TRPV6
entrez
55503
canonical
uniprot
Q9H1D0
canonical
ensembl
ENSG00000165125
resolver
ensp
ENSP00000352358
resolver
genesymbol
TRPV6
resolver
genesymbol_syn
ECAC2
resolver
hgnc
HGNC:14006
resolver
uniprot
A4D2I8
resolver
uniprot
Q8TDL3
resolver
uniprot
Q8WXR8
resolver
uniprot
Q96LC5
resolver
uniprot
Q9H1D1
resolver
uniprot
Q9H296
resolver
uniprot_entry
TRPV6_HUMAN
resolver
uniprot_sec
A4D2I8
resolver
uniprot_sec
Q8TDL3
resolver
uniprot_sec
Q8WXR8
resolver
uniprot_sec
Q96LC5
resolver
uniprot_sec
Q9H1D1
resolver
uniprot_sec
Q9H296
resolver
amino_acid_sequence
MGPLQGDGGPALGGADVAPRLSPVRVWPRPQAPKEPALHPMGLSLPKEKGLILCLWSKFCRWFQRRESWAQSRDEQNLLQQKRIWESPLLLAAKDNDVQALNKLLKYEDCKVHQRGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVVNQNMNLVRALLARRASVSARATGTAFRRSPCNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDRHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHTQWTYGPLTSTLYDLTEIDSSGDEQSLLELIITTKKREARQILDQTPVKELVSLKWKRYGRPYFCMLGAIYLLYIICFTMCCIYRPLKPRTNNRTSPRDNTLLQQKLLQEAYMTPKDDIRLVGELVTVIGAIIILLVEVPDIFRMGVTRFFGQTILGGPFHVLIITYAFMVLVTMVMRLISASGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPEELGHFYDYPMALFSTFELFLTIIDGPANYNVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQIVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIQRYAQAFHTRGSEDLDKDSVEKLELGCPFSPHLSLPMPSVSRSTSRSSANWERLRQGTLRRDLRGIINRGLEDGESWEYQI
uniprot
proteins
disease_involvement
DISEASE: Hyperparathyroidism, transient neonatal (HRPTTN) [MIM:618188]: An autosomal recessive disease characterized by impaired transplacental maternal-fetal transport of calcium, high serum PTH levels and signs of metabolic bone disease in the neonatal period. Skeletal anomalies include generalized osteopenia, narrow chest, short ribs with multiple healing fractures, and bowing or fractures of long bones. Affected individuals experience postnatal respiratory and feeding difficulties. The condition improves within a short time after birth once calcium is provided orally. {ECO:0000269|PubMed:29861107, ECO:0000269|PubMed:30820485}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine (PubMed:11097838, PubMed:11248124, PubMed:11278579, PubMed:15184369, PubMed:23612980, PubMed:29258289). 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:15184369). 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. {ECO:0000250|UniProtKB:Q91WD2, ECO:0000269|PubMed:11097838, ECO:0000269|PubMed:11248124, ECO:0000269|PubMed:11278579, ECO:0000269|PubMed:15184369, ECO:0000269|PubMed:23612980, ECO:0000269|PubMed:29258289, ECO:0000269|PubMed:29861107}.
uniprot
proteins
mass_dalton
87286
uniprot
proteins
mutagenesis
MUTAGEN 510; /note="R->E: Decreases channel opening, and thereby decreases channel activity."; /evidence="ECO:0000269|PubMed:29258289"; MUTAGEN 523; /note="Q->A: Decreases channel activity."; /evidence="ECO:0000269|PubMed:29258289"; MUTAGEN 582; /note="D->A: Abolishes channel activity."; /evidence="ECO:0000269|PubMed:15184369"; MUTAGEN 606; /note="A->T: Decreases channel opening, and thereby strongly decreases channel activity."; /evidence="ECO:0000269|PubMed:29258289"; MUTAGEN 742; /note="T->A: Abolishes phosphorylation by PKC/PRKCA, achieves faster channel inactivation and no effect on binding to calmodulin."; /evidence="ECO:0000269|PubMed:11248124
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000250|UniProtKB:Q91WD2, ECO:0000269|PubMed:23612980}.; PTM: Phosphorylation at Tyr-201 by SRC leads to an increased calcium influx through the channel. Probably dephosphorylated at this site by PTPN1 (By similarity). Phosphorylation by PRKCA at the calmodulin binding site delays channel inactivation (PubMed:11248124). {ECO:0000250|UniProtKB:Q9R186, ECO:0000269|PubMed:11248124}.
uniprot
proteins
protein_family
TRPV6 sub-subfamily
uniprot
proteins
protein_family
Transient receptor (TC 1.A.4) family
uniprot
proteins
protein_family
TrpV subfamily
uniprot
proteins
pubmed
11097838
uniprot
proteins
pubmed
11248124
uniprot
proteins
pubmed
11278579
uniprot
proteins
pubmed
11545681
uniprot
proteins
pubmed
11549322
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15184369
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
23612980
uniprot
proteins
pubmed
25559186
uniprot
proteins
pubmed
29258289
uniprot
proteins
pubmed
29861107
uniprot
proteins
pubmed
30820485
uniprot
proteins
sequence_length
765
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11097838, ECO:0000269|PubMed:11248124, ECO:0000269|PubMed:11278579, ECO:0000269|PubMed:15184369, ECO:0000269|PubMed:23612980, ECO:0000269|PubMed:29258289, ECO:0000269|PubMed:29861107}; Multi-pass membrane protein {ECO:0000269|PubMed:29258289}.
uniprot
proteins
transmembrane_region
TRANSMEM 368..388; /note="Helical"; /evidence="ECO:0000305|PubMed:29258289"; TRANSMEM 426..448; /note="Helical"; /evidence="ECO:0000305|PubMed:29258289"; TRANSMEM 464..483; /note="Helical"; /evidence="ECO:0000305|PubMed:29258289"; TRANSMEM 490..509; /note="Helical"; /evidence="ECO:0000305|PubMed:29258289"; TRANSMEM 530..552; /note="Helical"; /evidence="ECO:0000305|PubMed:29258289"; TRANSMEM 597..617; /note="Helical"; /evidence="ECO:0000305|PubMed:29258289
uniprot
proteins