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Database: UniProt
Entry: TRPV5_RAT
LinkDB: TRPV5_RAT
Original site: 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   22-NOV-2017, entry version 122.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, AND 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
CC       intestine (PubMed:10875938). Required for normal Ca(2+)
CC       reabsorption in the kidney distal convoluted tubules (By
CC       similarity). The channel is activated by low internal calcium
CC       level and the current exhibits an inward rectification (By
CC       similarity). A Ca(2+)-dependent feedback regulation includes fast
CC       channel inactivation and slow current decay (By similarity).
CC       Heteromeric assembly with TRPV6 seems to modify channel
CC       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   -!- ENZYME REGULATION: Activated by WNK3.
CC       {ECO:0000250|UniProtKB:Q9NQA5}.
CC   -!- SUBUNIT: Homotetramer and probably heterotetramer with TRPV6.
CC       Interacts with TRPV6 (By similarity). Interacts with S100A10 and
CC       probably with the ANAX2-S100A10 heterotetramer. The interaction
CC       with S100A10 is required for the trafficking to the plasma
CC       membrane. Interacts with calmodulin. Interacts with BSPRY, which
CC       results in its inactivation (By similarity).
CC       {ECO:0000250|UniProtKB:P69744, 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
CC       ANAX2 along the apical domain of kidney distal tubular cells (By
CC       similarity). The expression of the glycosylated form in the cell
CC       membrane is 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).
CC       Detected in kidney. {ECO:0000269|PubMed:10875938}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9NQA5}.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC       TrpV subfamily. TRPV5 sub-subfamily. {ECO:0000305}.
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.
DR   UniGene; Rn.137513; -.
DR   ProteinModelPortal; Q9JIP0; -.
DR   SMR; Q9JIP0; -.
DR   STRING; 10116.ENSRNOP00000020975; -.
DR   PaxDb; Q9JIP0; -.
DR   PRIDE; 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   eggNOG; ENOG4110DG4; LUCA.
DR   GeneTree; ENSGT00550000074425; -.
DR   HOGENOM; HOG000234397; -.
DR   HOVERGEN; HBG061442; -.
DR   InParanoid; Q9JIP0; -.
DR   KO; K04974; -.
DR   OMA; NMRGAVG; -.
DR   OrthoDB; EOG091G0314; -.
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; -.
DR   Genevisible; Q9JIP0; RN.
DR   GO; GO:0016324; C:apical plasma membrane; IDA: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: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:0051262; P:protein tetramerization; ISS:UniProtKB.
DR   GO; GO:0035809; P:regulation of urine volume; ISS:UniProtKB.
DR   CDD; cd00204; ANK; 2.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR004729; TRP_channel.
DR   InterPro; IPR024862; TRPV.
DR   InterPro; IPR008346; TRPV5.
DR   InterPro; IPR008344; TRPV5/TRPV6.
DR   PANTHER; PTHR10582; PTHR10582; 1.
DR   PANTHER; PTHR10582:SF11; PTHR10582:SF11; 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   TIGRFAMs; TIGR00870; trp; 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;
KW   Complete proteome; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    723       Transient receptor potential cation
FT                                channel subfamily V member 5.
FT                                /FTId=PRO_0000215353.
FT   TOPO_DOM      1    320       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    321    341       Helical. {ECO:0000255}.
FT   TOPO_DOM    342    380       Extracellular. {ECO:0000255}.
FT   TRANSMEM    381    401       Helical. {ECO:0000255}.
FT   TOPO_DOM    402    412       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    413    433       Helical. {ECO:0000255}.
FT   TOPO_DOM    434    441       Extracellular. {ECO:0000255}.
FT   TRANSMEM    442    462       Helical. {ECO:0000255}.
FT   TOPO_DOM    463    485       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    486    506       Helical. {ECO:0000255}.
FT   INTRAMEM    517    537       Pore-forming. {ECO:0000305}.
FT   TRANSMEM    550    570       Helical. {ECO:0000255}.
FT   TOPO_DOM    571    723       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       72    101       ANK 1. {ECO:0000255}.
FT   REPEAT      110    139       ANK 2. {ECO:0000255}.
FT   REPEAT      156    185       ANK 3. {ECO:0000255}.
FT   REPEAT      189    222       ANK 4. {ECO:0000255}.
FT   REPEAT      232    261       ANK 5. {ECO:0000255}.
FT   REGION      591    595       Interaction with S100A10. {ECO:0000250}.
FT   REGION      643    646       Involved in Ca(2+)-dependent
FT                                inactivation. {ECO:0000250}.
FT   REGION      693    723       Involved in Ca(2+)-dependent
FT                                inactivation. {ECO:0000250}.
FT   METAL       535    535       Calcium; shared with neighboring
FT                                subunits. {ECO:0000250|UniProtKB:Q9R186}.
FT   MOD_RES     678    678       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P69744}.
FT   MOD_RES     682    682       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P69744}.
FT   CARBOHYD    351    351       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ     248    296       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_013438.
FT   CONFLICT    290    290       V -> L (in Ref. 2; BAA99541).
FT                                {ECO:0000305}.
FT   CONFLICT    295    295       K -> I (in Ref. 2; BAA99541).
FT                                {ECO:0000305}.
FT   CONFLICT    331    331       F -> S (in Ref. 2; BAA99541).
FT                                {ECO:0000305}.
FT   CONFLICT    488    488       W -> R (in Ref. 2; BAA99541).
FT                                {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
//
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