S23A2_HUMAN
ID S23A2_HUMAN Reviewed; 650 AA.
AC Q9UGH3; B4DJZ1; Q8WWR4; Q92512; Q96D54; Q9UNU1; Q9UP85;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Solute carrier family 23 member 2;
DE AltName: Full=Na(+)/L-ascorbic acid transporter 2;
DE AltName: Full=Nucleobase transporter-like 1 protein {ECO:0000303|PubMed:9804989};
DE AltName: Full=Sodium-dependent vitamin C transporter 2 {ECO:0000303|PubMed:10471399};
DE Short=hSVCT2 {ECO:0000303|PubMed:10471399};
DE AltName: Full=Yolk sac permease-like molecule 2 {ECO:0000303|PubMed:9804989};
GN Name=SLC23A2;
GN Synonyms=KIAA0238 {ECO:0000303|PubMed:9039502}, NBTL1, SLC23A1,
GN SVCT2 {ECO:0000303|PubMed:10471399}, YSPL2 {ECO:0000303|PubMed:9804989};
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=9804989; DOI=10.1016/s0167-4781(98)00151-1;
RA Faaland C.A., Race J.E., Ricken G., Warner F.J., Williams W.J.,
RA Holtzman E.J.;
RT "Molecular characterization of two novel transporters from human and mouse
RT kidney and from LLC-PK1 cells reveals a novel conserved family that is
RT homologous to bacterial and Aspergillus nucleobase transporters.";
RL Biochim. Biophys. Acta 1442:353-360(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Choriocarcinoma;
RX PubMed=10471399; DOI=10.1006/bbrc.1999.1272;
RA Rajan D.P., Huang W., Dutta B., Devoe L.D., Leibach F.H., Ganapathy V.,
RA Prasad P.D.;
RT "Human placental sodium-dependent vitamin C transporter (SVCT2): molecular
RT cloning and transport function.";
RL Biochem. Biophys. Res. Commun. 262:762-768(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND PHOSPHORYLATION.
RC TISSUE=Kidney;
RX PubMed=10556521; DOI=10.1016/s0014-5793(99)01393-9;
RA Daruwala R.C., Song J., Koh W.S., Rumsey S.C., Levine M.;
RT "Cloning and functional characterization of the human sodium-dependent
RT vitamin C transporters hSVCT1 and hSVCT2.";
RL FEBS Lett. 460:480-484(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary carcinoma;
RX PubMed=10395795; DOI=10.1006/geno.1999.5847;
RA Hogue D.L., Ling V.;
RT "A human nucleobase transporter-like cDNA (SLC23A1): member of a
RT transporter family conserved from bacteria to mammals.";
RL Genomics 59:18-23(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=11396616; DOI=10.1080/09687680110033774;
RA Liang W.J., Johnson D., Jarvis S.M.;
RT "Vitamin C transport systems of mammalian cells.";
RL Mol. Membr. Biol. 18:87-95(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
RA Schwarzer C., Borcanski G., Widdicombe J., Fischer H., Illek B.;
RT "SVCT2 in ciliated human tracheal epithelial cultures.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-424 (ISOFORM 1).
RC TISSUE=Skin;
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 [12]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=19379732; DOI=10.1016/j.yexcr.2009.04.007;
RA Velho A.M., Jarvis S.M.;
RT "Topological studies of hSVCT1, the human sodium-dependent vitamin C
RT transporter and the influence of N-glycosylation on its intracellular
RT targeting.";
RL Exp. Cell Res. 315:2312-2321(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Sodium/ascorbate cotransporter (PubMed:10471399,
CC PubMed:10556521). Mediates electrogenic uptake of vitamin C, with a
CC stoichiometry of 2 Na(+) for each ascorbate (PubMed:10471399).
CC {ECO:0000269|PubMed:10471399, ECO:0000269|PubMed:10556521}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(out) + 2 Na(+)(out) = L-ascorbate(in) + 2
CC Na(+)(in); Xref=Rhea:RHEA:69883, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:10471399};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19379732};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19379732}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGH3-2; Sequence=VSP_056485;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10471399}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10556521}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13244.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF058319; AAC78806.1; -; mRNA.
DR EMBL; AJ269478; CAB58120.1; -; mRNA.
DR EMBL; AF164142; AAF80493.1; -; mRNA.
DR EMBL; AF092511; AAD11783.1; -; mRNA.
DR EMBL; AJ292318; CAC83100.1; -; mRNA.
DR EMBL; AY380556; AAQ79775.1; -; mRNA.
DR EMBL; D87075; BAA13244.2; ALT_INIT; mRNA.
DR EMBL; AK296304; BAG59003.1; -; mRNA.
DR EMBL; AL109841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL389886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013112; AAH13112.1; -; mRNA.
DR CCDS; CCDS13085.1; -. [Q9UGH3-1]
DR PIR; JC7095; JC7095.
DR RefSeq; NP_005107.4; NM_005116.5. [Q9UGH3-1]
DR RefSeq; NP_976072.1; NM_203327.1. [Q9UGH3-1]
DR RefSeq; XP_011527716.1; XM_011529414.2.
DR RefSeq; XP_011527717.1; XM_011529415.2.
DR RefSeq; XP_011527718.1; XM_011529416.2.
DR RefSeq; XP_011527719.1; XM_011529417.2.
DR RefSeq; XP_016883660.1; XM_017028171.1.
DR RefSeq; XP_016883661.1; XM_017028172.1.
DR RefSeq; XP_016883662.1; XM_017028173.1.
DR RefSeq; XP_016883663.1; XM_017028174.1.
DR RefSeq; XP_016883665.1; XM_017028176.1.
DR RefSeq; XP_016883666.1; XM_017028177.1.
DR AlphaFoldDB; Q9UGH3; -.
DR PCDDB; Q9UGH3; -.
DR SMR; Q9UGH3; -.
DR BioGRID; 115287; 24.
DR IntAct; Q9UGH3; 11.
DR MINT; Q9UGH3; -.
DR STRING; 9606.ENSP00000368637; -.
DR ChEMBL; CHEMBL3271; -.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugCentral; Q9UGH3; -.
DR TCDB; 2.A.40.6.2; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR GlyGen; Q9UGH3; 2 sites.
DR iPTMnet; Q9UGH3; -.
DR PhosphoSitePlus; Q9UGH3; -.
DR BioMuta; SLC23A2; -.
DR DMDM; 24212469; -.
DR EPD; Q9UGH3; -.
DR jPOST; Q9UGH3; -.
DR MassIVE; Q9UGH3; -.
DR MaxQB; Q9UGH3; -.
DR PaxDb; Q9UGH3; -.
DR PeptideAtlas; Q9UGH3; -.
DR PRIDE; Q9UGH3; -.
DR ProteomicsDB; 4421; -.
DR ProteomicsDB; 84214; -. [Q9UGH3-1]
DR Antibodypedia; 42663; 125 antibodies from 23 providers.
DR DNASU; 9962; -.
DR Ensembl; ENST00000338244.6; ENSP00000344322.1; ENSG00000089057.15. [Q9UGH3-1]
DR Ensembl; ENST00000379333.5; ENSP00000368637.1; ENSG00000089057.15. [Q9UGH3-1]
DR GeneID; 9962; -.
DR KEGG; hsa:9962; -.
DR MANE-Select; ENST00000338244.6; ENSP00000344322.1; NM_005116.6; NP_005107.4.
DR UCSC; uc002wlg.1; human. [Q9UGH3-1]
DR CTD; 9962; -.
DR DisGeNET; 9962; -.
DR GeneCards; SLC23A2; -.
DR HGNC; HGNC:10973; SLC23A2.
DR HPA; ENSG00000089057; Tissue enhanced (adrenal gland, retina).
DR MIM; 603791; gene.
DR neXtProt; NX_Q9UGH3; -.
DR OpenTargets; ENSG00000089057; -.
DR PharmGKB; PA35849; -.
DR VEuPathDB; HostDB:ENSG00000089057; -.
DR eggNOG; KOG1292; Eukaryota.
DR GeneTree; ENSGT00950000182953; -.
DR HOGENOM; CLU_017959_5_4_1; -.
DR InParanoid; Q9UGH3; -.
DR OMA; NNVSAYC; -.
DR PhylomeDB; Q9UGH3; -.
DR TreeFam; TF313272; -.
DR PathwayCommons; Q9UGH3; -.
DR Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
DR SignaLink; Q9UGH3; -.
DR BioGRID-ORCS; 9962; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; SLC23A2; human.
DR GeneWiki; SLC23A2; -.
DR GenomeRNAi; 9962; -.
DR Pharos; Q9UGH3; Tbio.
DR PRO; PR:Q9UGH3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UGH3; protein.
DR Bgee; ENSG00000089057; Expressed in adrenal tissue and 180 other tissues.
DR ExpressionAtlas; Q9UGH3; baseline and differential.
DR Genevisible; Q9UGH3; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008520; F:L-ascorbate:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0015229; F:L-ascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IBA:GO_Central.
DR GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:UniProtKB.
DR GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR029956; SlC23A2.
DR InterPro; IPR006042; Xan_ur_permease.
DR PANTHER; PTHR11119:SF33; PTHR11119:SF33; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sodium; Sodium transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..650
FT /note="Solute carrier family 23 member 2"
FT /id="PRO_0000165978"
FT TOPO_DOM 9..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 289..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..650
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPR4"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTW8"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPR4"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPR4"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 649
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPR4"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 162..275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056485"
FT CONFLICT 30
FT /note="P -> R (in Ref. 4; AAD11783)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="I -> T (in Ref. 4; AAD11783)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="A -> T (in Ref. 1; AAC78806)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="L -> S (in Ref. 4; AAD11783)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="I -> V (in Ref. 4; AAD11783)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="F -> L (in Ref. 5; CAC83100)"
FT /evidence="ECO:0000305"
FT CONFLICT 418..424
FT /note="GIFVEGL -> YVPEKTS (in Ref. 11)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 70337 MW; 28C9E190D9528D39 CRC64;
MMGIGKNTTS KSMEAGSSTE GKYEDEAKHP AFFTLPVVIN GGATSSGEQD NEDTELMAIY
TTENGIAEKS SLAETLDSTG SLDPQRSDMI YTIEDVPPWY LCIFLGLQHY LTCFSGTIAV
PFLLADAMCV GYDQWATSQL IGTIFFCVGI TTLLQTTFGC RLPLFQASAF AFLAPARAIL
SLDKWKCNTT DVSVANGTAE LLHTEHIWYP RIREIQGAII MSSLIEVVIG LLGLPGALLK
YIGPLTITPT VALIGLSGFQ AAGERAGKHW GIAMLTIFLV LLFSQYARNV KFPLPIYKSK
KGWTAYKLQL FKMFPIILAI LVSWLLCFIF TVTDVFPPDS TKYGFYARTD ARQGVLLVAP
WFKVPYPFQW GLPTVSAAGV IGMLSAVVAS IIESIGDYYA CARLSCAPPP PIHAINRGIF
VEGLSCVLDG IFGTGNGSTS SSPNIGVLGI TKVGSRRVIQ CGAALMLALG MIGKFSALFA
SLPDPVLGAL FCTLFGMITA VGLSNLQFID LNSSRNLFVL GFSIFFGLVL PSYLRQNPLV
TGITGIDQVL NVLLTTAMFV GGCVAFILDN TIPGTPEERG IRKWKKGVGK GNKSLDGMES
YNLPFGMNII KKYRCFSYLP ISPTFVGYTW KGLRKSDNSR SSDEDSQATG
