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Protein

Transient receptor potential cation channel subfamily V member 6

Gene

TRPV6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium selective cation channel probably involved in Ca2+ uptake in various tissues, including Ca2+ reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca2+-dependent and a slower Ca2+-calmodulin-dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg2+ in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity).By similarity4 Publications

GO - Molecular functioni

  • calcium channel activity Source: UniProtKB
  • calmodulin binding Source: UniProtKB

GO - Biological processi

  • calcium ion transmembrane transport Source: Reactome
  • calcium ion transport Source: UniProtKB
  • ion transmembrane transport Source: Reactome
  • regulation of calcium ion-dependent exocytosis Source: UniProtKB
  • transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.

Protein family/group databases

TCDBi1.A.4.2.11. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily V member 6
Short name:
TrpV6
Alternative name(s):
CaT-like
Short name:
CaT-L
Calcium transport protein 1
Short name:
CaT1
Epithelial calcium channel 2
Short name:
ECaC2
Gene namesi
Name:TRPV6
Synonyms:ECAC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:14006. TRPV6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 368368CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei369 – 38921HelicalSequence AnalysisAdd
BLAST
Topological domaini390 – 42738ExtracellularSequence AnalysisAdd
BLAST
Transmembranei428 – 44821HelicalSequence AnalysisAdd
BLAST
Topological domaini449 – 45911CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei460 – 48021HelicalSequence AnalysisAdd
BLAST
Topological domaini481 – 4888ExtracellularSequence Analysis
Transmembranei489 – 50921HelicalSequence AnalysisAdd
BLAST
Topological domaini510 – 53223CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei533 – 55321HelicalSequence AnalysisAdd
BLAST
Intramembranei564 – 58421Pore-formingBy similarityAdd
BLAST
Transmembranei597 – 61721HelicalSequence AnalysisAdd
BLAST
Topological domaini618 – 765148CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi582 – 5821D → A: Abolishes channel activity. 1 Publication
Mutagenesisi742 – 7421T → A: Abolishes phosphorylation by PKC/PRKCA, achieves faster channel inactivation and no effect on binding to calmodulin. 1 Publication

Organism-specific databases

PharmGKBiPA37832.

Polymorphism and mutation databases

DMDMi62901469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 765765Transient receptor potential cation channel subfamily V member 6PRO_0000215354Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011Phosphotyrosine; by SRCBy similarity
Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis
Modified residuei742 – 7421Phosphothreonine; by PKC/PRKCA1 Publication

Post-translational modificationi

Glycosylated.By similarity1 Publication
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.By similarity1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9H1D0.
PaxDbiQ9H1D0.
PRIDEiQ9H1D0.

PTM databases

PhosphoSiteiQ9H1D0.

Expressioni

Tissue specificityi

Expressed at high levels in the gastrointestinal tract, including esophagus, stomach, duodenum, jejunum, ileum and colon, and in pancreas, placenta, prostate and salivary gland. Expressed at moderate levels in liver, kidney and testis. Expressed in trophoblasts of placenta villus trees (at protein level)(PubMed:23612980). Expressed in locally advanced prostate cancer, metastatic and androgen-insensitive prostatic lesions but not detected in healthy prostate tissue and benign prostatic hyperplasia.3 Publications

Gene expression databases

BgeeiQ9H1D0.
CleanExiHS_TRPV6.
ExpressionAtlasiQ9H1D0. baseline.
GenevestigatoriQ9H1D0.

Organism-specific databases

HPAiHPA062864.

Interactioni

Subunit structurei

Homotetramer and probably heterotetramer 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 BSPRY (By similarity). Interacts with TCAF1 and TCAF2 isoform 2 (PubMed:25559186). Interacts with calmodulin.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN1P180316EBI-7198335,EBI-968788

Protein-protein interaction databases

BioGridi120683. 16 interactions.
IntActiQ9H1D0. 2 interactions.
MINTiMINT-1472896.
STRINGi9606.ENSP00000352358.

Structurei

3D structure databases

ProteinModelPortaliQ9H1D0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati84 – 11431ANK 1Add
BLAST
Repeati118 – 14730ANK 2Add
BLAST
Repeati156 – 18530ANK 3Add
BLAST
Repeati202 – 23130ANK 4Add
BLAST
Repeati235 – 27743ANK 5Add
BLAST
Repeati279 – 30830ANK 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 14311Interaction with calmodulinBy similarityAdd
BLAST
Regioni638 – 6425Interaction with S100A10By similarity
Regioni731 – 75121Interaction with calmodulinAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi581 – 5855Selectivity filterBy similarity

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG278734.
HOVERGENiHBG061442.
InParanoidiQ9H1D0.
KOiK04975.
OMAiRSSANWG.
OrthoDBiEOG70087C.
TreeFamiTF314711.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008344. TRPV5/TRPV6.
IPR008345. TRPV6_channel.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
PR01765. ECACCHANNEL.
PR01766. ECACCHANNEL1.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H1D0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGPLQGDGGP ALGGADVAPR LSPVRVWPRP QAPKEPALHP MGLSLPKEKG
60 70 80 90 100
LILCLWSKFC RWFQRRESWA QSRDEQNLLQ QKRIWESPLL LAAKDNDVQA
110 120 130 140 150
LNKLLKYEDC KVHQRGAMGE TALHIAALYD NLEAAMVLME AAPELVFEPM
160 170 180 190 200
TSELYEGQTA LHIAVVNQNM NLVRALLARR ASVSARATGT AFRRSPCNLI
210 220 230 240 250
YFGEHPLSFA ACVNSEEIVR LLIEHGADIR AQDSLGNTVL HILILQPNKT
260 270 280 290 300
FACQMYNLLL SYDRHGDHLQ PLDLVPNHQG LTPFKLAGVE GNTVMFQHLM
310 320 330 340 350
QKRKHTQWTY GPLTSTLYDL TEIDSSGDEQ SLLELIITTK KREARQILDQ
360 370 380 390 400
TPVKELVSLK WKRYGRPYFC MLGAIYLLYI ICFTMCCIYR PLKPRTNNRT
410 420 430 440 450
SPRDNTLLQQ KLLQEAYMTP KDDIRLVGEL VTVIGAIIIL LVEVPDIFRM
460 470 480 490 500
GVTRFFGQTI LGGPFHVLII TYAFMVLVTM VMRLISASGE VVPMSFALVL
510 520 530 540 550
GWCNVMYFAR GFQMLGPFTI MIQKMIFGDL MRFCWLMAVV ILGFASAFYI
560 570 580 590 600
IFQTEDPEEL GHFYDYPMAL FSTFELFLTI IDGPANYNVD LPFMYSITYA
610 620 630 640 650
AFAIIATLLM LNLLIAMMGD THWRVAHERD ELWRAQIVAT TVMLERKLPR
660 670 680 690 700
CLWPRSGICG REYGLGDRWF LRVEDRQDLN RQRIQRYAQA FHTRGSEDLD
710 720 730 740 750
KDSVEKLELG CPFSPHLSLP MPSVSRSTSR SSANWERLRQ GTLRRDLRGI
760
INRGLEDGES WEYQI
Length:765
Mass (Da):87,286
Last modified:April 1, 2015 - v3
Checksum:i626D515E12112546
GO
Isoform 2 (identifier: Q9H1D0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     65-232: Missing.

Show »
Length:597
Mass (Da):68,446
Checksum:i6EB713BE033FD580
GO

Sequence cautioni

The sequence AAK50426.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.1 Publication
The sequence AAL40230.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.1 Publication
The sequence AAM00356.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.1 Publication
The sequence AAO38052.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.1 Publication
The sequence BAF84396.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.1 Publication
The sequence CAC20416.2 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.1 Publication
The sequence CAC20417.2 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.1 Publication
The sequence CAD32311.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.1 Publication

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771N → D in AAG41951 (PubMed:11097838).Curated
Sequence conflicti114 – 1141Q → H in AAG41951 (PubMed:11097838).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti197 – 1971C → R.2 Publications
Corresponds to variant rs4987657 [ dbSNP | Ensembl ].
VAR_022251
Natural varianti399 – 3991R → Q.
Corresponds to variant rs4987665 [ dbSNP | Ensembl ].
VAR_052393
Natural varianti418 – 4181M → V.2 Publications
Corresponds to variant rs4987667 [ dbSNP | Ensembl ].
VAR_022252
Natural varianti721 – 7211M → T.2 Publications
Corresponds to variant rs4987682 [ dbSNP | Ensembl ].
VAR_022253

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei65 – 232168Missing in isoform 2. 1 PublicationVSP_013439Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF304463 mRNA. Translation: AAG41951.1.
AF365927 mRNA. Translation: AAL40230.1. Sequence problems.
AF365928 mRNA. Translation: AAM00356.1. Sequence problems.
AH010730 Genomic DNA. Translation: AAK50426.1. Sequence problems.
AJ243500 mRNA. Translation: CAC20416.2. Sequence problems.
AJ243501 mRNA. Translation: CAC20417.2. Sequence problems.
AJ487964 mRNA. Translation: CAD32311.1. Sequence problems.
AY225461 Genomic DNA. Translation: AAO38052.1. Sequence problems.
AK291707 mRNA. Translation: BAF84396.1. Sequence problems.
CH236959 Genomic DNA. Translation: EAL23776.1.
PIRiJC7531.
RefSeqiNP_061116.5. NM_018646.5. [Q9H1D0-1]
UniGeneiHs.302740.

Genome annotation databases

EnsembliENST00000359396; ENSP00000352358; ENSG00000165125.
GeneIDi55503.
KEGGihsa:55503.
UCSCiuc003wbw.1. human. [Q9H1D0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

TRPV6 entry

SeattleSNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF304463 mRNA. Translation: AAG41951.1.
AF365927 mRNA. Translation: AAL40230.1. Sequence problems.
AF365928 mRNA. Translation: AAM00356.1. Sequence problems.
AH010730 Genomic DNA. Translation: AAK50426.1. Sequence problems.
AJ243500 mRNA. Translation: CAC20416.2. Sequence problems.
AJ243501 mRNA. Translation: CAC20417.2. Sequence problems.
AJ487964 mRNA. Translation: CAD32311.1. Sequence problems.
AY225461 Genomic DNA. Translation: AAO38052.1. Sequence problems.
AK291707 mRNA. Translation: BAF84396.1. Sequence problems.
CH236959 Genomic DNA. Translation: EAL23776.1.
PIRiJC7531.
RefSeqiNP_061116.5. NM_018646.5. [Q9H1D0-1]
UniGeneiHs.302740.

3D structure databases

ProteinModelPortaliQ9H1D0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120683. 16 interactions.
IntActiQ9H1D0. 2 interactions.
MINTiMINT-1472896.
STRINGi9606.ENSP00000352358.

Chemistry

BindingDBiQ9H1D0.
ChEMBLiCHEMBL1628465.
GuidetoPHARMACOLOGYi512.

Protein family/group databases

TCDBi1.A.4.2.11. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteiQ9H1D0.

Polymorphism and mutation databases

DMDMi62901469.

Proteomic databases

MaxQBiQ9H1D0.
PaxDbiQ9H1D0.
PRIDEiQ9H1D0.

Protocols and materials databases

DNASUi55503.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359396; ENSP00000352358; ENSG00000165125.
GeneIDi55503.
KEGGihsa:55503.
UCSCiuc003wbw.1. human. [Q9H1D0-1]

Organism-specific databases

CTDi55503.
GeneCardsiGC07M142568.
H-InvDBHIX0007162.
HGNCiHGNC:14006. TRPV6.
HPAiHPA062864.
MIMi606680. gene.
neXtProtiNX_Q9H1D0.
PharmGKBiPA37832.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG278734.
HOVERGENiHBG061442.
InParanoidiQ9H1D0.
KOiK04975.
OMAiRSSANWG.
OrthoDBiEOG70087C.
TreeFamiTF314711.

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.

Miscellaneous databases

GeneWikiiTRPV6.
GenomeRNAii55503.
NextBioi59887.
PROiQ9H1D0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H1D0.
CleanExiHS_TRPV6.
ExpressionAtlasiQ9H1D0. baseline.
GenevestigatoriQ9H1D0.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008344. TRPV5/TRPV6.
IPR008345. TRPV6_channel.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
PR01765. ECACCHANNEL.
PR01766. ECACCHANNEL1.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. "1,25-dihydroxyvitamin D3 increases the expression of the CaT1 epithelial calcium channel in the Caco-2 human intestinal cell line."
    Wood R.J., Tchack L., Taparia S.
    BMC Physiol. 1:11-11(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  3. "Structural conservation of the genes encoding CaT1, CaT2, and related cation channels."
    Peng J.-B., Brown E.M., Hediger M.A.
    Genomics 76:99-109(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  4. "Expression of CaT-like, a novel calcium selective channel, correlates with the malignancy of prostate cancer."
    Wissenbach U., Niemeyer B.A., Fixemer T., Schneidewind A., Trost C., Cavalie A., Reus K., Meese E., Bonkhoff H., Flockerzi V.
    J. Biol. Chem. 276:19461-19468(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-197; VAL-418 AND THR-721, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Placenta.
  5. "A CaT1 splice variant lacking ankyrin repeats."
    Peng J.-B., Brown E.M., Hediger M.A.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  6. Kelsell R.E.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. SeattleSNPs variation discovery resource
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-197; VAL-418 AND THR-721.
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  9. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 41-765.
  10. "Competitive regulation of CaT-like-mediated Ca2+ entry by protein kinase C and calmodulin."
    Niemeyer B.A., Bergs C., Wissenbach U., Flockerzi V., Trost C.
    Proc. Natl. Acad. Sci. U.S.A. 98:3600-3605(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CALMODULIN, PHOSPHORYLATION AT THR-742, MUTAGENESIS OF THR-742.
  11. "Ca2+ dependence of the Ca2+-selective TRPV6 channel."
    Bodding M., Flockerzi V.
    J. Biol. Chem. 279:36546-36552(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-582.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "The in vivo TRPV6 protein starts at a non-AUG triplet, decoded as methionine, upstream of canonical initiation at AUG."
    Fecher-Trost C., Wissenbach U., Beck A., Schalkowsky P., Stoerger C., Doerr J., Dembek A., Simon-Thomas M., Weber A., Wollenberg P., Ruppert T., Middendorff R., Maurer H.H., Flockerzi V.
    J. Biol. Chem. 288:16629-16644(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION OF NON-CANONICAL INITIATION CODON, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
  14. Cited for: INTERACTION WITH TCAF1 AND TCAF2.

Entry informationi

Entry nameiTRPV6_HUMAN
AccessioniPrimary (citable) accession number: Q9H1D0
Secondary accession number(s): A4D2I8
, Q8TDL3, Q8WXR8, Q96LC5, Q9H1D1, Q9H296
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 1, 2015
Last modified: May 27, 2015
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.