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Transient receptor potential cation channel subfamily V member 6 (TrpV6) (Calcium transport protein 1) (CaT1) (Epithelial calcium channel 2) (ECaC2)

 TRPV6_RAT               Reviewed;         767 AA.
Q9R186;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-APR-2015, sequence version 2.
23-MAY-2018, entry version 129.
RecName: Full=Transient receptor potential cation channel subfamily V member 6;
Short=TrpV6;
AltName: Full=Calcium transport protein 1 {ECO:0000303|PubMed:10428857};
Short=CaT1 {ECO:0000303|PubMed:11287959};
AltName: Full=Epithelial calcium channel 2;
Short=ECaC2;
Name=Trpv6;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=Wistar; TISSUE=Intestine;
PubMed=10428857; DOI=10.1074/jbc.274.32.22739;
Peng J.-B., Chen X.Z., Berger U.V., Vassilev P.M., Tsukaguchi H.,
Brown E.M., Hediger M.A.;
"Molecular cloning and characterization of a channel-like transporter
mediating intestinal calcium absorption.";
J. Biol. Chem. 274:22739-22746(1999).
[2]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11287959; DOI=10.1038/35070596;
Yue L., Peng J.B., Hediger M.A., Clapham D.E.;
"CaT1 manifests the pore properties of the calcium-release-activated
calcium channel.";
Nature 410:705-709(2001).
[3]
PHOSPHORYLATION AT TYR-201 AND TYR-202, AND MUTAGENESIS OF TYR-201 AND
TYR-202.
PubMed=17197020; DOI=10.1016/j.ceca.2006.11.008;
Sternfeld L., Anderie I., Schmid A., Al-Shaldi H., Krause E., Magg T.,
Schreiner D., Hofer H.W., Schulz I.;
"Identification of tyrosines in the putative regulatory site of the
Ca2+ channel TRPV6.";
Cell Calcium 42:91-102(2007).
[4] {ECO:0000244|PDB:5IWK, ECO:0000244|PDB:5IWP, ECO:0000244|PDB:5IWR, ECO:0000244|PDB:5IWT}
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 41-709, FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, TOPOLOGY, AND REPEATS.
PubMed=27296226; DOI=10.1038/nature17975;
Saotome K., Singh A.K., Yelshanskaya M.V., Sobolevsky A.I.;
"Crystal structure of the epithelial calcium channel TRPV6.";
Nature 534:506-511(2016).
[5] {ECO:0000244|PDB:6BOB}
STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 41-708, SUBUNIT,
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=29258289; DOI=10.1038/nature25182;
McGoldrick L.L., Singh A.K., Saotome K., Yelshanskaya M.V.,
Twomey E.C., Grassucci R.A., Sobolevsky A.I.;
"Opening of the human epithelial calcium channel TRPV6.";
Nature 553:233-237(2018).
[6] {ECO:0000244|PDB:5WO6, ECO:0000244|PDB:5WO7, ECO:0000244|PDB:5WO8, ECO:0000244|PDB:5WO9, ECO:0000244|PDB:5WOA}
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 41-709 OF WILD-TYPE AND
MUTANT GLN-495, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, AND
MUTAGENESIS OF LEU-535.
PubMed=28878326; DOI=10.1038/s41598-017-10993-9;
Singh A.K., Saotome K., Sobolevsky A.I.;
"Swapping of transmembrane domains in the epithelial calcium channel
TRPV6.";
Sci. Rep. 7:10669-10669(2017).
-!- FUNCTION: Calcium selective cation channel that mediates Ca(2+)
uptake in various tissues, including the intestine
(PubMed:10428857, PubMed:11287959, PubMed:27296226,
PubMed:28878326). Important for normal Ca(2+) ion homeostasis in
the body, including bone and skin (By similarity). The channel is
activated by low internal calcium level, probably including
intracellular calcium store depletion, and the current exhibits an
inward rectification (PubMed:10428857, PubMed:11287959,
PubMed:27296226). Inactivation includes both a rapid Ca(2+)-
dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the
latter may be regulated by phosphorylation. In vitro, is slowly
inhibited by Mg(2+) in a voltage-independent manner. Heteromeric
assembly with TRPV5 seems to modify channel properties. TRPV5-
TRPV6 heteromultimeric concatemers exhibit voltage-dependent
gating (By similarity). {ECO:0000250|UniProtKB:Q91WD2,
ECO:0000250|UniProtKB:Q9H1D0, ECO:0000269|PubMed:10428857,
ECO:0000269|PubMed:11287959, ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
-!- SUBUNIT: Homotetramer (PubMed:27296226, PubMed:29258289,
PubMed:28878326). Probably forms also heterotetramers with TRPV5.
Interacts with TRPV5. 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. Interacts with TCAF1 and
TCAF2 (By similarity). {ECO:0000250|UniProtKB:Q9H1D0,
ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326,
ECO:0000269|PubMed:29258289}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-7198720, EBI-7198720;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10428857,
ECO:0000269|PubMed:17197020, ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326, ECO:0000269|PubMed:29258289}; Multi-
pass membrane protein {ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326, ECO:0000269|PubMed:29258289}.
-!- TISSUE SPECIFICITY: Expressed in duodenum, proximal jejunum,
cecum, and colon. {ECO:0000269|PubMed:10428857}.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q91WD2,
ECO:0000250|UniProtKB:Q9H1D0}.
-!- PTM: Phosphorylation at Tyr-201 and Tyr-202 by SRC leads to an
increased calcium influx through the channel. Probably
dephosphorylated at these sites by PTPN1.
{ECO:0000269|PubMed:17197020}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
TrpV subfamily. TRPV6 sub-subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-41 is the initiator.
In human and mouse, initiation starts at a conserved non-canonical
ACG threonine codon decoded as Met-1 upstream of the canonical
initiation at Met-41. {ECO:0000250|UniProtKB:Q91WD2,
ECO:0000250|UniProtKB:Q9H1D0}.
-!- SEQUENCE CAUTION:
Sequence=AAD47636.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000250|UniProtKB:Q9H1D0};
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EMBL; AF160798; AAD47636.1; ALT_SEQ; mRNA.
RefSeq; NP_446138.1; NM_053686.1.
UniGene; Rn.205943; -.
PDB; 5IWK; X-ray; 3.25 A; A=41-709.
PDB; 5IWP; X-ray; 3.65 A; A=41-709.
PDB; 5IWR; X-ray; 3.85 A; A=41-709.
PDB; 5IWT; X-ray; 3.80 A; A=41-709.
PDB; 5WO6; X-ray; 3.31 A; A=41-708.
PDB; 5WO7; X-ray; 3.25 A; A=41-709.
PDB; 5WO8; X-ray; 3.40 A; A=41-709.
PDB; 5WO9; X-ray; 3.70 A; A=41-709.
PDB; 5WOA; X-ray; 3.90 A; A=41-709.
PDB; 6BOB; EM; 3.90 A; A/B/C/D=41-708.
PDBsum; 5IWK; -.
PDBsum; 5IWP; -.
PDBsum; 5IWR; -.
PDBsum; 5IWT; -.
PDBsum; 5WO6; -.
PDBsum; 5WO7; -.
PDBsum; 5WO8; -.
PDBsum; 5WO9; -.
PDBsum; 5WOA; -.
PDBsum; 6BOB; -.
SMR; Q9R186; -.
DIP; DIP-47769N; -.
IntAct; Q9R186; 1.
MINT; Q9R186; -.
STRING; 10116.ENSRNOP00000020616; -.
TCDB; 1.A.4.2.7; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; Q9R186; -.
PhosphoSitePlus; Q9R186; -.
PaxDb; Q9R186; -.
GeneID; 114246; -.
KEGG; rno:114246; -.
UCSC; RGD:69335; rat.
CTD; 55503; -.
RGD; 69335; Trpv6.
eggNOG; KOG3676; Eukaryota.
eggNOG; ENOG4110DG4; LUCA.
HOGENOM; HOG000234397; -.
HOVERGEN; HBG061442; -.
InParanoid; Q9R186; -.
KO; K04975; -.
PRO; PR:Q9R186; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IC:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005227; F:calcium activated cation channel activity; TAS:RGD.
GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0070509; P:calcium ion import; IDA:RGD.
GO; GO:0098703; P:calcium ion import across plasma membrane; IMP:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
CDD; cd00204; ANK; 1.
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; IPR008344; TRPV5/TRPV6.
InterPro; IPR008345; TRPV6_channel.
PANTHER; PTHR10582; PTHR10582; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR01415; ANKYRIN.
PRINTS; PR01765; ECACCHANNEL.
PRINTS; PR01766; ECACCHANNEL1.
SMART; SM00248; ANK; 5.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 2.
1: Evidence at protein level;
3D-structure; 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 1 767 Transient receptor potential cation
channel subfamily V member 6.
/FTId=PRO_0000215356.
TOPO_DOM 1 366 Cytoplasmic.
{ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TRANSMEM 367 387 Helical. {ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TOPO_DOM 388 424 Extracellular.
{ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TRANSMEM 425 447 Helical. {ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TOPO_DOM 448 462 Cytoplasmic.
{ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TRANSMEM 463 482 Helical. {ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TOPO_DOM 483 488 Extracellular.
{ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TRANSMEM 489 508 Helical. {ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TOPO_DOM 509 528 Cytoplasmic.
{ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TRANSMEM 529 551 Helical. {ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TOPO_DOM 552 564 Extracellular.
{ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
INTRAMEM 565 584 Pore-forming.
{ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TOPO_DOM 585 595 Extracellular.
{ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TRANSMEM 596 616 Helical. {ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
TOPO_DOM 617 767 Cytoplasmic.
{ECO:0000269|PubMed:27296226,
ECO:0000269|PubMed:28878326}.
REPEAT 84 114 ANK 1. {ECO:0000255}.
REPEAT 118 147 ANK 2. {ECO:0000255}.
REPEAT 156 185 ANK 3. {ECO:0000255}.
REPEAT 202 231 ANK 4. {ECO:0000255}.
REPEAT 235 276 ANK 5. {ECO:0000255}.
REPEAT 278 307 ANK 6. {ECO:0000255}.
REGION 133 143 Interaction with calmodulin.
{ECO:0000250}.
REGION 637 641 Interaction with S100A10. {ECO:0000250}.
REGION 689 707 Interaction with calmodulin.
{ECO:0000250}.
MOTIF 580 584 Selectivity filter.
{ECO:0000269|PubMed:27296226}.
METAL 581 581 Calcium; shared with neighboring
subunits. {ECO:0000244|PDB:5IWK,
ECO:0000244|PDB:5IWP,
ECO:0000269|PubMed:27296226}.
MOD_RES 201 201 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:17197020}.
MOD_RES 202 202 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:17197020}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 201 201 Y->F: Prevents up-regulation of the
channel by phosphorylation; when
associated with F-202.
{ECO:0000269|PubMed:17197020}.
MUTAGEN 202 202 Y->F: Prevents up-regulation of the
channel by phosphorylation; when
associated with F-201.
{ECO:0000269|PubMed:17197020}.
MUTAGEN 535 535 L->Q: Alters subunit assembly via domain
swapping and reduces channel activity.
{ECO:0000269|PubMed:28878326}.
HELIX 70 86 {ECO:0000244|PDB:5WO7}.
HELIX 88 94 {ECO:0000244|PDB:5WO7}.
HELIX 98 105 {ECO:0000244|PDB:5WO7}.
TURN 106 108 {ECO:0000244|PDB:5WO8}.
HELIX 122 128 {ECO:0000244|PDB:5WO7}.
HELIX 132 141 {ECO:0000244|PDB:5WO7}.
HELIX 143 146 {ECO:0000244|PDB:5WO7}.
TURN 154 157 {ECO:0000244|PDB:5WO7}.
HELIX 160 166 {ECO:0000244|PDB:5WO7}.
HELIX 170 178 {ECO:0000244|PDB:5WO7}.
HELIX 190 192 {ECO:0000244|PDB:5WO7}.
HELIX 206 212 {ECO:0000244|PDB:5WO7}.
HELIX 216 224 {ECO:0000244|PDB:5WO7}.
HELIX 239 244 {ECO:0000244|PDB:5WO7}.
HELIX 249 261 {ECO:0000244|PDB:5WO7}.
STRAND 267 269 {ECO:0000244|PDB:5WO7}.
TURN 271 273 {ECO:0000244|PDB:5WO7}.
HELIX 282 289 {ECO:0000244|PDB:5WO7}.
HELIX 292 300 {ECO:0000244|PDB:5WO7}.
STRAND 303 309 {ECO:0000244|PDB:5WO7}.
STRAND 312 317 {ECO:0000244|PDB:5WO7}.
TURN 320 322 {ECO:0000244|PDB:5WO7}.
STRAND 323 326 {ECO:0000244|PDB:5WO8}.
TURN 327 329 {ECO:0000244|PDB:5WO7}.
HELIX 331 337 {ECO:0000244|PDB:5WO7}.
HELIX 341 346 {ECO:0000244|PDB:5WO7}.
HELIX 352 361 {ECO:0000244|PDB:5WO7}.
TURN 362 364 {ECO:0000244|PDB:5WO7}.
HELIX 365 387 {ECO:0000244|PDB:5WO7}.
HELIX 397 399 {ECO:0000244|PDB:5IWK}.
TURN 401 404 {ECO:0000244|PDB:5WO7}.
TURN 418 420 {ECO:0000244|PDB:5WO6}.
HELIX 421 442 {ECO:0000244|PDB:5WO7}.
HELIX 463 481 {ECO:0000244|PDB:5WO7}.
TURN 482 484 {ECO:0000244|PDB:5WO7}.
HELIX 487 489 {ECO:0000244|PDB:5IWK}.
HELIX 490 501 {ECO:0000244|PDB:5WO7}.
HELIX 504 510 {ECO:0000244|PDB:5WO7}.
HELIX 515 530 {ECO:0000244|PDB:5WO7}.
HELIX 533 552 {ECO:0000244|PDB:5WO7}.
TURN 556 558 {ECO:0000244|PDB:5WO7}.
HELIX 565 576 {ECO:0000244|PDB:5WO7}.
STRAND 586 588 {ECO:0000244|PDB:5WO7}.
HELIX 592 613 {ECO:0000244|PDB:5WO7}.
TURN 614 617 {ECO:0000244|PDB:5WO7}.
TURN 618 620 {ECO:0000244|PDB:5IWK}.
HELIX 622 646 {ECO:0000244|PDB:5WO7}.
STRAND 649 652 {ECO:0000244|PDB:5WO6}.
STRAND 655 659 {ECO:0000244|PDB:5WO7}.
STRAND 662 664 {ECO:0000244|PDB:5WO7}.
STRAND 668 675 {ECO:0000244|PDB:5WO7}.
SEQUENCE 767 AA; 87362 MW; 2197726C2F583720 CRC64;
MGPLQREGRP ALGDANVAPG SSPGGVWHQP QPPKDSAFHP MGWSLPKEKG LILCLWNKFC
RWFHRRESWA QSRDEQNLLQ QKRIWESPLL LAAKENNVQA LIKLLKFEGC EVHQKGAMGE
TALHIAALYD NLEAAMVLME AAPELVFEPM TSELYEGQTA LHIAVINQNV NLVRALLARG
ASVSARATGS VFHYRPHNLI YYGEHPLSFA ACVGSEEIVR LLIEHGADIR AQDSLGNTVL
HILILQPNKT FACQMYNLLL SYDGGDHLKS LELVPNNQGL TPFKLAGVEG NIVMFQHLMQ
KRKHIQWTYG PLTSTLYDLT EIDSSGDDQS LLELIVTTKK REARQILDQT PVKELVSLKW
KRYGRPYFCV LGAIYVLYII CFTMCCVYRP LKPRITNRTN PRDNTLLQQK LLQEAYVTPK
DDLRLVGELV SIVGAVIILL VEIPDIFRLG VTRFFGQTIL GGPFHVIIVT YAFMVLVTMV
MRLTNSDGEV VPMSFALVLG WCNVMYFARG FQMLGPFTIM IQKMIFGDLM RFCWLMAVVI
LGFASAFYII FQTEDPDELG HFYDYPMALF STFELFLTII DGPANYDVDL PFMYSITYAA
FAIIATLLML NLLIAMMGDT HWRVAHERDE LWRAQVVATT VMLERKLPRC LWPRSGICGR
EYGLGDRWFL RVEDRQDLNR QRIRRYAQAF QQQDDLYSED LEKDSGEKLE MARPFGAYLS
FPTPSVSRST SRSSTNWDRL RQGALRKDLQ GIINRGLEDG EGWEYQI


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