TRPM1_RAT
ID TRPM1_RAT Reviewed; 1628 AA.
AC Q2WEA5; Q2WEA4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 1;
DE AltName: Full=Melastatin-1;
GN Name=Trpm1 {ECO:0000312|EMBL:CAI30141.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAI30141.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RC STRAIN=Dark agouti {ECO:0000312|EMBL:CAI30141.1};
RC TISSUE=Eye {ECO:0000312|EMBL:CAI30141.1};
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).
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 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q7Z4N2}.
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}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q7Z4N2, ECO:0000255}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q7Z4N2}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q7Z4N2}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q2TV84}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15856355};
CC IsoId=Q2WEA5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15856355};
CC IsoId=Q2WEA5-2; Sequence=VSP_052740;
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; AJ867482; CAI30141.1; -; mRNA.
DR EMBL; AJ867483; CAI30142.1; -; mRNA.
DR RefSeq; NP_001032822.1; NM_001037733.1. [Q2WEA5-2]
DR RefSeq; NP_001032823.1; NM_001037734.1. [Q2WEA5-1]
DR AlphaFoldDB; Q2WEA5; -.
DR SMR; Q2WEA5; -.
DR STRING; 10116.ENSRNOP00000062990; -.
DR CarbonylDB; Q2WEA5; -.
DR GlyGen; Q2WEA5; 1 site.
DR iPTMnet; Q2WEA5; -.
DR PhosphoSitePlus; Q2WEA5; -.
DR PaxDb; Q2WEA5; -.
DR PRIDE; Q2WEA5; -.
DR GeneID; 361586; -.
DR KEGG; rno:361586; -.
DR UCSC; RGD:1597140; rat. [Q2WEA5-1]
DR CTD; 4308; -.
DR RGD; 1597140; Trpm1.
DR eggNOG; KOG3614; Eukaryota.
DR InParanoid; Q2WEA5; -.
DR OrthoDB; 738147at2759; -.
DR PhylomeDB; Q2WEA5; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR PRO; PR:Q2WEA5; -.
DR Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; ISO:RGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0060402; P:calcium ion transport into cytosol; ISO:RGD.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0071482; P:cellular response to light stimulus; ISO:RGD.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0046548; P:retinal rod cell development; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1628
FT /note="Transient receptor potential cation channel
FT subfamily M member 1"
FT /id="PRO_0000328932"
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..1105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1127..1156
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1157..1177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1178..1628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..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 1360..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1233..1253
FT /evidence="ECO:0000255"
FT COMPBIAS 1595..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1066..1072
FT /note="RKTRIHI -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15856355"
FT /id="VSP_052740"
SQ SEQUENCE 1628 AA; 184318 MW; 2CFB057DF62CB102 CRC64;
MGSMRKMSSS FKRGSIKSST SGSQKGQKAW IEKTFCKREC IFVIPSTKDP NRCCCGQLTN
QHIPPLPSVT PSSTAEDTKQ GDAQSGKWSV SKHTQSYPTD SYGILEFQGG GYSNKAMYIR
VSYDTKPDSL LHLMVKDWQL ELPKLLISVH GGLQSFEMQP KLKQVFGKGL IKAAMTTGAW
IFTGGVSTGV VSHVGDALKD HSSKSRGRLC AIGIAPWGMV ENKEDLVGKD VTRVYQTMSN
PLSKLSVLNN SHTHFILADN GTLGKYGAEV KLRRQLEKHI SLQKINTRLG QGVPVVGLVV
EGGPNVVSIV LEYLREDPPV PVVVCDGSGR ASDILSFAHK YCDEGGVINE SLRDQLLVTI
QKTFNYSKSQ SHQLFAIIME CMKKKELVTV FRMGSEGQQD VEMAILTALL KGTNVSAPDQ
LSLALAWNRV DIARSQIFVF GPHWPPLGSL APPVDTKVAE KEKKPPTATT KGRGKGKGKK
KGKVKEEVEE ETDPRKIELL 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 FRSYDDFSYQ TSKENEDGKE KEEENVDANA
DAGSRKGDEE NEHKKQRSIP IGTKICEFYN APIVKFWFYT ISYLGYLLLF NYVILVRMDG
WPSPQEWIVI SYIVSLALEK IREILMSEPG KLSQKIKVWL QEYWNITDLV AISMFMVGAI
LRLQNQPYMG YGRVIYCVDI ILWYIRVLDI FGVNKYLGPY VMMIGKMMID MLYFVVIMLV
VLMSFGVARQ AILHPEEKPS WKLARNIFYM PYWMIYGEVF ADQIDRKTRI HIYAMEINPP
CGENLYDEEG KRLPPCIPGA WLTPALMACY LLVANILLVN LLIAVFNNTF FEVKSISNQV
WKFQRYQLIM TFHDRPVLPP PMIILSHIYI IVMRLSGRCR KKREGDQEER DRGLKLFLSD
EELKKLHEFE EQCVQEHFRE KEDEQQSSSD ERIRVTSERV ENMSMRLEEI NERENFMKAS
LQTVDLRLSQ LEELSGRMVG ALENLAGIDR SDLIQARSRA SSECEATYLL RQSSINSADG
YSMYRYHFNG EELLFEEPAL STSPGTVFRK KTCSFRVKEE DVKPHLDQPS SLHHTPGPSP
PATPGRSRLA LDGPLSTELR PGLDPGISAG ELDPRADFKS AEVAPSLNTA NVASTQLTVE
STVSHPLRES KLARYYPGDL NTYKTMKSRS FVYSEGRKLV RGLSNWGAEY SSIMDQTWNS
AEWRCQVQRI TRSRSTDIPY IVSEAASQDE FEDEHRESLL APQISRSALT VSDRPEKENL
LSVKPHQTLG FPCLRSRSLH GHPRSAKPSP SKLDRAGHAS STSNLAVMSD APEGQNTQQE
KGNPETEC
