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Transient receptor potential cation channel subfamily V member 5 (TrpV5) (Calcium transporter 2) (CaT2) (Epithelial calcium channel 1) (ECaC1) (Osm-9-like TRP channel 3) (OTRPC3)

 TRPV5_RAT               Reviewed;         723 AA.
Q9JIP0; Q5UC98; Q9JJL2;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 121.
RecName: Full=Transient receptor potential cation channel subfamily V member 5;
Short=TrpV5;
AltName: Full=Calcium transporter 2 {ECO:0000303|PubMed:10875938};
Short=CaT2 {ECO:0000303|PubMed:10875938};
AltName: Full=Epithelial calcium channel 1;
Short=ECaC1;
AltName: Full=Osm-9-like TRP channel 3;
Short=OTRPC3;
Name=Trpv5; Synonyms=Cat2, Ecac, Ecac1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
STRAIN=CD1 Charles River; TISSUE=Kidney cortex;
PubMed=10875938; DOI=10.1074/jbc.M909686199;
Peng J.-B., Chen X.-Z., Berger U.V., Vassilev P.M., Brown E.M.,
Hediger M.A.;
"A rat kidney-specific calcium transporter in the distal nephron.";
J. Biol. Chem. 275:28186-28194(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
Ishibashi K., Suzuki M., Imai M.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Sprague-Dawley;
Nehrke K., Sherman T., Bushinsky D.;
"A variant of the TrpV5 calcium channel from rat.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Constitutively active calcium selective cation channel
thought to be involved in Ca(2+) reabsorption in kidney and
intestine (PubMed:10875938). Required for normal Ca(2+)
reabsorption in the kidney distal convoluted tubules (By
similarity). The channel is activated by low internal calcium
level and the current exhibits an inward rectification (By
similarity). A Ca(2+)-dependent feedback regulation includes fast
channel inactivation and slow current decay (By similarity).
Heteromeric assembly with TRPV6 seems to modify channel
properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit
voltage-dependent gating (By similarity).
{ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9XSM3,
ECO:0000269|PubMed:10875938}.
-!- ENZYME REGULATION: Activated by WNK3.
{ECO:0000250|UniProtKB:Q9NQA5}.
-!- SUBUNIT: Homotetramer and probably heterotetramer with TRPV6.
Interacts with TRPV6 (By similarity). Interacts with S100A10 and
probably with the ANAX2-S100A10 heterotetramer. The interaction
with S100A10 is required for the trafficking to the plasma
membrane. Interacts with calmodulin. Interacts with BSPRY, which
results in its inactivation (By similarity).
{ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9XSM3}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10875938};
Multi-pass membrane protein {ECO:0000305}. Apical cell membrane
{ECO:0000250|UniProtKB:Q9NQA5}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q9NQA5}. Note=Colocalized with S100A10 and
ANAX2 along the apical domain of kidney distal tubular cells (By
similarity). The expression of the glycosylated form in the cell
membrane is increased in the presence of WNK3 (By similarity).
{ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9NQA5}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9JIP0-1; Sequence=Displayed;
Name=2;
IsoId=Q9JIP0-2; Sequence=VSP_013438;
-!- TISSUE SPECIFICITY: Detected in kidney (at protein level).
Detected in kidney. {ECO:0000269|PubMed:10875938}.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9NQA5}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
TrpV subfamily. TRPV5 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF209196; AAF86309.1; -; mRNA.
EMBL; AB032019; BAA99541.1; -; mRNA.
EMBL; AY762624; AAV31121.1; -; mRNA.
RefSeq; NP_446239.2; NM_053787.2.
UniGene; Rn.137513; -.
ProteinModelPortal; Q9JIP0; -.
SMR; Q9JIP0; -.
STRING; 10116.ENSRNOP00000020975; -.
PaxDb; Q9JIP0; -.
PRIDE; Q9JIP0; -.
Ensembl; ENSRNOT00000020975; ENSRNOP00000020975; ENSRNOG00000015394. [Q9JIP0-1]
Ensembl; ENSRNOT00000051687; ENSRNOP00000046276; ENSRNOG00000015394. [Q9JIP0-2]
GeneID; 116469; -.
KEGG; rno:116469; -.
UCSC; RGD:620636; rat. [Q9JIP0-1]
CTD; 56302; -.
RGD; 620636; Trpv5.
eggNOG; KOG3676; Eukaryota.
eggNOG; ENOG4110DG4; LUCA.
GeneTree; ENSGT00550000074425; -.
HOGENOM; HOG000234397; -.
HOVERGEN; HBG061442; -.
InParanoid; Q9JIP0; -.
KO; K04974; -.
OMA; NMRGAVG; -.
OrthoDB; EOG091G0314; -.
PhylomeDB; Q9JIP0; -.
TreeFam; TF314711; -.
Reactome; R-RNO-3295583; TRP channels.
PRO; PR:Q9JIP0; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000015394; -.
Genevisible; Q9JIP0; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0031226; C:intrinsic component of plasma membrane; IMP:UniProtKB.
GO; GO:0005262; F:calcium channel activity; IDA:RGD.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
GO; GO:0060402; P:calcium ion transport into cytosol; IDA:RGD.
GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
GO; GO:0035809; P:regulation of urine volume; ISS:UniProtKB.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR004729; TRP_channel.
InterPro; IPR024862; TRPV.
InterPro; IPR008346; TRPV5.
InterPro; IPR008344; TRPV5/TRPV6.
PANTHER; PTHR10582; PTHR10582; 1.
PANTHER; PTHR10582:SF11; PTHR10582:SF11; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR01415; ANKYRIN.
PRINTS; PR01765; ECACCHANNEL.
PRINTS; PR01767; ECACCHANNEL2.
SMART; SM00248; ANK; 4.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 2.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Calcium; Calcium channel;
Calcium transport; Calmodulin-binding; Cell membrane;
Complete proteome; Glycoprotein; Ion channel; Ion transport; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 723 Transient receptor potential cation
channel subfamily V member 5.
/FTId=PRO_0000215353.
TOPO_DOM 1 320 Cytoplasmic. {ECO:0000255}.
TRANSMEM 321 341 Helical. {ECO:0000255}.
TOPO_DOM 342 380 Extracellular. {ECO:0000255}.
TRANSMEM 381 401 Helical. {ECO:0000255}.
TOPO_DOM 402 412 Cytoplasmic. {ECO:0000255}.
TRANSMEM 413 433 Helical. {ECO:0000255}.
TOPO_DOM 434 441 Extracellular. {ECO:0000255}.
TRANSMEM 442 462 Helical. {ECO:0000255}.
TOPO_DOM 463 485 Cytoplasmic. {ECO:0000255}.
TRANSMEM 486 506 Helical. {ECO:0000255}.
INTRAMEM 517 537 Pore-forming. {ECO:0000305}.
TRANSMEM 550 570 Helical. {ECO:0000255}.
TOPO_DOM 571 723 Cytoplasmic. {ECO:0000255}.
REPEAT 72 101 ANK 1. {ECO:0000255}.
REPEAT 110 139 ANK 2. {ECO:0000255}.
REPEAT 156 185 ANK 3. {ECO:0000255}.
REPEAT 189 222 ANK 4. {ECO:0000255}.
REPEAT 232 261 ANK 5. {ECO:0000255}.
REGION 591 595 Interaction with S100A10. {ECO:0000250}.
REGION 643 646 Involved in Ca(2+)-dependent
inactivation. {ECO:0000250}.
REGION 693 723 Involved in Ca(2+)-dependent
inactivation. {ECO:0000250}.
METAL 535 535 Calcium; shared with neighboring
subunits. {ECO:0000250|UniProtKB:Q9R186}.
MOD_RES 678 678 Phosphothreonine.
{ECO:0000250|UniProtKB:P69744}.
MOD_RES 682 682 Phosphoserine.
{ECO:0000250|UniProtKB:P69744}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 248 296 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_013438.
CONFLICT 290 290 V -> L (in Ref. 2; BAA99541).
{ECO:0000305}.
CONFLICT 295 295 K -> I (in Ref. 2; BAA99541).
{ECO:0000305}.
CONFLICT 331 331 F -> S (in Ref. 2; BAA99541).
{ECO:0000305}.
CONFLICT 488 488 W -> R (in Ref. 2; BAA99541).
{ECO:0000305}.
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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