SL7A1_HUMAN
ID SL7A1_HUMAN Reviewed; 629 AA.
AC P30825; Q5JR50;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=High affinity cationic amino acid transporter 1;
DE Short=CAT-1 {ECO:0000303|PubMed:10485994};
DE Short=CAT1;
DE AltName: Full=Ecotropic retroviral leukemia receptor homolog;
DE AltName: Full=Ecotropic retrovirus receptor homolog;
DE AltName: Full=Solute carrier family 7 member 1 {ECO:0000312|HGNC:HGNC:11057};
DE AltName: Full=System Y+ basic amino acid transporter;
GN Name=SLC7A1 {ECO:0000312|HGNC:HGNC:11057};
GN Synonyms=ATRC1 {ECO:0000303|PubMed:1348489},
GN ERR {ECO:0000312|HGNC:HGNC:11057}, REC1L;
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], AND TISSUE SPECIFICITY.
RX PubMed=1718082; DOI=10.1016/0042-6822(91)90748-z;
RA Yoshimoto T., Yoshimoto E., Meruelo D.;
RT "Molecular cloning and characterization of a novel human gene homologous to
RT the murine ecotropic retroviral receptor.";
RL Virology 185:10-17(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Urinary bladder;
RX PubMed=1348489; DOI=10.1016/0888-7543(92)90431-q;
RA Albritton L.M., Bowcock A.M., Eddy R.L., Morton C.C., Tseng L.,
RA Farrer L.A., Cavalli-Sforza L.L., Shows T.B., Cunningham J.M.;
RT "The human cationic amino acid transporter (ATRC1): physical and genetic
RT mapping to 13q12-q14.";
RL Genomics 12:430-434(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=10485994; DOI=10.1007/s002329900558;
RA Kamath S.G., Furesz T.C., Way B.A., Smith C.H.;
RT "Identification of three cationic amino acid transporters in placental
RT trophoblast: cloning, expression, and characterization of hCAT-1.";
RL J. Membr. Biol. 171:55-62(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 PROTEIN SEQUENCE OF 5-15; 131-142 AND 361-373, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-226.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP INTERACTION WITH TM4SF5.
RX PubMed=30956113; DOI=10.1016/j.cmet.2019.03.005;
RA Jung J.W., Macalino S.J.Y., Cui M., Kim J.E., Kim H.J., Song D.G.,
RA Nam S.H., Kim S., Choi S., Lee J.W.;
RT "Transmembrane 4 L six family member 5 senses arginine for mTORC1
RT signaling.";
RL Cell Metab. 29:1306-1319(2019).
CC -!- FUNCTION: High-affinity, low capacity permease involved in the
CC transport of the cationic amino acids (arginine, lysine and ornithine)
CC in non-hepatic tissues. {ECO:0000269|PubMed:10485994}.
CC -!- SUBUNIT: Interacts with TM4SF5; the interaction is negatively regulated
CC by arginine (PubMed:30956113). Forms tissue-specific complexes with
CC ASL, ASS1 and nitric oxide synthase NOS1 or NOS3; the complex regulates
CC cell-autonomous L-arginine synthesis and citrulline recycling while
CC channeling extracellular L-arginine to nitric oxide synthesis pathway
CC (By similarity). {ECO:0000250|UniProtKB:Q09143,
CC ECO:0000269|PubMed:30956113}.
CC -!- INTERACTION:
CC P30825; O60242: ADGRB3; NbExp=3; IntAct=EBI-4289564, EBI-2682765;
CC P30825; P02652: APOA2; NbExp=3; IntAct=EBI-4289564, EBI-1171525;
CC P30825; Q13520: AQP6; NbExp=3; IntAct=EBI-4289564, EBI-13059134;
CC P30825; P27449: ATP6V0C; NbExp=3; IntAct=EBI-4289564, EBI-721179;
CC P30825; P07357: C8A; NbExp=3; IntAct=EBI-4289564, EBI-9021639;
CC P30825; P27352: CBLIF; NbExp=3; IntAct=EBI-4289564, EBI-3953638;
CC P30825; P13236: CCL4; NbExp=3; IntAct=EBI-4289564, EBI-2873970;
CC P30825; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-4289564, EBI-10271156;
CC P30825; P25942: CD40; NbExp=3; IntAct=EBI-4289564, EBI-525714;
CC P30825; P11912: CD79A; NbExp=3; IntAct=EBI-4289564, EBI-7797864;
CC P30825; O14735: CDIPT; NbExp=3; IntAct=EBI-4289564, EBI-358858;
CC P30825; Q9HA82: CERS4; NbExp=3; IntAct=EBI-4289564, EBI-2622997;
CC P30825; Q8TAZ6: CMTM2; NbExp=3; IntAct=EBI-4289564, EBI-2339374;
CC P30825; P21964: COMT; NbExp=3; IntAct=EBI-4289564, EBI-372265;
CC P30825; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-4289564, EBI-6942903;
CC P30825; Q9BV81: EMC6; NbExp=3; IntAct=EBI-4289564, EBI-2820492;
CC P30825; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-4289564, EBI-12118888;
CC P30825; Q969F0: FATE1; NbExp=6; IntAct=EBI-4289564, EBI-743099;
CC P30825; Q8N3T1: GALNT15; NbExp=3; IntAct=EBI-4289564, EBI-3925203;
CC P30825; O00258: GET1; NbExp=3; IntAct=EBI-4289564, EBI-18908258;
CC P30825; P16278: GLB1; NbExp=3; IntAct=EBI-4289564, EBI-989638;
CC P30825; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-4289564, EBI-13345167;
CC P30825; Q9BSE4: HERPUD2; NbExp=3; IntAct=EBI-4289564, EBI-2868124;
CC P30825; O15243: LEPROT; NbExp=3; IntAct=EBI-4289564, EBI-15672507;
CC P30825; O95214: LEPROTL1; NbExp=3; IntAct=EBI-4289564, EBI-750776;
CC P30825; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-4289564, EBI-11956541;
CC P30825; O14880: MGST3; NbExp=3; IntAct=EBI-4289564, EBI-724754;
CC P30825; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-4289564, EBI-12070086;
CC P30825; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-4289564, EBI-721750;
CC P30825; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-4289564, EBI-16427978;
CC P30825; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-4289564, EBI-8652812;
CC P30825; P43378: PTPN9; NbExp=3; IntAct=EBI-4289564, EBI-742898;
CC P30825; P50876: RNF144A; NbExp=3; IntAct=EBI-4289564, EBI-2340657;
CC P30825; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-4289564, EBI-3917235;
CC P30825; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-4289564, EBI-17247926;
CC P30825; Q15436: SEC23A; NbExp=3; IntAct=EBI-4289564, EBI-81088;
CC P30825; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-4289564, EBI-18159983;
CC P30825; Q05940: SLC18A2; NbExp=3; IntAct=EBI-4289564, EBI-18036244;
CC P30825; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-4289564, EBI-8644112;
CC P30825; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-4289564, EBI-12898013;
CC P30825; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-4289564, EBI-2823239;
CC P30825; Q9NWF4: SLC52A1; NbExp=3; IntAct=EBI-4289564, EBI-12904614;
CC P30825; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-4289564, EBI-8640191;
CC P30825; Q96JF0-2: ST6GAL2; NbExp=3; IntAct=EBI-4289564, EBI-12908338;
CC P30825; Q13586: STIM1; NbExp=3; IntAct=EBI-4289564, EBI-448878;
CC P30825; P55061: TMBIM6; NbExp=3; IntAct=EBI-4289564, EBI-1045825;
CC P30825; Q9Y6G1: TMEM14A; NbExp=3; IntAct=EBI-4289564, EBI-2800360;
CC P30825; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-4289564, EBI-741829;
CC P30825; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-4289564, EBI-10982110;
CC P30825; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-4289564, EBI-12195249;
CC P30825; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-4289564, EBI-11988865;
CC P30825; Q9BSR8: YIPF4; NbExp=4; IntAct=EBI-4289564, EBI-751253;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q09143};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:1718082}.
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 ---------------------------------------------------------------------------
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; X59155; CAA41869.1; -; mRNA.
DR EMBL; X57303; CAA40560.1; -; mRNA.
DR EMBL; AF078107; AAC27721.1; -; mRNA.
DR EMBL; AL596114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063303; AAH63303.1; -; mRNA.
DR EMBL; BC069358; AAH69358.1; -; mRNA.
DR EMBL; BC115407; AAI15408.1; -; mRNA.
DR CCDS; CCDS9333.1; -.
DR PIR; S29685; S29685.
DR RefSeq; NP_003036.1; NM_003045.4.
DR RefSeq; XP_005266564.1; XM_005266507.3.
DR RefSeq; XP_016876205.1; XM_017020716.1.
DR AlphaFoldDB; P30825; -.
DR SMR; P30825; -.
DR BioGRID; 112432; 288.
DR IntAct; P30825; 111.
DR MINT; P30825; -.
DR STRING; 9606.ENSP00000370128; -.
DR DrugBank; DB00125; Arginine.
DR DrugBank; DB00123; Lysine.
DR DrugBank; DB00129; Ornithine.
DR TCDB; 2.A.3.3.9; the amino acid-polyamine-organocation (apc) family.
DR GlyConnect; 1314; 1 N-Linked glycan (1 site).
DR GlyGen; P30825; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P30825; -.
DR PhosphoSitePlus; P30825; -.
DR SwissPalm; P30825; -.
DR BioMuta; SLC7A1; -.
DR DMDM; 1706185; -.
DR EPD; P30825; -.
DR jPOST; P30825; -.
DR MassIVE; P30825; -.
DR MaxQB; P30825; -.
DR PaxDb; P30825; -.
DR PeptideAtlas; P30825; -.
DR PRIDE; P30825; -.
DR ProteomicsDB; 54739; -.
DR Antibodypedia; 22734; 215 antibodies from 27 providers.
DR DNASU; 6541; -.
DR Ensembl; ENST00000380752.10; ENSP00000370128.5; ENSG00000139514.13.
DR GeneID; 6541; -.
DR KEGG; hsa:6541; -.
DR MANE-Select; ENST00000380752.10; ENSP00000370128.5; NM_003045.5; NP_003036.1.
DR UCSC; uc001uso.4; human.
DR CTD; 6541; -.
DR DisGeNET; 6541; -.
DR GeneCards; SLC7A1; -.
DR HGNC; HGNC:11057; SLC7A1.
DR HPA; ENSG00000139514; Tissue enhanced (esophagus).
DR MIM; 104615; gene.
DR neXtProt; NX_P30825; -.
DR OpenTargets; ENSG00000139514; -.
DR PharmGKB; PA35917; -.
DR VEuPathDB; HostDB:ENSG00000139514; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000155349; -.
DR HOGENOM; CLU_007946_15_7_1; -.
DR InParanoid; P30825; -.
DR OMA; WQLTMIS; -.
DR OrthoDB; 439017at2759; -.
DR PhylomeDB; P30825; -.
DR TreeFam; TF315212; -.
DR PathwayCommons; P30825; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR SignaLink; P30825; -.
DR BioGRID-ORCS; 6541; 141 hits in 1093 CRISPR screens.
DR ChiTaRS; SLC7A1; human.
DR GeneWiki; SLC7A1; -.
DR GenomeRNAi; 6541; -.
DR Pharos; P30825; Tbio.
DR PRO; PR:P30825; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P30825; protein.
DR Bgee; ENSG00000139514; Expressed in tongue squamous epithelium and 206 other tissues.
DR ExpressionAtlas; P30825; baseline and differential.
DR Genevisible; P30825; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0009925; C:basal plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:ARUK-UCL.
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; IBA:GO_Central.
DR GO; GO:0015807; P:L-amino acid transport; IDA:ARUK-UCL.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; ISS:ARUK-UCL.
DR GO; GO:1903826; P:L-arginine transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:1903810; P:L-histidine import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:1903352; P:L-ornithine transmembrane transport; IBA:GO_Central.
DR GO; GO:0015819; P:lysine transport; IDA:ARUK-UCL.
DR GO; GO:0015822; P:ornithine transport; IMP:ARUK-UCL.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004755; Cat_AA_permease.
DR InterPro; IPR029485; CAT_C.
DR Pfam; PF13520; AA_permease_2; 1.
DR Pfam; PF13906; AA_permease_C; 1.
DR TIGRFAMs; TIGR00906; 2A0303; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Direct protein sequencing;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..629
FT /note="High affinity cationic amino acid transporter 1"
FT /id="PRO_0000054261"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..526
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 23
FT /note="R -> P (in Ref. 2; CAA40560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 629 AA; 67638 MW; 717734D4793647C5 CRC64;
MGCKVLLNIG QQMLRRKVVD CSREETRLSR CLNTFDLVAL GVGSTLGAGV YVLAGAVARE
NAGPAIVISF LIAALASVLA GLCYGEFGAR VPKTGSAYLY SYVTVGELWA FITGWNLILS
YIIGTSSVAR AWSATFDELI GRPIGEFSRT HMTLNAPGVL AENPDIFAVI IILILTGLLT
LGVKESAMVN KIFTCINVLV LGFIMVSGFV KGSVKNWQLT EEDFGNTSGR LCLNNDTKEG
KPGVGGFMPF GFSGVLSGAA TCFYAFVGFD CIATTGEEVK NPQKAIPVGI VASLLICFIA
YFGVSAALTL MMPYFCLDNN SPLPDAFKHV GWEGAKYAVA VGSLCALSAS LLGSMFPMPR
VIYAMAEDGL LFKFLANVND RTKTPIIATL ASGAVAAVMA FLFDLKDLVD LMSIGTLLAY
SLVAACVLVL RYQPEQPNLV YQMASTSDEL DPADQNELAS TNDSQLGFLP EAEMFSLKTI
LSPKNMEPSK ISGLIVNIST SLIAVLIITF CIVTVLGREA LTKGALWAVF LLAGSALLCA
VVTGVIWRQP ESKTKLSFKV PFLPVLPILS IFVNVYLMMQ LDQGTWVRFA VWMLIGFIIY
FGYGLWHSEE ASLDADQART PDGNLDQCK
