ID YLAT2_HUMAN Reviewed; 515 AA. AC Q92536; Q68DS4; Q7L1N3; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 3. DT 27-MAR-2024, entry version 176. DE RecName: Full=Y+L amino acid transporter 2 {ECO:0000305}; DE AltName: Full=Cationic amino acid transporter, y+ system; DE AltName: Full=Solute carrier family 7 member 6; DE AltName: Full=y(+)L-type amino acid transporter 2; DE Short=Y+LAT2; DE Short=y+LAT-2; GN Name=SLC7A6 {ECO:0000312|HGNC:HGNC:11064}; GN Synonyms=KIAA0245 {ECO:0000312|EMBL:BAA13376.2}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000312|EMBL:BAA13376.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAA13376.2}; RX PubMed=9039502; DOI=10.1093/dnares/3.5.321; RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., RA Tanaka A., Kotani H., Miyajima N., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. VI. The RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of RT cDNA clones from cell line KG-1 and brain."; RL DNA Res. 3:321-329(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Salivary gland; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] {ECO:0000312|EMBL:CAH18146.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000312|EMBL:AAH28216.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Leukocyte {ECO:0000312|EMBL:AAH28216.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION. RC TISSUE=Myoblast; RX PubMed=9829974; DOI=10.1074/jbc.273.49.32437; RA Torrents D., Estevez R., Pineda M., Fernandez E., Lloberas J., Shi Y.-B., RA Zorzano A., Palacin M.; RT "Identification and characterization of a membrane protein (y+L amino acid RT transporter-1) that associates with 4F2hc to encode the amino acid RT transport activity y+L. A candidate gene for lysinuric protein RT intolerance."; RL J. Biol. Chem. 273:32437-32445(1998). RN [6] {ECO:0000305} RP TISSUE SPECIFICITY. RX PubMed=11078698; DOI=10.1152/ajpcell.2000.279.6.c1829; RA Dall'Asta V., Bussolati O., Sala R., Rotoli B.M., Sebastio G., RA Sperandeo M.P., Andria G., Gazzola G.C.; RT "Arginine transport through system y(+)L in cultured human fibroblasts: RT normal phenotype of cells from LPI subjects."; RL Am. J. Physiol. 279:C1829-C1837(2000). RN [7] {ECO:0000305} RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND TISSUE SPECIFICITY. RX PubMed=10903140; DOI=10.1042/bj3490787; RA Broeer A., Wagner C.A., Lang F., Broeer S.; RT "The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine RT efflux in exchange with glutamine."; RL Biochem. J. 349:787-795(2000). RN [8] {ECO:0000305} RP FUNCTION, AND SUBUNIT. RX PubMed=11311135; DOI=10.1042/bj3550725; RA Broeer A., Friedrich B., Wagner C.A., Fillon S., Ganapathy V., Lang F., RA Broeer S.; RT "Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires RT different domains."; RL Biochem. J. 355:725-731(2001). RN [9] {ECO:0000305} RP TISSUE SPECIFICITY. RX PubMed=11742806; DOI=10.1152/ajpcell.2002.282.1.c134; RA Sala R., Rotoli B.M., Colla E., Visigalli R., Parolari A., Bussolati O., RA Gazzola G.C., Dall'Asta V.; RT "Two-way arginine transport in human endothelial cells: TNF-alpha RT stimulation is restricted to system y(+)."; RL Am. J. Physiol. 282:C134-C143(2002). RN [10] {ECO:0000305} RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=14603368; DOI=10.1113/eph8802647; RA Arancibia-Garavilla Y., Toledo F., Casanello P., Sobrevia L.; RT "Nitric oxide synthesis requires activity of the cationic and neutral amino RT acid transport system y+L in human umbilical vein endothelium."; RL Exp. Physiol. 88:699-710(2003). RN [11] {ECO:0000305} RP TISSUE SPECIFICITY. RX PubMed=15280038; DOI=10.1016/j.febslet.2004.06.086; RA Rotoli B.M., Bussolati O., Sala R., Barilli A., Talarico E., Gazzola G.C., RA Dall'Asta V.; RT "INFgamma stimulates arginine transport through system y+L in human RT monocytes."; RL FEBS Lett. 571:177-181(2004). RN [12] {ECO:0000305} RP FUNCTION. RX PubMed=15756301; DOI=10.1038/sj.ejhg.5201376; RA Sperandeo M.P., Paladino S., Maiuri L., Maroupulos G.D., Zurzolo C., RA Taglialatela M., Andria G., Sebastio G.; RT "A y(+)LAT-1 mutant protein interferes with y(+)LAT-2 activity: RT implications for the molecular pathogenesis of lysinuric protein RT intolerance."; RL Eur. J. Hum. Genet. 13:628-634(2005). RN [13] {ECO:0000305} RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP SUBCELLULAR LOCATION, AND INHIBITION. RX PubMed=16785209; DOI=10.1080/09687860600652968; RA Chubb S., Kingsland A.L., Broeer A., Broeer S.; RT "Mutation of the 4F2 heavy-chain carboxy terminus causes y+ LAT2 light- RT chain dysfunction."; RL Mol. Membr. Biol. 23:255-267(2006). RN [14] {ECO:0000305} RP FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY REGULATION. RX PubMed=17329401; DOI=10.1152/ajpcell.00323.2006; RA Rotmann A., Simon A., Martine U., Habermeier A., Closs E.I.; RT "Activation of classical protein kinase C decreases transport via systems RT y+ and y+L."; RL Am. J. Physiol. 292:C2259-C2268(2007). RN [15] {ECO:0000305} RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=17197568; DOI=10.1167/iovs.06-0398; RA Kaneko S., Ando A., Okuda-Ashitaka E., Maeda M., Furuta K., Suzuki M., RA Matsumura M., Ito S.; RT "Ornithine transport via cationic amino acid transporter-1 is involved in RT ornithine cytotoxicity in retinal pigment epithelial cells."; RL Invest. Ophthalmol. Vis. Sci. 48:464-471(2007). RN [16] RP FUNCTION. RX PubMed=19562367; DOI=10.1007/s00424-009-0692-9; RA Rotoli B.M., Closs E.I., Barilli A., Visigalli R., Simon A., Habermeier A., RA Bianchi N., Gambari R., Gazzola G.C., Bussolati O., Dall'Asta V.; RT "Arginine transport in human erythroid cells: discrimination of CAT1 and RT 4F2hc/y+LAT2 roles."; RL Pflugers Arch. 458:1163-1173(2009). RN [17] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY. RX PubMed=31705628; DOI=10.1111/jcmm.14801; RA Rotoli B.M., Barilli A., Visigalli R., Ferrari F., Dall'Asta V.; RT "y+LAT1 and y+LAT2 contribution to arginine uptake in different human cell RT models: Implications in the pathophysiology of Lysinuric Protein RT Intolerance."; RL J. Cell. Mol. Med. 24:921-929(2020). CC -!- FUNCTION: Heterodimer with SLC3A2, that functions as an antiporter CC which operates as an efflux route by exporting cationic amino acids CC such as L-arginine from inside the cells in exchange with neutral amino CC acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and CC may participate in nitric oxide synthesis (PubMed:9829974, CC PubMed:10903140, PubMed:16785209, PubMed:31705628, PubMed:15756301, CC PubMed:11311135, PubMed:17329401, PubMed:14603368, PubMed:19562367). CC Also exchanges L-arginine with L-lysine in a sodium-independent manner CC (PubMed:10903140). The transport mechanism is electroneutral and CC operates with a stoichiometry of 1:1 (PubMed:10903140). Contributes to CC ammonia-induced increase of L-arginine uptake in cerebral cortical CC astrocytes leading to ammonia-dependent increase of nitric oxide (NO) CC production via inducible nitric oxide synthase (iNOS) induction, and CC protein nitration (By similarity). May mediate transport of ornithine CC in retinal pigment epithelial (RPE) cells (PubMed:17197568). May also CC transport glycine betaine in a sodium dependent manner from the cumulus CC granulosa into the enclosed oocyte (By similarity). CC {ECO:0000250|UniProtKB:D3ZMM8, ECO:0000250|UniProtKB:Q8BGK6, CC ECO:0000269|PubMed:10903140, ECO:0000269|PubMed:11311135, CC ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15756301, CC ECO:0000269|PubMed:16785209, ECO:0000269|PubMed:17197568, CC ECO:0000269|PubMed:17329401, ECO:0000269|PubMed:19562367, CC ECO:0000269|PubMed:31705628, ECO:0000269|PubMed:9829974}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine(in) + L-lysine(out) = L-arginine(out) + L- CC lysine(in); Xref=Rhea:RHEA:70827, ChEBI:CHEBI:32551, CC ChEBI:CHEBI:32682; Evidence={ECO:0000269|PubMed:10903140}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine(in) + L-leucine(out) + Na(+)(out) = L-arginine(out) CC + L-leucine(in) + Na(+)(in); Xref=Rhea:RHEA:70831, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:32682, ChEBI:CHEBI:57427; CC Evidence={ECO:0000269|PubMed:10903140, ECO:0000269|PubMed:16785209}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine(in) + L-glutamine(out) + Na(+)(out) = L- CC arginine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:70835, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:58359; CC Evidence={ECO:0000269|PubMed:10903140}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine(in) + L-histidine(out) + Na(+)(out) = L- CC arginine(out) + L-histidine(in) + Na(+)(in); Xref=Rhea:RHEA:70839, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57595; CC Evidence={ECO:0000269|PubMed:10903140}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine(in) + L-cysteine(out) + Na(+)(out) = L- CC arginine(out) + L-cysteine(in) + Na(+)(in); Xref=Rhea:RHEA:70847, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:35235; CC Evidence={ECO:0000269|PubMed:10903140}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine(in) + L-methionine(out) + Na(+)(out) = L- CC arginine(out) + L-methionine(in) + Na(+)(in); Xref=Rhea:RHEA:70843, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57844; CC Evidence={ECO:0000269|PubMed:10903140}; CC -!- ACTIVITY REGULATION: Arginine transport is strongly inhibited by CC lysine, glutamate, leucine, glutamine, methionine and histidine, in the CC presence of Na(+) (PubMed:10903140). Also inhibited by protein kinase C CC (PKC) and treatment with phorbol-12-myristate-13-acetate (PMA) CC (PubMed:17329401). {ECO:0000269|PubMed:10903140, CC ECO:0000269|PubMed:17329401}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=295 uM for L-glutamine (in the presence of NaCl) CC {ECO:0000269|PubMed:10903140}; CC KM=236 uM for L-leucine (in the presence of NaCl) CC {ECO:0000269|PubMed:10903140}; CC KM=120 uM for L-arginine (in the presence of NaCl) CC {ECO:0000269|PubMed:10903140}; CC KM=138 uM for L-arginine (in the absence of NaCl) CC {ECO:0000269|PubMed:10903140}; CC KM=185 uM for L-arginine {ECO:0000269|PubMed:16785209}; CC KM=201 uM for L-leucine {ECO:0000269|PubMed:16785209}; CC KM=5100 uM for sodium ion (in the presence of 100 mM L-leucine and CC with different sodium ions concentrations.) CC {ECO:0000269|PubMed:16785209}; CC KM=0.145 uM for L-arginine (in fibroblasts from healthy donors) CC {ECO:0000269|PubMed:31705628}; CC Vmax=1.479 nmol/min/mg enzyme toward L-arginine (in fibroblasts from CC healthy donors) {ECO:0000269|PubMed:31705628}; CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport CC protein SLC3A2/4F2hc. {ECO:0000269|PubMed:11311135, CC ECO:0000269|PubMed:16785209}. CC -!- INTERACTION: CC Q92536; Q9UPQ8: DOLK; NbExp=3; IntAct=EBI-2880595, EBI-8645574; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16785209}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Expressed in normal fibroblasts and those from LPI CC patients (PubMed:11078698). Also expressed in HUVECs, monocytes, RPE CC cells, and various carcinoma cell lines (PubMed:11742806, CC PubMed:14603368, PubMed:15280038, PubMed:17197568, PubMed:17329401). CC Expressed in brain, heart, testis, kidney, small intestine and parotis CC (PubMed:10903140). Highly expressed in T lymphocytes (PubMed:31705628). CC {ECO:0000269|PubMed:10903140, ECO:0000269|PubMed:11078698, CC ECO:0000269|PubMed:11742806, ECO:0000269|PubMed:14603368, CC ECO:0000269|PubMed:15280038, ECO:0000269|PubMed:17197568, CC ECO:0000269|PubMed:17329401, ECO:0000269|PubMed:31705628}. CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) CC superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family. CC {ECO:0000255}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA13376.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D87432; BAA13376.2; ALT_INIT; mRNA. DR EMBL; CR749291; CAH18146.1; -; mRNA. DR EMBL; CH471092; EAW83219.1; -; Genomic_DNA. DR EMBL; BC028216; AAH28216.1; -; mRNA. DR CCDS; CCDS32470.1; -. DR RefSeq; NP_001070253.1; NM_001076785.2. DR RefSeq; NP_003974.3; NM_003983.5. DR RefSeq; XP_011521735.1; XM_011523433.1. DR RefSeq; XP_011521736.1; XM_011523434.1. DR RefSeq; XP_011521740.1; XM_011523438.1. DR AlphaFoldDB; Q92536; -. DR EMDB; EMD-30341; -. DR SMR; Q92536; -. DR BioGRID; 114519; 76. DR ComplexPortal; CPX-8188; Y+LAT2-4F2 heteromeric amino acid transporter complex. DR IntAct; Q92536; 5. DR STRING; 9606.ENSP00000455064; -. DR DrugBank; DB00130; L-Glutamine. DR TCDB; 2.A.3.8.23; the amino acid-polyamine-organocation (apc) family. DR iPTMnet; Q92536; -. DR PhosphoSitePlus; Q92536; -. DR SwissPalm; Q92536; -. DR BioMuta; SLC7A6; -. DR DMDM; 190462822; -. DR EPD; Q92536; -. DR jPOST; Q92536; -. DR MassIVE; Q92536; -. DR MaxQB; Q92536; -. DR PaxDb; 9606-ENSP00000455064; -. DR PeptideAtlas; Q92536; -. DR ProteomicsDB; 75294; -. DR Pumba; Q92536; -. DR Antibodypedia; 55124; 122 antibodies from 18 providers. DR DNASU; 9057; -. DR Ensembl; ENST00000219343.11; ENSP00000219343.6; ENSG00000103064.15. DR Ensembl; ENST00000566454.5; ENSP00000455064.1; ENSG00000103064.15. DR GeneID; 9057; -. DR KEGG; hsa:9057; -. DR MANE-Select; ENST00000219343.11; ENSP00000219343.6; NM_003983.6; NP_003974.3. DR UCSC; uc002evt.3; human. DR AGR; HGNC:11064; -. DR CTD; 9057; -. DR DisGeNET; 9057; -. DR GeneCards; SLC7A6; -. DR HGNC; HGNC:11064; SLC7A6. DR HPA; ENSG00000103064; Tissue enhanced (skeletal). DR MIM; 605641; gene. DR neXtProt; NX_Q92536; -. DR OpenTargets; ENSG00000103064; -. DR PharmGKB; PA35924; -. DR VEuPathDB; HostDB:ENSG00000103064; -. DR eggNOG; KOG1287; Eukaryota. DR GeneTree; ENSGT00940000158295; -. DR HOGENOM; CLU_007946_3_0_1; -. DR InParanoid; Q92536; -. DR OMA; QIVFRRR; -. DR OrthoDB; 1103451at2759; -. DR PhylomeDB; Q92536; -. DR TreeFam; TF313355; -. DR BioCyc; MetaCyc:ENSG00000103064-MONOMER; -. DR PathwayCommons; Q92536; -. DR Reactome; R-HSA-210991; Basigin interactions. DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane. DR SABIO-RK; Q92536; -. DR SignaLink; Q92536; -. DR BioGRID-ORCS; 9057; 24 hits in 1156 CRISPR screens. DR ChiTaRS; SLC7A6; human. DR GeneWiki; SLC7A6; -. DR GenomeRNAi; 9057; -. DR Pharos; Q92536; Tbio. DR PRO; PR:Q92536; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q92536; Protein. DR Bgee; ENSG00000103064; Expressed in apex of heart and 171 other cell types or tissues. DR ExpressionAtlas; Q92536; baseline and differential. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:ProtInc. DR GO; GO:0034618; F:arginine binding; IDA:UniProtKB. DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IMP:ARUK-UCL. DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0106439; F:L-lysine:L-arginine antiporter activity; IDA:UniProtKB. DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central. DR GO; GO:0031460; P:glycine betaine transport; ISS:UniProtKB. DR GO; GO:1903826; P:L-arginine transmembrane transport; IDA:UniProtKB. DR GO; GO:0015820; P:leucine transport; IDA:UniProtKB. DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB. DR GO; GO:0006809; P:nitric oxide biosynthetic process; ISS:UniProtKB. DR GO; GO:0015822; P:ornithine transport; IMP:ARUK-UCL. DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1. DR InterPro; IPR002293; AA/rel_permease1. DR PANTHER; PTHR11785; AMINO ACID TRANSPORTER; 1. DR PANTHER; PTHR11785:SF398; Y+L AMINO ACID TRANSPORTER 2; 1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. DR Genevisible; Q92536; HS. PE 1: Evidence at protein level; KW Amino-acid transport; Antiport; Cell membrane; Disulfide bond; Membrane; KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..515 FT /note="Y+L amino acid transporter 2" FT /id="PRO_0000341477" FT TOPO_DOM 1..44 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 45..65 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 66..78 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 79..99 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 100..114 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 115..135 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 136..167 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 168..188 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 189..194 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 195..215 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 216..235 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 236..256 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 257..266 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 267..287 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 288..311 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 312..332 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 333..363 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 364..384 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 385 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 386..406 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 407..425 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 426..446 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 447..451 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 452..472 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 473..515 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 13..36 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BGK6" FT CONFLICT 8 FT /note="R -> G (in Ref. 2; CAH18146)" FT /evidence="ECO:0000305" FT CONFLICT 388 FT /note="Q -> R (in Ref. 2; CAH18146)" FT /evidence="ECO:0000305" SQ SEQUENCE 515 AA; 56828 MW; 4E92F6E1972351A9 CRC64; MEAREPGRPT PTYHLVPNTS QSQVEEDVSS PPQRSSETMQ LKKEISLLNG VSLVVGNMIG SGIFVSPKGV LVHTASYGMS LIVWAIGGLF SVVGALCYAE LGTTITKSGA SYAYILEAFG GFIAFIRLWV SLLVVEPTGQ AIIAITFANY IIQPSFPSCD PPYLACRLLA AACICLLTFV NCAYVKWGTR VQDTFTYAKV VALIAIIVMG LVKLCQGHSE HFQDAFEGSS WDMGNLSLAL YSALFSYSGW DTLNFVTEEI KNPERNLPLA IGISMPIVTL IYILTNVAYY TVLNISDVLS SDAVAVTFAD QTFGMFSWTI PIAVALSCFG GLNASIFASS RLFFVGSREG HLPDLLSMIH IERFTPIPAL LFNCTMALIY LIVEDVFQLI NYFSFSYWFF VGLSVVGQLY LRWKEPKRPR PLKLSVFFPI VFCICSVFLV IVPLFTDTIN SLIGIGIALS GVPFYFMGVY LPESRRPLFI RNVLAAITRG TQQLCFCVLT ELDVAEEKKD ERKTD //