TRPV3_MOUSE
ID TRPV3_MOUSE Reviewed; 791 AA.
AC Q8K424; Q5SV08;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 3;
DE Short=TrpV3;
GN Name=Trpv3;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12016205; DOI=10.1126/science.1073140;
RA Peier A.M., Reeve A.J., Andersson D.A., Moqrich A., Earley T.J.,
RA Hergarden A.C., Story G.M., Colley S., Hogenesch J., McIntyre P., Bevan S.,
RA Patapoutian A.;
RT "A heat-sensitive TRP channel expressed in keratinocytes.";
RL Science 296:2046-2049(2002).
RN [2]
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).
CC -!- FUNCTION: Putative receptor-activated non-selective calcium permeant
CC cation channel. It is activated by innocuous (warm) temperatures and
CC shows an increased response at noxious temperatures greater than 39
CC degrees Celsius. Activation exhibits an outward rectification. May
CC associate with TRPV1 and may modulate its activity. Is a negative
CC regulator of hair growth and cycling: TRPV3-coupled signaling
CC suppresses keratinocyte proliferation in hair follicles and induces
CC apoptosis and premature hair follicle regression (catagen) (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:12016205}.
CC -!- SUBUNIT: May form a heteromeric channel with TRPV1. Interacts with
CC TRPV1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8K424; P00533: EGFR; Xeno; NbExp=2; IntAct=EBI-2650739, EBI-297353;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes and hair follicles.
CC {ECO:0000269|PubMed:12016205}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV3 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF510316; AAM33069.1; -; mRNA.
DR EMBL; AL645739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25004.1; -.
DR RefSeq; NP_659567.2; NM_145099.2.
DR PDB; 4N5Q; X-ray; 1.95 A; A/B=118-367.
DR PDB; 6LGP; EM; 3.40 A; A/B/C/D=118-756.
DR PDB; 6PVL; EM; 4.40 A; A/B/C/D=1-791.
DR PDB; 6PVM; EM; 4.50 A; A/B/C/D=1-791.
DR PDB; 6PVN; EM; 4.07 A; A/B/C/D=1-791.
DR PDB; 6PVO; EM; 5.18 A; A/B/C/D=1-791.
DR PDB; 6PVP; EM; 4.48 A; A/B/C/D=1-791.
DR PDB; 6PVQ; EM; 4.75 A; A/B/C/D=1-791.
DR PDB; 7MIJ; EM; 1.98 A; A/B/C/D=1-791.
DR PDB; 7MIK; EM; 3.12 A; A/B/C/D=1-791.
DR PDB; 7MIL; EM; 3.86 A; A/B/C/D=1-791.
DR PDB; 7MIM; EM; 3.42 A; A/B/C/D=1-791.
DR PDB; 7MIN; EM; 3.09 A; A/B/C/D=1-791.
DR PDB; 7MIO; EM; 3.48 A; A/B/C/D=1-791.
DR PDB; 7RAS; EM; 3.64 A; A/B/C/D=1-791.
DR PDB; 7RAU; EM; 3.99 A; A/B/C/D=1-791.
DR PDBsum; 4N5Q; -.
DR PDBsum; 6LGP; -.
DR PDBsum; 6PVL; -.
DR PDBsum; 6PVM; -.
DR PDBsum; 6PVN; -.
DR PDBsum; 6PVO; -.
DR PDBsum; 6PVP; -.
DR PDBsum; 6PVQ; -.
DR PDBsum; 7MIJ; -.
DR PDBsum; 7MIK; -.
DR PDBsum; 7MIL; -.
DR PDBsum; 7MIM; -.
DR PDBsum; 7MIN; -.
DR PDBsum; 7MIO; -.
DR PDBsum; 7RAS; -.
DR PDBsum; 7RAU; -.
DR AlphaFoldDB; Q8K424; -.
DR SMR; Q8K424; -.
DR IntAct; Q8K424; 1.
DR STRING; 10090.ENSMUSP00000053755; -.
DR BindingDB; Q8K424; -.
DR ChEMBL; CHEMBL3879838; -.
DR GuidetoPHARMACOLOGY; 509; -.
DR iPTMnet; Q8K424; -.
DR PhosphoSitePlus; Q8K424; -.
DR PaxDb; Q8K424; -.
DR PRIDE; Q8K424; -.
DR ABCD; Q8K424; 2 sequenced antibodies.
DR Antibodypedia; 23030; 414 antibodies from 33 providers.
DR DNASU; 246788; -.
DR Ensembl; ENSMUST00000049676; ENSMUSP00000053755; ENSMUSG00000043029.
DR GeneID; 246788; -.
DR KEGG; mmu:246788; -.
DR UCSC; uc007kaj.1; mouse.
DR CTD; 162514; -.
DR MGI; MGI:2181407; Trpv3.
DR VEuPathDB; HostDB:ENSMUSG00000043029; -.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000158281; -.
DR HOGENOM; CLU_012795_0_0_1; -.
DR InParanoid; Q8K424; -.
DR OMA; RYIFRAV; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; Q8K424; -.
DR TreeFam; TF314711; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 246788; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q8K424; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K424; protein.
DR Bgee; ENSMUSG00000043029; Expressed in lip and 41 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005261; F:cation channel activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005216; F:ion channel activity; IDA:MGI.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0042636; P:negative regulation of hair cycle; ISO:MGI.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISO:MGI.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0009266; P:response to temperature stimulus; IDA:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR024862; TRPV.
DR InterPro; IPR008347; TrpV1-4.
DR InterPro; IPR024866; TrpV3.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR PANTHER; PTHR10582:SF6; PTHR10582:SF6; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01768; TRPVRECEPTOR.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Ion channel; Ion transport; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..791
FT /note="Transient receptor potential cation channel
FT subfamily V member 3"
FT /id="PRO_0000215346"
FT TOPO_DOM 1..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 567..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 621..637
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..791
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 214..243
FT /note="ANK 1"
FT REPEAT 261..291
FT /note="ANK 2"
FT REPEAT 340..369
FT /note="ANK 3"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 9
FT /note="A -> V (in Ref. 1; AAM33069)"
FT /evidence="ECO:0000305"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:4N5Q"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:4N5Q"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:6LGP"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:7MIJ"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:4N5Q"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:7MIO"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:4N5Q"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:4N5Q"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:7MIJ"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:7MIJ"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:7MIJ"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:7MIJ"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:7MIN"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 423..435
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 437..460
FT /evidence="ECO:0007829|PDB:7MIJ"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:7MIN"
FT TURN 472..475
FT /evidence="ECO:0007829|PDB:7MIJ"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 485..507
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 513..518
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 521..541
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 547..560
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 561..568
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 570..585
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 587..606
FT /evidence="ECO:0007829|PDB:7MIJ"
FT TURN 613..615
FT /evidence="ECO:0007829|PDB:7MIN"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:7MIN"
FT HELIX 625..636
FT /evidence="ECO:0007829|PDB:7MIJ"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 651..665
FT /evidence="ECO:0007829|PDB:7MIJ"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 669..684
FT /evidence="ECO:0007829|PDB:7MIJ"
FT TURN 685..687
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 688..705
FT /evidence="ECO:0007829|PDB:7MIJ"
FT HELIX 709..712
FT /evidence="ECO:0007829|PDB:7MIJ"
FT TURN 713..715
FT /evidence="ECO:0007829|PDB:7MIK"
FT STRAND 718..724
FT /evidence="ECO:0007829|PDB:7MIJ"
FT STRAND 727..737
FT /evidence="ECO:0007829|PDB:7MIJ"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:7MIK"
SQ SEQUENCE 791 AA; 90663 MW; 76A244781D223C6E CRC64;
MNAHSKEMAP LMGKRTTAPG GNPVVLTEKR PADLTPTKKS AHFFLEIEGF EPNPTVTKTS
PPIFSKPMDS NIRQCLSGNC DDMDSPQSPQ DDVTETPSNP NSPSANLAKE EQRQKKKRLK
KRIFAAVSEG CVEELRELLQ DLQDLCRRRR GLDVPDFLMH KLTASDTGKT CLMKALLNIN
PNTKEIVRIL LAFAEENDIL DRFINAEYTE EAYEGQTALN IAIERRQGDI TAVLIAAGAD
VNAHAKGVFF NPKYQHEGFY FGETPLALAA CTNQPEIVQL LMENEQTDIT SQDSRGNNIL
HALVTVAEDF KTQNDFVKRM YDMILLRSGN WELETMRNND GLTPLQLAAK MGKAEILKYI
LSREIKEKPL RSLSRKFTDW AYGPVSSSLY DLTNVDTTTD NSVLEIIVYN TNIDNRHEML
TLEPLHTLLH TKWKKFAKYM FFLSFCFYFF YNITLTLVSY YRPREDEDLP HPLALTHKMS
WLQLLGRMFV LIWATCISVK EGIAIFLLRP SDLQSILSDA WFHFVFFVQA VLVILSVFLY
LFAYKEYLAC LVLAMALGWA NMLYYTRGFQ SMGMYSVMIQ KVILHDVLKF LFVYILFLLG
FGVALASLIE KCSKDKKDCS SYGSFSDAVL ELFKLTIGLG DLNIQQNSTY PILFLFLLIT
YVILTFVLLL NMLIALMGET VENVSKESER IWRLQRARTI LEFEKMLPEW LRSRFRMGEL
CKVADEDFRL CLRINEVKWT EWKTHVSFLN EDPGPIRRTA DLNKIQDSSR SNSKTTLYAF
DELDEFPETS V
