ID   CTR2_HUMAN              Reviewed;         658 AA.
AC   P52569; B7ZL54; O15291; O15292; Q14CQ6; Q6NSZ7; Q86TC6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Cationic amino acid transporter 2 {ECO:0000305};
DE            Short=CAT-2;
DE            Short=CAT2;
DE   AltName: Full=Low affinity cationic amino acid transporter 2;
DE   AltName: Full=Solute carrier family 7 member 2;
GN   Name=SLC7A2 {ECO:0000312|HGNC:HGNC:11060};
GN   Synonyms=ATRC2, CAT2 {ECO:0000303|PubMed:8954799};
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), AND TISSUE SPECIFICITY.
RC   TISSUE=Intestine;
RX   PubMed=8954799; DOI=10.1006/geno.1996.0613;
RA   Hoshide R., Ikeda Y., Karashima S., Matsuura T., Komaki S., Kishino T.,
RA   Niikawa N., Endo F., Matsuda I.;
RT   "Molecular cloning, tissue distribution, and chromosomal localization of
RT   human cationic amino acid transporter 2 (HCAT2).";
RL   Genomics 38:174-178(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   337-469 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, VARIANT THR-531,
RP   TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Liver;
RX   PubMed=9174363; DOI=10.1021/bi962829p;
RA   Closs E.I., Graef P., Habermeier A., Cunningham J.M., Foerstermann U.;
RT   "Human cationic amino acid transporters hCAT-1, hCAT-2A, and hCAT-2B: three
RT   related carriers with distinct transport properties.";
RL   Biochemistry 36:6462-6468(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP   VARIANT THR-531.
RC   TISSUE=Liver;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 313-658 (ISOFORM 2).
RC   TISSUE=Skeletal muscle;
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; THR-28; SER-446; SER-464;
RP   SER-646 AND SER-647, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=28684763; DOI=10.1038/s41598-017-04965-2;
RA   Chafai A., Fromm M.F., Koenig J., Maas R.;
RT   "The prognostic biomarker L-homoarginine is a substrate of the cationic
RT   amino acid transporters CAT1, CAT2A and CAT2B.";
RL   Sci. Rep. 7:4767-4767(2017).
CC   -!- FUNCTION: Functions as a permease involved in the transport of the
CC       cationic amino acids (L-arginine, L-lysine, L-ornithine and L-
CC       homoarginine); the affinity for its substrates differs between isoforms
CC       created by alternative splicing (PubMed:9174363, PubMed:28684763). May
CC       play a role in classical or alternative activation of macrophages via
CC       its role in arginine transport (By similarity).
CC       {ECO:0000250|UniProtKB:P18581, ECO:0000269|PubMed:28684763,
CC       ECO:0000269|PubMed:9174363}.
CC   -!- FUNCTION: [Isoform 1]: Functions as a permease that mediates the
CC       transport of the cationic amino acids (L-arginine, L-lysine, L-
CC       ornithine and L-homoarginine). Shows a much higher affinity for L-
CC       arginine and L-homoarginine than isoform 2.
CC       {ECO:0000269|PubMed:28684763, ECO:0000269|PubMed:9174363}.
CC   -!- FUNCTION: [Isoform 2]: Functions as a low-affinity, high capacity
CC       permease involved in the transport of the cationic amino acids (L-
CC       arginine, L-lysine, L-ornithine and L-homoarginine).
CC       {ECO:0000269|PubMed:28684763, ECO:0000269|PubMed:9174363}.
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143,
CC         ChEBI:CHEBI:32682; Evidence={ECO:0000269|PubMed:9174363};
CC   -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC       Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143,
CC         ChEBI:CHEBI:32682; Evidence={ECO:0000269|PubMed:9174363};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935,
CC         ChEBI:CHEBI:32551; Evidence={ECO:0000250|UniProtKB:P18581};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ornithine(in) = L-ornithine(out); Xref=Rhea:RHEA:71199,
CC         ChEBI:CHEBI:46911; Evidence={ECO:0000250|UniProtKB:P18581};
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=L-homoarginine(in) = L-homoarginine(out);
CC         Xref=Rhea:RHEA:71203, ChEBI:CHEBI:143006;
CC         Evidence={ECO:0000269|PubMed:28684763};
CC   -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC       Reaction=L-homoarginine(in) = L-homoarginine(out);
CC         Xref=Rhea:RHEA:71203, ChEBI:CHEBI:143006;
CC         Evidence={ECO:0000269|PubMed:28684763};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC       Kinetic parameters:
CC         KM=0.32 mM for L-arginine {ECO:0000269|PubMed:9174363};
CC         KM=0.523 mM for L-homoarginine {ECO:0000269|PubMed:28684763};
CC         Vmax=11 nmol/min/mg enzyme for L-homoarginine uptake
CC         {ECO:0000269|PubMed:28684763};
CC       pH dependence:
CC         Optimum pH is 7.5 for L-arginine transport.
CC         {ECO:0000269|PubMed:9174363};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]:
CC       Kinetic parameters:
CC         KM=3.36 mM for L-arginine {ECO:0000269|PubMed:9174363};
CC         Note=In contrast with isoform 1, saturation of L-homoarginine uptake
CC         could not be reached. {ECO:0000269|PubMed:28684763};
CC       pH dependence:
CC         Optimum pH is 7-8.5 for L-arginine transport.
CC         {ECO:0000269|PubMed:9174363};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9174363};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:9174363}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=CAT-2B {ECO:0000303|PubMed:9174363}, CAT2B
CC       {ECO:0000269|PubMed:28684763}, SLC7A2B {ECO:0000269|PubMed:28684763};
CC         IsoId=P52569-1; Sequence=Displayed;
CC       Name=2; Synonyms=CAT-2A {ECO:0000303|PubMed:9174363}, CAT2A
CC       {ECO:0000269|PubMed:28684763}, SLC7A2A {ECO:0000269|PubMed:28684763};
CC         IsoId=P52569-2; Sequence=VSP_037354, VSP_023354;
CC       Name=3;
CC         IsoId=P52569-3; Sequence=VSP_037354;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the skeletal muscle,
CC       placenta and ovary. Expressed at intermediate levels in the liver and
CC       pancreas and at low levels in the kidney and heart.
CC       {ECO:0000269|PubMed:8954799}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH69648.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI04906.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI13662.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI43584.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAB62810.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D29990; BAA06271.1; -; mRNA.
DR   EMBL; U76368; AAB62810.1; ALT_FRAME; mRNA.
DR   EMBL; U76369; AAB62811.1; -; mRNA.
DR   EMBL; AB020863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471080; EAW63813.1; -; Genomic_DNA.
DR   EMBL; BC069648; AAH69648.1; ALT_INIT; mRNA.
DR   EMBL; BC104905; AAI04906.1; ALT_INIT; mRNA.
DR   EMBL; BC113661; AAI13662.1; ALT_INIT; mRNA.
DR   EMBL; BC143583; AAI43584.1; ALT_INIT; mRNA.
DR   EMBL; AL832016; CAD89909.1; -; mRNA.
DR   CCDS; CCDS34852.1; -. [P52569-1]
DR   CCDS; CCDS55203.1; -. [P52569-3]
DR   CCDS; CCDS6002.2; -. [P52569-2]
DR   RefSeq; NP_001008539.3; NM_001008539.3. [P52569-1]
DR   RefSeq; NP_001158243.1; NM_001164771.1. [P52569-3]
DR   RefSeq; NP_003037.4; NM_003046.5. [P52569-2]
DR   RefSeq; XP_005273667.1; XM_005273610.4.
DR   RefSeq; XP_005273668.1; XM_005273611.4. [P52569-1]
DR   RefSeq; XP_005273669.1; XM_005273612.4. [P52569-1]
DR   RefSeq; XP_016869235.1; XM_017013746.1. [P52569-1]
DR   RefSeq; XP_016869236.1; XM_017013747.1.
DR   AlphaFoldDB; P52569; -.
DR   SMR; P52569; -.
DR   BioGRID; 112433; 107.
DR   IntAct; P52569; 33.
DR   MINT; P52569; -.
DR   STRING; 9606.ENSP00000004531; -.
DR   DrugBank; DB00123; Lysine.
DR   DrugBank; DB00129; Ornithine.
DR   TCDB; 2.A.3.3.8; the amino acid-polyamine-organocation (apc) family.
DR   GlyCosmos; P52569; 3 sites, No reported glycans.
DR   GlyGen; P52569; 3 sites.
DR   iPTMnet; P52569; -.
DR   PhosphoSitePlus; P52569; -.
DR   SwissPalm; P52569; -.
DR   BioMuta; SLC7A2; -.
DR   DMDM; 126302539; -.
DR   EPD; P52569; -.
DR   jPOST; P52569; -.
DR   MassIVE; P52569; -.
DR   MaxQB; P52569; -.
DR   PaxDb; 9606-ENSP00000004531; -.
DR   PeptideAtlas; P52569; -.
DR   ProteomicsDB; 56491; -. [P52569-1]
DR   ProteomicsDB; 56492; -. [P52569-2]
DR   ProteomicsDB; 56493; -. [P52569-3]
DR   Pumba; P52569; -.
DR   Antibodypedia; 2114; 141 antibodies from 24 providers.
DR   DNASU; 6542; -.
DR   Ensembl; ENST00000004531.14; ENSP00000004531.10; ENSG00000003989.18. [P52569-3]
DR   Ensembl; ENST00000398090.3; ENSP00000381164.3; ENSG00000003989.18. [P52569-2]
DR   Ensembl; ENST00000494857.6; ENSP00000419140.2; ENSG00000003989.18. [P52569-1]
DR   Ensembl; ENST00000522656.5; ENSP00000430464.1; ENSG00000003989.18. [P52569-1]
DR   Ensembl; ENST00000640220.1; ENSP00000492016.2; ENSG00000003989.18. [P52569-1]
DR   GeneID; 6542; -.
DR   KEGG; hsa:6542; -.
DR   MANE-Select; ENST00000494857.6; ENSP00000419140.2; NM_001370338.1; NP_001357267.1.
DR   UCSC; uc011kyc.3; human. [P52569-1]
DR   AGR; HGNC:11060; -.
DR   CTD; 6542; -.
DR   DisGeNET; 6542; -.
DR   GeneCards; SLC7A2; -.
DR   HGNC; HGNC:11060; SLC7A2.
DR   HPA; ENSG00000003989; Tissue enhanced (liver, parathyroid gland).
DR   MIM; 601872; gene.
DR   neXtProt; NX_P52569; -.
DR   OpenTargets; ENSG00000003989; -.
DR   PharmGKB; PA35920; -.
DR   VEuPathDB; HostDB:ENSG00000003989; -.
DR   eggNOG; KOG1286; Eukaryota.
DR   GeneTree; ENSGT00940000160440; -.
DR   HOGENOM; CLU_007946_15_7_1; -.
DR   InParanoid; P52569; -.
DR   OMA; WQLTMIS; -.
DR   OrthoDB; 1421713at2759; -.
DR   PhylomeDB; P52569; -.
DR   TreeFam; TF315212; -.
DR   PathwayCommons; P52569; -.
DR   Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR   SignaLink; P52569; -.
DR   BioGRID-ORCS; 6542; 18 hits in 1162 CRISPR screens.
DR   ChiTaRS; SLC7A2; human.
DR   GeneWiki; SLC7A2; -.
DR   GenomeRNAi; 6542; -.
DR   Pharos; P52569; Tbio.
DR   PRO; PR:P52569; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P52569; Protein.
DR   Bgee; ENSG00000003989; Expressed in skeletal muscle tissue of rectus abdominis and 160 other cell types or tissues.
DR   ExpressionAtlas; P52569; baseline and differential.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015174; F:basic amino acid transmembrane transporter activity; TAS:ProtInc.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015189; F:L-lysine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR   GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:0015807; P:L-amino acid transport; IDA:ARUK-UCL.
DR   GO; GO:0097638; P:L-arginine import across plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:1903826; P:L-arginine transmembrane transport; IDA:UniProtKB.
DR   GO; GO:1903352; P:L-ornithine transmembrane transport; IBA:GO_Central.
DR   GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 2.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004755; Cat_AA_permease.
DR   InterPro; IPR029485; CAT_C.
DR   NCBIfam; TIGR00906; 2A0303; 1.
DR   PANTHER; PTHR43243:SF35; CATIONIC AMINO ACID TRANSPORTER 2; 1.
DR   PANTHER; PTHR43243; INNER MEMBRANE TRANSPORTER YGJI-RELATED; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   Pfam; PF13906; AA_permease_C; 1.
DR   Genevisible; P52569; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amino-acid transport; Cell membrane; Glycoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..658
FT                   /note="Cationic amino acid transporter 2"
FT                   /id="PRO_0000054264"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..63
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..163
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..289
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..339
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        361..386
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        408..410
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        432..490
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        512..524
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        525..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        550..557
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        558..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        579..582
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        583..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        604..658
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         28
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         446
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         646
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         647
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MKIETSGYNSDKLICRGFIGTPAPPVCDSKFLLSPSSDVRM (in
FT                   isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:9174363"
FT                   /id="VSP_037354"
FT   VAR_SEQ         357..398
FT                   /note="IFPMPRVIYAMAEDGLLFKCLAQINSKTKTPIIATLSSGAVA -> MFPLPR
FT                   ILFAMARDGLLFRFLARVSKRQSPVAATLTAGVIS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:9174363"
FT                   /id="VSP_023354"
FT   VARIANT         20
FT                   /note="V -> M (in dbSNP:rs12680645)"
FT                   /id="VAR_030799"
FT   VARIANT         376
FT                   /note="C -> F (in dbSNP:rs1134975)"
FT                   /id="VAR_030800"
FT   VARIANT         531
FT                   /note="A -> T (in dbSNP:rs62622371)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9174363"
FT                   /id="VAR_030801"
FT   VARIANT         547
FT                   /note="Q -> L (in dbSNP:rs1981498)"
FT                   /id="VAR_058414"
FT   CONFLICT        134
FT                   /note="W -> G (in Ref. 1; BAA06271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        364
FT                   /note="I -> N (in Ref. 1; BAA06271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520
FT                   /note="T -> Y (in Ref. 1; BAA06271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        552
FT                   /note="Q -> R (in Ref. 1; BAA06271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="A -> T (in Ref. 1; BAA06271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="S -> T (in Ref. 1; BAA06271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        605
FT                   /note="H -> R (in Ref. 6; CAD89909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        619
FT                   /note="D -> V (in Ref. 6; CAD89909)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   658 AA;  71673 MW;  633FD86A333E9208 CRC64;
     MIPCRAALTF ARCLIRRKIV TLDSLEDTKL CRCLSTMDLI ALGVGSTLGA GVYVLAGEVA
     KADSGPSIVV SFLIAALASV MAGLCYAEFG ARVPKTGSAY LYTYVTVGEL WAFITGWNLI
     LSYVIGTSSV ARAWSGTFDE LLSKQIGQFL RTYFRMNYTG LAEYPDFFAV CLILLLAGLL
     SFGVKESAWV NKVFTAVNIL VLLFVMVAGF VKGNVANWKI SEEFLKNISA SAREPPSENG
     TSIYGAGGFM PYGFTGTLAG AATCFYAFVG FDCIATTGEE VRNPQKAIPI GIVTSLLVCF
     MAYFGVSAAL TLMMPYYLLD EKSPLPVAFE YVGWGPAKYV VAAGSLCALS TSLLGSIFPM
     PRVIYAMAED GLLFKCLAQI NSKTKTPIIA TLSSGAVAAL MAFLFDLKAL VDMMSIGTLM
     AYSLVAACVL ILRYQPGLSY DQPKCSPEKD GLGSSPRVTS KSESQVTMLQ RQGFSMRTLF
     CPSLLPTQQS ASLVSFLVGF LAFLVLGLSV LTTYGVHAIT RLEAWSLALL ALFLVLFVAI
     VLTIWRQPQN QQKVAFMVPF LPFLPAFSIL VNIYLMVQLS ADTWVRFSIW MAIGFLIYFS
     YGIRHSLEGH LRDENNEEDA YPDNVHAAAE EKSAIQANDH HPRNLSSPFI FHEKTSEF
//