAVSQFETHPYFQRDSLVKFCMKHGVLPTAHTPLGGAAANKDMFGSVSPLDDPVLNDVAKKYGKSVAQICLRWGIQRKTAVIPKSSKIQRLKENLEVLEFQLSDEDMQLIYSIDRKYRTSLPSKTWGLDVYA | Function: Synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family.
Catalytic Activity: D-sorbitol 6-phosphate + NADP(+) = aldehydo-D-glucose 6-phosphate + H(+) + NADPH
Sequence Mass (Da): 34905
Sequence Length: 310
... |
Q68FL4 | MSVQVVSAAAAAKVPEVELKDLSPSEAEPQLGLSAAAVGAMVPPAGGGDPEAPAPAPAAERPPAPGPGSGPTAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVKKQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNSKGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVEGWQPNMILDDGGDLTHWI... | Cofactor: Binds 1 NAD(+) per subunit.
Function: May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate.
PTM: Phosphorylated during neuronal differentiation at the LI... |
Q5R889 | MLGSKKKYIVNGNSGIKAQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNSKGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEI... | Cofactor: Binds 1 NAD(+) per subunit.
Function: May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosi... |
O93477 | MSDKLSYKVADISLADWGRKAIEIAENEMPGLMKMREMYSESKPLKGARIAGCLHMTLQTAVLIETLTAIGAEVQWSSCNIFSTQDHAAAAIAKTGVPVYAWKGETDEEYIWCIEQTIYFKDGKPLNMILDDGGDLTNLVHTKYPQLLKGIKGISEETTTGVHNLYKMKSSGTLQVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRAFGARVLITEIDPINALQAAMEGYEVTTMDEASKEGNIFVTTTGCADIVEGRHFENMKDDSIVCNIGHFDVELDVKWLNDNAAKKI... | Cofactor: Binds 1 NAD(+) per subunit.
Function: Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form adenosine and homocysteine (By similarity). Binds copper ions (By similarity).
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 47745
Sequence Length: 433
Pat... |
Q8A407 | MIYNMSTELFSTLPYKVADITLADFGRKEIDLAEKEMPGLMALREKYGESKPLKGARIMGSLHMTIQTAVLIETLVALGAEVRWCSCNIYSTQDHAAAAIAASGVAVFAWKGENLADYWWCTLQALNFPGGKGPNVIVDDGGDATMMIHVGYDAENDAAVLDKEVHAEDEIELNAILKKVLAEDKTRWHRVAEEMRGVSEETTTGVHRLYQMQEEGKLLFPAFNVNDSVTKSKFDNLYGCRESLADGIKRATDVMIAGKVVVVCGYGDVGKGCSHSMRSYGARVLVTEVDPICALQAAMEGFEVVTMEDACTEGNIFVTT... | Cofactor: Binds 1 NAD(+) per subunit.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 52739
Sequence Length: 476
Pathway: Amino-acid biosynthesis; L-homocystei... |
Q8KEG8 | MTTEAAVLDYKVADISLAEWGRKEIEIAEKEMPGLMATRKKYEGKKPLAGARIAGSLHMTIQTAVLIETLVELGADVRWASCNIFSTQDHAAAAIAAAGVPVFAWKGETLDEYWWCTRQILEFEGGLGPNLIVDDGGDATLMIHFGYKIENDPSMLDKTPGNAEEKALLQQLKAVFAEDNQRWHKVAAGMKGVSEETTTGVHRLYQMMEKGELLFPAINVNDSVTKSKFDNLYGCRESLADGIKRATDVMIAGKVVVVLGYGDVGKGCAHSMRSYGARVIVTEIDPICALQAAMEGFEVTTMEEAVKEGNIFVTATGNKD... | Cofactor: Binds 1 NAD(+) per subunit.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 51949
Sequence Length: 471
Pathway: Amino-acid biosynthesis; L-homocystei... |
Q0KF25 | MNAVTDLKQDYLVADINLAGWGRKEIAIAETEMPGLMAIRDEFAAAQPLKGARIAGSLHMTIQTAVLIETLKALGADVRWASCNIFSTQDHAAAAIAAGGTPVFAFKGESLKEYWDFTHRIFDWADGGTPNMILDDGGDATLLLHLGARAEKDQSVIAKATSEEETYLFAAIKEKLAKDPSWYSRNLAAIRGVTEETTTGVHRLYQMAQKGELRFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAIVAGYGDVGKGSAQALRALSAQVWVTEIDPICALQAAMEGYRVVTMDYAAEHGDIFVTCTGNYH... | Cofactor: Binds 1 NAD(+) per subunit.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 51961
Sequence Length: 472
Pathway: Amino-acid biosynthesis; L-homocystei... |
Q72EH1 | MTDAKRAQKLDLSLDHKVADMSLADYGRKDLQLSEREMPGLMELIRKYGGTKPLKGLKVTGSLHMTIQTAMLIRTLYELGADIRWASCNIFSTQDHAAAAIAASGMAKVFAWKGETLEDYWWCTEMALTWPDGSGPDLLVDDGGDATLFIHKGVEVENDPSLLKKAYDNKEFQIIMDRLALAYEQDPGRWQRVAAKVRGVSEETTTGVHRLYQLEQEGKLLFPAINVNDAVTKSKFDNLYGCRESLADGIKRATDVMVAGKVVVVAGYGDVGKGCAQSMRGFGARVLVTEIDPICALQAAMEGYEVTTMEEAVRTGDIFV... | Cofactor: Binds 1 NAD(+) per subunit.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 52897
Sequence Length: 479
Pathway: Amino-acid biosynthesis; L-homocystei... |
P10819 | MTKLHYKVKDISLAAWGRKEIEIAENEMPGLMTLRKKYGPAQILKGARIAGCLHMTIQTAVLIETLTALGAQVQWSSCNIFSTQDQAAAAIAATGVPVYAWKGETEEEYNWCVEQTIVFQDGQPLNMILDDGGDLTNLVHEKYPQFLAGIKGISEETTTGVHNLYKMFKEGKLKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQSLSKMGARVLVTEIDPINALQACMDGYQIVTMETAAPLSNIFVTTTGCRDIVRGEHFAVMKEDAIVCNIGHFDCEIDVAWLNANAKKDTV... | Cofactor: Binds 1 NAD(+) per subunit.
Function: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine... |
J7MAN2 | MHRFVLALVVFAGAAIVWAADDAAHEEGVEWTGKPWMGKWESDPSKDENVEEFKKKLQLPMSHSEMNKNSKVWIHHYKKGDEYHHKIIINDAHYKNDIVFKLGQESAGSYNGSSFSVKYEDKDGALVGSVHYTGTKEQSLDKTINNVFKLEGDHLVKTSTIEGVTMKRHYNKRQ | Function: Secreted heat soluble protein acting as a molecular shield in water-deficient condition . Tardigrade-specific intrinsically disordered proteins (TDPs) are essential for desiccation tolerance by forming non-crystalline amorphous solids upon desiccation, and this vitrified state mirrors their protective capabil... |
P0CU41 | MSRTIVALILLGLAALAAADHHEGHGAEKEWAGKAWLGKWVSTDRSENWDAFVEALGLPLAAYGGNHKTVHKLWKEGDHYHHQIIIADKSYKQDIQFKLGEEGRTAHNGTEVTFKYTEVGDNLQNEVKIPSKNKTISDSYVVKGDELEKTYKINDVVAKRWYKKHAHEPSTA | Function: Secreted heat soluble protein acting as a molecular shield in water-deficient condition . Tardigrade-specific intrinsically disordered proteins (TDPs) are essential for desiccation tolerance by forming non-crystalline amorphous solids upon desiccation, and this vitrified state mirrors their protective capabil... |
Q9SPV4 | MDVRQVLHMKGGAGENSYAMNSFIQRQVISITKPITEAAITALYSGDTVTTRLAIADLGCSSGPNALFAVTELIKTVEELRKKMGRENSPEYQIFLNDLPGNDFNAIFRSLPIENDVDGVCFINGVPGSFYGRLFPRNTLHFIHSSYSLMWLSQVPIGIESNKGNIYMANTCPQSVLNAYYKQFQEDHALFLRCRAQEVVPGGRMVLTILGRRSEDRASTECCLIWQLLAMALNQMVSEGLIEEEKMDKFNIPQYTPSPTEVEAEILKEGSFLIDHIEASEIYWSSCTKDGDGGGSVEEEGYNVARCMRAVAEPLLLDHF... | Function: Catalyzes the methylation of the free carboxyl end of the plant hormone salicylic acid (SA). Converts SA to SA methyl ester (MSA). The volatile compound MSA is hypothesized to act as an airborne signal that triggers defense responses in uninfected plants. MSA is an important chemoattractant for moth pollinate... |
Q9ZE70 | MNDALKTYLNGICWFLLSLVTSSINDVMSKYLGTRLHSFEVAFFRFFFSSIVLLPFVVYYGKNALKTSRPFVHVLRGLLLFFGMTSWTYGLTIAPVTTATVVSFAIPLFTLILAVFILNENIIWQRWVVTVVGFIGLVVMLKPHTKDFNPEILYLILAAISFAMLDIINKKFVVKESMLSMLFYSAIVTAMVSLPVAMQYWITPSSFELALLFVLGSSGSFILFFLLKAFSIVDATATAPYRYLELVISAIAAYFIFNEFPDKSTVHGAVIIIPATLFIIYSEKKSMSSKHESQ | Function: Transports S-adenosylmethionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33092
Sequence Length: 294
Subcellular Location: Cell inner membrane
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P0AFY4 | MLKRVFLSLLVLIGLLLLTVLGLDRWMSWKTAPYIYDELQDLPYRQVGVVLGTAKYYRTGVINQYYRYRIQGAINAYNSGKVNYLLLSGDNALQSYNEPMTMRKDLIAAGVDPSDIVLDYAGFRTLDSIVRTRKVFDTNDFIIITQRFHCERALFIALHMGIQAQCYAVPSPKDMLSVRIREFAARFGALADLYIFKREPRFLGPLVPIPAMHQVPEDAQGYPAVTPEQLLELQKKQGK | Function: Participates in the barrier function of the cell envelope.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27287
Sequence Length: 239
Subcellular Location: Cell inner membrane
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P0AGH6 | MPYDSVYSEKRPPGTLRTAWRKFYSDASAMVGLYGCAGLAVLCIFGGWFAPYGIDQQFLGYQLLPPSWSRYGEVSFFLGTDDLGRDVLSRLLSGAAPTVGGAFVVTLAATICGLVLGTFAGATHGLRSAVLNHILDTLLAIPSLLLAIIVVAFAGPSLSHAMFAVWLALLPRMVRSIYSMVHDELEKEYVIAARLDGASTLNILWFAVMPNITAGLVTEITRALSMAILDIAALGFLDLGAQLPSPEWGAMLGDALELIYVAPWTVMLPGAAIMISVLLVNLLGDGVRRAIIAGVE | Function: Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31548
Sequence Length: 296
Subcellular Location: Cell inner membrane
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P45287 | MQNKEPDEFRESTSIFQIWLRFRQNTIALFSFYLLIALIFTALFASYLAPYADNRQFIGQELMPPSWVDRGKIAFFFGTDDLGRDILSRLIMGTRYTLGSALLVVFSVAIIGGALGIIAGLLKGIKARFVGHIFDAFLSLPILLIAVVISTLMEPSLWNAMFATLLAILPYFIHTIYRAIQKELEKDYVVMLKLEGISNQALLKSTILPNITVIYIQEVARAFVIAVLDISALSFISLGAQRPTPEWGAMIKDSLELLYLAPWTVLLPGFAIIFTILLSIIFSNGLTKAINQHQE | Function: Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33014
Sequence Length: 295
Subcellular Location: Cell inner membrane
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P0AAH6 | MPLLDIRNLTIEFKTGDEWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVNKDNWRVTADRMRFDDIDLLRLSARERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIVTPRLTGAKNHLYA... | Function: Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37661
Sequence Length: 330
Subcellular Location: Cell inner membrane
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P45288 | MALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEISGLVGESGSGKSLIAKVICNAIKENWIITADRFRFHDVELLKLSPNKRRKLVGKEISMIFQNPLSCLDPSRKIGKQLIQNIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHPYTQALINAVPDFTQPLGFKTKLGTLEGTAPILEQMPIGCRLGPRCPFAQKKCMEKPRRLKIKQHEFS... | Function: Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39478
Sequence Length: 349
Subcellular Location: Cell inner membrane
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H8ZPX2 | MRDYREFYIDGQWVRPKGAREAEVINPATEKIVGLISLGTEEHVDLAVRAARRAFDGWSRTSKDQRLELLEQVCRAFESKLDEIAKAITEEMGAPLVQLALPLQAPAGLGHFLTAASILRDYDFEESLGTTRVVREPAGVCGLITPWNWPLNQIAAKVAPALAAGCTMVLKPSEIAPFSAYLLARIFDEVGVPPGVFNLVNGDGPGVGAPLAAHPEVDLVSFTGSTRAGTLVSTAAAPTVKRVALELGGKSANIILDDADLETAVKHGVRTMMLNTGQSCNAPSRMLVPLSKLDEVEHLAEHFCKEIVVGDPMHSDTNIG... | Function: Catalyzes the dehydrogenation of 3-succinoylsemialdehyde-pyridine to 3-succinoyl-pyridine in the nicotine degradation pathway.
Catalytic Activity: 4-oxo-4-(pyridin-3-yl)butanal + H2O + NADP(+) = 4-oxo-4-(pyridin-3-yl)butanoate + 2 H(+) + NADPH
Sequence Mass (Da): 51246
Sequence Length: 477
Pathway: Alkaloid d... |
P36636 | MPLLDIRNLTIEFKTSEGWVKAVDRVSMTLSEGEIRGLVGESGSGKSLIAKAICGVAKDNWRVTADRMRFDDIDLLRLSSRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRLGWRKRRAIELLHRVGIKDHKDAMRSFPYELTDGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKDLVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIITPRLTGAKNHLYA... | Function: Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37572
Sequence Length: 330
Subcellular Location: Cell inner membrane
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Q81FZ0 | MSIVNELVNRIDETYDVSQIEKEIKLDNIALSDLELLATGGYSPLTGFLGKEDYDSVVETLRLANGSVWSIPITLPVTEKVAESLKAGEEVKLVNNGNIYGVIQIEDIFVPDKEKEALLVYKTTDEAHPGVKKLYERPNVYVGGTIILTKRFENNQFPSYHLDPIETREAFKKRGWKTVVGFQTRNPVHRAHEYIQKSALEIVDGLFLNPLVGETKSDDIPADVRMESYEVLLQNYYPKNRVFLSVFPAAMRYAGPREAIFHALVRKNFGCTHFIVGRDHAGVGDYYGTYEAQEIFTNFTIEELGITPLFFEHSFYCTKC... | Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 42719
Sequence Length: 378
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
EC: 2.7.7.4
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O17731 | MKNFEIVTVTPDHAEQLISMIHELAEFEKMKSSVVNTAEKLRKDIENKAVHGFIAFIGEEPAGMNLFYYAYSTWVGQYLHMEDLYIRPQFRRMGLARTLWKKLAELARDKGIVRLEWAVLDWNKNAIALYDTVDYVNLTKSEGWFTFRMDGAAINKFADE | Function: Catalyzes the N-acetylation of the amino acid thialysine (S-(2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene group substituted with a sulfur . Substrate specificity: thialysine > O-(2-aminoethyl)-L-serine > S-(2-aminoethyl)-D,L-homocysteine . Does not act on polyamines, such as spermidine an... |
Q3A8R0 | MVNYHGRKEVSNILTSEEYEELKGQNFLKLSVSKTEYFDLFLLGVGLYAPLEGFMDEDDYYSTLEQFTLSSGFLWSIPIVLRVSEEEARLYDGREKVLLTAANGELLGLLESPRAFKLNKILEVEKVFKTSSPEHPGVQKILGEDEWAVAGKIKIYPPAFREIDLNLSLFPQKTREIFKSRNYKTVVGFQTRNPIHRAHEYLQKIALEIFDGLFVNPLVGETKGDDIPADVRLKCYEALLNNYYPKDRFVFATLPAPMRYAGPREAVHHAIIRQNYGCTHFIVGRDHAGVGNFYGPFEAQEIFDTFPENALEIKIVKFDN... | Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 43651
Sequence Length: 381
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
EC: 2.7.7.4
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Q9SL45 | MAIKRSSKATSSQAASIKQIVKRCSSLRKMKNVNGCYYNQEDDLPQDVPKGHFPVYVGPNRSRYIVPISWLHHSEFQTLLRLAEEEFGFDHDMGLTIPCDEVFFRSLISMFR | Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the ... |
Q41220 | MAFLRSFLGAKQIIRRESSSTPRGFMAVYVGENDQKKKRYVVPVSYLNQPLFQQLLSKSEEEFGYDHPMGGLTIPCHESLFFTVTSQIQ | Function: Functions as a positive effector of cell expansion through modulation of auxin transport.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10206
Sequence Length: 89
Subcellular Location: Cell membrane
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Q6NMM4 | MALVRSLFSAKKILGGSLVKTSKAPPKGFLAVYVGESQKKQRHFVPVSYLNQPLFQDLLSKCEEEFGFDHPMGGLTIPCPVDTFISITSQLQG | Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the ... |
Q9SRW1 | MALVRSLFVSNKILGGSLAGMRKSTSAPKGFLAVYVGESQKKQRYLVLVSYLSQPLFQDLLSKSEEEFGFDHPMGGLTIPCPEDTFLTVTSRIQG | Function: Functions as positive effectors of cell expansion through modulation of auxin transport (By similarity). Involved in thermo-responsiveness of plant architecture . Enhances plasma membrane H(+)-ATPase .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10415
Sequence Length: 95
Subcellular Loc... |
Q9SRV9 | MALVRGFMAAKKILGGSVAGTRKETSAPKGFLAVYVGESQRKKQRHLVPVSYLNQPLFQALLIKAEEEFGFNHPMGGLTIPCPEDTFLTVTSQIQG | Function: Functions as positive effectors of cell expansion through modulation of auxin transport (By similarity). Involved in thermo-responsiveness of plant architecture . Enhances plasma membrane H(+)-ATPase .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10449
Sequence Length: 96
Subcellular Loc... |
O65695 | MAIMKKTSKLTQTAMLKQILKRCSSLGKKNGGGYDEDCLPLDVPKGHFPVYVGENRSRYIVPISFLTHPEFQSLLQRAEEEFGFDHDMGLTIPCDELVFQTLTSMIR | Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the ... |
Q2G1N2 | MNREMLYLNRSDIEQAGGNHSQVYVDALTEALTAHAHNDFVQPLKPYLRQDPENGHIADRIIAMPSHIGGEHAISGIKWIGSKHDNPSKRNMERASGVIILNDPETNYPIAVMEASLISSMRTAAVSVIAAKHLAKKGFKDLTIIGCGLIGDKQLQSMLEQFDHIERVFVYDQFSEACARFVDRWQQQRPEINFIATENAKEAVSNGEVVITCTVTDQPYIEYDWLQKGAFISNISIMDVHKEVFIKADKVVVDDWSQCNREKKTINQLVLEGKFSKEALHAELGQLVTGDIPGREDDDEIILLNPMGMAIEDISSAYFI... | Function: Catalyzes the hydrolysis of N-((2S)-2-amino-2-carboxyethyl)-L-glutamate (ACEGA) to form L-2,3-diaminopropionic acid and 2-oxoglutarate. Involved in the biosynthesis of L-2,3-diaminopropionic acid (L-Dap), a precursor of staphyloferrin B and antibiotics.
Catalytic Activity: H2O + N-[(2S)-2-amino-2-carboxyethyl... |
Q2G1N1 | MQNHTAVNTAQAIILRDLVDALLFEDIAGIVSNSEITKENGQTLLIYERETQQIKIPVYFSALNMFRYESSQPITIEGRVSKQPLTAAEFWQTIANMNCDLSHEWEVARVEEGLTTAATQLAKQLSELDLASHPFVMSEQFASLKDRPFHPLAKEKRGLREADYQVYQAELNQSFPLMVAAVKKTHMIHGDTANIDELENLTVPIKEQATDMLNDQGLSIDDYVLFPVHPWQYQHILPNVFAKEISEKLVVLLPLKFGDYLSSSSMRSLIDIGAPYNHVKVPFAMQSLGALRLTPTRYMKNGEQAEQLLRQLIEKDEALA... | Function: Catalyzes the condensation of L-2,3-diaminopropionyl-citryl-diaminoethane and 2-oxoglutarate to form staphyloferrin B, the fourth and last step in staphyloferrin B biosynthesis.
Catalytic Activity: 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate + ATP = AMP + ... |
Q2G1N0 | MINQSIWRSNFRILWLSQFIAIAGLTVLVPLLPIYMASLQNLSVVEIQLWSGIAIAAPAVTTMIASPIWGKLGDKISRKWMVLRALLGLAVCLFLMALCTTPLQFVLVRLLQGLFGGVVDASSAFASAEAPAEDRGKVLGRLQSSVSAGSLVGPLIGGVTASILGFSALLMSIAVITFIVCIFGALKLIETTHMPKSQTPNINKGIRRSFQCLLCTQQTCRFIIVGVLANFAMYGMLTALSPLASSVNHTAIDDRSVIGFLQSAFWTASILSAPLWGRFNDKSYVKSVYIFATIACGCSAILQGLATNIEFLMAARILQG... | Function: Involved in staphyloferrin B secretion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44835
Sequence Length: 418
Subcellular Location: Cell membrane
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Q2G1M9 | MQNKELIQHAAYAAIERILNEYFREENLYQVPPQNHQWSIQLSELETLTGEFRYWSAMGHHMYHPEVWLIDGKSKKITTYKEAIARILQHMAQSADNQTAVQQHMAQIMSDIDNSIHRTARYLQSNTIDYVEDRYIVSEQSLYLGHPFHPTPKSASGFSEADLEKYAPECHTSFQLHYLAVHQDVLLTRYVEGKEDQVEKVLYQLADIDISEIPKDFILLPTHPYQINVLRQHPQYMQYSEQGLIKDLGVSGDSVYPTSSVRTVFSKALNIYLKLPIHVKITNFIRTNDLEQIERTIDAAQVIASVKDEVETPHFKLMFE... | Function: Catalyzes the synthesis of citryl-L-2,3-diaminopropionic acid from L-2,3-diaminopropionic acid (L-Dap) and citrate, the first step in staphyloferrin B biosynthesis.
Catalytic Activity: (S)-2,3-diaminopropanoate + ATP + citrate = 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate + AMP + diphosphate
Sequ... |
Q2G1M8 | MIVVQTLFIHIYQIQFVITRRYRIVNQTILNRVKTRVMHQLVSSLIYENIVVYKASYQDGVGHFTIEGHDSEYRFTAEKTHSFDRIRITSPIERVVGDEADTTTDYTQLLREVVFTFPKNDEKLEQFIVELLQTELKDTQSMQYRESNPPATPETFNDYEFYAMEGHQYHPSYKSRLGFTLSDNLKFGPDFVPNVKLQWLAIDKDKVETTVSRNVVVNEMLRQQVGDKTYEHFVQQIEASGKHVNDVEMIPVHPWQFEHVIQVDLAEERLNGTVLWLGESDELYHPQQSIRTMSPIDTTKYYLKVPISITNTSTKRVLAP... | Function: Catalyzes the condensation of L-2,3-diaminopropionic acid (L-Dap) and citryl-diaminoethane to form L-2,3-diaminopropionyl-citryl-diaminoethane, the third step in staphyloferrin B biosynthesis.
Catalytic Activity: (S)-2,3-diaminopropanoate + 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate + ATP = 2-[(L... |
Q2G1M6 | MRIVQPVIEQLKAQSHPVCHYIYDLVGLEHHLQHITSSLPSNCQMYYAMKANSERKILDTISQYVEGFEVASQGEIAKGLAFKPANHIIFGGPGKTDEELRYAVSEGVQRIHVESMHELQRLNAILEDEDKTQHILLRVNLAGPFPNATLHMAGRPTQFGISEDEVDDVIEAALAMPKIHLDGFHFHSISNNLDSNLHVDVVKLYFKKAKAWSEKHRFPLKHINLGGGIGVNYADLTNQFEWDNFVERFKTLIVEQEMEDVTLNFECGRFIVAHIGYYVTEVLDIKKVHGAWYAILRGGTQQFRLPVSWQHNHPFDIYRY... | Function: Catalyzes the decarboxylation of citryl-L-2,3-diaminopropionic acid to citryl-diaminoethane, the second step in staphyloferrin B biosynthesis.
Catalytic Activity: 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate + H(+) = 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate + CO2
Sequence Mass (Da):... |
Q2G1M5 | MNHIHEHLKLVPVDKIDLHETFEPLRLEKTKSSIEADDFIRHPILVTAMQHGRYMVIDGVHRYTSLKALGCKKVPVQEIHETQYSISTWQHKVPFGVWWETLQQEHRLPWTTETRQEAPFITMCHGDTEQYLYTKDLGEAHFQVWEKVVASYSGCCSVERIAQGTYPCLSQQDVLMKYQPLSYKEIEAVVHKGETVPAGVTRFNISGRCLNLQVPLALLKQDDDVEQLRNWKQFLADKFANMRCYTEKVYLVEQ | Function: Free serine kinase that uses ATP to phosphorylate L-serine to yield O-phospho-L-serine and ADP. O-phospho-L-serine serves as a substrate for SbnA and is a precursor for staphyloferrin B biosynthesis . Is also a DNA-binding regulatory protein that senses heme to control gene expression for siderophore biosynth... |
P13866 | MDSSTWSPKTTAVTRPVETHELIRNAADISIIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAASGIAIGGFEWNALVLVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSLLSLLLYIFTKISADIFSGAIFINLALGLNLYLAIFLLLAITALYTITGGLAAVIYTDTLQTVIMLVGSLILTGFAFHEVGGYDAFMEKYMKAIPTIVSDGNTTFQEKCYTPRADSFHIFRDPLTGDLPWPGFIFGMSILTLWYWCTDQVIVQRCLSAKNMSHVKGGCILCGYL... | Function: Electrogenic Na(+)-coupled sugar simporter that actively transports D-glucose or D-galactose at the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump . Has a primary role in the transport of... |
P53791 | MDSSTWSPPATATAEPLQAYERIRNAADISVIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAAAGIATGGFEWNALILVVLLGWVFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSVLSLVLYIFTKISADIFSGAIFINLALGLDLYLAIFILLAITALYTITGGLAAVIYTDTLQTVIMLLGSFILTGFAFHEVGGYSAFVTKYMNAIPTVTSYGNTTVKKECYTPRADSFHIFRDPLKGDLPWPGLIFGLTIISLWYWCTDQVIVQRCLSAKNMSHVKAGCIMCGYM... | Function: Electrogenic Na(+)-coupled sugar simporter that actively transports D-glucose or D-galactose at the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (By similarity). Has a primary role in t... |
P31639 | MEEHTEAGSAPEMGAQKALIDNPADILVIAAYFLLVIGVGLWSMCRTNRGTVGGYFLAGRSMVWWPVGASLFASNIGSGHFVGLAGTGAASGLAVAGFEWNALFVVLLLGWLFAPVYLTAGVITMPQYLRKRFGGRRIRLYLSVLSLFLYIFTKISVDMFSGAVFIQQALGWNIYASVIALLGITMIYTVTGGLAALMYTDTVQTFVILGGACILMGYAFHEVGGYSGLFDKYLGAATSLTVSEDPAVGNISSFCYRPRPDSYHLLRHPVTGDLPWPALLLGLTIVSGWYWCSDQVIVQRCLAGKSLTHIKAGCILCGYL... | Function: Electrogenic Na(+)-coupled sugar simporter that actively transports D-glucose at the plasma membrane, with a Na(+) to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump . Has a primary role in D-glucose reabsorption from glo... |
Q00589 | MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGGGLPVFFLEVIIGQYTSEGGITCWEKICPLFSGIGYASIVIVSLLNIYYVIILAWATYYLFQSFQSELPWAHCNHSWNTPQCMEDTMRKNKSLWITLSTKNFTSPVTEFWERNVLSLSSGIDDPGSLKWDLALCLLLVWLVCFFCIWKGVKSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDISRLEDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKY... | Function: Mediates sodium- and chloride-dependent transport of taurine . Can also mediate transport of beta-alanine, hypotaurine and gamma-aminobutyric acid (GABA) (By similarity).
PTM: Taurine transport activity is down-regulated upon Ser-322 phosphorylation by PKC.
Location Topology: Multi-pass membrane protein
Catal... |
P31641 | MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLFSGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNKSVWITISSTNFTSPVIEFWERNVLSLSPGIDHPGSLKWDLALCLLLVWLVCFFCIWKGVRSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKY... | Function: Mediates sodium- and chloride-dependent transport of taurine . Mediates transport of beta-alanine . Can also mediate transport of hypotaurine and gamma-aminobutyric acid (GABA) (By similarity).
PTM: Taurine transport activity is down-regulated upon Ser-322 phosphorylation.
Location Topology: Multi-pass membra... |
Q99884 | MKKLQGAHLRKPVTPDLLMTPSDQGDVDLDVDFAAHRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSDLPWEHCGNWWNTELCLEHRVSKDGNGALPLNLTCTVSPSEEYWSRYVLHIQGSQGIGSPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIY... | Function: Brain specific sodium (and chloride)-dependent proline transporter . Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals (Probable).
Catalytic Activity: chloride(out) + L-proline(out) + 2 Na(+)(out) = chloride(in) + L-proline(in) + 2 Na(+)(in)
Location To... |
Q6PGE7 | MKKLQEAHLRKPITPDLLMTPSDQGDVDLDVDFAADRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSNLPWEHCGNWWNTELCLEHRGPKSGNGVLPLNLSSTVSPSEEYWSRYVLHIQGSQGIGRPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIY... | Function: Brain specific sodium (and chloride)-dependent proline transporter. Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals.
Catalytic Activity: chloride(out) + L-proline(out) + 2 Na(+)(out) = chloride(in) + L-proline(in) + 2 Na(+)(in)
Location Topology: Mult... |
P28573 | MKKLQEAHLRKPVTPDLLMTPSDQGDVDLDVDFAADRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSNLPWEHCGNWWNTERCLEHRGPKDGNGALPLNLSSTVSPSEEYWSRYVLHIQGSQGIGRPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIY... | Function: Brain specific sodium (and chloride)-dependent proline transporter . Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals (Probable).
Catalytic Activity: chloride(out) + L-proline(out) + 2 Na(+)(out) = chloride(in) + L-proline(in) + 2 Na(+)(in)
Location To... |
P48029 | MAKKSAENGIYSVSGDEKKGPLIAPGPDGAPAKGDGPVGLGTPGGRLAVPPRETWTRQMDFIMSCVGFAVGLGNVWRFPYLCYKNGGGVFLIPYVLIALVGGIPIFFLEISLGQFMKAGSINVWNICPLFKGLGYASMVIVFYCNTYYIMVLAWGFYYLVKSFTTTLPWATCGHTWNTPDCVEIFRHEDCANASLANLTCDQLADRRSPVIEFWENKVLRLSGGLEVPGALNWEVTLCLLACWVLVYFCVWKGVKSTGKIVYFTATFPYVVLVVLLVRGVLLPGALDGIIYYLKPDWSKLGSPQVWIDAGTQIFFSYAIG... | Function: Creatine:sodium symporter which mediates the uptake of creatine . Plays an important role in supplying creatine to the brain via the blood-brain barrier (By similarity).
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: chloride(out) + creatine(out) + 2 Na(+)(out) = chlorid... |
Q91502 | MPSRAVRRCPGHLCKEMRAPRRAQPPDVPAGEPGSRVTWSRQMDFIMSCVGFAVGLGNVWRFPYLCYKNGGGVFLIPYLLVAVFGGIPIFFLEISLGQFMKAGGINAWNIAPLFKGLGYASMVIVFFCNTYYILVLTWSSFYLVQSFSSPLPWASCNNTWNTAACYEAGANASTEIYPPTAPAQSSIVQFWERRVLRLSSGLGDVGEIGWELTLCLTATWMLVYFCIWKGVKTSGKVVYVTATFPYIILVILLVRGVTLHGAVQGIVYYLQPDWGKLGEAQVWIDAGTQIFFSYAIGLGTLTALGSYNQLHNDCYKDAFI... | Function: Required for the uptake of creatine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68099
Sequence Length: 611
Subcellular Location: Membrane
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P28571 | MIGGDTRAASAHPGMASAQGPVATPSPEQPFPGTTSVSLARPVLRVWHGAHSSGLLPNLIAQHSPAMAQNGAVPSEATKKDQNLTRGNWGNQIEFVLTSVGYAVGLGNVWRFPYLCYRNGGGAFMFPYFIMLIFCGIPLFFMELSFGQFASQGCLGVWRISPMFKGVGYGMMVVSTYIGIYYNVVICIAFYYFFSSMTHVLPWAYCNNPWNTPDCAGVLDASNLTNGSRPAALSGNLSHLFNYTLQRTSPSEEYWRLYVLKLSDDIGNFGEVRLPLLGCLGVSWVVVFLCLIRGVKSSGKVVYFTATFPYVVLTILFVRG... | Function: Sodium- and chloride-dependent glycine transporter which is essential for regulating glycine concentrations at inhibitory glycinergic synapses.
Catalytic Activity: chloride(out) + glycine(out) + 2 Na(+)(out) = chloride(in) + glycine(in) + 2 Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mas... |
Q54IJ1 | MNQNSSLSSSGMMGSGGFGFDQFSNNFSIKTKQIESINKMLSLKSESSSSNNNNNNNKAISGWQEVWKVLIFDTHCSNIIAPILTKGALRNQGVTLYLPLHSDRQPIQDVPAIYFVLPTSDNIKRIAEDCKNKLYDNIYLNFASKLSNQLMEELATLTIQSDSVSMISKVYDQFLNFISLENDLFVLNNPRDSYLSFNDTRIKDTQAQENIDMVVDSLFSVLVTLGVVPIIRAPKNSAAEMIALALEKRISTTLQSSGGSNVFSNMNEMGSQLSSFYRPVLILLDRNVDLSVCLHHPWTYQALVHDVLNMSLNQVRIDVT... | Function: Involved in vesicular transport between the endoplasmic reticulum and the Golgi.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75522
Sequence Length: 673
Subcellular Location: Cytoplasm
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Q8WVM8 | MAAAAAATAAAAASIRERQTVALKRMLNFNVPHIKNSTGEPVWKVLIYDRFGQDIISPLLSVKELRDMGITLHLLLHSDRDPIPDVPAVYFVMPTEENIDRMCQDLRNQLYESYYLNFISAISRSKLEDIANAALAASAVTQVAKVFDQYLNFITLEDDMFVLCNQNKELVSYRAINRPDITDTEMETVMDTIVDSLFCFFVTLGAVPIIRCSRGTAAEMVAVKLDKKLRENLRDARNSLFTGDTLGAGQFSFQRPLLVLVDRNIDLATPLHHTWTYQALVHDVLDFHLNRVNLEESSGVENSPAGARPKRKNKKSYDLT... | Function: Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with COG4. Involved in vesicular transport between the endoplasmic reticulum and the Golgi (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 72380
Sequence Length: 642
Subcellular Loca... |
Q8BMD8 | MLRWLRAFVLPTAACHDAEPPTRYETLFRALDRNGDGVVDIGELQQGLQSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEPSEIVQSLQMLGLHISEKQAELILQSIDSDGTMTVDWNEWRDYFLFNPVTDIEEIIRFWKHSTGIDIGDSLTIPDEFTEDEKKSGQWWRQLLAGGVAGAVSRTSTAPLDRLKVMMQVHGSKSMNIFGGFRQMVKEGGIRSLWRGNGTNVIKIAPETAVKFWAYEQYKKLLTEEGQKLGTFERFISGSMAGATAQTFIYPMEVLKTRLAVAKTG... | Function: Electroneutral antiporter that mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenyl nucleo... |
O18757 | MLRWLRGFVLPTAACQGAEPPTRYETLFQALDRNGDGVVDIRELQEGLKSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQTLGLTISEQQAELILQSIDADGTMTVDWNEWRDYFLFNPVADIEEIIRFWKHSTGIDIGDSLTIPDEFTEEERKSGQWWRQLLAGGIAGAVSRTSTAPLDRLKVMMQVHGSKSMNIFGGFRQMIKEGGVRSLWRGNGTNVIKIAPETAVKFWVYEQYKKLLTEEGQKIGTFERFISGSMAGATAQTFIYPMEVMKTRLAVGKTG... | Function: Electroneutral antiporter that mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenyl nucleo... |
A2ASZ8 | MLCLCLYVPIAGAAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWKQKIVQAGDKDLDGQLDFEEFVHYLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRDYHLLHPVENIPEIILYWKHSTIFDVGENLTVPDEFTVEERQTGMWWRHLVAGGGAGAVSRTCTAPLDRLKVLMQVHASRSNNMCIVGGFTQMIREGGAKSLWRGNGINVLKIAPESAIKFMAYEQMKRLVGSDQETLRIHERLVAGSLAGAIAQSSIYPMEVLKTRMALRKTGQYSGML... | Function: Electroneutral antiporter that most probably mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it could have a broader specificity for adenyl nucleotides. By regulating the mitochondrial matrix adeny... |
Q9BV35 | MRGSPGDAERRQRWGRLFEELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQGISSEGDADPDGGLDLEEFSRYLQEREQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEWRDHFLLHSLENVEDVLYFWKHSTVLDIGECLTVPDEFSKQEKLTGMWWKQLVAGAVAGAVSRTGTAPLDRLKVFMQVHASKTNRLNILGGLRSMVLEGGIRSLWRGNGINVLKIAPESAIKFMAYEQIKRAILGQQETLHVQERFVAGSLAGATAQTIIYPMEVLKTRLTLRRTGQYKGLLD... | Function: Electroneutral antiporter that mediates the transport of adenine nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenine nucl... |
P54950 | MTSKKKQIKLGVFLAGTGHHVASWRHPDAPSDASMNLDYFKELAKTAERGKLDMLFLADSLSIDSKSHPNVLTRFEPFTLLSALAQVTSKIGLTATASTTYSEPFHIARQFASLDHLSNGRAGWNVVTSSIESTALNFSGEKHLEHHLRYQRAEEFVEIVKGLWDSWEEDAFIRNKETGEFFDKEKMHELNHKGEYFSVRGPLNVSRTPQGQPVIIQAGSSGDGKALAAKTAEVIFTAQNHLESAQEFYQSIKEQAAEFGRDPEKIAIMPGIFPIIADTEEAAQAKYKELQDLIIPSVGLQILQNYLGGIDLSAYPLDGP... | Function: Catalyzes the oxidative cleavage of the C-S bond of N-acetyl-S-(2-succino)cysteine, forming oxaloacetate and N-acetylcysteine (NAC) . Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine . Shows almos... |
P0C7I8 | MAWTRDQMAARAARELTDGAYVNLGIGLPTLVANHIPDGVDVWLQSENGLLGIGPFPGEDEVDADLINAGKQTVTARSGASYFGSHDSFAMIRGGHIDLAILGAMQVTDRGDLANWMVPGKMVKGMGGAMDLVAGVKRVVVLMEHVAKDGTHKILPQCDLPLTGVGVVDRIITDLAVFDVTDGGLVLVEAAEGVGLEELRAKTGVAFVVQTRG | Catalytic Activity: a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate
Sequence Mass (Da): 22344
Sequence Length: 213
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
EC: 2.8.3.5
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Q08BG7 | MEGDVDEDDGTFTNISLADDSADGEPTVLRFRSEEQYSTMNCEIDGDMENQVEQEEKTRLINQVLELQHTLEDLSARVDAVKEENLKLKSENQVLGQYIENLMSASSVFQTTDTKSKRK | Function: Positive regulator of amino acid starvation-induced autophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13509
Sequence Length: 119
Subcellular Location: Golgi apparatus membrane
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Q5XJK1 | MDGDIENQVELEEKTRLINQVLELQNTLEDLSARVDAVKEENLKLKSENQVLGQYIENLMSASSVFQTTDSKSKRK | Function: Positive regulator of amino acid starvation-induced autophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 8684
Sequence Length: 76
Subcellular Location: Golgi apparatus membrane
|
A8NJZ7 | MVEINCFRLMSTDTTVTNETDNFPLVDDESQGSSIDTGGRIPRPAQPLPRDESDDQEEKARLISQVLELQNTLDDLSQRVDSVKEESLKLRSENQVLGQYIQNLMASSAVFQPAQSKAPQTK | Function: Positive regulator of amino acid starvation-induced autophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13625
Sequence Length: 122
Subcellular Location: Golgi apparatus membrane
|
Q9UIL1 | MRRRVFSSQDWRASGWDGMGFFSRRTFCGRSGRSCRGQLVQVSRPEVSAGSLLLPAPQAEDHSSRILYPRPKSLLPKMMNADMDAVDAENQVELEEKTRLINQVLELQHTLEDLSARVDAVKEENLKLKSENQVLGQYIENLMSASSVFQTTDTKSKRK | Function: Positive regulator of amino acid starvation-induced autophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18045
Sequence Length: 159
Subcellular Location: Golgi apparatus membrane
|
Q78YZ6 | MSKMDGLSTGEEEDSTFTSISLEDDTDHSLKSWRSRAESLLPKMMNADMDAVDAENQVELEEKTRLINQVLELQHTLEDLSARVDAVKEENLKLKSENQVLGQYIENLMSASSVFQTTDTKSKRK | Function: Positive regulator of amino acid starvation-induced autophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14155
Sequence Length: 125
Subcellular Location: Golgi apparatus membrane
|
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