TRPM1_MOUSE
ID TRPM1_MOUSE Reviewed; 1622 AA.
AC Q2TV84; O70334; Q2WEA6; Q3TPG5; Q3UEW7; Q3UFV6; Q3UFW1; Q3UG69; Q5U4B3;
AC Q640P5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 1;
DE AltName: Full=Long transient receptor potential channel 1;
DE Short=LTrpC1;
DE AltName: Full=Melastatin-1;
GN Name=Trpm1 {ECO:0000312|MGI:MGI:1330305}; Synonyms=Ltrpc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC13683.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9537257;
RA Duncan L.M., Deeds J., Hunter J., Shao J., Holmgren L.M., Woolf E.A.,
RA Tepper R.I., Shyjan A.W.;
RT "Down-regulation of the novel gene melastatin correlates with potential for
RT melanoma metastasis.";
RL Cancer Res. 58:1515-1520(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAI30140.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RC STRAIN=C57BL/6J X 129/SvJ {ECO:0000312|EMBL:CAI30140.1};
RC TISSUE=Eye {ECO:0000312|EMBL:CAI30140.1};
RX PubMed=15856355; DOI=10.1007/s00210-005-1050-x;
RA Lis A., Wissenbach U., Philipp S.E.;
RT "Transcriptional regulation and processing increase the functional
RT variability of TRPM channels.";
RL Naunyn Schmiedebergs Arch. Pharmacol. 371:315-324(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19966281; DOI=10.1073/pnas.0912730107;
RA Koike C., Obara T., Uriu Y., Numata T., Sanuki R., Miyata K., Koyasu T.,
RA Ueno S., Funabiki K., Tani A., Ueda H., Kondo M., Mori Y., Tachibana M.,
RA Furukawa T.;
RT "TRPM1 is a component of the retinal ON bipolar cell transduction channel
RT in the mGluR6 cascade.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:332-337(2010).
RN [4] {ECO:0000305}
RP SEQUENCE REVISION TO N-TERMINUS.
RA Koike C., Furukawa T.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAE28794.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-828 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE28794.1};
RC TISSUE=Embryonic eye {ECO:0000312|EMBL:BAE37771.1}, and
RC Retina {ECO:0000312|EMBL:BAE28794.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAH82560.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH82560.1};
RC TISSUE=Eye {ECO:0000312|EMBL:AAH82560.1};
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 [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19861548; DOI=10.1073/pnas.0908711106;
RA Morgans C.W., Zhang J., Jeffrey B.G., Nelson S.M., Burke N.S.,
RA Duvoisin R.M., Brown R.L.;
RT "TRPM1 is required for the depolarizing light response in retinal ON-
RT bipolar cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19174-19178(2009).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30027108; DOI=10.1523/eneuro.0143-18.2018;
RA Agosto M.A., Anastassov I.A., Robichaux M.A., Wensel T.G.;
RT "A Large Endoplasmic Reticulum-Resident Pool of TRPM1 in Retinal ON-Bipolar
RT Cells.";
RL ENeuro 5:0-0(2018).
CC -!- FUNCTION: Forms nonselective divalent cation-conducting channels which
CC mediate the influx of Na(2+), Ca(2+), Mg(2+), Mn(2+), Ba(2+), and
CC Ni(2+) into the cytoplasm, leading to membrane depolarization (By
CC similarity). Impermeable to zinc ions (By similarity). In addition,
CC forms heteromultimeric ion channels with TRPM3 which are permeable for
CC calcium and zinc ions (By similarity). Essential for the depolarizing
CC photoresponse of retinal ON bipolar cells. It is part of the GRM6
CC signaling cascade. Calcium channel which may play a role in metastasis
CC suppression. May act as a spontaneously active, calcium-permeable
CC plasma membrane channel. {ECO:0000250|UniProtKB:Q7Z4N2,
CC ECO:0000269|PubMed:19861548, ECO:0000269|PubMed:19966281,
CC ECO:0000269|PubMed:9537257}.
CC -!- ACTIVITY REGULATION: Inhibited by zinc ions.
CC {ECO:0000250|UniProtKB:Q7Z4N2}.
CC -!- SUBUNIT: Interacts with TRPM3; the interaction results in the formation
CC of a heteromultimeric cation channel complex.
CC {ECO:0000250|UniProtKB:Q7Z4N2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255, ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000255, ECO:0000305}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:30027108}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7Z4N2}. Cell projection, axon
CC {ECO:0000269|PubMed:30027108}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q2TV84-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15856355};
CC IsoId=Q2TV84-2; Sequence=VSP_052753, VSP_052754;
CC Name=3 {ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:9537257};
CC IsoId=Q2TV84-3; Sequence=VSP_052752, VSP_052757, VSP_052758;
CC Name=4 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q2TV84-4; Sequence=VSP_052752, VSP_052755, VSP_052756;
CC Name=5 {ECO:0000269|PubMed:15489334};
CC IsoId=Q2TV84-5; Sequence=VSP_052751, VSP_052755, VSP_052756;
CC -!- TISSUE SPECIFICITY: Expressed in the retina where it localizes on
CC dendritic tips of ON bipolar cells. Specifically, it is expressed in
CC retinal bipolar cells (BPCs) of the ON subtype (PubMed:30027108). Not
CC detected in brain, lung, liver, heart, kidney, spleen or small
CC intestine. Also expressed at high levels in poorly metastatic variants
CC of B16 melanoma and at much reduced levels in highly metastatic
CC variants of B16 melanoma. {ECO:0000269|PubMed:19861548,
CC ECO:0000269|PubMed:19966281, ECO:0000269|PubMed:30027108,
CC ECO:0000269|PubMed:9537257}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. LTrpC
CC subfamily. TRPM1 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF047714; AAC13683.1; -; mRNA.
DR EMBL; AJ867481; CAI30140.1; -; mRNA.
DR EMBL; AY180104; AAO43093.2; -; mRNA.
DR EMBL; AK148094; BAE28340.1; -; mRNA.
DR EMBL; AK148268; BAE28448.1; -; mRNA.
DR EMBL; AK148275; BAE28453.1; -; mRNA.
DR EMBL; AK149290; BAE28794.1; -; mRNA.
DR EMBL; AK164395; BAE37771.1; -; mRNA.
DR EMBL; AC127565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082560; AAH82560.1; -; mRNA.
DR EMBL; BC085168; AAH85168.1; -; mRNA.
DR CCDS; CCDS21332.2; -. [Q2TV84-1]
DR CCDS; CCDS39975.2; -. [Q2TV84-3]
DR RefSeq; NP_001034193.2; NM_001039104.2. [Q2TV84-1]
DR RefSeq; NP_061222.3; NM_018752.3. [Q2TV84-3]
DR RefSeq; XP_017177502.1; XM_017322013.1. [Q2TV84-3]
DR PDB; 6RMV; X-ray; 1.94 A; C=610-623.
DR PDBsum; 6RMV; -.
DR AlphaFoldDB; Q2TV84; -.
DR SMR; Q2TV84; -.
DR BioGRID; 201440; 1.
DR STRING; 10090.ENSMUSP00000082318; -.
DR GlyGen; Q2TV84; 1 site.
DR iPTMnet; Q2TV84; -.
DR PhosphoSitePlus; Q2TV84; -.
DR MaxQB; Q2TV84; -.
DR PaxDb; Q2TV84; -.
DR PRIDE; Q2TV84; -.
DR ProteomicsDB; 297522; -. [Q2TV84-1]
DR ProteomicsDB; 297523; -. [Q2TV84-2]
DR ProteomicsDB; 297524; -. [Q2TV84-3]
DR ProteomicsDB; 297525; -. [Q2TV84-4]
DR ProteomicsDB; 297526; -. [Q2TV84-5]
DR Antibodypedia; 9410; 82 antibodies from 22 providers.
DR DNASU; 17364; -.
DR Ensembl; ENSMUST00000085222; ENSMUSP00000082318; ENSMUSG00000030523. [Q2TV84-1]
DR Ensembl; ENSMUST00000177102; ENSMUSP00000134947; ENSMUSG00000030523. [Q2TV84-3]
DR Ensembl; ENSMUST00000205731; ENSMUSP00000145776; ENSMUSG00000030523. [Q2TV84-4]
DR Ensembl; ENSMUST00000206314; ENSMUSP00000145593; ENSMUSG00000030523. [Q2TV84-2]
DR Ensembl; ENSMUST00000206706; ENSMUSP00000146265; ENSMUSG00000030523. [Q2TV84-5]
DR GeneID; 17364; -.
DR KEGG; mmu:17364; -.
DR UCSC; uc009hfp.2; mouse. [Q2TV84-2]
DR UCSC; uc009hfr.2; mouse. [Q2TV84-4]
DR UCSC; uc009hft.2; mouse. [Q2TV84-5]
DR UCSC; uc009hfu.2; mouse. [Q2TV84-3]
DR UCSC; uc009hfw.2; mouse. [Q2TV84-1]
DR CTD; 4308; -.
DR MGI; MGI:1330305; Trpm1.
DR VEuPathDB; HostDB:ENSMUSG00000030523; -.
DR eggNOG; KOG3614; Eukaryota.
DR GeneTree; ENSGT00940000155024; -.
DR HOGENOM; CLU_022373_0_0_1; -.
DR InParanoid; Q2TV84; -.
DR OrthoDB; 738147at2759; -.
DR PhylomeDB; Q2TV84; -.
DR TreeFam; TF314204; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 17364; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Trpm1; mouse.
DR PRO; PR:Q2TV84; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q2TV84; protein.
DR Bgee; ENSMUSG00000030523; Expressed in iris and 67 other tissues.
DR ExpressionAtlas; Q2TV84; baseline and differential.
DR Genevisible; Q2TV84; MM.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0035841; C:new growing cell tip; IDA:MGI.
DR GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IDA:MGI.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:UniProtKB.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0046548; P:retinal rod cell development; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IGI:MGI.
DR GO; GO:0007601; P:visual perception; ISO:MGI.
DR Gene3D; 1.20.5.1010; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR029588; TRPM1.
DR InterPro; IPR041491; TRPM_SLOG.
DR InterPro; IPR032415; TRPM_tetra.
DR InterPro; IPR037162; TRPM_tetra_sf.
DR PANTHER; PTHR13800:SF13; PTHR13800:SF13; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR Pfam; PF16519; TRPM_tetra; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Coiled coil; Endoplasmic reticulum; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision.
FT CHAIN 1..1622
FT /note="Transient receptor potential cation channel
FT subfamily M member 1"
FT /id="PRO_0000328931"
FT TOPO_DOM 1..875
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 876..896
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 897..942
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 943..963
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 964..973
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 974..994
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 995..1006
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1007..1027
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1028..1099
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1100..1120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1121..1150
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1151..1171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1172..1622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1224..1252
FT /evidence="ECO:0000255"
FT COMPBIAS 1590..1613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052751"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9537257"
FT /id="VSP_052752"
FT VAR_SEQ 189
FT /note="G -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15856355"
FT /id="VSP_052753"
FT VAR_SEQ 190..1073
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15856355"
FT /id="VSP_052754"
FT VAR_SEQ 504..559
FT /note="NALEQAMLDALVLDRVDFVKLLIENGVNMQHFLTIPRLEELYNTRLGPPNTL
FT HLLV -> CAHVLVSLPVCLQSSGLAFPKFSGRDSLVTFASSLPGWGTDGLMSILHGNS
FT VFTSM (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052755"
FT VAR_SEQ 560..1622
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052756"
FT VAR_SEQ 612..658
FT /note="PKALKLLGMEDDEPPAKGKKKKKKKKEEEIDIDVDDPAVSRFQYPFH -> V
FT ELSRHTVSCASQSNMWFLDVLPQKPTCAECNSSPHLSQTDITPPLP (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9537257"
FT /id="VSP_052757"
FT VAR_SEQ 659..1622
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9537257"
FT /id="VSP_052758"
FT CONFLICT 160
FT /note="P -> S (in Ref. 1; AAC13683)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="S -> Y (in Ref. 5; BAE28794)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="T -> A (in Ref. 1; AAC13683 and 5; BAE28340/
FT BAE28448/BAE28453)"
FT /evidence="ECO:0000305"
FT CONFLICT 1481
FT /note="S -> G (in Ref. 1; CAI30140)"
FT /evidence="ECO:0000305"
FT HELIX 611..618
FT /evidence="ECO:0007829|PDB:6RMV"
SQ SEQUENCE 1622 AA; 183527 MW; FB4786BD92D4ED5E CRC64;
MGSMRKMSSS FKRGSIKSST SGSQKGQKAW IEKTFCKREC IFVIPSTKDP NRCCCGQLTN
QHIPPLPSGA PSTTGEDTKQ ADTQSGKWSV SKHTQSYPTD SYGILEFQGG GYSNKAMYIR
VSYDTKPDSL LHLMVKDWQL ELPKLLISVH GGLQSFEMQP KLKQVFGKGL IKAAMTTGAW
IFTGGVSTGV VSHVGDALKD HSSKSRGRLC AIGIAPWGMV ENKEDLIGKD VTRVYQTMSN
PLSKLSVLNN SHTHFILADN GTLGKYGAEV KLRRQLEKHI SLQKINTRLG QGVPVVGLVV
EGGPNVVSIV LEYLKEDPPV PVVVCDGSGR ASDILSFAHK YCDEGGVINE SLRDQLLVTI
QKTFNYSKSQ SYQLFAIIME CMKKKELVTV FRMGSEGQQD VEMAILTALL KGTNASAPDQ
LSLALAWNRV DIARSQIFVF GPHWPPLGSL APPVDTKATE KEKKPPTATT KGRGKGKGKK
KGKVKEEVEE ETDPRKLELL NWVNALEQAM LDALVLDRVD FVKLLIENGV NMQHFLTIPR
LEELYNTRLG PPNTLHLLVR DVKKSNLPPD YHISLIDIGL VLEYLMGGAY RCNYTRKSFR
TLYNNLFGPK RPKALKLLGM EDDEPPAKGK KKKKKKKEEE IDIDVDDPAV SRFQYPFHEL
MVWAVLMKRQ KMAVFLWQRG EECMAKALVA CKLYKAMAHE SSESELVDDI SQDLDNNSKD
FGQLAVELLD QSYKHDEQVA MKLLTYELKN WSNSTCLKLA VAAKHRDFIA HTCSQMLLTD
MWMGRLRMRK NPGLKVIMGI LIPPTILFLE FRTYDDFSYQ TSKENEDGKE KEEENVDANA
DAGSRKGDEE NEHKKQRSIP IGTKICEFYN APIVKFWFYT ISYLGYLLLF NYVILVRMDG
WPSPQEWIVI SYIVSLALEK IREILMSEPG KLSQKIKVWL QEYWNITDLV AISMFMVGAI
LRLQSQPYMG YGRVIYCVDI ILWYIRVLDI FGVNKYLGPY VMMIGKMMID MLYFVVIMLV
VLMSFGVARQ AILHPEEKPS WKLARNIFYM PYWMIYGEVF ADQIDLYAME INPPCGENLY
DEEGKRLPPC IPGAWLTPAL MACYLLVANI LLVNLLIAVF NNTFFEVKSI SNQVWKFQRY
QLIMTFHDRP VLPPPMIILS HIYIIIMRLS GRCRKKREGD QEERDRGLKL FLSDEELKKL
HEFEEQCVQE HFREKEDEQQ SSSDERIRVT SERVENMSMR LEEINERENF MKTSLQTVDL
RLSQLEELSG RMVSALENLA GIDRSDLIQA RSRASSECEA TYLLRQSSIN SADGYSLYRY
HFNGEELLFE EPALSTSPGT AFRKKTYSFR VKDEDAKSHL DQPSNLHHTP GPSPPATPGR
SRLALEGPLS TELRPGSDPG ISAGEFDPRA DFKSTEAAPS LNAAGVTGTQ LTVESTDSHP
LRESKLVRYY PGDPNTYKTM KSRSFVYTEG RKLVRGLSNW SAEYSSIMDQ AWNATEWRCQ
VQRITRSRST DIPYIVSEAA SQDELEDEHR GSLLDPQISR SALTVSDRPE KENLLSVKPH
QTLGFPCLRS RSLHGRPRSA EPAPSKLDRA GHASSTSNLA VMSVVPEGQN TQQEKRSAET
EC
