S23A1_HUMAN
ID S23A1_HUMAN Reviewed; 598 AA.
AC Q9UHI7; O95191; Q8WWB6; Q9UGH4; Q9UI39;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Solute carrier family 23 member 1 {ECO:0000305};
DE AltName: Full=Na(+)/L-ascorbic acid transporter 1;
DE AltName: Full=Sodium-dependent vitamin C transporter 1 {ECO:0000303|PubMed:10556483};
DE Short=hSVCT1 {ECO:0000303|PubMed:10556483};
DE AltName: Full=Yolk sac permease-like molecule 3 {ECO:0000303|PubMed:9804989};
GN Name=SLC23A1 {ECO:0000312|HGNC:HGNC:10974};
GN Synonyms=SVCT1 {ECO:0000303|PubMed:10556483},
GN YSPL3 {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=Fetal liver, and 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] (ISOFORMS 1 AND 2), FUNCTION, TRANSPORTER
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Intestinal epithelium;
RX PubMed=10556483; DOI=10.1016/s0005-2736(99)00182-0;
RA Wang H., Dutta B., Huang W., Devoe L.D., Leibach F.H., Ganapathy V.,
RA Prasad P.D.;
RT "Human Na(+)-dependent vitamin C transporter 1 (hSVCT1): primary structure,
RT functional characteristics and evidence for a non-functional splice
RT variant.";
RL Biochim. Biophys. Acta 1461:1-9(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), FUNCTION, TRANSPORTER ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=10631088; DOI=10.1006/bbrc.1999.1929;
RA Wang Y., Mackenzie B., Tsukaguchi H., Weremowicz S., Morton C.C.,
RA Hediger M.A.;
RT "Human vitamin C (L-ascorbic acid) transporter SVCT1.";
RL Biochem. Biophys. Res. Commun. 267:488-494(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=11584081; DOI=10.1093/jn/131.10.2623;
RA Erichsen H.C., Eck P., Levine M., Chanock S.;
RT "Characterization of the genomic structure of the human vitamin C
RT transporter SVCT1 (SLC23A2).";
RL J. Nutr. 131:2623-2627(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver cancer;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Colon, and Kidney;
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 [9]
RP GLYCOSYLATION AT ASN-138 AND ASN-144, 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).
CC -!- FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake
CC of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.
CC {ECO:0000269|PubMed:10556483, ECO:0000269|PubMed:10556521,
CC ECO:0000269|PubMed:10631088}.
CC -!- FUNCTION: [Isoform 2]: Inactive transporter.
CC {ECO:0000269|PubMed:10556483}.
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:10556483,
CC ECO:0000305|PubMed:10631088};
CC -!- INTERACTION:
CC Q9UHI7; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1759386, EBI-10173507;
CC Q9UHI7; O43865: AHCYL1; NbExp=3; IntAct=EBI-1759386, EBI-2371423;
CC Q9UHI7; Q9UBQ7: GRHPR; NbExp=6; IntAct=EBI-1759386, EBI-372445;
CC Q9UHI7; Q15323: KRT31; NbExp=3; IntAct=EBI-1759386, EBI-948001;
CC Q9UHI7; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-1759386, EBI-10172150;
CC Q9UHI7; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-1759386, EBI-10172290;
CC Q9UHI7; P60410: KRTAP10-8; NbExp=4; IntAct=EBI-1759386, EBI-10171774;
CC Q9UHI7; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1759386, EBI-10172052;
CC Q9UHI7; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-1759386, EBI-10172511;
CC Q9UHI7; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1759386, EBI-742948;
CC Q9UHI7; P16333: NCK1; NbExp=2; IntAct=EBI-1759386, EBI-389883;
CC Q9UHI7; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-1759386, EBI-945833;
CC Q9UHI7-3; O43865: AHCYL1; NbExp=3; IntAct=EBI-11998660, EBI-2371423;
CC Q9UHI7-3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11998660, EBI-3867333;
CC Q9UHI7-3; O95967: EFEMP2; NbExp=3; IntAct=EBI-11998660, EBI-743414;
CC Q9UHI7-3; P49639: HOXA1; NbExp=3; IntAct=EBI-11998660, EBI-740785;
CC Q9UHI7-3; Q15323: KRT31; NbExp=3; IntAct=EBI-11998660, EBI-948001;
CC Q9UHI7-3; O76011: KRT34; NbExp=3; IntAct=EBI-11998660, EBI-1047093;
CC Q9UHI7-3; Q6A162: KRT40; NbExp=3; IntAct=EBI-11998660, EBI-10171697;
CC Q9UHI7-3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11998660, EBI-11959885;
CC Q9UHI7-3; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-11998660, EBI-11749135;
CC Q9UHI7-3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-11998660, EBI-10171774;
CC Q9UHI7-3; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-11998660, EBI-11953334;
CC Q9UHI7-3; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-11998660, EBI-10302392;
CC Q9UHI7-3; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-11998660, EBI-1043191;
CC Q9UHI7-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11998660, EBI-16439278;
CC Q9UHI7-3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-11998660, EBI-22310682;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10631088,
CC ECO:0000269|PubMed:19379732}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19379732}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9UHI7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHI7-2; Sequence=VSP_006814;
CC Name=3;
CC IsoId=Q9UHI7-3; Sequence=VSP_006813;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult small intestine, kidney,
CC thymus, ovary, colon, prostate and liver, and in fetal kidney, liver
CC and thymus. {ECO:0000269|PubMed:10556483}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10556521}.
CC -!- MISCELLANEOUS: Treatment with the protein kinase C stimulator PMA
CC results in a 10-fold decrease in ascorbate accumulation in transfected
CC cells. {ECO:0000269|PubMed:10556521}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
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DR EMBL; AF058317; AAC78804.1; -; mRNA.
DR EMBL; AF170911; AAF24759.1; -; mRNA.
DR EMBL; AJ269477; CAB58119.1; -; mRNA.
DR EMBL; AF098277; AAF22490.1; -; mRNA.
DR EMBL; AF375875; AAK97398.1; -; Genomic_DNA.
DR EMBL; AJ250807; CAC15384.1; -; mRNA.
DR EMBL; AC135457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF458016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019225; AAH19225.1; -; mRNA.
DR EMBL; BC050261; AAH50261.1; -; mRNA.
DR CCDS; CCDS4212.1; -. [Q9UHI7-1]
DR CCDS; CCDS4213.1; -. [Q9UHI7-2]
DR PIR; JC7182; JC7182.
DR RefSeq; NP_005838.3; NM_005847.4.
DR RefSeq; NP_689898.2; NM_152685.3.
DR AlphaFoldDB; Q9UHI7; -.
DR BioGRID; 115288; 25.
DR IntAct; Q9UHI7; 28.
DR STRING; 9606.ENSP00000302851; -.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugCentral; Q9UHI7; -.
DR GuidetoPHARMACOLOGY; 1041; -.
DR TCDB; 2.A.40.6.5; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR GlyGen; Q9UHI7; 2 sites.
DR iPTMnet; Q9UHI7; -.
DR PhosphoSitePlus; Q9UHI7; -.
DR BioMuta; SLC23A1; -.
DR DMDM; 296452969; -.
DR jPOST; Q9UHI7; -.
DR MassIVE; Q9UHI7; -.
DR PaxDb; Q9UHI7; -.
DR PeptideAtlas; Q9UHI7; -.
DR PRIDE; Q9UHI7; -.
DR ProteomicsDB; 84358; -. [Q9UHI7-1]
DR ProteomicsDB; 84359; -. [Q9UHI7-2]
DR ProteomicsDB; 84360; -. [Q9UHI7-3]
DR Antibodypedia; 26736; 109 antibodies from 17 providers.
DR DNASU; 9963; -.
DR Ensembl; ENST00000348729.8; ENSP00000302701.4; ENSG00000170482.17. [Q9UHI7-1]
DR Ensembl; ENST00000353963.7; ENSP00000302851.5; ENSG00000170482.17. [Q9UHI7-2]
DR GeneID; 9963; -.
DR KEGG; hsa:9963; -.
DR MANE-Select; ENST00000348729.8; ENSP00000302701.4; NM_005847.5; NP_005838.3.
DR UCSC; uc003leg.4; human. [Q9UHI7-1]
DR CTD; 9963; -.
DR DisGeNET; 9963; -.
DR GeneCards; SLC23A1; -.
DR HGNC; HGNC:10974; SLC23A1.
DR HPA; ENSG00000170482; Group enriched (fallopian tube, intestine, kidney, liver).
DR MIM; 603790; gene.
DR neXtProt; NX_Q9UHI7; -.
DR OpenTargets; ENSG00000170482; -.
DR PharmGKB; PA35850; -.
DR VEuPathDB; HostDB:ENSG00000170482; -.
DR eggNOG; KOG1292; Eukaryota.
DR GeneTree; ENSGT00950000182953; -.
DR HOGENOM; CLU_017959_5_4_1; -.
DR InParanoid; Q9UHI7; -.
DR OrthoDB; 387031at2759; -.
DR PhylomeDB; Q9UHI7; -.
DR TreeFam; TF313272; -.
DR PathwayCommons; Q9UHI7; -.
DR Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
DR SignaLink; Q9UHI7; -.
DR BioGRID-ORCS; 9963; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; SLC23A1; human.
DR GeneWiki; SLC23A1; -.
DR GenomeRNAi; 9963; -.
DR Pharos; Q9UHI7; Tchem.
DR PRO; PR:Q9UHI7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UHI7; protein.
DR Bgee; ENSG00000170482; Expressed in ileal mucosa and 111 other tissues.
DR ExpressionAtlas; Q9UHI7; baseline and differential.
DR Genevisible; Q9UHI7; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043229; C:intracellular organelle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IMP: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:0015205; F:nucleobase transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IMP:UniProtKB.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; TAS:Reactome.
DR GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:UniProtKB.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0015851; P:nucleobase transport; TAS:ProtInc.
DR GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR029954; SLC23A1.
DR PANTHER; PTHR11119:SF21; PTHR11119:SF21; 1.
DR Pfam; PF00860; Xan_ur_permease; 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..598
FT /note="Solute carrier family 23 member 1"
FT /id="PRO_0000165975"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:19379732"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 230..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..426
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:19379732"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J0"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J0"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J0"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19379732"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19379732"
FT VAR_SEQ 92..430
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006813"
FT VAR_SEQ 156
FT /note="V -> VGLHV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10556483,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_006814"
FT VARIANT 218
FT /note="I -> V (in dbSNP:rs34521685)"
FT /id="VAR_053451"
FT VARIANT 258
FT /note="M -> V (in dbSNP:rs35817838)"
FT /id="VAR_053452"
FT VARIANT 264
FT /note="V -> M (in dbSNP:rs33972313)"
FT /id="VAR_053453"
FT VARIANT 421
FT /note="A -> S (in dbSNP:rs6596474)"
FT /id="VAR_062111"
FT CONFLICT 11
FT /note="T -> A (in Ref. 2; AAF24759)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..57
FT /note="YLTCFS -> IHDCLR (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..80
FT /note="DQHMVS -> SQTLHC (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="W -> S (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="I -> N (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="E -> D (in Ref. 2; AAF22490)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..183
FT /note="YI -> SL (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="A -> P (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="Y -> I (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="D -> E (in Ref. 2; AAF22490)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Y -> I (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="T -> S (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 451..452
FT /note="DM -> AL (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
FT CONFLICT 476..477
FT /note="ES -> SP (in Ref. 2; AAF22490)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="I -> F (in Ref. 1; AAC78804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 64815 MW; 939C52B9D1157029 CRC64;
MRAQEDLEGR TQHETTRDPS TPLPTEPKFD MLYKIEDVPP WYLCILLGFQ HYLTCFSGTI
AVPFLLAEAL CVGHDQHMVS QLIGTIFTCV GITTLIQTTV GIRLPLFQAS AFAFLVPAKA
ILALERWKCP PEEEIYGNWS LPLNTSHIWH PRIREVQGAI MVSSVVEVVI GLLGLPGALL
NYIGPLTVTP TVSLIGLSVF QAAGDRAGSH WGISACSILL IILFSQYLRN LTFLLPVYRW
GKGLTLLRIQ IFKMFPIMLA IMTVWLLCYV LTLTDVLPTD PKAYGFQART DARGDIMAIA
PWIRIPYPCQ WGLPTVTAAA VLGMFSATLA GIIESIGDYY ACARLAGAPP PPVHAINRGI
FTEGICCIIA GLLGTGNGST SSSPNIGVLG ITKVGSRRVV QYGAAIMLVL GTIGKFTALF
ASLPDPILGG MFCTLFGMIT AVGLSNLQFV DMNSSRNLFV LGFSMFFGLT LPNYLESNPG
AINTGILEVD QILIVLLTTE MFVGGCLAFI LDNTVPGSPE ERGLIQWKAG AHANSDMSSS
LKSYDFPIGM GIVKRITFLK YIPICPVFKG FSSSSKDQIA IPEDTPENTE TASVCTKV
