ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
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stringlengths 108
11.1k
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Q76M72 | MSFQELLNQVGSLGRFQILQIVFLLLLNAIVVPHIAMENFTAAIPNHRCWVPILDNDTASDNGSRILSQDDLLRISIPLDSNLRPEKCRRFAQPQWHLLHLNGTFSNVSEPDTEPCVDGWVYDRSNFLSTIVTEWDLVCESQALNSVTKFSFMIGLFIGGIICGHLSDRLGRKFILTCALLQFAITETCVAFAPSFFIYCSLRFLAGLSVEPILVNSHLLMLEWTSPKFLTMMAALLSCAPNIGYMISAGLAFLFRIWHHLQLTMSVPIFFFLILTRWLSESARWLIVTNKPQKGLKELRKVAHMNGMKNSGDLTMEIVRTSMKAELEAAKTKPSLRDLFHTSILRKRICVLSFMRLFFTVSIFGLAVHLQHLSSNIILLQFLISALAILVSVIGPFVLNHIGRRITYLVLMSLRGIFILIAVFVPQEMQTLRIIMATLAEGISSLCVGVSRLHTNELLPTTLRATAVGVIGFFGNSGSFLSPLFMLLATYYANMPWIFYGGFSIFNAFTVFLLPETKNQPLPDSTHDVGNDWKESRKGKKEDPIIKVTRF | 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 | MEQEARVLRAAGGFGRARRLLASASWVPCIVLGLVLSSEELLTAQPAPHCRPDPTLLPPALRALRGPALLDAAIPRLGPTRAPAEALGVLSPSYLAPLTRAPRPSSWASCSGAAAGPTWNLVCGDGWKVPLEQVSHLLGWLLGCVILGAGCDRFGRRAVFVASLVLTTGLGASEALAASFPTLLVLRLLHGGTLAGALLALYLARLELCDPPHRLAFSMGAGLFSVVGTLLLPGLAALVQDWRLLQGLGALMSGLLLLFWGFPALFPESPCWLLATGQVARARKILWRFAEASGVGPGDSSLEENSLATELTMLSARSPQPRYHSPLGLLRTRVTWRNGLILGFSSLVGGGIRASFRRSLAPQVPTFYLPYFLEAGLEAAALVFLLLTADCCGRRPVLLLGTMVTGLASLLLLAGAQYLPGWTVLFLSVLGLLASRAVSALSSLFAAEVFPTVIRGAGLGLVLGAGFLGQAAGPLDTLHGRQGFFLQQVVFASLAVLALLCVLLLPESRSRGLPQSLQDADRLRRSPLLRGRPRQDHLPLLPPSNSYWAGHTPEQH | 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 membrane
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Q28ES4 | MDLDEAFLYIGEFGCCQKRLTAFLTLLQVYVACQSMLIVLVGAVPEYLIDNEDISASKEEYTKHLHDTNNFTSIVSEWHLIKNEAYKVNLASSLFFAGLLIGNILFGPLSDKLGRRPVYLSGLFFDITFGYCTALAPSYEVFAVSRFFVGIMNGGMALVSFVLTQEYVGKSYWALTGSLTNLIFAVGIAFYALLGFYIRNWRTLAFVANSPGIFFFLLSFLLPESPRWLYSHGYTTEAEGVLQSMAVGNGVERPVVKLKSCPGTSSKSAHSVFDLVKYGVLRWRTILLMYIWYVCSLVYYGLTLNAGELKGNLYLNVALYGLVEVPAFPLCLYFIEKSWSGRRKATAGFLGFAGFACIFTIFLPETNGDLLNPTVLALFGKLSVSAAFNVVYIYTSELYPTVVRNAGLGVCAMACRFGGILSPFIPTMKSLNPSMPFVAFGISGISAGILSLLLPETRNKPIAESIEDLQSPAYQLLSRGNEVLAST | 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 | MRAQEDLEGRTQHETTRDPSTPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTIAVPFLLAEALCVGHDQHMVSQLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKAILALERWKCPPEEEIYGNWSLPLNTSHIWHPRIREVQGAIMVSSVVEVVIGLLGLPGALLNYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIILFSQYLRNLTFLLPVYRWGKGLTLLRIQIFKMFPIMLAIMTVWLLCYVLTLTDVLPTDPKAYGFQARTDARGDIMAIAPWIRIPYPCQWGLPTVTAAAVLGMFSATLAGIIESIGDYYACARLAGAPPPPVHAINRGIFTEGICCIIAGLLGTGNGSTSSSPNIGVLGITKVGSRRVVQYGAAIMLVLGTIGKFTALFASLPDPILGGMFCTLFGMITAVGLSNLQFVDMNSSRNLFVLGFSMFFGLTLPNYLESNPGAINTGILEVDQILIVLLTTEMFVGGCLAFILDNTVPGSPEERGLIQWKAGAHANSDMSSSLKSYDFPIGMGIVKRITFLKYIPICPVFKGFSSSSKDQIAIPEDTPENTETASVCTKV | 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 serving as a renal urate re-absorber .
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): 64815
Sequence Length: 598
Subcellular Location: Cell membrane
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Q9Z2J0 | MKTPEDPGSPKQHEVVDSAGTSTRDRQAPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTIAVPFLLAEALCVGRDQHMVSQLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKSILALERWKCPSEEEIYGNWSMPLNTSHIWHPRIREVQGAIMVSSMVEVVIGLMGLPGALLSYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIVLFSQYLRNLTFLLPVYRWGKGLTLFRVQIFKMFPIVLAIMTVWLLCYVLTLTDVLPADPTVYGFQARTDARGDIMAISPWIRIPYPCQWGLPTVTVAAVLGMFSATLAGIIESIGDYYACARLAGAPPPPVHAINRGIFTEGICCIIAGLLGTGNGSTSSSPNIGVLGITKVGSRRVVQYGAGIMLILGAIGKFTALFASLPDPILGGMFCTLFGMITAVGLSNLQFVDMNSSRNLFVLGFSMFFGLTLPNYLDSNPGAINTGIPEVDQILTVLLTTEMFVGGCLAFILDNTVPGSPEERGLIQWKAGAHANSETSASLKSYDFPFGMGMVKRTTFFRYIPICPVFRGFSKKTQNQPPVLEDTPDNIETGSVCTKV | 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 by serving as a renal urate re-absorber (By similarity).
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): 65554
Sequence Length: 605
Subcellular Location: Cell membrane
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Q9UGH3 | MMGIGKNTTSKSMEAGSSTEGKYEDEAKHPAFFTLPVVINGGATSSGEQDNEDTELMAIYTTENGIAEKSSLAETLDSTGSLDPQRSDMIYTIEDVPPWYLCIFLGLQHYLTCFSGTIAVPFLLADAMCVGYDQWATSQLIGTIFFCVGITTLLQTTFGCRLPLFQASAFAFLAPARAILSLDKWKCNTTDVSVANGTAELLHTEHIWYPRIREIQGAIIMSSLIEVVIGLLGLPGALLKYIGPLTITPTVALIGLSGFQAAGERAGKHWGIAMLTIFLVLLFSQYARNVKFPLPIYKSKKGWTAYKLQLFKMFPIILAILVSWLLCFIFTVTDVFPPDSTKYGFYARTDARQGVLLVAPWFKVPYPFQWGLPTVSAAGVIGMLSAVVASIIESIGDYYACARLSCAPPPPIHAINRGIFVEGLSCVLDGIFGTGNGSTSSSPNIGVLGITKVGSRRVIQCGAALMLALGMIGKFSALFASLPDPVLGALFCTLFGMITAVGLSNLQFIDLNSSRNLFVLGFSIFFGLVLPSYLRQNPLVTGITGIDQVLNVLLTTAMFVGGCVAFILDNTIPGTPEERGIRKWKKGVGKGNKSLDGMESYNLPFGMNIIKKYRCFSYLPISPTFVGYTWKGLRKSDNSRSSDEDSQATG | 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
Sequence Length: 650
Subcellular Location: Cell membrane
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O35488 | MLPVLYTGLAGLLLLPLLLTCCCPYLLQDVRYFLRLANMARRVRSYRQRRPVRTILRAFLEQARKTPHKPFLLFRDETLTYAQVDRRSNQVARALHDQLGLRQGDCVALFMGNEPAYVWIWLGLLKLGCPMACLNYNIRAKSLLHCFQCCGAKVLLASPDLQEAVEEVLPTLKKDAVSVFYVSRTSNTNGVDTILDKVDGVSAEPTPESWRSEVTFTTPAVYIYTSGTTGLPKAATINHHRLWYGTGLAMSSGITAQDVIYTTMPLYHSAALMIGLHGCIVVGATLALRSKFSASQFWDDCRKYNVTVIQYIGELLRYLCNTPQKPNDRDHKVKKALGNGLRGDVWREFIKRFGDIHVYEFYASTEGNIGFVNYPRKIGAVGRANYLQRKVARYELIKYDVEKDEPVRDANGYCIKVPKGEVGLLVCKITQLTPFIGYAGGKTQTEKKKLRDVFKKGDIYFNSGDLLMIDRENFVYFHDRVGDTFRWKGENVATTEVADIVGLVDFVEEVNVYGVPVPGHEGRIGMASLKIKENYEFNGKKLFQHIAEYLPSYARPRFLRIQDTIEITGTFKHRKVTLMEEGFNPTVIKDTLYFMDDAEKTFVPMTENIYNAIIDKTLKL | 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 acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake . Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis . Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid (By similarity). May contribute to the synthesis of sphingosine-1-phosphate (By similarity). Does not activate C24 bile acids, cholate and chenodeoxycholate (By similarity). In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. However, it is not critical for THCA activation and bile synthesis in vivo (By similarity).
Catalytic Activity: a fatty acid(in) = a fatty acid(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70423
Sequence Length: 620
Subcellular Location: Endoplasmic reticulum membrane
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Q5K4L6 | MAALLLLPLLLLLPLLLLKLHLWPQLRWLPADLAFAVRALCCKRALRARALAAAAADPEGPEGGCSLAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAFLRALGWDWGPDGGDSGEGSAGEGERAAPGAGDAAAGSGAEFAGGDGAARGGGAAAPLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGLHLWAAGPGTHPAGISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMATSPGEPGLLVAPVSQQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSTLSDPLYVLDQAVGAYLPLTTARYSALLAGNLRI | 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 Activity: a fatty acid(in) = a fatty acid(out)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73550
Sequence Length: 683
Subcellular Location: Mitochondrion membrane
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O88561 | MAALLLLLPLLLLLPLLLKLDVWPQLRWLPADLAFTVRALRCKRALRARALAAAAADPESSESGCSLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLRARGWTGGRRGSGRGSTEEGARVAPPAGDAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSVLSDPLYVLDQDIGAYLPLTPARYSALLSGDLRI | 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 acid(in) = a fatty acid(out)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 72965
Sequence Length: 667
Subcellular Location: Mitochondrion membrane
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Q6P1M0 | MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLLKVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL | 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 and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake . Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis (By similarity). Probably involved in fatty acid transport across the blood barrier . Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones (By similarity).
Catalytic Activity: a fatty acid(in) = a fatty acid(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72064
Sequence Length: 643
Subcellular Location: Endoplasmic reticulum membrane
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Q91VE0 | MLLGASLVGALLFSKLVLKLPWTQVGFSLLLLYLGSGGWRFIRVFIKTVRRDIFGGMVLLKVKTKVRRYLQERKTVPLLFASMVQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLPSHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSRVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIIQQDPLRRFDGYLNQGANNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSVVKDPLFYLDARKGCYVALDQEAYTRIQAGEEKL | 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 LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake (By similarity). Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis . Probably involved in fatty acid transport across the blood barrier (By similarity). Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones .
Catalytic Activity: a fatty acid(in) = a fatty acid(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72319
Sequence Length: 643
Subcellular Location: Endoplasmic reticulum membrane
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Q9Y2P5 | MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWVPHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAFERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVDPLFVLDNRAQSFRPLTAEMYQAVCEGTWRL | 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 activation of bile acids via ATP-dependent formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine . Both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates . In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate ((25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate or THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol . Plays an important role in hepatic fatty acid uptake and bile acid reconjugation and recycling but not in de novo synthesis of bile acids (By similarity).
Catalytic Activity: a fatty acid(in) = a fatty acid(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75385
Sequence Length: 690
Subcellular Location: Endoplasmic reticulum membrane
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Q9Y2P4 | MLLSWLTVLGAGMVVLHFLQKLLFPYFWDDFWFVLKVVLIIIRLKKYEKRGELVTVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLSENISVWGMKDSVPQGVISLKEKLSTSPDEPVPRSHHVVSLLKSTCLYIFTSGTTGLPKAAVISQLQVLRGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGNIKVCELYAATESSISFMNYTGRIGAIGRTNLFYKLLSTFDLIKYDFQKDEPMRNEQGWCIHVKKGEPGLLISRVNAKNPFFGYAGPYKHTKDKLLCDVFKKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVEDGFNPLKISEPLYFMDNLKKSYVLLTRELYDQIMLGEIKL | 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 pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation such as the heart .
Catalytic Activity: a fatty acid(in) = a fatty acid(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70112
Sequence Length: 619
Subcellular Location: Cell membrane
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E9Q9W4 | MLLSWLTGLGAGLLSLHFLQKLLFPYFWDDFWYLLKVVRYGIQMEMYKLRGELVTVLDKFLSHTRKQPRKAFIIYEGDVYTYEDVDKRSNRIAHALLNHSSLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFDSLLHCINTCEPTAVVVGGDLLGSIEEILPSLPKHVRVWGMKDSVPEGIDSLQEKLSLASDEPVPPSHHVTSSLKSTCLYIFTSGTTGLPKAAVISQLQVLKGSVGLWAFGCTADDIIYITLPLYHSSGSLLGIGGCVELGATCVLKKKFSASQFWNDCKKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGLSSDVWRQFLDRFGNIKMCELYGATEGNIVFMNHTGKIGSVGRANFFYSLFFSFELIKYDFQKDEPWRNGQGWCSCVRKGEPGLLISRVNKKNPFFGYAGSDTHTKSKLLFDVFRKGDVYFNTGDLMFQDQENFVYFWDRLGDTFRWKGENVATTEVADVLGRLDFIQEANVYGVRVPGYEGKAGMTSVILKPNKSLDLEKMYNQVVTSLPAYACPLFLRIQDKMETTGTFKLKKLQLVEEGFDPLKISDPLYFMDNLKKSYVPLTEEIYNQIMSEEVKL | 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 pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation such as the heart (By similarity).
Catalytic Activity: a fatty acid(in) = a fatty acid(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70192
Sequence Length: 619
Subcellular Location: Cell membrane
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O00337 | MENDPSRRRESISLTPVAKGLENMGADFLESLEEGQLPRSDLSPAEIRSSWSEAAPKPFSRWRNLQPALRARSFCREHMQLFRWIGTGLLCTGLSAFLLVACLLDFQRALALFVLTCVVLTFLGHRLLKRLLGPKLRRFLKPQGHPRLLLWFKRGLALAAFLGLVLWLSLDTSQRPEQLVSFAGICVFVALLFACSKHHCAVSWRAVSWGLGLQFVLGLLVIRTEPGFIAFEWLGEQIRIFLSYTKAGSSFVFGEALVKDVFAFQVLPIIVFFSCVISVLYHVGLMQWVILKIAWLMQVTMGTTATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEVHVVMTGGYATIAGSLLGAYISFGIDATSLIAASVMAAPCALALSKLVYPEVEESKFRREEGVKLTYGDAQNLIEAASTGAAISVKVVANIAANLIAFLAVLDFINAALSWLGDMVDIQGLSFQLICSYILRPVAFLMGVAWEDCPVVAELLGIKLFLNEFVAYQDLSKYKQRRLAGAEEWVGDRKQWISVRAEVLTTFALCGFANFSSIGIMLGGLTSMVPQRKSDFSQIVLRALFTGACVSLVNACMAGILYMPRGAEVDCMSLLNTTLSSSSFEIYQCCREAFQSVNPEFSPEALDNCCRFYNHTICAQ | 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 velocity. Therefore, exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit) . Involved in renal nucleoside (re)absorption .
PTM: N-glycosylated. N-glycosylation is required for localization to the plasma membrane and the transporter activity.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in)
Sequence Mass (Da): 71584
Sequence Length: 649
Subcellular Location: Cell membrane
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Q62674 | MADNTQRQRESISLTPMAHGLENMGAEFLESMEEGRLPHSHSSLPEGEGGLNKAERKAFSRWRSLQPTVQARSFCREHRQLFGWICKGLLSTACLGFLMVACLLDLQRALALLIITCVVLVFLAYDLLKRLLGSKLRRCVKFQGHSCLSLWLKRGLALAAGVGLILWLSLDTAQRPEQLVSFAGICVFLVLLFAGSKHHRAVSWRAVSWGLGLQFVLGLFVIRTEPGFIAFQWLGDQIQVFLSYTEAGSSFVFGEALVKDVFAFQVLPIIIFFSCVMSVLYYLGLMQWVILKIAWLMQVTMGTSATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEVHVVMTGGYATIAGSLLGAYISFGIDAASLIAASVMAAPCALALSKLVYPEVEESKFRSENGVKLTYGDAQNLLEAASAGAAISVKVVANIAANLIAFLAVLAFVNAALSWLGDMVDIQGLSFQLICSYVLRPVAFLMGVAWEDCPVVAELLGIKFFLNEFVAYQELSQYKQRRLAGAEEWLGDKKQWISVRAEILTTYALCGFANFSSIGIMLGGLTSLVPQRRSDFSQIVLRALITGAFVSLLNACVAGILYVPRGVEVDCVSLLNQTVSSSSFEVYLCCRQVFQSTSSEFSQVALDNCCRFYNHTVCT | 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 velocity. Therefore, exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit) . Involved in renal nucleoside (re)absorption (By similarity).
PTM: N-glycosylated. N-glycosylation is required for localization to the plasma membrane and the transporter activity.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in)
Sequence Mass (Da): 71001
Sequence Length: 648
Subcellular Location: Cell membrane
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O43868 | MEKASGRQSIALSTVETGTVNPGLELMEKEVEPEGSKRTDAQGHSLGDGLGPSTYQRRSRWPFSKARSFCKTHASLFKKILLGLLCLAYAAYLLAACILNFQRALALFVITCLVIFVLVHSFLKKLLGKKLTRCLKPFENSRLRLWTKWVFAGVSLVGLILWLALDTAQRPEQLIPFAGICMFILILFACSKHHSAVSWRTVFSGLGLQFVFGILVIRTDLGYTVFQWLGEQVQIFLNYTVAGSSFVFGDTLVKDVFAFQALPIIIFFGCVVSILYYLGLVQWVVQKVAWFLQITMGTTATETLAVAGNIFVGMTEAPLLIRPYLGDMTLSEIHAVMTGGFATISGTVLGAFIAFGVDASSLISASVMAAPCALASSKLAYPEVEESKFKSEEGVKLPRGKERNVLEAASNGAVDAIGLATNVAANLIAFLAVLAFINAALSWLGELVDIQGLTFQVICSYLLRPMVFMMGVEWTDCPMVAEMVGIKFFINEFVAYQQLSQYKNKRLSGMEEWIEGEKQWISVRAEIITTFSLCGFANLSSIGITLGGLTSIVPHRKSDLSKVVVRALFTGACVSLISACMAGILYVPRGAEADCVSFPNTSFTNRTYETYMCCRGLFQSTSLNGTNPPSFSGPWEDKEFSAMALTNCCGFYNNTVCA | 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 contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable).
Catalytic Activity: adenosine(out) + Na(+)(out) = adenosine(in) + Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71926
Sequence Length: 658
Subcellular Location: Membrane
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Q5M7S0 | MDSDQTPLINPSLFEECAQNHFAATDPRSRRPFHIEPSYITSINDDDPQRITSVASAMNKRIHYYSKLSNPSDKGLIAPDHVLPAPEEIYVYSPLGTALKIDGSDGTGKNSSIVTIFMIWNTMMGTSILSIPWGIKQAGFTTGVCILFLMGILTLYCCYRVVKSRGTIPLTDTSNWEFPDVCQYYFGSFGRWSSLLFSLVSLIGAMIVYWVLMSNFLFNTGKFIYNYVNDVNVTDDVLSNNGSDKVICPNPDSTRPLNKSMDTYFGNGTNYEQFETWWSKTNTVPFYLVVLLLPLLSFRSPSFFAKFNILGTVSIIYLVSLVTLKAAHLGFHLRFSWNQVQEFFVPEFRLSFPQLTGILTLAFFIHNCIITLLKNNRNQKNNVRDLSIAYLLVGLTYIYVGVAVFASFPSPPLSKQCIQQNFLDNFPSSDILAFVARIFLLFQMMTVYPLLGYLVRVQLLGHIFGDIYPSVFHVLALNIAVVGVGVIMARFYPNIGGIIRFSGAACGLAFVFVYPSLIHMISLHRRGQLKVHSILIHVSIIVLGIANLIAQFFM | 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 to growth factors, energy levels, and amino acids. Following activation by amino acids, the Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. SLC38A9 mediates transport of amino acids with low capacity and specificity with a slight preference for polar amino acids. Acts as an arginine sensor. Following activation by arginine binding, mediates transport of L-glutamine, leucine and tyrosine with high efficiency, and is required for the efficient utilization of these amino acids after lysosomal protein degradation. However, the transport mechanism is not well defined and the role of sodium is not clear. Guanine exchange factor (GEF) that, upon arginine binding, stimulates GDP release from RRAGA and therefore activates the Rag GTPase heterodimer and the mTORC1 pathway in response to nutrient sufficiency.
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: L-leucine(in) = L-leucine(out)
Sequence Mass (Da): 62278
Sequence Length: 554
Domain: The cytosolic N-terminus part of the protein mediates interaction with the Ragulator complex. The cytosolic N-terminus part of the protein mediates interaction with the Rag GTPase heterodimer in a RRAGA GDP-loaded state dependent and upon arginine binding, leading to the GDP release and SLC38A9 dissociation from the activated Rag GTPase heterodimer (By similarity). The cytosolic N-terminus part of the protein exists at least in two distinct conformations; The first is when the N-terminus is bound snugly in the arginine binding site (in the absence of arginine, low luminal arginine state) and the second is where the N-terminus is released and the substrate-binding site is occupied by arginine (in the presence of arginine, high luminal arginine state) (By similarity).
Subcellular Location: Lysosome membrane
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Q08AI6 | MKQAGFPLGILLLFWVSYVTDFSLVLLIKGGALSGTDTYQSLVNKTFGFPGYLLLSVLQFLYPFIAMISYNIIAGDTLSKVFQRIPGVDPENVFIGRHFIIGLSTVTFTLPLSLYRNIAKLGKVSLISTGLTTLILGIVMARAISLGPHIPKTEDAWVFAKPNAIQAVGVMSFAFICHHNSFLVYSSLEEPTVAKWSRLIHMSIVISVFICIFFATCGYLTFTGFTQGDLFENYCRNDDLVTFGRFCYGVTVILTYPMECFVTREVIANVFFGGNLSSVFHIVVTVMVITVATLVSLLIDCLGIVLELNGVLCATPLIFIIPSACYLKLSEEPRTHSDKIMSCVMLPIGAVVMVFGFVMAITNTQDCTHGQEMFYCFPDNFSLTNTSESHVQQTTQLSTLNISIFQ | 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 | MGPWGEPELLVWRPEAVASEPPVPVGLEVKLGALVLLLVLTLLCSLVPICVLRRPGANHEGSASRQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALAALHVTLQFPLQEFILAMGFFLVLVMEQITLAYKEQSGPSPLEETRALLGTVNGGPQHWHDGPGVPQASGAPATPSALRACVLVFSLALHSVFEGLAVGLQRDRARAMELCLALLLHKGILAVSLSLRLLQSHLRAQVVAGCGILFSCMTPLGIGLGAALAESAGPLHQLAQSVLEGMAAGTFLYITFLEILPQELASSEQRILKVILLLAGFALLTGLLFIQI | 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 (Da): 34250
Sequence Length: 324
Subcellular Location: Cell membrane
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Q9QZ03 | MGPWGEPELLVWRPEAVASEPSVPVGLEVKLGALVLLLLLTLICSLVPVCVLRRSGANHEASASGQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALEALHVTLQFPLQEFILAMGFFLVLVMEQITLAYKEQTSPPHPEETRALLGTVNGGPQHWHDGPGIPQAGGTPAAPSALRACVLVFSLALHSVFEGLAVGLQRDRARAMELCLALLLHKGILAVSLSLRLLQSHLRVQVVAGCGILFSCMTPLGIGLGAALAESAGPLHQLAQSVLEGMAAGTFLYITFLEILPQELATSEQRILKVILLLAGFALLTGLLFVQI | 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 | MKMAPQNADPESMQVQELSVPLPDPQKAGGAEAENCETISEGSIDRIPMRLWVMHGAVMFGREFCYAMETALVTPILLQIGLPEQYYSLTWFLSPILGLIFTPLIGSASDRCTLSWGRRRPFILALCVGVLFGVALFLNGSAIGLALGDVPNRQPIGIVLTVLGVVVLDFSADATEGPIRAYLLDVVDSEEQDMALNIHAFSAGLGGAIGYVLGGLDWTQTFLGSWFRTQNQVLFFFAAIIFTVSVALHLFSIDEEQYSPQQERSAEEPGALDGGEPHGVPAFPDEVQSEHELALDYPDVDIMRSKSDSALHVPDTALDLEPELLFLHDIEPSIFHDASYPATPRSTSQELAKTKLPRLATFLKEAAKEDETLLDNHLNEAKVPNGSGSPTKDALGGYTRVDTKPSATSSSMRRRRHAFRRQASSTFSYYGKLGSHCYRYRRANAVVLIKPSRSMSDLYDMQKRQRQHRHRNQSGATTSSGDTESEEGEGETTVRLLWLSMLKMPRELMRLCLCHLLTWFSVIAEAVFYTDFMGQVIFEGDPKAPSNSTAWQAYNAGVKMGCWGLVIYAATGAICSALLQKYLDNYDLSVRVIYVLGTLGFSVGTAVMAMFPNVYVAMVTISTMGIVSMSISYCPYALLGQYHDIKQYIHHSPGNSKRGFGIDCAILSCQVYISQILVASALGGVVDAVGTVRVIPMVASVGSFLGFLTATFLVIYPNVSEEAKEEQKGLSSPLAGEGRAGGNSEKPTVLKLTRKEGLQGPVETESVV | 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 | MKMAPQNADSESMQVQELPVPLPDPQKPRDPEAETQEETTSEGSIDRIPTRLWVMHGAVMFGREFCYAMETALVTPILLQIGLPEKYYSLTWFLSPVLGLIFTPLIGSASDRCTLSWGRRRPFILALCVGVLIGVALFLNGSAIGLALGDVPSRQPIGIVLTVLGVVVLDFSADATEGPIRAYLLDVVDSEEQDMALNIHAFSAGLGGAIGYVLGGLDWTQTFLGDWFQTQNQVLFFFAAVIFSVSVALHLFSIEEEQYSPQQDRGPEDPTLPGTSVQPGAPAPASRLSSLGGGMQDGSPPFPDEVQSEHELSLDYLDVDIVRSKSDSVLHMADATLDMEPQLLFLHDIEPSIFQDASYPSTPQSTSQELLRAKLPRLSTFLRESTKEDDTLLDNHLNEAKVPNGRGSPPINSLSRSKVDLKPSVTSGSMRRRRHMFHRQASSTFSYYGKIGSHCYRYRRANAVVLIKPSRSMSDLYDLQQRQRSRHRNQSGATASSGDTESEEGETETTVRLLWLSMLKMPKELMWLCLCHLLTWFSVIAEAVFYTDFMGQVIFKGNPQAPSNSTKWHAYNAGVKMGCWGLVIYAATGAICSALLQKYLDNYDLSIRIIYMLGTLGFSVGTAVMAMFPNVYVAMVTISTMGVVSMSISYCPYALLGHYHDIKEYVHHSPGNSKRGFGIDCAILSCQVYISQILVASALGGVVDAVNSIVVIPIVASVGSFLGFLTATFLVIYPEVSEEPKEEQKGLSSGPAGEGEGGAGSEKPTVLKLSRKGGLRGLVETESMV | 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 | MGPGGTCPWSSRLSGFRVRTWIEPVVASTQVAGSLYDAGLLLVVKESFKSEAGGSSNYSANQSLVEYQEDQQQKAISNFNIIYNLVLGLTPLLSAYGLGWLSDRYHRKISICTAMLGFLLSRIGLLLKVMLDWPVEVMYGAAALNGLCGSFSAYWSGVMALGSLGCSEGRRSVRLILIDLVLGLAGFSGSMASGHLFKQIVGHSAQGLLLTACSVGCAAFALFYSLFVLKVPESKPNKVHPTVDTVSGMMGTYRTLDPDQQDKQNVPRNPRTPGKGKSSQREVVALLFVGAIIYDLAAVGTVDVMALFVLKEPLHWNQVQLGYGMASGYIIFITSFLGVLVFSRCFRDTTMIIIGMLSFGSGALLLAFVKETYMFYIARAIMLFALIPITTIRSAMSKLIKDSSYGKIFVILQLCLTLTGVVTSTIYNKIYQLTLDKFIGTCFVLSSFLSFLAIVPIGVVAYKQVPRSQQGECAEKQRS | 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 peptidoglycan muropeptides) including Tri-DAP and tracheal toxin (TCT), common in Gram-negative bacteria and Gram-positive bacilli. In the context of immune recognition of skin microbiota, shuttles bacterial muropeptides across the endolysosomal membranes into the cytosol for recognition by NOD1, triggering MYD88-dependent secretion of IL1A and neutrophil recruitment in a pyroptosis-type inflammatory process . To a lesser extent and redundantly, transports muramyl dipeptides derived from most bacterial proteoglycans, eliciting NOD2 receptor activation and downstream inflammatory responses . Postulated to function as an importer of cyclic GMP-AMP dinucleotides (cGAMPs) in monocyte and macrophage cell lineages. Selectively imports cGAMPs derived from pathogenic bacteria such as 3'3'-cGAMP thus providing for differential immune recognition of pathogenic versus commensal bacteria. During tumorigenesis may transport extracellular tumor-derived 2'3'-cGAMP across the plasma membrane of M1-polarized macrophages to activate the anti-tumoral stimulator of interferon genes (STING) pathway . The transport mechanism, its electrogenicity and stoichiometry remain to be elucidated (Probable).
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: n H(+)(out) + N-acetyl-beta-D-glucosaminyl-(1->4)-1,6-anhydro-N-acetyl-beta-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate-D-alanine(out) = n H(+)(in) + N-acetyl-beta-D-glucosaminyl-(1->4)-1,6-anhydro-N-acetyl-beta-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate-D-alanine(in)
Sequence Mass (Da): 52083
Sequence Length: 479
Subcellular Location: Endosome membrane
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Q5F4B8 | MRKVLLVEPVIFIYIFASSLTSPVVQQFIYRKLWEEEYNSTAISSDNSSHCERNKSSPTYVMEKAIQEKTSFFNMQLDLTGAVPSLIVAFIIVANGDHQGRKKSLVLPSIGALIADIFLTIVSYFSWPTSVLFLATFISGLFGSMATFLGGGFAYIADQCHDEKQKTTRIAVIDLIFGVVSGLAGLSSGYFLREMGFTWTFATASLLHVVNIIYITFFLQDTVHISEFQQQAPLSYKEHLKETFSGVYMLFKTAPSKKRILIIVLLFIFMTYLFTMFGGSSLFTLYELDEPLCWTEVYIGYGAAAFTSISLTSFLGVYLFSKCLKDIYIVFIGIFSYIGGIVMAAFAKTTLLMFLVRVPSLFSIMPIPVLRSMLSKVVLPSEQGAVFACIACLEVLTGTISLSVFNVIYAATVAWFSGFSFLLSASLCLIPLGVLCWLLCTSWNGEDLALLVPEEVSSIDSVDS | 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 lysosomal copper transporter and sequestering copper ions in the lysosome (By similarity).
Catalytic Activity: estrone 3-sulfate(out) + n H(+)(out) = estrone 3-sulfate(in) + n H(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51398
Sequence Length: 464
Subcellular Location: Lysosome membrane
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Q7Z3Q1 | MKILFVEPAIFLSAFAMTLTGPLTTQYVYRRIWEETGNYTFSSDSNISECEKNKSSPIFAFQEEVQKKVSRFNLQMDISGLIPGLVSTFILLSISDHYGRKFPMILSSVGALATSVWLCLLCYFAFPFQLLIASTFIGAFCGNYTTFWGACFAYIVDQCKEHKQKTIRIAIIDFLLGLVTGLTGLSSGYFIRELGFEWSFLIIAVSLAVNLIYILFFLGDPVKECSSQNVTMSCSEGFKNLFYRTYMLFKNASGKRRFLLCLLLFTVITYFFVVIGIAPIFILYELDSPLCWNEVFIGYGSALGSASFLTSFLGIWLFSYCMEDIHMAFIGIFTTMTGMAMTAFASTTLMMFLARVPFLFTIVPFSVLRSMLSKVVRSTEQGTLFACIAFLETLGGVTAVSTFNGIYSATVAWYPGFTFLLSAGLLLLPAISLCVVKCTSWNEGSYELLIQEESSEDASDR | 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 transporter and sequestering copper ions in the lysosome (By similarity). Transports catabolites of non-cleavable antibody-drug conjugates from the lysosome to the cytoplasm . Delivers pathogen-associated molecular patterns to cytosolic pattern recognition receptors as part of the innate immune response to microbes. Selectively transports bacterial muramyl dipeptide (MDP) into the cytosol for recognition by NOD2, triggering inflammatory responses (By similarity). Likely acts as a redundant importer of cyclic GMP-AMP dinucleotides (cGAMPs) in monocyte and macrophage cell lineages . The transport mechanism, its electrogenicity and stoichiometry remain to be elucidated (Probable).
Catalytic Activity: estrone 3-sulfate(out) + n H(+)(out) = estrone 3-sulfate(in) + n H(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51519
Sequence Length: 461
Subcellular Location: Lysosome membrane
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Q9DC26 | MKISFIEPAILLNAFAMTLTIPLTAQYVYRRIWEETGNYTFASNSNGSECDQNKSSSIFAFREEVQKKASLFNLQVEMSALIPGLVSTFMLLASSDNHGRKLPMVLSSLGSLGTNTWLCMMSYFDLPLQLLIASTFIGALFGNYTTFWGACFAYIVDQQKEYKHRIIRIAILDFMLGVVTGLTGLSSGYFIRELGFVWSYFITAMVLIVNLAYILFFLNDPIKESSSQIVTMSCIESLKDLFYRTYMLFKNGSSKRQALLCLLIFTLVIYFFVIIGISPIFTLYELGPPLCWNEVYIGYGSALGSVSFLSSFLGIWLFSYCLKDIHIAYIGIFTTMVGMTLAAFTRTTLMMFLVRIPFIFTIMPLSVLRSMLSKVVHSTEQGALFACIAFLETLAGVTSTSAYSGIYSATVAWYPGFIFLLSAGLLVLPAISLCCVKSIGWEEGSYTLLVHEEPSEHTSD | 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 lysosomal copper transporter and sequestering copper ions in the lysosome . Delivers pathogen-associated molecular patterns to cytosolic pattern recognition receptors as part of the innate immune response to microbes. Selectively transports bacterial muramyl dipeptide (MDP) into the cytosol for recognition by NOD2, triggering inflammatory responses . Likely acts as a redundant importer of cyclic GMP-AMP dinucleotides (cGAMPs) in monocyte and macrophage cell lineages . The transport mechanism, its electrogenicity and stoichiometry remain to be elucidated (Probable).
Catalytic Activity: estrone 3-sulfate(out) + n H(+)(out) = estrone 3-sulfate(in) + n H(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51383
Sequence Length: 460
Subcellular Location: Lysosome membrane
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A1Z7R6 | MNEEPHAHENLVAKAQRSGDADPEVASTASEKQRSSGASAIAVGTEFPGNPQASRPQSLGMYLLEPFILILLFAYNFSSTVLKNEVIYQSCTAGFGYPDSVCQLLGTKNITNETKRIEEQVQPYAAQVTLAMRLVECFIPAFCGLFAGSWADHYGRKPLLMCSFLGYGLQYLISAAIAYCAMYTQGLVSPWWYVLSIVPLSCLGSSVTYSVAAVCFIADVSGGKVRSYRMIAYELAIYVGLLLGSLGSGYAYEATDAYIVFSISAVCIFTALFLMALLLPESLPARNRTLSTPTTDTSVVSMLKSLWSTCSKPREHQNRFMLTTIMVVLLLTAFVSDGSNSVFYKFMRIKFHWTVKQFTEYETVGILVPAVAGSGGVLFIWSLRKCTNSAILWLALVSLLSHCSSSLMKGFALESWQIYVAIGLGVFKSLVNPMCRTMITNLLPADERGKIFALLGVLQALSPLISSTLYVAIYTRTLNTEPGIFNVFSAFLFGIGIILLGTVWHKKSRNLVYYEPVFK | 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) such as tracheal toxin (TCT), common in Gram-negative bacteria. May transport TCT across the phagosome membrane for cytosolic recognition by PGRP-LE, triggering the activation of imd/Relish pathway and production of antimicrobial peptides . The transport mechanism, its electrogenicity and stoichiometry remain to be elucidated (Probable).
Catalytic Activity: n H(+)(out) + N-acetyl-beta-D-glucosaminyl-(1->4)-1,6-anhydro-N-acetyl-beta-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate-D-alanine(out) = n H(+)(in) + N-acetyl-beta-D-glucosaminyl-(1->4)-1,6-anhydro-N-acetyl-beta-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate-D-alanine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56997
Sequence Length: 519
Subcellular Location: Cytoplasmic vesicle
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A1L1P9 | MDSITSYNVTQMNGDTKQEKCDDVLSTSSTQKFCGGCRKKLRSLLPVNYKTEIVELLKLAGPVFISQLMIFLISFVSTVFCGHLGKTELAGVALAIAVINVTGISIGSGLASACDTLISQTFGSNNLKRVGVILQRGILILLLACFPCWALLINTEPILLAVRQSPNVASLSQLYVKIFMPALPAAFMYQLQGRYLQNQGIIWPQVITGAAGNILNALINYVFLHLLELGVAGSAAANTISQYSLAVFLYVYIRWKNLHKATWDGWSRDCLQEWGAFIRLALPSMLMLCVEWWTYEIGGFLAGLISETELGAQSVVYELATIAYMFPLGFAVAASVRVGNALGAGNTERAKLSAKVALVCGVLVSCVVATLIGCTKDVIAYIFTTEEEIVSRVSQVMIMYGFFHLFDAIAGITGGIVRGAGKQLLGALCNIVGYYFVGFPTGVSLMFALSMGIIGLWIGFFGCVFLQSLFFIILIYKLDWKKATQEALIRAGVQLTETKDESFGLENKGCTEEAAKESQITEEGLTDANTDLEGLSKGGEGISEAGAKTTVGAVLTTKQLIVRRGLAVLLMVLILAGGIVLNEMLVRYLR | 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
Sequence Mass (Da): 63759
Sequence Length: 590
Subcellular Location: Cell membrane
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Q96FL8 | MEAPEEPAPVRGGPEATLEVRGSRCLRLSAFREELRALLVLAGPAFLVQLMVFLISFISSVFCGHLGKLELDAVTLAIAVINVTGVSVGFGLSSACDTLISQTYGSQNLKHVGVILQRSALVLLLCCFPCWALFLNTQHILLLFRQDPDVSRLTQTYVTIFIPALPATFLYMLQVKYLLNQGIVLPQIVTGVAANLVNALANYLFLHQLHLGVIGSALANLISQYTLALLLFLYILGKKLHQATWGGWSLECLQDWASFLRLAIPSMLMLCMEWWAYEVGSFLSGILGMVELGAQSIVYELAIIVYMVPAGFSVAASVRVGNALGAGDMEQARKSSTVSLLITVLFAVAFSVLLLSCKDHVGYIFTTDRDIINLVAQVVPIYAVSHLFEALACTSGGVLRGSGNQKVGAIVNTIGYYVVGLPIGIALMFATTLGVMGLWSGIIICTVFQAVCFLGFIIQLNWKKACQQAQVHANLKVNNVPRSGNSALPQDPLHPGCPENLEGILTNDVGKTGEPQSDQQMRQEEPLPEHPQDGAKLSRKQLVLRRGLLLLGVFLILLVGILVRFYVRIQ | 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 creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate . May also contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (Probable).
Catalytic Activity: H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61922
Sequence Length: 570
Subcellular Location: Cell membrane
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Q5I0E9 | MEVLEEPAPGPGGADAAERRGLRRLLLSGFQEELRALLVLAGPAFLAQLMMFLISFISSVFCGHLGKLELDAVTLAIAVINVTGISVGHGLSSACDTLISQTYGSQNLKHVGVILQRGTLILLLCCFPCWALFINTEQILLLFRQDPDVSRLTQTYVMVFIPALPAAFLYTLQVKYLLNQGIVLPQVITGIAANLVNALANYLFLHQLHLGVMGSALANTISQFALAIFLFLYILWRKLHHATWGGWSWECLQDWASFLQLAIPSMLMLCIEWWAYEVGSFLSGILGMVELGAQSITYELAIIVYMIPAGFSVAANVRVGNALGAGNIDQAKKSSAISLIVTELFAVTFCVLLLGCKDLVGYIFTTDWDIVALVAQVVPIYAVSHLFEALACTCGGVLRGTGNQKVGAIVNAIGYYVIGLPIGISLMFVAKLGVIGLWSGIIICSVCQTSCFLVFIARLNWKLACQQAQVHANLKVNVALNSAVSQEPAHPVGPESHGEIMMTDLEKKDEIQLDQQMNQQQALPVHPKDSNKLSGKQLALRRGLLFLGVVLVLVGGILVRVYIRTE | 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 creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate . May also contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (Probable).
Catalytic Activity: H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61440
Sequence Length: 566
Subcellular Location: Cell membrane
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Q86VL8 | MDSLQDTVALDHGGCCPALSRLVPRGFGTEMWTLFALSGPLFLFQVLTFMIYIVSTVFCGHLGKVELASVTLAVAFVNVCGVSVGVGLSSACDTLMSQSFGSPNKKHVGVILQRGALVLLLCCLPCWALFLNTQHILLLFRQDPDVSRLTQDYVMIFIPGLPVIFLYNLLAKYLQNQGWLKGQEEESPFQTPGLSILHPSHSHLSRASFHLFQKITWPQVLSGVVGNCVNGVANYALVSVLNLGVRGSAYANIISQFAQTVFLLLYIVLKKLHLETWAGWSSQCLQDWGPFFSLAVPSMLMICVEWWAYEIGSFLMGLLSVVDLSAQAVIYEVATVTYMIPLGLSIGVCVRVGMALGAADTVQAKRSAVSGVLSIVGISLVLGTLISILKNQLGHIFTNDEDVIALVSQVLPVYSVFHVFEAICCVYGGVLRGTGKQAFGAAVNAITYYIIGLPLGILLTFVVRMRIMGLWLGMLACVFLATAAFVAYTARLDWKLAAEEAKKHSGRQQQQRAESTATRPGPEKAVLSSVATGSSPGITLTTYSRSECHVDFFRTPEEAHALSAPTSRLSVKQLVIRRGAALGAASATLMVGLTVRILATRH | 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, cimetidine, the platinum-based drugs cisplatin and oxaliplatin or the antidiabetic drug metformin. Mediates the efflux of endogenous compounds such as, creatinine, thiamine and estrone-3-sulfate. Plays a physiological role in the excretion of drugs, toxins and endogenous metabolites through the kidney.
Catalytic Activity: H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65085
Sequence Length: 602
Subcellular Location: Cell membrane
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P31662 | MPKNSKVTQREHSNEHVTESVADLLALEEPVDYKQSVLNVAGETGGKQKVAEEELDAEDRPAWNSKLQYILAQIGFSVGLGNIWRFPYLCQKNGGGAYLVPYLVLLIIIGIPLFFLELAVGQRIRRGSIGVWHYVCPRLGGIGFSSCIVCLFVGLYYNVIIGWSVFYFFKSFQYPLPWSECPVIRNGTVAVVEPECEKSSATTYFWYREALDISNSISESGGLNWKMTVCLLVAWSIVGMAVVKGIQSSGKVMYFSSLFPYVVLACFLVRGLLLRGAVDGILHMFTPKLDKMLDPQVWREAATQVFFALGLGFGGVIAFSSYNKQDNNCHFDAALVSFINFFTSVLATLVVFAVLGFKANIMNEKCVVENAEKILGYLNSNVLSRDLIPPHVNFSHLTTKDYSEMYNVIMTVKEKQFSALGLDPCLLEDELDKSVQGTGLAFIAFTEAMTHFPASPFWSVMFFLMLINLGLGSMIGTMAGITTPIIDTFKVPKEMFTVGCCVFAFFVGLLFVQRSGNYFVTMFDDYSATLPLTVIVILENIAVAWIYGTKKFMQELTEMLGFRPYRFYFYMWKFVSPLCMAVLTTASIIQLGVSPPGYSAWIKEEAAERYLYFPNWAMALLITLIAVATLPIPVVFILRHFHLLSDGSNTLSVSYKKGRMMKDISNLEENDETRFILSKVPSEAPSPMPTHRSYLGPGSTSPLESSSHPNGRYGSGYLLASTPESEL | 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 Length: 727
Subcellular Location: Cytoplasmic vesicle
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Q96N87 | MAHAPEPDPAACDLGDERPKWDNKAQYLLSCTGFAVGLGNIWRFPYLCQTYGGGAFLIPYVIALVFEGIPIFHVELAIGQRLRKGSVGVWTAISPYLSGVGLGCVTLSFLISLYYNTIVAWVLWYLLNSFQHPLPWSSCPPDLNRTGFVEECQGSSAVSYFWYRQTLNITADINDSGSIQWWLLICLAASWAVVYMCVIRGIETTGKVIYFTALFPYLVLTIFLIRGLTLPGATKGLIYLFTPNMHILQNPRVWLDAATQIFFSLSLAFGGHIAFASYNSPRNDCQKDAVVIALVNRMTSLYASIAVFSVLGFKATNDYEHCLDRNILSLINDFDFPEQSISRDDYPAVLMHLNATWPKRVAQLPLKACLLEDFLDKSASGPGLAFVVFTETDLHMPGAPVWAMLFFGMLFTLGLSTMFGTVEAVITPLLDVGVLPRWVPKEALTGLVCLVCFLSATCFTLQSGNYWLEIFDNFAASPNLLMLAFLEVVGVVYVYGMKRFCDDIAWMTGRRPSPYWRLTWRVVSPLLLTIFVAYIILLFWKPLRYKAWNPKYELFPSRQEKLYPGWARAACVLLSLLPVLWVPVAALAQLLTRRRRTWRDRDARPDTDMRPDTDTRPDTDMRPDTDMR | 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 | MAQASGMDPLVDIEDERPKWDNKLQYLLSCIGFAVGLGNIWRFPYLCQTHGGGAFLIPYFIALVFEGIPLFYIELAIGQRLRRGSIGVWKTISPYLGGVGLGCFSVSFLVSLYYNTVLLWVLWFFLNSFQHPLPWSTCPLDLNRTGFVQECQSSGTVSYFWYRQTLNITSDISNTGTIQWKLFLCLVACWSTVYLCVIRGIESTGKVIYFTALFPYLVLTIFLIRGLTLPGATEGLIYLFTPNMKTLQNPRVWLDAATQIFFSLSLAFGGHIAFASYNPPRNNCEKDAVIIALVNSMTSLYASIAIFSVMGFKASNDYGRCLDRNILSLINEFDLPELSISRDEYPSVLMYLNATQTARVAQLPLKTCHLEDFLDKSASGPGLAFIVFTEAVLHMPGASVWSVLFFGMLFTLGLSSMFGNMEGVITPLLDMGILPKGIPKEVMTGVICFACFLSAICFTLQSGGYWLEIFDSFAASLNLIIFAFMEVVGVIHIYGMKRFCDDIEWMTGRRPGLYWQVTWRVVSPMLLFGIFLSYIVLLIQTPPSYKAWNPQYEHFPSREEKFYPGWVQVTCVLLSFLPSLWVPGVALAQLLSQYKQRWKATHLESGLKLQESRGC | 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 surface expression and for its amino acid transporter activity . The transport mechanism is pH-independent .
Catalytic Activity: chloride(out) + L-alanine(out) + 2 Na(+)(out) = chloride(in) + L-alanine(in) + 2 Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69229
Sequence Length: 615
Subcellular Location: Apical cell membrane
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Q695T7 | MVRLVLPNPGLDARIPSLAELETIEQEEASSRPKWDNKAQYMLTCLGFCVGLGNVWRFPYLCQSHGGGAFMIPFLILLVLEGIPLLYLEFAIGQRLRRGSLGVWSSIHPALKGLGLASMLTSFMVGLYYNTIISWIMWYLFNSFQEPLPWSDCPLNENQTGYVDECARSSPVDYFWYRETLNISTSISDSGSIQWWMLLCLACAWSVLYMCTIRGIETTGKAVYITSTLPYVVLTIFLIRGLTLKGATNGIVFLFTPNVTELAQPDTWLDAGAQVFFSFSLAFGGLISFSSYNSVHNNCEKDSVIVSIINGFTSVYVAIVVYSVIGFRATQRYDDCFSTNILTLINGFDLPEGNVTQENFVDMQQRCNASDPAAYAQLVFQTCDINAFLSEAVEGTGLAFIVFTEAITKMPLSPLWSVLFFIMLFCLGLSSMFGNMEGVVVPLQDLRVIPPKWPKEVLTGLICLGTFLIGFIFTLNSGQYWLSLLDSYAGSIPLLIIAFCEMFSVVYVYGVDRFNKDIEFMIGHKPNIFWQVTWRVVSPLLMLIIFLFFFVVEVSQELTYSIWDPGYEEFPKSQKISYPNWVYVVVVIVAGVPSLTIPGYAIYKLIRNHCQKPGDHQGLVSTLSTASMNGDLKY | 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 Activity: L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71110
Sequence Length: 634
Subcellular Location: Cell membrane
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Q9NP91 | MEKARPLWANSLQFVFACISYAVGLGNVWRFPYLCQMYGGGSFLVPYIIMLIVEGMPLLYLELAVGQRMRQGSIGAWRTISPYLSGVGVASVVVSFFLSMYYNVINAWAFWYLFHSFQDPLPWSVCPLNGNHTGYDEECEKASSTQYFWYRKTLNISPSLQENGGVQWEPALCLLLAWLVVYLCILRGTESTGKVVYFTASLPYCVLIIYLIRGLTLHGATNGLMYMFTPKIEQLANPKAWINAATQIFFSLGLGFGSLIAFASYNEPSNNCQKHAIIVSLINSFTSIFASIVTFSIYGFKATFNYENCLKKVSLLLTNTFDLEDGFLTASNLEQVKGYLASAYPSKYSEMFPQIKNCSLESELDTAVQGTGLAFIVYTEAIKNMEVSQLWSVLYFFMLLMLGIGSMLGNTAAILTPLTDSKIISSHLPKEAISGLVCLVNCAIGMVFTMEAGNYWFDIFNDYAATLSLLLIVLVETIAVCYVYGLRRFESDLKAMTGRAVSWYWKVMWAGVSPLLIVSLFVFYLSDYILTGTLKYQAWDASQGQLVTKDYPAYALAVIGLLVASSTMCIPLAALGTFVQRRLKRGDADPVA | 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: chloride(out) + L-proline(out) + 2 Na(+)(out) = chloride(in) + L-proline(in) + 2 Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65914
Sequence Length: 592
Subcellular Location: Apical cell membrane
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Q9VWQ2 | MGNSQPRNASRSRRTSQWPQGAAELGASASDHHYHQEELYQEQQQQQQQPQQEQPSSRRIQFQAHTNQPTQSHPPGDEEQPVQSQQQQLSTWSLGSLSGGRLNWSFSGARNSFRHRNKATRKSLTSLHGSRRGKTQWHRPLTNSIFNSHFKETSKNDLYRIDHLVAKGAFGVVFKVSSKSDISQCYALKVLKKSKLIEDNSVRQIKDEADIQKVCGHHPFIVKQIDLWQNRHNLHILSEYVPNGELFSKITHFSIDLVRLYIGEIALALDFLHNAGIIYRDAKPENILLTEQFHIKLTDFGLSKWLKLGANTRTMCGTFKYMAPEILCGEPYGHAVDWWALGVIACQMLTQKSPNIKRHLLRRRESVEPEDGLSNAPSIAQINGCLQDSDGDSEDFLPEEVQHLTHEGRDVLRKLLTIEPRQRIRSVMALQRIAIYKDYNLSSKQLLSLSPREIIARDGIRIYEDRHFDQLTNQCAIDAFLDF | 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.-
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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
EC: 1.1.1.200
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Q68FL4 | MSVQVVSAAAAAKVPEVELKDLSPSEAEPQLGLSAAAVGAMVPPAGGGDPEAPAPAPAAERPPAPGPGSGPTAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVKKQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNSKGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY | 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 LISN domain.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 66899
Sequence Length: 613
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
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Q5R889 | MLGSKKKYIVNGNSGIKAQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNSKGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNIGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY | 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 = adenosine + L-homocysteine
Sequence Mass (Da): 56679
Sequence Length: 508
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
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O93477 | MSDKLSYKVADISLADWGRKAIEIAENEMPGLMKMREMYSESKPLKGARIAGCLHMTLQTAVLIETLTAIGAEVQWSSCNIFSTQDHAAAAIAKTGVPVYAWKGETDEEYIWCIEQTIYFKDGKPLNMILDDGGDLTNLVHTKYPQLLKGIKGISEETTTGVHNLYKMKSSGTLQVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRAFGARVLITEIDPINALQAAMEGYEVTTMDEASKEGNIFVTTTGCADIVEGRHFENMKDDSIVCNIGHFDVELDVKWLNDNAAKKINIKPQVDRYLLKNGRHIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTNTDKYPVGVYFLPKKLDEAVAAAHLDKLGVKLTKLTDKQAKYLGLDKEGPFKPDHYRY | 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
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
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Q8A407 | MIYNMSTELFSTLPYKVADITLADFGRKEIDLAEKEMPGLMALREKYGESKPLKGARIMGSLHMTIQTAVLIETLVALGAEVRWCSCNIYSTQDHAAAAIAASGVAVFAWKGENLADYWWCTLQALNFPGGKGPNVIVDDGGDATMMIHVGYDAENDAAVLDKEVHAEDEIELNAILKKVLAEDKTRWHRVAEEMRGVSEETTTGVHRLYQMQEEGKLLFPAFNVNDSVTKSKFDNLYGCRESLADGIKRATDVMIAGKVVVVCGYGDVGKGCSHSMRSYGARVLVTEVDPICALQAAMEGFEVVTMEDACTEGNIFVTTTGNIDIIRIDHMEKMKDQAIVCNIGHFDNEIQVDALKHYSGIKCVNIKPQVDRYYFPDGHSILLLADGRLVNLGCATGHPSFVMSNSFTNQTLAQIELFNKKYEVNVYRLPKHLDEEVARLHLEKIGVKLTKLTPEQAAYIGVSVDGPYKAEHYRY | 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-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
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Q8KEG8 | MTTEAAVLDYKVADISLAEWGRKEIEIAEKEMPGLMATRKKYEGKKPLAGARIAGSLHMTIQTAVLIETLVELGADVRWASCNIFSTQDHAAAAIAAAGVPVFAWKGETLDEYWWCTRQILEFEGGLGPNLIVDDGGDATLMIHFGYKIENDPSMLDKTPGNAEEKALLQQLKAVFAEDNQRWHKVAAGMKGVSEETTTGVHRLYQMMEKGELLFPAINVNDSVTKSKFDNLYGCRESLADGIKRATDVMIAGKVVVVLGYGDVGKGCAHSMRSYGARVIVTEIDPICALQAAMEGFEVTTMEEAVKEGNIFVTATGNKDVITLDHIKQMRDEAIVCNIGHFDNEIQVDALNNFKGATRINIKPQVDKYVFENGNCIYLLAEGRLVNLGCATGHPSFVMSNSFTNQTLAQIELWQNDYKVGVYRLPKKLDEEVARLHLGQIGAKLTTLTKEQADYIGVPVEGPYKPEHYRY | 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-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
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Q0KF25 | MNAVTDLKQDYLVADINLAGWGRKEIAIAETEMPGLMAIRDEFAAAQPLKGARIAGSLHMTIQTAVLIETLKALGADVRWASCNIFSTQDHAAAAIAAGGTPVFAFKGESLKEYWDFTHRIFDWADGGTPNMILDDGGDATLLLHLGARAEKDQSVIAKATSEEETYLFAAIKEKLAKDPSWYSRNLAAIRGVTEETTTGVHRLYQMAQKGELRFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAIVAGYGDVGKGSAQALRALSAQVWVTEIDPICALQAAMEGYRVVTMDYAAEHGDIFVTCTGNYHVITHDHMAKMKDQAIVCNIGHFDNEIDIASIEKYEWDEIKPQVDHVKFPDGKKLIILAKGRLVNLGCATGHPSYVMSSSFANQTIAQIELWQERDSGKYPVGVYTLPKHLDEKVARLQLRKLNAQLTELTEQQAAYIGVKKEGPYKADHYRY | 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-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
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Q72EH1 | MTDAKRAQKLDLSLDHKVADMSLADYGRKDLQLSEREMPGLMELIRKYGGTKPLKGLKVTGSLHMTIQTAMLIRTLYELGADIRWASCNIFSTQDHAAAAIAASGMAKVFAWKGETLEDYWWCTEMALTWPDGSGPDLLVDDGGDATLFIHKGVEVENDPSLLKKAYDNKEFQIIMDRLALAYEQDPGRWQRVAAKVRGVSEETTTGVHRLYQLEQEGKLLFPAINVNDAVTKSKFDNLYGCRESLADGIKRATDVMVAGKVVVVAGYGDVGKGCAQSMRGFGARVLVTEIDPICALQAAMEGYEVTTMEEAVRTGDIFVTATGNCNVITGAHMEAMKDEAIVCNIGHFDNEIDMHYLENTEGCVCLNIKPQVDKWTLRSGRSIIVLAEGRLVNLGCATGHPSFVMSASFTNQTLAQIELATNPDLERKVYTLPKKLDEEVARLHLDRLGVKLTRLSKDQADYIGVSPEGPFKPDHYRY | 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-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
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P10819 | MTKLHYKVKDISLAAWGRKEIEIAENEMPGLMTLRKKYGPAQILKGARIAGCLHMTIQTAVLIETLTALGAQVQWSSCNIFSTQDQAAAAIAATGVPVYAWKGETEEEYNWCVEQTIVFQDGQPLNMILDDGGDLTNLVHEKYPQFLAGIKGISEETTTGVHNLYKMFKEGKLKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQSLSKMGARVLVTEIDPINALQACMDGYQIVTMETAAPLSNIFVTTTGCRDIVRGEHFAVMKEDAIVCNIGHFDCEIDVAWLNANAKKDTVKPQVDRYTLANGVHIILLAEGRLVNLGCGTGHPSFVMSNSFCNQTLAQIALWTKTEEYPLGVHFLPKILDEEVARLHLDQLGAKLTTLTEKQSEYLSVPVAGPYKVDHYRY | 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.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 47280
Sequence Length: 431
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
EC: 3.13.2.1
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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 capabilities (By similarity).
Sequence Mass (Da): 19878
Sequence Length: 174
Domain: SAHS-c1, SAHS-c2 and SAHS-c3 are 3 highly conserved regions within the SAHS protein family .
Subcellular Location: Secreted
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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 capabilities .
Sequence Mass (Da): 19346
Sequence Length: 172
Domain: SAHS-c1, SAHS-c2 and SAHS-c3 are 3 highly conserved regions within the SAHS protein family .
Subcellular Location: Secreted
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Q9SPV4 | MDVRQVLHMKGGAGENSYAMNSFIQRQVISITKPITEAAITALYSGDTVTTRLAIADLGCSSGPNALFAVTELIKTVEELRKKMGRENSPEYQIFLNDLPGNDFNAIFRSLPIENDVDGVCFINGVPGSFYGRLFPRNTLHFIHSSYSLMWLSQVPIGIESNKGNIYMANTCPQSVLNAYYKQFQEDHALFLRCRAQEVVPGGRMVLTILGRRSEDRASTECCLIWQLLAMALNQMVSEGLIEEEKMDKFNIPQYTPSPTEVEAEILKEGSFLIDHIEASEIYWSSCTKDGDGGGSVEEEGYNVARCMRAVAEPLLLDHFGEAIIEDVFHRYKLLIIERMSKEKTKFINVIVSLIRKSD | 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 pollinated flowering plants.
Catalytic Activity: S-adenosyl-L-methionine + salicylate = methyl salicylate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40289
Sequence Length: 359
EC: 2.1.1.274
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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 | MPLLDIRNLTIEFKTGDEWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVNKDNWRVTADRMRFDDIDLLRLSARERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIVTPRLTGAKNHLYACHFPLNMEKE | 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 | MALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEISGLVGESGSGKSLIAKVICNAIKENWIITADRFRFHDVELLKLSPNKRRKLVGKEISMIFQNPLSCLDPSRKIGKQLIQNIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHPYTQALINAVPDFTQPLGFKTKLGTLEGTAPILEQMPIGCRLGPRCPFAQKKCMEKPRRLKIKQHEFSCHYPINLREKNFKEKTTATPFILNCKGNE | 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 | MRDYREFYIDGQWVRPKGAREAEVINPATEKIVGLISLGTEEHVDLAVRAARRAFDGWSRTSKDQRLELLEQVCRAFESKLDEIAKAITEEMGAPLVQLALPLQAPAGLGHFLTAASILRDYDFEESLGTTRVVREPAGVCGLITPWNWPLNQIAAKVAPALAAGCTMVLKPSEIAPFSAYLLARIFDEVGVPPGVFNLVNGDGPGVGAPLAAHPEVDLVSFTGSTRAGTLVSTAAAPTVKRVALELGGKSANIILDDADLETAVKHGVRTMMLNTGQSCNAPSRMLVPLSKLDEVEHLAEHFCKEIVVGDPMHSDTNIGPLASGMQYEKVQDCIRQGVAEGAKLICGGLGRPDGLESGYFAQPTIFSAVNKQMYIAREEIFGPVLCIMPYGDENEAIQIANDSCYGLSGYVSSGSLERARNVAKQLRTGAVHLNGAALDFTAPFGGYKQSGNGREWGKYGFEEFLEIKAVMGYEGS | 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 degradation; nicotine degradation.
EC: 1.2.1.83
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P36636 | MPLLDIRNLTIEFKTSEGWVKAVDRVSMTLSEGEIRGLVGESGSGKSLIAKAICGVAKDNWRVTADRMRFDDIDLLRLSSRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRLGWRKRRAIELLHRVGIKDHKDAMRSFPYELTDGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKDLVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIITPRLTGAKNHLYACHFPLNMERE | 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 | MSIVNELVNRIDETYDVSQIEKEIKLDNIALSDLELLATGGYSPLTGFLGKEDYDSVVETLRLANGSVWSIPITLPVTEKVAESLKAGEEVKLVNNGNIYGVIQIEDIFVPDKEKEALLVYKTTDEAHPGVKKLYERPNVYVGGTIILTKRFENNQFPSYHLDPIETREAFKKRGWKTVVGFQTRNPVHRAHEYIQKSALEIVDGLFLNPLVGETKSDDIPADVRMESYEVLLQNYYPKNRVFLSVFPAAMRYAGPREAIFHALVRKNFGCTHFIVGRDHAGVGDYYGTYEAQEIFTNFTIEELGITPLFFEHSFYCTKCEAMASTKTCPHGKEDHVILSGTKVRELLRNGEIPPSTFSRKEVVEVLIKGLKKEVVTE | 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 and spermine, nor on diamines putrescine and cadaverine .
Catalytic Activity: acetyl-CoA + S-(2-aminoethyl)-L-cysteine = CoA + H(+) + S-(2-acetamidoethyl)-L-cysteine
Sequence Mass (Da): 18647
Sequence Length: 160
EC: 2.3.1.-
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Q3A8R0 | MVNYHGRKEVSNILTSEEYEELKGQNFLKLSVSKTEYFDLFLLGVGLYAPLEGFMDEDDYYSTLEQFTLSSGFLWSIPIVLRVSEEEARLYDGREKVLLTAANGELLGLLESPRAFKLNKILEVEKVFKTSSPEHPGVQKILGEDEWAVAGKIKIYPPAFREIDLNLSLFPQKTREIFKSRNYKTVVGFQTRNPIHRAHEYLQKIALEIFDGLFVNPLVGETKGDDIPADVRLKCYEALLNNYYPKDRFVFATLPAPMRYAGPREAVHHAIIRQNYGCTHFIVGRDHAGVGNFYGPFEAQEIFDTFPENALEIKIVKFDNAFYCSKCGQMATKKTCPHGPEHHLSLSGTKVREMLREGKPLPEEFTRPEVAEVLRRYYQSL | 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 acidification of the apoplast and the facilitation of solutes and water uptake to drive cell expansion (By similarity). Triggers plant growth probably by promoting cell elongation . Regulates branch angles and bending .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12942
Sequence Length: 112
Subcellular Location: Cell membrane
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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 acidification of the apoplast and the facilitation of solutes and water uptake to drive cell expansion (By similarity). 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 . Probably involved in light intensity mediated root development .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10200
Sequence Length: 93
Subcellular Location: Cell membrane
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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 Location: Cell membrane
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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 Location: Cell membrane
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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 acidification of the apoplast and the facilitation of solutes and water uptake to drive cell expansion (By similarity). Triggers plant growth probably by promoting cell elongation (By similarity). Regulates branch angles and bending (By similarity). Effector of hormonal and environmental signals in plant growth (Probable).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12139
Sequence Length: 107
Subcellular Location: Cell membrane
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Q2G1N2 | MNREMLYLNRSDIEQAGGNHSQVYVDALTEALTAHAHNDFVQPLKPYLRQDPENGHIADRIIAMPSHIGGEHAISGIKWIGSKHDNPSKRNMERASGVIILNDPETNYPIAVMEASLISSMRTAAVSVIAAKHLAKKGFKDLTIIGCGLIGDKQLQSMLEQFDHIERVFVYDQFSEACARFVDRWQQQRPEINFIATENAKEAVSNGEVVITCTVTDQPYIEYDWLQKGAFISNISIMDVHKEVFIKADKVVVDDWSQCNREKKTINQLVLEGKFSKEALHAELGQLVTGDIPGREDDDEIILLNPMGMAIEDISSAYFIYQQAQQQNIGTTLNLY | 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]-L-glutamate + NAD(+) = (S)-2,3-diaminopropanoate + 2-oxoglutarate + H(+) + NADH
Sequence Mass (Da): 37749
Sequence Length: 336
Pathway: Siderophore biosynthesis.
EC: 1.5.1.51
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Q2G1N1 | MQNHTAVNTAQAIILRDLVDALLFEDIAGIVSNSEITKENGQTLLIYERETQQIKIPVYFSALNMFRYESSQPITIEGRVSKQPLTAAEFWQTIANMNCDLSHEWEVARVEEGLTTAATQLAKQLSELDLASHPFVMSEQFASLKDRPFHPLAKEKRGLREADYQVYQAELNQSFPLMVAAVKKTHMIHGDTANIDELENLTVPIKEQATDMLNDQGLSIDDYVLFPVHPWQYQHILPNVFAKEISEKLVVLLPLKFGDYLSSSSMRSLIDIGAPYNHVKVPFAMQSLGALRLTPTRYMKNGEQAEQLLRQLIEKDEALAKYVMVCDETAWWSYMGQDNDIFKDQLGHLTVQLRKYPEVLAKNDTQQLVSMAALAANDRTLYQMICGKDNISKNDVMTLFEDIAQVFLKVTLSFMQYGALPELHGQNILLSFEDGRVQKCVLRDHDTVRIYKPWLTAHQLSLPKYVVREDTPNTLINEDLETFFAYFQTLAVSVNLYAIIDAIQDLFGVSEHELMSLLKQILKNEVATISWVTTDQLAVRHILFDKQTWPFKQILLPLLYQRDSGGGSMPSGLTTVPNPMVTYD | 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 + diphosphate + H(+) + staphyloferrin B
Sequence Mass (Da): 66433
Sequence Length: 584
Pathway: Siderophore biosynthesis.
EC: 6.3.2.56
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Q2G1N0 | MINQSIWRSNFRILWLSQFIAIAGLTVLVPLLPIYMASLQNLSVVEIQLWSGIAIAAPAVTTMIASPIWGKLGDKISRKWMVLRALLGLAVCLFLMALCTTPLQFVLVRLLQGLFGGVVDASSAFASAEAPAEDRGKVLGRLQSSVSAGSLVGPLIGGVTASILGFSALLMSIAVITFIVCIFGALKLIETTHMPKSQTPNINKGIRRSFQCLLCTQQTCRFIIVGVLANFAMYGMLTALSPLASSVNHTAIDDRSVIGFLQSAFWTASILSAPLWGRFNDKSYVKSVYIFATIACGCSAILQGLATNIEFLMAARILQGLTYSALIQSVMFVVVNACHQQLKGTFVGTTNSMLVVGQIIGSLSGAAITSYTTPATTFIVMGVVFAVSSLFLICSTITNQINDHTLMKLWELKQKSAK | 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 | MQNKELIQHAAYAAIERILNEYFREENLYQVPPQNHQWSIQLSELETLTGEFRYWSAMGHHMYHPEVWLIDGKSKKITTYKEAIARILQHMAQSADNQTAVQQHMAQIMSDIDNSIHRTARYLQSNTIDYVEDRYIVSEQSLYLGHPFHPTPKSASGFSEADLEKYAPECHTSFQLHYLAVHQDVLLTRYVEGKEDQVEKVLYQLADIDISEIPKDFILLPTHPYQINVLRQHPQYMQYSEQGLIKDLGVSGDSVYPTSSVRTVFSKALNIYLKLPIHVKITNFIRTNDLEQIERTIDAAQVIASVKDEVETPHFKLMFEEGYRALLPNPLGQTVEPEMDLLTNSAMIVREGIPNYHADKDIHVLASLFETMPDSPMSKLSQVIEQSGLAPEAWLECYLNRTLLPILKLFSNTGISLEAHVQNTLIELKDGIPDVCFVRDLEGICLSRTIATEKQLVPNVVAASSPVVYAHDEAWHRLKYYVVVNHLGHLVSTIGKATRNEVVLWQLVAHRLMTWKKEYANNAVFVDCVEDLYQTPTIAAKANLMSKLNDCGANPIYTHIPNPICHNKEVSYCESNNS | 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
Sequence Mass (Da): 65999
Sequence Length: 578
Pathway: Siderophore biosynthesis.
EC: 6.3.2.54
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Q2G1M8 | MIVVQTLFIHIYQIQFVITRRYRIVNQTILNRVKTRVMHQLVSSLIYENIVVYKASYQDGVGHFTIEGHDSEYRFTAEKTHSFDRIRITSPIERVVGDEADTTTDYTQLLREVVFTFPKNDEKLEQFIVELLQTELKDTQSMQYRESNPPATPETFNDYEFYAMEGHQYHPSYKSRLGFTLSDNLKFGPDFVPNVKLQWLAIDKDKVETTVSRNVVVNEMLRQQVGDKTYEHFVQQIEASGKHVNDVEMIPVHPWQFEHVIQVDLAEERLNGTVLWLGESDELYHPQQSIRTMSPIDTTKYYLKVPISITNTSTKRVLAPHTIENAAQITDWLKQIQQQDMYLKDELKTVFLGEVLGQSYLNTQLSPYKQTQVYGALGVIWRENIYHMLIDEEDAIPFNALYASDKDGVPFIENWIKQYGSEAWTKQFLAVAIRPMIHMLYYHGIAFESHAQNMMLIHENGWPTRIALKDFHDGVRFKREHLSEAASHLTLKPMPEAHKKVNSNSFIETDDERLVRDFLHDAFFFINIAEIILFIEKQYGIDEELQWQWVKGIIEAYQEAFPELNNYQHFDLFEPTIQVEKLTTRRLLSDSELRIHHVTNPLGVGGINDATTISET | 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-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + AMP + diphosphate
Sequence Mass (Da): 71952
Sequence Length: 616
Pathway: Siderophore biosynthesis.
EC: 6.3.2.55
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Q2G1M6 | MRIVQPVIEQLKAQSHPVCHYIYDLVGLEHHLQHITSSLPSNCQMYYAMKANSERKILDTISQYVEGFEVASQGEIAKGLAFKPANHIIFGGPGKTDEELRYAVSEGVQRIHVESMHELQRLNAILEDEDKTQHILLRVNLAGPFPNATLHMAGRPTQFGISEDEVDDVIEAALAMPKIHLDGFHFHSISNNLDSNLHVDVVKLYFKKAKAWSEKHRFPLKHINLGGGIGVNYADLTNQFEWDNFVERFKTLIVEQEMEDVTLNFECGRFIVAHIGYYVTEVLDIKKVHGAWYAILRGGTQQFRLPVSWQHNHPFDIYRYKDNPYSFEKVSISRQDTTLVGQLCTPKDVFAREVQIDAISTGDVIVFKYAGAYGWSISHHDFLSHPHPEFIYLTQTKEDE | 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): 45760
Sequence Length: 400
Pathway: Siderophore biosynthesis.
EC: 4.1.1.117
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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 biosynthesis. Binds to DNA within the sbnC coding region and is required for expression of genes in the sbn operon from sbnD onward .
Catalytic Activity: ATP + L-serine = ADP + H(+) + O-phospho-L-serine
Sequence Mass (Da): 29633
Sequence Length: 254
Pathway: Siderophore biosynthesis.
EC: 2.7.1.225
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P13866 | MDSSTWSPKTTAVTRPVETHELIRNAADISIIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAASGIAIGGFEWNALVLVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSLLSLLLYIFTKISADIFSGAIFINLALGLNLYLAIFLLLAITALYTITGGLAAVIYTDTLQTVIMLVGSLILTGFAFHEVGGYDAFMEKYMKAIPTIVSDGNTTFQEKCYTPRADSFHIFRDPLTGDLPWPGFIFGMSILTLWYWCTDQVIVQRCLSAKNMSHVKGGCILCGYLKLMPMFIMVMPGMISRILYTEKIACVVPSECEKYCGTKVGCTNIAYPTLVVELMPNGLRGLMLSVMLASLMSSLTSIFNSASTLFTMDIYAKVRKRASEKELMIAGRLFILVLIGISIAWVPIVQSAQSGQLFDYIQSITSYLGPPIAAVFLLAIFWKRVNEPGAFWGLILGLLIGISRMITEFAYGTGSCMEPSNCPTIICGVHYLYFAIILFAISFITIVVISLLTKPIPDVHLYRLCWSLRNSKEERIDLDAEEENIQEGPKETIEIETQVPEKKKGIFRRAYDLFCGLEQHGAPKMTEEEEKAMKMKMTDTSEKPLWRTVLNVNGIILVTVAVFCHAYFA | 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 dietary monosaccharides from enterocytes to blood. Responsible for the absorption of D-glucose or D-galactose across the apical brush-border membrane of enterocytes, whereas basolateral exit is provided by GLUT2. Additionally, functions as a D-glucose sensor in enteroendocrine cells, triggering the secretion of the incretins GCG and GIP that control food intake and energy homeostasis (By similarity). Together with SGLT2, functions in reabsorption of D-glucose from glomerular filtrate, playing a nonredundant role in the S3 segment of the proximal tubules (By similarity). Transports D-glucose into endometrial epithelial cells, controlling glycogen synthesis and nutritional support for the embryo as well as the decidual transformation of endometrium prior to conception . Acts as a water channel enabling passive water transport across the plasma membrane in response to the osmotic gradient created upon sugar and Na(+) uptake. Has high water conductivity, comparable to aquaporins, and therefore is expected to play an important role in transepithelial water permeability, especially in the small intestine.
PTM: N-glycosylation is not necessary for the cotransporter function.
Location Topology: Multi-pass membrane protein
Catalytic Activity: D-glucose(out) + 2 Na(+)(out) = D-glucose(in) + 2 Na(+)(in)
Sequence Mass (Da): 73498
Sequence Length: 664
Domain: The cholesterol-binding site is formed by transmembrane helices TM1, TM7 and TM13.
Subcellular Location: Apical cell membrane
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P53791 | MDSSTWSPPATATAEPLQAYERIRNAADISVIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAAAGIATGGFEWNALILVVLLGWVFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSVLSLVLYIFTKISADIFSGAIFINLALGLDLYLAIFILLAITALYTITGGLAAVIYTDTLQTVIMLLGSFILTGFAFHEVGGYSAFVTKYMNAIPTVTSYGNTTVKKECYTPRADSFHIFRDPLKGDLPWPGLIFGLTIISLWYWCTDQVIVQRCLSAKNMSHVKAGCIMCGYMKLLPMFLMVMPGMISRILFTEKVACTVPSECEKYCGTKVGCTNIAYPTLVVELMPNGLRGLMLSVMLASLMSSLTSIFNSASTLFTMDIYTKIRKKASEKELMIAGRLFMLVLIGVSIAWVPIVQSAQSGQLFDYIQSITSYLGPPIAAVFLLAIFCKRVNEPGAFWGLIIGFLIGVSRMITEFAYGTGSCMEPSNCPTIICGVHYLYFAIILFVITIIVILAISLFTKPIADVHLYRLCWSLRNSKEERIDLDAEDEDIQDAREDALEIDTEASEEKKGCLRQAYDMFCGLDQQKGPKMTKEEEAAMKLKMTDTSEKRLWRMVVNINGIILLAVAVFCHAYFA | 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 the transport of dietary monosaccharides from enterocytes to blood. Responsible for the absorption of D-glucose or D-galactose across the apical brush-border membrane of enterocytes, whereas basolateral exit is provided by GLUT2. Additionally, functions as a D-glucose sensor in enteroendocrine cells, triggering the secretion of the incretins GCG and GIP that control food intake and energy homeostasis (By similarity). Together with SGLT2, functions in reabsorption of D-glucose from glomerular filtrate, playing a nonredundant role in the S3 segment of the proximal tubules (By similarity). Transports D-glucose into endometrial epithelial cells, controlling glycogen synthesis and nutritional support for the embryo as well as the decidual transformation of endometrium prior to conception (By similarity). Acts as a water channel enabling passive water transport in response to the osmotic gradient created upon sugar and Na(+) uptake. Has high water conductivity comparable to aquaporins and therefore is expected to play an important role in transepithelial water permeability, especially in the small intestine.
PTM: N-glycosylation is not necessary for the cotransporter function.
Location Topology: Multi-pass membrane protein
Catalytic Activity: D-glucose(out) + 2 Na(+)(out) = D-glucose(in) + 2 Na(+)(in)
Sequence Mass (Da): 73179
Sequence Length: 664
Domain: The cholesterol-binding site is formed by transmembrane helices TM1, TM7 and TM13.
Subcellular Location: Apical cell membrane
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P31639 | MEEHTEAGSAPEMGAQKALIDNPADILVIAAYFLLVIGVGLWSMCRTNRGTVGGYFLAGRSMVWWPVGASLFASNIGSGHFVGLAGTGAASGLAVAGFEWNALFVVLLLGWLFAPVYLTAGVITMPQYLRKRFGGRRIRLYLSVLSLFLYIFTKISVDMFSGAVFIQQALGWNIYASVIALLGITMIYTVTGGLAALMYTDTVQTFVILGGACILMGYAFHEVGGYSGLFDKYLGAATSLTVSEDPAVGNISSFCYRPRPDSYHLLRHPVTGDLPWPALLLGLTIVSGWYWCSDQVIVQRCLAGKSLTHIKAGCILCGYLKLTPMFLMVMPGMISRILYPDEVACVVPEVCRRVCGTEVGCSNIAYPRLVVKLMPNGLRGLMLAVMLAALMSSLASIFNSSSTLFTMDIYTRLRPRAGDRELLLVGRLWVVFIVVVSVAWLPVVQAAQGGQLFDYIQAVSSYLAPPVSAVFVLALFVPRVNEQGAFWGLIGGLLMGLARLIPEFSFGSGSCVQPSACPAFLCGVHYLYFAIVLFFCSGLLTLTVSLCTAPIPRKHLHRLVFSLRHSKEEREDLDADEQQGSSLPVQNGCPESAMEMNEPQAPAPSLFRQCLLWFCGMSRGGVGSPPPLTQEEAAAAARRLEDISEDPSWARVVNLNALLMMAVAVFLWGFYA | 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 glomerular filtrate across the brush border of the early proximal tubules of the kidney (By similarity).
Catalytic Activity: D-glucose(out) + Na(+)(out) = D-glucose(in) + Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72897
Sequence Length: 672
Subcellular Location: Apical cell membrane
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Q00589 | MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGGGLPVFFLEVIIGQYTSEGGITCWEKICPLFSGIGYASIVIVSLLNIYYVIILAWATYYLFQSFQSELPWAHCNHSWNTPQCMEDTMRKNKSLWITLSTKNFTSPVTEFWERNVLSLSSGIDDPGSLKWDLALCLLLVWLVCFFCIWKGVKSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDISRLEDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIADVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQVTSLVDLYPSFLRKGFRREIFIAFMCSISYLLGLSMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIAWIYGSDNLYDGIEDMIGYRPGPWMKYSWAVVTPVLCVGCFIFSLVKYVPLTYNKVYVYPTWAIGLGWSLALSSMMCVPLVMVIRLCQTEGPFLVRLKYLLTPREPNRWAVEREGATPYSSRLAVNGALMKPTHIIVETMM | 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
Catalytic Activity: 4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chloride(in) + 2 Na(+)(in)
Sequence Mass (Da): 69729
Sequence Length: 620
Subcellular Location: Cell membrane
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P31641 | MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLFSGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNKSVWITISSTNFTSPVIEFWERNVLSLSPGIDHPGSLKWDLALCLLLVWLVCFFCIWKGVRSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIADVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQITSLVDLYPSFLRKGYRREIFIAFVCSISYLLGLTMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIAWIYGGDNLYDGIEDMIGYRPGPWMKYSWAVITPVLCVGCFIFSLVKYVPLTYNKTYVYPNWAIGLGWSLALSSMLCVPLVIVIRLCQTEGPFLVRVKYLLTPREPNRWAVEREGATPYNSRTVMNGALVKPTHIIVETMM | 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 membrane protein
Catalytic Activity: 4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chloride(in) + 2 Na(+)(in)
Sequence Mass (Da): 69830
Sequence Length: 620
Subcellular Location: Cell membrane
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Q99884 | MKKLQGAHLRKPVTPDLLMTPSDQGDVDLDVDFAAHRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSDLPWEHCGNWWNTELCLEHRVSKDGNGALPLNLTCTVSPSEEYWSRYVLHIQGSQGIGSPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIYRDTFIVTLGNAITSILAGFAIFSVLGYMSQELGVPVDQVAKAGPGLAFVVYPQAMTMLPLSPFWSFLFFFMLLTLGLDSQFAFLETIVTAVTDEFPYYLRPKKAVFSGLICVAMYLMGLILTTDGGMYWLVLLDDYSASFGLMVVVITTCLAVTRVYGIQRFCRDIHMMLGFKPGLYFRACWLFLSPATLLALMVYSIVKYQPSEYGSYRFPPWAELLGILMGLLSCLMIPAGMLVAVLREEGSLWERLQQASRPAMDWGPSLEENRTGMYVATLAGSQSPKPLMVHMRKYGGITSFENTAIEVDREIAEEEESMM | 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 Topology: Multi-pass membrane protein
Sequence Mass (Da): 70911
Sequence Length: 636
Subcellular Location: Synaptic cell membrane
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Q6PGE7 | MKKLQEAHLRKPITPDLLMTPSDQGDVDLDVDFAADRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSNLPWEHCGNWWNTELCLEHRGPKSGNGVLPLNLSSTVSPSEEYWSRYVLHIQGSQGIGRPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIYRDTFIVTLGNAITSILAGFAIFSVLGYMSQELGVPVDQVAKAGPGLAFVVYPQAMTMLPLSPFWSFLFFFMLLTLGLDSQFAFLETIVTAVTDEFPYYLRPKKAVFSGLICVAMYLMGLILTTDGGMYWLVLLDDYSASFGLMVVVITTCLAVTRVYGIQRFCRDIHMMLGFKPGLYFRACWLFLSPATLLALLVYSIVKYQPSEYGSYRFPAWAELLGILMGLLSCLMIPAGMLVAVLREEGSLWERLQQASRPAMDWGPSLEENRTGMYVATLAGSQSPKPLMVHMRKYGGITSFENTAIEVDREIAEEEEESMM | 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: Multi-pass membrane protein
Sequence Mass (Da): 71066
Sequence Length: 637
Subcellular Location: Synaptic cell membrane
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P28573 | MKKLQEAHLRKPVTPDLLMTPSDQGDVDLDVDFAADRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSNLPWEHCGNWWNTERCLEHRGPKDGNGALPLNLSSTVSPSEEYWSRYVLHIQGSQGIGRPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIYRDTFIVTLGNAITSILAGFAIFSVLGYMSQELGVPVDQVAKAGPGLAFVIYPQAMTMLPLSPFWSFLFFFMLLTLGLDSQFAFLETIVTAVTDEFPYYLRPKKAVFSGLICVAMYLMGLILTTDGGMYWLVLLDDYSASFGLMVVVITTCLAVTRVYGIQRFCRDIHMMLGFKPGLYFRACWLFLSPATLLALLVYSIVKYQPSEYGSYRFPAWAELLGILMGLLSCLMIPAGMLVAVLREEGSLWERLQQASRPAIDWGPSLEENRTGMYVATLAGSQSPKPLMVHMRKYGGITSFENTAIEVDREIAEEEEESMM | 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 Topology: Multi-pass membrane protein
Sequence Mass (Da): 71091
Sequence Length: 637
Subcellular Location: Synaptic cell membrane
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P48029 | MAKKSAENGIYSVSGDEKKGPLIAPGPDGAPAKGDGPVGLGTPGGRLAVPPRETWTRQMDFIMSCVGFAVGLGNVWRFPYLCYKNGGGVFLIPYVLIALVGGIPIFFLEISLGQFMKAGSINVWNICPLFKGLGYASMVIVFYCNTYYIMVLAWGFYYLVKSFTTTLPWATCGHTWNTPDCVEIFRHEDCANASLANLTCDQLADRRSPVIEFWENKVLRLSGGLEVPGALNWEVTLCLLACWVLVYFCVWKGVKSTGKIVYFTATFPYVVLVVLLVRGVLLPGALDGIIYYLKPDWSKLGSPQVWIDAGTQIFFSYAIGLGALTALGSYNRFNNNCYKDAIILALINSGTSFFAGFVVFSILGFMAAEQGVHISKVAESGPGLAFIAYPRAVTLMPVAPLWAALFFFMLLLLGLDSQFVGVEGFITGLLDLLPASYYFRFQREISVALCCALCFVIDLSMVTDGGMYVFQLFDYYSASGTTLLWQAFWECVVVAWVYGADRFMDDIACMIGYRPCPWMKWCWSFFTPLVCMGIFIFNVVYYEPLVYNNTYVYPWWGEAMGWAFALSSMLCVPLHLLGCLLRAKGTMAERWQHLTQPIWGLHHLEYRAQDADVRGLTTLTPVSESSKVVVVESVM | 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) = chloride(in) + creatine(in) + 2 Na(+)(in)
Sequence Mass (Da): 70523
Sequence Length: 635
Subcellular Location: Cell membrane
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Q91502 | MPSRAVRRCPGHLCKEMRAPRRAQPPDVPAGEPGSRVTWSRQMDFIMSCVGFAVGLGNVWRFPYLCYKNGGGVFLIPYLLVAVFGGIPIFFLEISLGQFMKAGGINAWNIAPLFKGLGYASMVIVFFCNTYYILVLTWSSFYLVQSFSSPLPWASCNNTWNTAACYEAGANASTEIYPPTAPAQSSIVQFWERRVLRLSSGLGDVGEIGWELTLCLTATWMLVYFCIWKGVKTSGKVVYVTATFPYIILVILLVRGVTLHGAVQGIVYYLQPDWGKLGEAQVWIDAGTQIFFSYAIGLGTLTALGSYNQLHNDCYKDAFILSLVNSATSFFAGLVVFSILGFMAVEEGVDISVVAESGPGLAFIAYPKAVTLMPFPQVWAVLFFIMLLCLGLGSQFVGVEGFVTAILDLWPSKFSFRYLREVVVAMVICLSFLIDLSMITEGGMYIFQIFDYYSASGTTLLWTAFWECVAVAWVYGGDRYLDDLAWMLGYRPWALVKWCWSVITPLVCMGIFTFHLVNYKPLTYNKTYTYPWWGEAIGWCLALASMLCVPTTVLYSLSRGRGSLKERWRKLTTPVWASHHLAYKMAGAKINQPCEGVVSCEEKVVIFESVL | 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 | MIGGDTRAASAHPGMASAQGPVATPSPEQPFPGTTSVSLARPVLRVWHGAHSSGLLPNLIAQHSPAMAQNGAVPSEATKKDQNLTRGNWGNQIEFVLTSVGYAVGLGNVWRFPYLCYRNGGGAFMFPYFIMLIFCGIPLFFMELSFGQFASQGCLGVWRISPMFKGVGYGMMVVSTYIGIYYNVVICIAFYYFFSSMTHVLPWAYCNNPWNTPDCAGVLDASNLTNGSRPAALSGNLSHLFNYTLQRTSPSEEYWRLYVLKLSDDIGNFGEVRLPLLGCLGVSWVVVFLCLIRGVKSSGKVVYFTATFPYVVLTILFVRGVTLEGAFTGIMYYLTPQWDKILEAKVWGDAASQIFYSLGCAWGGLITMASYNKFHNNCYRDSVIISITNCATSVYAGFVIFSILGFMANHLGVDVSRVADHGPGLAFVAYPEALTLLPISPLWSLLFFFMLILLGLGTQFCLLETLVTAIVDEVGNEWILQKKTYVTLGVAVAGFLLGIPLTSQAGIYWLLLMDNYAASFSLVVISCIMCVSIMYIYGHRNYFQDIQMMLGFPPPLFFQICWRFVSPAIIFFILIFTVIQYRPITYNHYQYPGWAVAIGFLMALSSVICIPLYALFQLCRTDGDTLLQRLKNATKPSRDWGPALLEHRTGRYAPTTTPSPEDGFEVQPLHPDKAQIPIVGSNGSSRFQDSRI | 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 Mass (Da): 76544
Sequence Length: 692
Subcellular Location: Cell membrane
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Q54IJ1 | MNQNSSLSSSGMMGSGGFGFDQFSNNFSIKTKQIESINKMLSLKSESSSSNNNNNNNKAISGWQEVWKVLIFDTHCSNIIAPILTKGALRNQGVTLYLPLHSDRQPIQDVPAIYFVLPTSDNIKRIAEDCKNKLYDNIYLNFASKLSNQLMEELATLTIQSDSVSMISKVYDQFLNFISLENDLFVLNNPRDSYLSFNDTRIKDTQAQENIDMVVDSLFSVLVTLGVVPIIRAPKNSAAEMIALALEKRISTTLQSSGGSNVFSNMNEMGSQLSSFYRPVLILLDRNVDLSVCLHHPWTYQALVHDVLNMSLNQVRIDVTQNGQTSKKSYGLDSSSDSFWSSNTGAAFSSVAGEIKSQINEYYQQMEKLQQITDIKLDDSDDFDNNNKKSNENKTKGLGNLVQEMDEKKRLIDIHTNLATDLTKNIRDRQIDCFFAMEESIITRSLTDKKELHSLITSPIVGETGGRGTLEDKIRLLIIYFLSTKNVPQSEMDQYEDALTKMGADLSTLDFFKKTKAFNESLTAIANVNQSSTQSSNTASGKIGGFMQMMTSVTGYQGVESFTNFFQQGVRALLPKSKDLFVTRIVESIMDLKNTLDADYLYLDPKIQNKSNVPKRTTPFKEAIVFTVGGGNYVEYQNLQDFSKKHNKKIIYGSNELLTSKEFLNQIKNLNKN | 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 | MAAAAAATAAAAASIRERQTVALKRMLNFNVPHIKNSTGEPVWKVLIYDRFGQDIISPLLSVKELRDMGITLHLLLHSDRDPIPDVPAVYFVMPTEENIDRMCQDLRNQLYESYYLNFISAISRSKLEDIANAALAASAVTQVAKVFDQYLNFITLEDDMFVLCNQNKELVSYRAINRPDITDTEMETVMDTIVDSLFCFFVTLGAVPIIRCSRGTAAEMVAVKLDKKLRENLRDARNSLFTGDTLGAGQFSFQRPLLVLVDRNIDLATPLHHTWTYQALVHDVLDFHLNRVNLEESSGVENSPAGARPKRKNKKSYDLTPVDKFWQKHKGSPFPEVAESVQQELESYRAQEDEVKRLKSIMGLEGEDEGAISMLSDNTAKLTSAVSSLPELLEKKRLIDLHTNVATAVLEHIKARKLDVYFEYEEKIMSKTTLDKSLLDIISDPDAGTPEDKMRLFLIYYISTQQAPSEADLEQYKKALTDAGCNLNPLQYIKQWKAFTKMASAPASYGSTTTKPMGLLSRVMNTGSQFVMEGVKNLVLKQQNLPVTRILDNLMEMKSNPETDDYRYFDPKMLRGNDSSVPRNKNPFQEAIVFVVGGGNYIEYQNLVDYIKGKQGKHILYGCSELFNATQFIKQLSQLGQK | 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 Location: Cytoplasm
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Q8BMD8 | MLRWLRAFVLPTAACHDAEPPTRYETLFRALDRNGDGVVDIGELQQGLQSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEPSEIVQSLQMLGLHISEKQAELILQSIDSDGTMTVDWNEWRDYFLFNPVTDIEEIIRFWKHSTGIDIGDSLTIPDEFTEDEKKSGQWWRQLLAGGVAGAVSRTSTAPLDRLKVMMQVHGSKSMNIFGGFRQMVKEGGIRSLWRGNGTNVIKIAPETAVKFWAYEQYKKLLTEEGQKLGTFERFISGSMAGATAQTFIYPMEVLKTRLAVAKTGQYSGIYGCAKKILKHEGFGAFYKGYIPNLLGIIPYAGIDLAVYELLKSYWLDNFAKDSVNPGVMVLLSCGALSSTCGQLASYPLALVRTRMQAQATVEGAPQLSMVGLFQRIVSKEGVSGLYRGITPNFMKVLPAVGISYVVYENMKQTLGVAQK | 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 nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenyl nucleotide-dependent metabolic pathways. In vitro, a low activity is also observed with guanyl and pyrimidine nucleotides. May play a role in protecting cells against oxidative stress-induced cell death, by buffering calcium levels in the mitochondrial matrix through the formation of calcium-phosphate precipitates.
Catalytic Activity: ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52902
Sequence Length: 475
Domain: The regulatory N-terminal domain/NTD formed of two pairs of fused calcium-binding EF-hands, binds calcium in the mitochondrial intermembrane space and regulates the antiporter activity of the transmembrane domain/TMD. In absence of calcium, the apo form of the N-terminal domain is intrinsically disordered and binds to the transmembrane domain, inhibiting the transporter activity. Binding of calcium leads to a major conformational change and abolishes the interaction with the transmembrane domain and the inhibition of the transporter activity.
Subcellular Location: Mitochondrion inner membrane
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O18757 | MLRWLRGFVLPTAACQGAEPPTRYETLFQALDRNGDGVVDIRELQEGLKSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQTLGLTISEQQAELILQSIDADGTMTVDWNEWRDYFLFNPVADIEEIIRFWKHSTGIDIGDSLTIPDEFTEEERKSGQWWRQLLAGGIAGAVSRTSTAPLDRLKVMMQVHGSKSMNIFGGFRQMIKEGGVRSLWRGNGTNVIKIAPETAVKFWVYEQYKKLLTEEGQKIGTFERFISGSMAGATAQTFIYPMEVMKTRLAVGKTGQYSGIYDCAKKILKYEGFGAFYKGYVPNLLGIIPYAGIDLAVYELLKSHWLDNFAKDSVNPGVLVLLGCGALSSTCGQLASYPLALVRTRMQAQAMLEGAPQLNMVGLFRRIISKEGLPGLYRGITPNFMKVLPAVGISYVVYENMKQTLGVTQK | 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 nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenyl nucleotide-dependent metabolic pathways. In vitro, a low activity is also observed with guanyl and pyrimidine nucleotides. May play a role in protecting cells against oxidative stress-induced cell death, by buffering calcium levels in the mitochondrial matrix through the formation of calcium-phosphate precipitates.
Catalytic Activity: ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53006
Sequence Length: 475
Domain: The regulatory N-terminal domain/NTD formed of two pairs of fused calcium-binding EF-hands, binds calcium in the mitochondrial intermembrane space and regulates the antiporter activity of the transmembrane domain/TMD. In absence of calcium, the apo form of the N-terminal domain is intrinsically disordered and binds to the transmembrane domain, inhibiting the transporter activity. Binding of calcium leads to a major conformational change and abolishes the interaction with the transmembrane domain and the inhibition of the transporter activity.
Subcellular Location: Mitochondrion inner membrane
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A2ASZ8 | MLCLCLYVPIAGAAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWKQKIVQAGDKDLDGQLDFEEFVHYLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRDYHLLHPVENIPEIILYWKHSTIFDVGENLTVPDEFTVEERQTGMWWRHLVAGGGAGAVSRTCTAPLDRLKVLMQVHASRSNNMCIVGGFTQMIREGGAKSLWRGNGINVLKIAPESAIKFMAYEQMKRLVGSDQETLRIHERLVAGSLAGAIAQSSIYPMEVLKTRMALRKTGQYSGMLDCARRILAKEGVAAFYKGYIPNMLGIIPYAGIDLAVYETLKNTWLQRYAVNSADPGVFVLLACGTISSTCGQLASYPLALVRTRMQAQASIEGAPEVTMSSLFKQILRTEGAFGLYRGLAPNFMKVIPAVSISYVVYENLKITLGVQSR | 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 adenyl nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenyl nucleotide-dependent metabolic pathways.
Catalytic Activity: ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52621
Sequence Length: 469
Domain: The regulatory N-terminal domain/NTD, binds calcium in the mitochondrial intermembrane space and regulates the antiporter activity of the transmembrane domain/TMD. In absence of calcium, the apo form of the N-terminal domain is intrinsically disordered and binds to the transmembrane domain, inhibiting the transporter activity. Binding of calcium leads to a major conformational change and abolishes the interaction with the transmembrane domain and the inhibition of the transporter activity.
Subcellular Location: Mitochondrion inner membrane
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Q9BV35 | MRGSPGDAERRQRWGRLFEELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQGISSEGDADPDGGLDLEEFSRYLQEREQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEWRDHFLLHSLENVEDVLYFWKHSTVLDIGECLTVPDEFSKQEKLTGMWWKQLVAGAVAGAVSRTGTAPLDRLKVFMQVHASKTNRLNILGGLRSMVLEGGIRSLWRGNGINVLKIAPESAIKFMAYEQIKRAILGQQETLHVQERFVAGSLAGATAQTIIYPMEVLKTRLTLRRTGQYKGLLDCARRILEREGPRAFYRGYLPNVLGIIPYAGIDLAVYETLKNWWLQQYSHDSADPGILVLLACGTISSTCGQIASYPLALVRTRMQAQASIEGGPQLSMLGLLRHILSQEGMRGLYRGIAPNFMKVIPAVSISYVVYENMKQALGVTSR | 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 nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenine nucleotide-dependent metabolic pathways . Also acts as a regulator of mitochondrial calcium uptake and can probably transport trace amounts of other divalent metal cations in complex with ATP . In vitro, a low activity is also observed with guanyl and pyrimidine nucleotides .
Catalytic Activity: ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52378
Sequence Length: 468
Domain: The regulatory N-terminal domain/NTD, binds calcium in the mitochondrial intermembrane space and regulates the antiporter activity of the transmembrane domain/TMD. In absence of calcium, the apo form of the N-terminal domain is intrinsically disordered and binds to the transmembrane domain, inhibiting the transporter activity. Binding of calcium leads to a major conformational change and abolishes the interaction with the transmembrane domain and the inhibition of the transporter activity.
Subcellular Location: Mitochondrion inner membrane
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P54950 | MTSKKKQIKLGVFLAGTGHHVASWRHPDAPSDASMNLDYFKELAKTAERGKLDMLFLADSLSIDSKSHPNVLTRFEPFTLLSALAQVTSKIGLTATASTTYSEPFHIARQFASLDHLSNGRAGWNVVTSSIESTALNFSGEKHLEHHLRYQRAEEFVEIVKGLWDSWEEDAFIRNKETGEFFDKEKMHELNHKGEYFSVRGPLNVSRTPQGQPVIIQAGSSGDGKALAAKTAEVIFTAQNHLESAQEFYQSIKEQAAEFGRDPEKIAIMPGIFPIIADTEEAAQAKYKELQDLIIPSVGLQILQNYLGGIDLSAYPLDGPLPKLDAEASNAVKSRFKLVQEMAERDNMTIRELYKYVAGSRGHHIFVGTPEQLADKMQEWVDTKACDGFNIMPPLLPEGIEVFVDQVVPILQERGVFRKEYEGTTLREHFGLEKPVNRYAK | 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 almost no activity on S-succinylglutathione and 2SC .
Catalytic Activity: H(+) + N-acetyl-S-(2-succino)-L-cysteine + NADH + O2 = H2O + N-acetyl-L-cysteine + NAD(+) + oxaloacetate
Sequence Mass (Da): 49339
Sequence Length: 441
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis.
EC: 1.14.13.-
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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
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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
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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
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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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