TRPV5_RAT
ID TRPV5_RAT Reviewed; 723 AA.
AC Q9JIP0; Q5UC98; Q9JJL2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 5;
DE Short=TrpV5;
DE AltName: Full=Calcium transporter 2 {ECO:0000303|PubMed:10875938};
DE Short=CaT2 {ECO:0000303|PubMed:10875938};
DE AltName: Full=Epithelial calcium channel 1;
DE Short=ECaC1;
DE AltName: Full=Osm-9-like TRP channel 3;
DE Short=OTRPC3;
GN Name=Trpv5; Synonyms=Cat2, Ecac, Ecac1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=CD1 Charles River; TISSUE=Kidney cortex;
RX PubMed=10875938; DOI=10.1074/jbc.m909686199;
RA Peng J.-B., Chen X.-Z., Berger U.V., Vassilev P.M., Brown E.M.,
RA Hediger M.A.;
RT "A rat kidney-specific calcium transporter in the distal nephron.";
RL J. Biol. Chem. 275:28186-28194(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Ishibashi K., Suzuki M., Imai M.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley;
RA Nehrke K., Sherman T., Bushinsky D.;
RT "A variant of the TrpV5 calcium channel from rat.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Constitutively active calcium selective cation channel
CC thought to be involved in Ca(2+) reabsorption in kidney and intestine
CC (PubMed:10875938). Required for normal Ca(2+) reabsorption in the
CC kidney distal convoluted tubules (By similarity). The channel is
CC activated by low internal calcium level and the current exhibits an
CC inward rectification (By similarity). A Ca(2+)-dependent feedback
CC regulation includes fast channel inactivation and slow current decay
CC (By similarity). Heteromeric assembly with TRPV6 seems to modify
CC channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit
CC voltage-dependent gating (By similarity).
CC {ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9XSM3,
CC ECO:0000269|PubMed:10875938}.
CC -!- ACTIVITY REGULATION: Activated by WNK3. {ECO:0000250|UniProtKB:Q9NQA5}.
CC -!- SUBUNIT: Homotetramer and probably heterotetramer with TRPV6. Interacts
CC with TRPV6 (By similarity). Interacts with S100A10 and probably with
CC the ANAX2-S100A10 heterotetramer. The interaction with S100A10 is
CC required for the trafficking to the plasma membrane. Interacts with
CC calmodulin. Interacts with BSPRY, which results in its inactivation (By
CC similarity). {ECO:0000250|UniProtKB:P69744,
CC ECO:0000250|UniProtKB:Q9XSM3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10875938};
CC Multi-pass membrane protein {ECO:0000305}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9NQA5}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NQA5}. Note=Colocalized with S100A10 and ANAX2
CC along the apical domain of kidney distal tubular cells (By similarity).
CC The expression of the glycosylated form in the cell membrane is
CC increased in the presence of WNK3 (By similarity).
CC {ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9NQA5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JIP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JIP0-2; Sequence=VSP_013438;
CC -!- TISSUE SPECIFICITY: Detected in kidney (at protein level). Detected in
CC kidney. {ECO:0000269|PubMed:10875938}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9NQA5}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV5 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF209196; AAF86309.1; -; mRNA.
DR EMBL; AB032019; BAA99541.1; -; mRNA.
DR EMBL; AY762624; AAV31121.1; -; mRNA.
DR RefSeq; NP_446239.2; NM_053787.2. [Q9JIP0-1]
DR AlphaFoldDB; Q9JIP0; -.
DR SMR; Q9JIP0; -.
DR STRING; 10116.ENSRNOP00000020975; -.
DR GlyGen; Q9JIP0; 1 site.
DR PaxDb; Q9JIP0; -.
DR Ensembl; ENSRNOT00000020975; ENSRNOP00000020975; ENSRNOG00000015394. [Q9JIP0-1]
DR Ensembl; ENSRNOT00000051687; ENSRNOP00000046276; ENSRNOG00000015394. [Q9JIP0-2]
DR GeneID; 116469; -.
DR KEGG; rno:116469; -.
DR UCSC; RGD:620636; rat. [Q9JIP0-1]
DR CTD; 56302; -.
DR RGD; 620636; Trpv5.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000161809; -.
DR HOGENOM; CLU_012795_2_0_1; -.
DR InParanoid; Q9JIP0; -.
DR OMA; SFKWRKY; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; Q9JIP0; -.
DR TreeFam; TF314711; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR PRO; PR:Q9JIP0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000015394; Expressed in kidney and 2 other tissues.
DR Genevisible; Q9JIP0; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0034704; C:calcium channel complex; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IDA:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0035809; P:regulation of urine volume; ISS:UniProtKB.
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; IPR008346; TRPV5.
DR InterPro; IPR008344; TRPV5/TRPV6.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR01765; ECACCHANNEL.
DR PRINTS; PR01767; ECACCHANNEL2.
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 Alternative splicing; ANK repeat; Calcium; Calcium channel;
KW Calcium transport; Calmodulin-binding; Cell membrane; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..723
FT /note="Transient receptor potential cation channel
FT subfamily V member 5"
FT /id="PRO_0000215353"
FT TOPO_DOM 1..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 342..378
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 402..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 413..435
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 436..441
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 463..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT INTRAMEM 517..537
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 571..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT REPEAT 72..101
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 110..139
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 156..185
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 189..222
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 232..261
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REGION 591..595
FT /note="Interaction with S100A10"
FT /evidence="ECO:0000250|UniProtKB:P69744"
FT REGION 643..646
FT /note="Involved in Ca(2+)-dependent inactivation"
FT /evidence="ECO:0000250"
FT REGION 651..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..723
FT /note="Involved in Ca(2+)-dependent inactivation"
FT /evidence="ECO:0000250"
FT COMPBIAS 657..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 535
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT MOD_RES 678
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P69744"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69744"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 248..296
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_013438"
FT CONFLICT 290
FT /note="V -> L (in Ref. 2; BAA99541)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="K -> I (in Ref. 2; BAA99541)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="F -> S (in Ref. 2; BAA99541)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="W -> R (in Ref. 2; BAA99541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 82454 MW; F41FCF2F2B431A25 CRC64;
MGVKKPWIQL QKRLNWWVRE QDWNQHVDQL HMLQQKSIWE SPLLRAAKEN DMCTLKRLQH
DQNCDFRQRG ALGETALHVA ALYDNLDAAI MLMETAPYLV TESTLCEPFV GQTALHIAIM
NQNVNLVRAL LARGASASAR ATGSAFHRSS HNLIYYGEHP LSFAACVGSE EIVRLLIEHG
ADIRAQDSLG NTVLHILVLQ PNKTFACQMY NLLLSHDGGD HLKSLELVPN NQGLTPFKLA
GVEGNTVMFQ HLMQKRKHIQ WSLGPLTSSI YDLTEIDSWG EDLSFLELVV SSKKKEARQI
LEQTPVKELV SLKWKKYGQP YFCLLGMLYI FYMICFTTCC VYRPLKFRDA NRTHVRDNTV
LEQKPLQEAY VTYQDKVRLV GELVTVIGAV VILLIEIPDI FRVGASRYFG HTVLGGPFHV
IIITYASLVL LIMVMRLTSM NGEVVPISMA LVLGWCSVMY FSRGFQMLGP FTIMIQKMIF
GDLLRFCWLM AMVILGFASA FYIIFQTEDP ESLGEFSDYP TAMFSTFELF LTIIDGPANY
SVDLPFMYHL TYFAFAIIAT LLMLNLFIAM MGDTHWRVAQ ERDELWRAQV VATTVMLERK
MPRFLWPRSG ICGCEYGLGD RWFLRVEHHQ EQNPYRVLRY VEAFKSSDKE EVQEQLSEKQ
PSGTETGTLA RGSVVLQTPP LSRTTSLSSN SHRGWEILRR NTLGHLNLGQ DLGEGDGEEI
YHF
