TRPM3_HUMAN
ID TRPM3_HUMAN Reviewed; 1732 AA.
AC Q9HCF6; A2A3F6; A9Z1Y7; Q5VW02; Q5VW03; Q5VW04; Q5W5T7; Q86SH0; Q86SH6;
AC Q86UL0; Q86WK1; Q86WK2; Q86WK3; Q86WK4; Q86YZ9; Q86Z00; Q86Z01; Q9H0X2;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 3;
DE AltName: Full=Long transient receptor potential channel 3;
DE Short=LTrpC-3;
DE Short=LTrpC3;
DE AltName: Full=Melastatin-2;
DE Short=MLSN2;
GN Name=TRPM3; Synonyms=KIAA1616, LTRPC3;
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] (ISOFORMS 2 AND 10), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12672799; DOI=10.1074/jbc.m300945200;
RA Grimm C., Kraft R., Sauerbruch S., Schultz G., Harteneck C.;
RT "Molecular and functional characterization of the melastatin-related cation
RT channel TRPM3.";
RL J. Biol. Chem. 278:21493-21501(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12).
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 [LARGE SCALE MRNA] OF 1-324 (ISOFORM 11).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 154-1732 (ISOFORMS 1; 2; 3; 4; 5 AND 6),
RP VARIANT THR-1732, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12672827; DOI=10.1074/jbc.m211232200;
RA Lee N., Chen J., Sun L., Wu S., Gray K.R., Rich A., Huang M., Lin J.-H.,
RA Feder J.N., Janovitz E.B., Levesque P.C., Blanar M.A.;
RT "Expression and characterization of human transient receptor potential
RT melastatin 3 (hTRPM3).";
RL J. Biol. Chem. 278:20890-20897(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-1732 (ISOFORMS 1; 2; 4; 7 AND
RP 8), AND VARIANT THR-1732.
RC TISSUE=Brain;
RA Okabayashi K., Hirano K., Sano M., Murahashi Y., Miyauchi A., Gonoi T.;
RT "ProX human full-length cDNA cloning project.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 716-1732 (ISOFORMS
RP 1/2/3/4/5/7/8), AND VARIANTS LYS-1717 AND THR-1732.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [8]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH TRPM3, AND SUBCELLULAR LOCATION.
RX PubMed=21278253; DOI=10.1074/jbc.m110.202945;
RA Lambert S., Drews A., Rizun O., Wagner T.F., Lis A., Mannebach S.,
RA Plant S., Portz M., Meissner M., Philipp S.E., Oberwinkler J.;
RT "Transient receptor potential melastatin 1 (TRPM1) is an ion-conducting
RT plasma membrane channel inhibited by zinc ions.";
RL J. Biol. Chem. 286:12221-12233(2011).
CC -!- FUNCTION: Calcium channel mediating constitutive calcium ion entry. Its
CC activity is increased by reduction in extracellular osmolarity, by
CC store depletion and muscarinic receptor activation. In addition, forms
CC heteromultimeric ion channels with TRPM1 which are permeable for
CC calcium and zinc ions (PubMed:21278253). {ECO:0000269|PubMed:12672799,
CC ECO:0000269|PubMed:12672827, ECO:0000269|PubMed:21278253}.
CC -!- SUBUNIT: Interacts with TRPM1; the interaction results in the formation
CC of a heteromultimeric cation channel complex.
CC {ECO:0000269|PubMed:21278253}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12672827,
CC ECO:0000305|PubMed:21278253}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12672827}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=1; Synonyms=TRPM3f;
CC IsoId=Q9HCF6-1; Sequence=Displayed;
CC Name=2; Synonyms=TRPM3a;
CC IsoId=Q9HCF6-2; Sequence=VSP_012826;
CC Name=3; Synonyms=TRPM3b;
CC IsoId=Q9HCF6-3; Sequence=VSP_012826, VSP_012828;
CC Name=4; Synonyms=TRPM3d;
CC IsoId=Q9HCF6-4; Sequence=VSP_012826, VSP_012829;
CC Name=5; Synonyms=TRPM3e;
CC IsoId=Q9HCF6-5; Sequence=VSP_012826, VSP_012828, VSP_012829;
CC Name=6; Synonyms=TRPM3c;
CC IsoId=Q9HCF6-6; Sequence=VSP_012826, VSP_012830;
CC Name=7;
CC IsoId=Q9HCF6-7; Sequence=VSP_012829;
CC Name=8;
CC IsoId=Q9HCF6-8; Sequence=VSP_012826, VSP_012827, VSP_012829;
CC Name=10;
CC IsoId=Q9HCF6-10; Sequence=VSP_012826, VSP_012831, VSP_012832;
CC Name=11;
CC IsoId=Q9HCF6-11; Sequence=VSP_039107;
CC Name=12;
CC IsoId=Q9HCF6-12; Sequence=VSP_043515, VSP_012826, VSP_043516;
CC -!- TISSUE SPECIFICITY: Expressed primarily in the kidney and, at lower
CC levels, in brain, testis, ovary, pancreas and spinal cord. Expression
CC in the brain and kidney was determined at protein level. In the kidney,
CC expressed predominantly in the collecting tubular epithelium in the
CC medulla, medullary rays, and periglomerular regions; in the brain,
CC highest levels are found in the cerebellum, choroid plexus, the locus
CC coeruleus, the posterior thalamus and the substantia nigra. Down-
CC regulated in renal tumors compared to normal kidney.
CC {ECO:0000269|PubMed:12672799, ECO:0000269|PubMed:12672827}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. LTrpC
CC subfamily. TRPM3 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66480.2; Type=Miscellaneous discrepancy; Note=Cloning artifact in C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ505025; CAD43604.1; -; mRNA.
DR EMBL; AJ505026; CAD43605.1; -; mRNA.
DR EMBL; AL159990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL442645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC121821; AAI21822.2; -; mRNA.
DR EMBL; BC134414; AAI34415.1; -; mRNA.
DR EMBL; BC142972; AAI42973.1; -; mRNA.
DR EMBL; AL136545; CAB66480.2; ALT_SEQ; mRNA.
DR EMBL; AF536748; AAO49153.1; -; mRNA.
DR EMBL; AF536749; AAO49154.1; -; mRNA.
DR EMBL; AF536750; AAO49155.1; -; mRNA.
DR EMBL; AF536751; AAO49156.1; -; mRNA.
DR EMBL; AF536752; AAO49157.1; -; mRNA.
DR EMBL; AF536753; AAO49158.1; -; mRNA.
DR EMBL; AB099661; BAC55102.1; -; mRNA.
DR EMBL; AB099662; BAC55103.1; -; mRNA.
DR EMBL; AB099663; BAC55104.1; -; mRNA.
DR EMBL; AB099664; BAC55105.1; -; mRNA.
DR EMBL; AB099665; BAC55106.1; -; mRNA.
DR EMBL; AB046836; BAB13442.1; -; mRNA.
DR CCDS; CCDS43835.1; -. [Q9HCF6-2]
DR CCDS; CCDS6637.1; -. [Q9HCF6-12]
DR RefSeq; NP_001007472.2; NM_001007471.2. [Q9HCF6-2]
DR RefSeq; NP_996831.1; NM_206948.2. [Q9HCF6-12]
DR RefSeq; XP_011517340.1; XM_011519038.2. [Q9HCF6-1]
DR RefSeq; XP_011517341.1; XM_011519039.2. [Q9HCF6-7]
DR RefSeq; XP_011517343.1; XM_011519041.2.
DR RefSeq; XP_011517346.1; XM_011519044.2.
DR RefSeq; XP_011517348.1; XM_011519046.2. [Q9HCF6-4]
DR RefSeq; XP_011517349.1; XM_011519047.2.
DR RefSeq; XP_016870631.1; XM_017015142.1.
DR AlphaFoldDB; Q9HCF6; -.
DR SMR; Q9HCF6; -.
DR BioGRID; 123085; 26.
DR IntAct; Q9HCF6; 5.
DR STRING; 9606.ENSP00000366314; -.
DR ChEMBL; CHEMBL3559708; -.
DR DrugBank; DB00794; Primidone.
DR GuidetoPHARMACOLOGY; 495; -.
DR TCDB; 1.A.4.5.6; the transient receptor potential ca(2+) channel (trp-cc) family.
DR iPTMnet; Q9HCF6; -.
DR PhosphoSitePlus; Q9HCF6; -.
DR BioMuta; TRPM3; -.
DR DMDM; 322510140; -.
DR EPD; Q9HCF6; -.
DR MassIVE; Q9HCF6; -.
DR MaxQB; Q9HCF6; -.
DR PaxDb; Q9HCF6; -.
DR PeptideAtlas; Q9HCF6; -.
DR PRIDE; Q9HCF6; -.
DR ProteomicsDB; 81697; -. [Q9HCF6-1]
DR ProteomicsDB; 81698; -. [Q9HCF6-10]
DR ProteomicsDB; 81699; -. [Q9HCF6-11]
DR ProteomicsDB; 81701; -. [Q9HCF6-2]
DR ProteomicsDB; 81702; -. [Q9HCF6-3]
DR ProteomicsDB; 81703; -. [Q9HCF6-4]
DR ProteomicsDB; 81704; -. [Q9HCF6-5]
DR ProteomicsDB; 81705; -. [Q9HCF6-6]
DR ProteomicsDB; 81706; -. [Q9HCF6-7]
DR ProteomicsDB; 81707; -. [Q9HCF6-8]
DR Antibodypedia; 12418; 164 antibodies from 19 providers.
DR DNASU; 80036; -.
DR Ensembl; ENST00000361823.9; ENSP00000355395.4; ENSG00000083067.24. [Q9HCF6-12]
DR Ensembl; ENST00000377110.9; ENSP00000366314.4; ENSG00000083067.24. [Q9HCF6-2]
DR Ensembl; ENST00000377111.8; ENSP00000366315.4; ENSG00000083067.24. [Q9HCF6-10]
DR Ensembl; ENST00000677713.2; ENSP00000503830.2; ENSG00000083067.24. [Q9HCF6-3]
DR GeneID; 80036; -.
DR KEGG; hsa:80036; -.
DR MANE-Select; ENST00000677713.2; ENSP00000503830.2; NM_001366145.2; NP_001353074.1. [Q9HCF6-3]
DR UCSC; uc004aic.4; human. [Q9HCF6-1]
DR CTD; 80036; -.
DR DisGeNET; 80036; -.
DR GeneCards; TRPM3; -.
DR HGNC; HGNC:17992; TRPM3.
DR HPA; ENSG00000083067; Tissue enriched (choroid).
DR MalaCards; TRPM3; -.
DR MIM; 608961; gene.
DR neXtProt; NX_Q9HCF6; -.
DR OpenTargets; ENSG00000083067; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR PharmGKB; PA38271; -.
DR VEuPathDB; HostDB:ENSG00000083067; -.
DR eggNOG; KOG3614; Eukaryota.
DR GeneTree; ENSGT00940000157366; -.
DR HOGENOM; CLU_001390_4_1_1; -.
DR InParanoid; Q9HCF6; -.
DR OMA; EAQADCE; -.
DR OrthoDB; 738147at2759; -.
DR PhylomeDB; Q9HCF6; -.
DR TreeFam; TF314204; -.
DR PathwayCommons; Q9HCF6; -.
DR Reactome; R-HSA-3295583; TRP channels.
DR SignaLink; Q9HCF6; -.
DR BioGRID-ORCS; 80036; 6 hits in 1070 CRISPR screens.
DR ChiTaRS; TRPM3; human.
DR GeneWiki; TRPM3; -.
DR GenomeRNAi; 80036; -.
DR Pharos; Q9HCF6; Tchem.
DR PRO; PR:Q9HCF6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9HCF6; protein.
DR Bgee; ENSG00000083067; Expressed in pigmented layer of retina and 141 other tissues.
DR ExpressionAtlas; Q9HCF6; baseline and differential.
DR Genevisible; Q9HCF6; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005227; F:calcium activated cation channel activity; IEA:InterPro.
DR GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
DR GO; GO:0005261; F:cation channel activity; IDA:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; IDA:MGI.
DR GO; GO:0016048; P:detection of temperature stimulus; IEA:InterPro.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0050951; P:sensory perception of temperature stimulus; IEA:InterPro.
DR Gene3D; 1.20.5.1010; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR029583; TRPM3.
DR InterPro; IPR041491; TRPM_SLOG.
DR InterPro; IPR032415; TRPM_tetra.
DR InterPro; IPR037162; TRPM_tetra_sf.
DR PANTHER; PTHR13800:SF7; PTHR13800:SF7; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR Pfam; PF16519; TRPM_tetra; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Coiled coil; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1732
FT /note="Transient receptor potential cation channel
FT subfamily M member 3"
FT /id="PRO_0000215328"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..794
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 816..897
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 919..964
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 965..985
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 986..995
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1028
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1029..1049
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1050..1116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1117..1137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1138..1732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1459..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1241..1301
FT /evidence="ECO:0000255"
FT COMPBIAS 1459..1474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043515"
FT VAR_SEQ 1..59
FT /note="MPEPWGTVYFLGIAQVFSFLFSWWNLEGVMNQADAPRPLNWTIRKLCHAAFL
FT PSVRLLK -> MGKKWRDAAEMERGCSDREDNAESRRRSRSASRGRFAESWKRLSSKQG
FT STKRSGLPSQQTP (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_039107"
FT VAR_SEQ 326..350
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6, isoform 8, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:12672799,
FT ECO:0000303|PubMed:12672827, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.6"
FT /id="VSP_012826"
FT VAR_SEQ 409..1732
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043516"
FT VAR_SEQ 535..552
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_012827"
FT VAR_SEQ 569
FT /note="K -> KREYPGFGWIYFK (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12672827"
FT /id="VSP_012828"
FT VAR_SEQ 617..626
FT /note="Missing (in isoform 4, isoform 5, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:12672827, ECO:0000303|Ref.6"
FT /id="VSP_012829"
FT VAR_SEQ 1088
FT /note="P -> RKQVYDSHTPKSA (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12672827"
FT /id="VSP_012830"
FT VAR_SEQ 1344..1350
FT /note="GEETMSP -> EHPLYSV (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:12672799"
FT /id="VSP_012831"
FT VAR_SEQ 1351..1732
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:12672799"
FT /id="VSP_012832"
FT VARIANT 1653
FT /note="T -> I (in dbSNP:rs13440436)"
FT /id="VAR_057305"
FT VARIANT 1695
FT /note="R -> Q (in dbSNP:rs6560142)"
FT /id="VAR_021257"
FT VARIANT 1717
FT /note="R -> K (in dbSNP:rs41287373)"
FT /evidence="ECO:0000269|PubMed:10997877"
FT /id="VAR_061862"
FT VARIANT 1732
FT /note="N -> T (in dbSNP:rs17535963)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:12672827, ECO:0000269|Ref.6"
FT /id="VAR_057306"
FT CONFLICT 335
FT /note="R -> H (in Ref. 6; BAC55103)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="C -> Y (in Ref. 6; BAC55106)"
FT /evidence="ECO:0000305"
FT CONFLICT 1032
FT /note="D -> E (in Ref. 6; BAC55106)"
FT /evidence="ECO:0000305"
FT CONFLICT 1730
FT /note="K -> Q (in Ref. 6; BAC55104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1732 AA; 197571 MW; 0D6BE312C56646A4 CRC64;
MPEPWGTVYF LGIAQVFSFL FSWWNLEGVM NQADAPRPLN WTIRKLCHAA FLPSVRLLKA
QKSWIERAFY KRECVHIIPS TKDPHRCCCG RLIGQHVGLT PSISVLQNEK NESRLSRNDI
QSEKWSISKH TQLSPTDAFG TIEFQGGGHS NKAMYVRVSF DTKPDLLLHL MTKEWQLELP
KLLISVHGGL QNFELQPKLK QVFGKGLIKA AMTTGAWIFT GGVNTGVIRH VGDALKDHAS
KSRGKICTIG IAPWGIVENQ EDLIGRDVVR PYQTMSNPMS KLTVLNSMHS HFILADNGTT
GKYGAEVKLR RQLEKHISLQ KINTRCLPFF SLDSRLFYSF WGSCQLDSVG IGQGVPVVAL
IVEGGPNVIS IVLEYLRDTP PVPVVVCDGS GRASDILAFG HKYSEEGGLI NESLRDQLLV
TIQKTFTYTR TQAQHLFIIL MECMKKKELI TVFRMGSEGH QDIDLAILTA LLKGANASAP
DQLSLALAWN RVDIARSQIF IYGQQWPVGS LEQAMLDALV LDRVDFVKLL IENGVSMHRF
LTISRLEELY NTRHGPSNTL YHLVRDVKKG NLPPDYRISL IDIGLVIEYL MGGAYRCNYT
RKRFRTLYHN LFGPKRPKAL KLLGMEDDIP LRRGRKTTKK REEEVDIDLD DPEINHFPFP
FHELMVWAVL MKRQKMALFF WQHGEEAMAK ALVACKLCKA MAHEASENDM VDDISQELNH
NSRDFGQLAV ELLDQSYKQD EQLAMKLLTY ELKNWSNATC LQLAVAAKHR DFIAHTCSQM
LLTDMWMGRL RMRKNSGLKV ILGILLPPSI LSLEFKNKDD MPYMSQAQEI HLQEKEAEEP
EKPTKEKEEE DMELTAMLGR NNGESSRKKD EEEVQSKHRL IPLGRKIYEF YNAPIVKFWF
YTLAYIGYLM LFNYIVLVKM ERWPSTQEWI VISYIFTLGI EKMREILMSE PGKLLQKVKV
WLQEYWNVTD LIAILLFSVG MILRLQDQPF RSDGRVIYCV NIIYWYIRLL DIFGVNKYLG
PYVMMIGKMM IDMMYFVIIM LVVLMSFGVA RQAILFPNEE PSWKLAKNIF YMPYWMIYGE
VFADQIDPPC GQNETREDGK IIQLPPCKTG AWIVPAIMAC YLLVANILLV NLLIAVFNNT
FFEVKSISNQ VWKFQRYQLI MTFHERPVLP PPLIIFSHMT MIFQHLCCRW RKHESDPDER
DYGLKLFITD DELKKVHDFE EQCIEEYFRE KDDRFNSSND ERIRVTSERV ENMSMRLEEV
NEREHSMKAS LQTVDIRLAQ LEDLIGRMAT ALERLTGLER AESNKIRSRT SSDCTDAAYI
VRQSSFNSQE GNTFKLQESI DPAGEETMSP TSPTLMPRMR SHSFYSVNMK DKGGIEKLES
IFKERSLSLH RATSSHSVAK EPKAPAAPAN TLAIVPDSRR PSSCIDIYVS AMDELHCDID
PLDNSVNILG LGEPSFSTPV PSTAPSSSAY ATLAPTDRPP SRSIDFEDIT SMDTRSFSSD
YTHLPECQNP WDSEPPMYHT IERSKSSRYL ATTPFLLEEA PIVKSHSFMF SPSRSYYANF
GVPVKTAEYT SITDCIDTRC VNAPQAIADR AAFPGGLGDK VEDLTCCHPE REAELSHPSS
DSEENEAKGR RATIAISSQE GDNSERTLSN NITVPKIERA NSYSAEEPSA PYAHTRKSFS
ISDKLDRQRN TASLRNPFQR SKSSKPEGRG DSLSMRRLSR TSAFQSFESK HN
