VMAT1_HUMAN
ID VMAT1_HUMAN Reviewed; 525 AA.
AC P54219; E9PDJ5; Q9BRE4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Chromaffin granule amine transporter;
DE AltName: Full=Solute carrier family 18 member 1;
DE AltName: Full=Vesicular amine transporter 1;
DE Short=VAT1;
GN Name=SLC18A1; Synonyms=VAT1, VMAT1;
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), FUNCTION, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pheochromocytoma;
RX PubMed=8643547; DOI=10.1073/pnas.93.10.5166;
RA Erickson J.D., Schaefer M.K.-H., Bonner T.I., Eiden L.E., Weihe E.;
RT "Distinct pharmacological properties and distribution in neurons and
RT endocrine cells of two isoforms of the human vesicular monoamine
RT transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5166-5171(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS PRO-4 AND
RP THR-136.
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 445-472 (ISOFORM 2), FUNCTION, ALTERNATIVE
RP SPLICING, AND SUBCELLULAR LOCATION.
RX PubMed=16326835; DOI=10.1677/jme.1.01875;
RA Essand M., Vikman S., Grawe J., Gedda L., Hellberg C., Oberg K.,
RA Totterman T.H., Giandomenico V.;
RT "Identification and characterization of a novel splicing variant of
RT vesicular monoamine transporter 1.";
RL J. Mol. Endocrinol. 35:489-501(2005).
CC -!- FUNCTION: Involved in the transport of biogenic monoamines, such as
CC serotonin, from the cytoplasm into the secretory vesicles of
CC neuroendocrine and endocrine cells. {ECO:0000269|PubMed:16326835,
CC ECO:0000269|PubMed:8643547}.
CC -!- ACTIVITY REGULATION: Strongly inhibited by reserpine. Also inhibited to
CC a lesser extent by ketanserin and fenfluramine. Not significantly
CC inhibited by tetrabenazine. {ECO:0000269|PubMed:8643547}.
CC -!- INTERACTION:
CC P54219-3; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-17595455, EBI-11522760;
CC P54219-3; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-17595455, EBI-12109402;
CC P54219-3; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-17595455, EBI-4290634;
CC P54219-3; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-17595455, EBI-12244618;
CC P54219-3; O14523: C2CD2L; NbExp=3; IntAct=EBI-17595455, EBI-12822627;
CC P54219-3; P13236: CCL4; NbExp=3; IntAct=EBI-17595455, EBI-2873970;
CC P54219-3; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-17595455, EBI-10271156;
CC P54219-3; O95406: CNIH1; NbExp=3; IntAct=EBI-17595455, EBI-12172273;
CC P54219-3; P29400-2: COL4A5; NbExp=3; IntAct=EBI-17595455, EBI-12211159;
CC P54219-3; O14569: CYB561D2; NbExp=3; IntAct=EBI-17595455, EBI-717654;
CC P54219-3; Q92520: FAM3C; NbExp=3; IntAct=EBI-17595455, EBI-2876774;
CC P54219-3; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-17595455, EBI-12175685;
CC P54219-3; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-17595455, EBI-11991950;
CC P54219-3; P29033: GJB2; NbExp=3; IntAct=EBI-17595455, EBI-3905204;
CC P54219-3; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-17595455, EBI-11955647;
CC P54219-3; O43561-2: LAT; NbExp=3; IntAct=EBI-17595455, EBI-8070286;
CC P54219-3; Q13021: MALL; NbExp=3; IntAct=EBI-17595455, EBI-750078;
CC P54219-3; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-17595455, EBI-2858252;
CC P54219-3; O43451: MGAM; NbExp=3; IntAct=EBI-17595455, EBI-2829774;
CC P54219-3; P30301: MIP; NbExp=3; IntAct=EBI-17595455, EBI-8449636;
CC P54219-3; P11836: MS4A1; NbExp=3; IntAct=EBI-17595455, EBI-2808234;
CC P54219-3; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-17595455, EBI-12070086;
CC P54219-3; Q99519: NEU1; NbExp=3; IntAct=EBI-17595455, EBI-721517;
CC P54219-3; Q8IXM6: NRM; NbExp=3; IntAct=EBI-17595455, EBI-10262547;
CC P54219-3; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-17595455, EBI-2804156;
CC P54219-3; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-17595455, EBI-1054848;
CC P54219-3; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-17595455, EBI-981985;
CC P54219-3; P60201-2: PLP1; NbExp=3; IntAct=EBI-17595455, EBI-12188331;
CC P54219-3; Q04941: PLP2; NbExp=3; IntAct=EBI-17595455, EBI-608347;
CC P54219-3; Q01453: PMP22; NbExp=3; IntAct=EBI-17595455, EBI-2845982;
CC P54219-3; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-17595455, EBI-8652812;
CC P54219-3; Q59EV6: PPGB; NbExp=3; IntAct=EBI-17595455, EBI-14210385;
CC P54219-3; Q9NS64: RPRM; NbExp=3; IntAct=EBI-17595455, EBI-1052363;
CC P54219-3; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-17595455, EBI-8644112;
CC P54219-3; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-17595455, EBI-10262251;
CC P54219-3; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-17595455, EBI-10281213;
CC P54219-3; Q2M3R5: SLC35G1; NbExp=3; IntAct=EBI-17595455, EBI-13311257;
CC P54219-3; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-17595455, EBI-10314552;
CC P54219-3; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-17595455, EBI-12898013;
CC P54219-3; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-17595455, EBI-8640191;
CC P54219-3; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-17595455, EBI-12188413;
CC P54219-3; P32856-2: STX2; NbExp=3; IntAct=EBI-17595455, EBI-11956649;
CC P54219-3; Q9UNK0: STX8; NbExp=3; IntAct=EBI-17595455, EBI-727240;
CC P54219-3; P02786: TFRC; NbExp=3; IntAct=EBI-17595455, EBI-355727;
CC P54219-3; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-17595455, EBI-10171534;
CC P54219-3; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-17595455, EBI-10694905;
CC P54219-3; Q9Y6G1: TMEM14A; NbExp=3; IntAct=EBI-17595455, EBI-2800360;
CC P54219-3; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-17595455, EBI-8638294;
CC P54219-3; Q969S6: TMEM203; NbExp=3; IntAct=EBI-17595455, EBI-12274070;
CC P54219-3; A2RU14: TMEM218; NbExp=3; IntAct=EBI-17595455, EBI-10173151;
CC P54219-3; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-17595455, EBI-11528917;
CC P54219-3; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-17595455, EBI-12038591;
CC P54219-3; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-17595455, EBI-2852148;
CC P54219-3; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-17595455, EBI-6656213;
CC P54219-3; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-17595455, EBI-12015604;
CC P54219-3; O95183: VAMP5; NbExp=3; IntAct=EBI-17595455, EBI-10191195;
CC P54219-3; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-17595455, EBI-751253;
CC P54219-3; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-17595455, EBI-751210;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:16326835, ECO:0000269|PubMed:8643547}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16326835}. Cytoplasmic vesicle,
CC secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:Q8R090}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16326835}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16326835}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P54219-1; Sequence=Displayed;
CC Name=2; Synonyms=VMAT1delta15;
CC IsoId=P54219-2; Sequence=VSP_046305;
CC Name=3;
CC IsoId=P54219-3; Sequence=VSP_046304;
CC -!- TISSUE SPECIFICITY: Highly expressed in chromaffin cells of the adrenal
CC medulla (at protein level). Detected in peripheral sympathetic ganglia
CC (at protein level). Found in some paracrine cells in stomach and
CC duodenum (at protein level). {ECO:0000269|PubMed:8643547}.
CC -!- MISCELLANEOUS: [Isoform 2]: Unable to uptake serotonin. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC transporter family. {ECO:0000305}.
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DR EMBL; U39905; AAC50472.1; -; mRNA.
DR EMBL; AC025853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006317; AAH06317.1; -; mRNA.
DR CCDS; CCDS47814.1; -. [P54219-3]
DR CCDS; CCDS47815.1; -. [P54219-2]
DR CCDS; CCDS6013.1; -. [P54219-1]
DR RefSeq; NP_001129163.1; NM_001135691.2. [P54219-1]
DR RefSeq; NP_001135796.1; NM_001142324.1. [P54219-3]
DR RefSeq; NP_001135797.1; NM_001142325.1. [P54219-2]
DR RefSeq; NP_003044.1; NM_003053.3. [P54219-1]
DR RefSeq; XP_011542928.1; XM_011544626.1. [P54219-3]
DR RefSeq; XP_011542929.1; XM_011544627.1.
DR AlphaFoldDB; P54219; -.
DR SMR; P54219; -.
DR BioGRID; 112458; 125.
DR IntAct; P54219; 104.
DR STRING; 9606.ENSP00000387549; -.
DR BindingDB; P54219; -.
DR ChEMBL; CHEMBL1838; -.
DR DrugBank; DB01363; Ephedra sinica root.
DR DrugBank; DB01577; Metamfetamine.
DR DrugBank; DB01442; MMDA.
DR DrugBank; DB00368; Norepinephrine.
DR DrugBank; DB00206; Reserpine.
DR DrugCentral; P54219; -.
DR GuidetoPHARMACOLOGY; 1011; -.
DR TCDB; 2.A.1.2.12; the major facilitator superfamily (mfs).
DR GlyGen; P54219; 3 sites.
DR iPTMnet; P54219; -.
DR PhosphoSitePlus; P54219; -.
DR BioMuta; SLC18A1; -.
DR DMDM; 1722741; -.
DR MassIVE; P54219; -.
DR PaxDb; P54219; -.
DR PeptideAtlas; P54219; -.
DR PRIDE; P54219; -.
DR ProteomicsDB; 19679; -.
DR ProteomicsDB; 56654; -. [P54219-1]
DR Antibodypedia; 1514; 177 antibodies from 32 providers.
DR DNASU; 6570; -.
DR Ensembl; ENST00000265808.11; ENSP00000265808.7; ENSG00000036565.15. [P54219-3]
DR Ensembl; ENST00000276373.10; ENSP00000276373.5; ENSG00000036565.15. [P54219-1]
DR Ensembl; ENST00000381608.8; ENSP00000371021.4; ENSG00000036565.15. [P54219-2]
DR Ensembl; ENST00000437980.3; ENSP00000413361.1; ENSG00000036565.15. [P54219-2]
DR Ensembl; ENST00000440926.3; ENSP00000387549.1; ENSG00000036565.15. [P54219-1]
DR Ensembl; ENST00000519026.5; ENSP00000429664.1; ENSG00000036565.15. [P54219-3]
DR GeneID; 6570; -.
DR KEGG; hsa:6570; -.
DR MANE-Select; ENST00000276373.10; ENSP00000276373.5; NM_003053.4; NP_003044.1.
DR UCSC; uc003wzm.3; human. [P54219-1]
DR CTD; 6570; -.
DR DisGeNET; 6570; -.
DR GeneCards; SLC18A1; -.
DR HGNC; HGNC:10934; SLC18A1.
DR HPA; ENSG00000036565; Tissue enriched (adrenal).
DR MIM; 193002; gene.
DR neXtProt; NX_P54219; -.
DR OpenTargets; ENSG00000036565; -.
DR PharmGKB; PA324; -.
DR VEuPathDB; HostDB:ENSG00000036565; -.
DR eggNOG; KOG3764; Eukaryota.
DR GeneTree; ENSGT00940000159352; -.
DR HOGENOM; CLU_001265_10_9_1; -.
DR InParanoid; P54219; -.
DR OMA; FGWCVDR; -.
DR PhylomeDB; P54219; -.
DR TreeFam; TF313494; -.
DR PathwayCommons; P54219; -.
DR Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters.
DR SignaLink; P54219; -.
DR SIGNOR; P54219; -.
DR BioGRID-ORCS; 6570; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; SLC18A1; human.
DR GenomeRNAi; 6570; -.
DR Pharos; P54219; Tchem.
DR PRO; PR:P54219; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P54219; protein.
DR Bgee; ENSG00000036565; Expressed in rectum and 56 other tissues.
DR ExpressionAtlas; P54219; baseline and differential.
DR Genevisible; P54219; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0070083; C:clathrin-sculpted monoamine transport vesicle membrane; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0008504; F:monoamine transmembrane transporter activity; TAS:UniProtKB.
DR GO; GO:0005335; F:serotonin:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; IBA:GO_Central.
DR GO; GO:0015844; P:monoamine transport; TAS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004734; Multidrug-R.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00880; 2_A_01_02; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Neurotransmitter transport; Reference proteome;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..525
FT /note="Chromaffin granule amine transporter"
FT /id="PRO_0000127510"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..138
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..197
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..256
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..335
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..397
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..448
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 503..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 307..338
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046304"
FT VAR_SEQ 445..525
FT /note="PSTGGAIVKAIGFPWLMVITGVINIVYAPLCYYLRSPPAKEEKLAILSQDCP
FT METRMYATQKPTKEFPLGEDSDEEPDHEE -> YSESGLPHGDPDVCNPEAHEGISSGG
FT GQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16326835"
FT /id="VSP_046305"
FT VARIANT 4
FT /note="T -> P (in dbSNP:rs2270641)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_021856"
FT VARIANT 11
FT /note="R -> Q (in dbSNP:rs17092144)"
FT /id="VAR_052002"
FT VARIANT 74
FT /note="A -> V (in dbSNP:rs17215815)"
FT /id="VAR_024632"
FT VARIANT 82
FT /note="F -> C (in dbSNP:rs17215822)"
FT /id="VAR_029149"
FT VARIANT 84
FT /note="F -> S (in dbSNP:rs17215801)"
FT /id="VAR_024633"
FT VARIANT 98
FT /note="S -> T (in dbSNP:rs2270637)"
FT /id="VAR_020033"
FT VARIANT 101
FT /note="A -> P (in dbSNP:rs17222218)"
FT /id="VAR_024634"
FT VARIANT 136
FT /note="I -> T (in dbSNP:rs1390938)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_012065"
FT VARIANT 140
FT /note="G -> R (in dbSNP:rs17215808)"
FT /id="VAR_029150"
FT VARIANT 164
FT /note="I -> M (in dbSNP:rs17222092)"
FT /id="VAR_024635"
FT VARIANT 202
FT /note="I -> T (in dbSNP:rs17222120)"
FT /id="VAR_029151"
FT VARIANT 249
FT /note="V -> I (in dbSNP:rs17215759)"
FT /id="VAR_024636"
FT VARIANT 392
FT /note="L -> V (in dbSNP:rs17092104)"
FT /id="VAR_024637"
SQ SEQUENCE 525 AA; 56257 MW; 041F2959F4F2BFBC CRC64;
MLRTILDAPQ RLLKEGRASR QLVLVVVFVA LLLDNMLFTV VVPIVPTFLY DMEFKEVNSS
LHLGHAGSSP HALASPAFST IFSFFNNNTV AVEESVPSGI AWMNDTASTI PPPATEAISA
HKNNCLQGTG FLEEEITRVG VLFASKAVMQ LLVNPFVGPL TNRIGYHIPM FAGFVIMFLS
TVMFAFSGTY TLLFVARTLQ GIGSSFSSVA GLGMLASVYT DDHERGRAMG TALGGLALGL
LVGAPFGSVM YEFVGKSAPF LILAFLALLD GALQLCILQP SKVSPESAKG TPLFMLLKDP
YILVAAGSIC FANMGVAILE PTLPIWMMQT MCSPKWQLGL AFLPASVSYL IGTNLFGVLA
NKMGRWLCSL IGMLVVGTSL LCVPLAHNIF GLIGPNAGLG LAIGMVDSSM MPIMGHLVDL
RHTSVYGSVY AIADVAFCMG FAIGPSTGGA IVKAIGFPWL MVITGVINIV YAPLCYYLRS
PPAKEEKLAI LSQDCPMETR MYATQKPTKE FPLGEDSDEE PDHEE
