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Protein

Transient receptor potential cation channel subfamily V member 4

Gene

TRPV4

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:11081638). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:11081638). Also activated by phorbol esters (PubMed:19864432). Channel activity seems to be regulated by a calmodulin-dependent mechanism (By similarity).By similarity2 Publications

Enzyme regulationi

ATP binding enhances channel sensitivity to agonists. Ca2+-calmodulin prevents the ATP-mediated increased sensitivity to agonists.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei178ATPBy similarity1
Binding sitei183ATPBy similarity1
Binding sitei187ATPBy similarity1
Binding sitei234ATPBy similarity1
Binding sitei330Phosphatidylinositol-1,4,5-trisphosphateCombined sources1 Publication1
Metal bindingi668Calcium; shared with neighboring subunitsBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi222 – 225ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionCalcium channel, Calmodulin-binding, Ion channel
Biological processCalcium transport, Ion transport, Transport
LigandATP-binding, Calcium, Lipid-binding, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily V member 4
Short name:
TrpV4
Alternative name(s):
Vanilloid receptor-related osmotically activated channel1 Publication
Short name:
VR-OAC1 Publication
Gene namesi
Name:TRPV4Imported
OrganismiGallus gallus (Chicken)Imported
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 15

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 455CytoplasmicBy similarityAdd BLAST455
Transmembranei456 – 476HelicalBy similarityAdd BLAST21
Topological domaini477 – 493ExtracellularBy similarityAdd BLAST17
Transmembranei494 – 520HelicalBy similarityAdd BLAST27
Topological domaini521 – 533CytoplasmicBy similarityAdd BLAST13
Transmembranei534 – 554HelicalBy similarityAdd BLAST21
Topological domaini555 – 558ExtracellularBy similarity4
Transmembranei559 – 579HelicalBy similarityAdd BLAST21
Topological domaini580 – 594CytoplasmicBy similarityAdd BLAST15
Transmembranei595 – 622HelicalBy similarityAdd BLAST28
Topological domaini623 – 651ExtracellularBy similarityAdd BLAST29
Intramembranei652 – 671Pore-formingBy similarityAdd BLAST20
Topological domaini672 – 679ExtracellularBy similarity8
Transmembranei680 – 708HelicalBy similarityAdd BLAST29
Topological domaini709 – 852CytoplasmicBy similarityAdd BLAST144

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi178K → A: Strongly decreased affinity for ATP and Ca(2+)-calmodulin. Abolishes ATP-mediated increase in channel sensitivity to agonists. 1 Publication1
Mutagenesisi183K → A: Strongly decreased affinity for ATP and slightly decreased affinity for Ca(2+)-calmodulin. 1 Publication1
Mutagenesisi205K → A: No significant effect on affinity for ATP and Ca(2+)-calmodulin. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004434811 – 852Transient receptor potential cation channel subfamily V member 4Add BLAST852

Interactioni

Subunit structurei

Homotetramer (By similarity). Interacts with Ca2+-calmodulin (PubMed:19864432).By similarity1 Publication

GO - Molecular functioni

Structurei

Secondary structure

1852
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi137 – 146Combined sources10
Helixi149 – 152Combined sources4
Helixi155 – 161Combined sources7
Helixi169 – 171Combined sources3
Turni174 – 176Combined sources3
Helixi180 – 185Combined sources6
Beta strandi189 – 191Combined sources3
Helixi195 – 205Combined sources11
Helixi209 – 214Combined sources6
Beta strandi220 – 225Combined sources6
Helixi227 – 233Combined sources7
Helixi237 – 245Combined sources9
Beta strandi260 – 262Combined sources3
Helixi274 – 280Combined sources7
Helixi284 – 292Combined sources9
Helixi310 – 317Combined sources8
Helixi322 – 342Combined sources21
Helixi348 – 350Combined sources3
Helixi359 – 365Combined sources7
Helixi369 – 382Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JXIX-ray2.30A/B/C/D133-382[»]
3JXJX-ray2.80A/B133-382[»]
3W9FX-ray1.90A/B/C/D133-382[»]
3W9GX-ray2.00A/B/C/D133-382[»]
SMRiA0A1D5PXA5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DFS3

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati223 – 252ANK 1Sequence analysisAdd BLAST30
Repeati270 – 299ANK 2Sequence analysisAdd BLAST30
Repeati355 – 387ANK 3Sequence analysisAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni235 – 237Phosphatidylinositol-1,4,5-trisphosphate bindingCombined sources1 Publication3
Regioni282 – 285Phosphatidylinositol-1,4,5-trisphosphate bindingCombined sources1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi665 – 668Selectivity filterBy similarity4

Domaini

The ANK repeat region mediates interaction with Ca2+-calmodulin and ATP binding (PubMed:19864432). The ANK repeat region mediates interaction with phosphatidylinositol-4,5-bisphosphate and related phosphatidylinositides (PubMed:25256292).2 Publications

Sequence similaritiesi

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3676 Eukaryota
ENOG4110DG4 LUCA
GeneTreeiENSGT00550000074425
HOGENOMiHOG000234630
HOVERGENiHBG054085
KOiK04973

Family and domain databases

CDDicd00204 ANK, 1 hit
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR005821 Ion_trans_dom
IPR004729 TRP_channel
IPR024862 TRPV
IPR008347 TRPV1-4_channel
IPR008348 TRPV4_channel
PANTHERiPTHR10582 PTHR10582, 1 hit
PTHR10582:SF4 PTHR10582:SF4, 1 hit
PfamiView protein in Pfam
PF00023 Ank, 1 hit
PF00520 Ion_trans, 1 hit
PRINTSiPR01768 TRPVRECEPTOR
PR01769 VRL2RECEPTOR
SMARTiView protein in SMART
SM00248 ANK, 3 hits
SUPFAMiSSF48403 SSF48403, 2 hits
TIGRFAMsiTIGR00870 trp, 1 hit
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 1 hit

Sequencei

Sequence statusi: Complete.

A0A1D5PXA5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADPEDPRDA GDVLGDDSFP LSSLANLFEV EDTPSPAEPS RGPPGAVDGK
60 70 80 90 100
QNLRMKFHGA FRKGPPKPME LLESTIYESS VVPAPKKAPM DSLFDYGTYR
110 120 130 140 150
QHPSENKRWR RRVVEKPVAG TKGPAPNPPP ILKVFNRPIL FDIVSRGSPD
160 170 180 190 200
GLEGLLSFLL THKKRLTDEE FREPSTGKTC LPKALLNLSA GRNDTIPILL
210 220 230 240 250
DIAEKTGNMR EFINSPFRDV YYRGQTALHI AIERRCKHYV ELLVEKGADV
260 270 280 290 300
HAQARGRFFQ PKDEGGYFYF GELPLSLAAC TNQPHIVHYL TENGHKQADL
310 320 330 340 350
RRQDSRGNTV LHALVAIADN TRENTKFVTK MYDLLLIKCA KLFPDTNLEA
360 370 380 390 400
LLNNDGLSPL MMAAKTGKIG IFQHIIRREI ADEDVRHLSR KFKDWAYGPV
410 420 430 440 450
YSSLYDLSSL DTCGEEVSVL EILVYNSKIE NRHEMLAVEP INELLRDKWR
460 470 480 490 500
KFGAVSFYIS VVSYLCAMII FTLIAYYRPM EGPPPYPYTT TIDYLRLAGE
510 520 530 540 550
IITLLTGILF FFSNIKDLFM KKCPGVNSFF IDGSFQLLYF IYSVLVIVTA
560 570 580 590 600
GLYLGGVEAY LAVMVFALVL GWMNALYFTR GLKLTGTYSI MIQKILFKDL
610 620 630 640 650
FRFLLVYLLF MIGYASALVS LLNPCPSSES CSEDHSNCTL PTYPSCRDSQ
660 670 680 690 700
TFSTFLLDLF KLTIGMGDLE MLESAKYPGV FIILLVTYII LTFVLLLNML
710 720 730 740 750
IALMGETVGQ VSKESKHIWK LQWATTILDI ERSFPLFLRR VFRSGEMVTV
760 770 780 790 800
GKGTDGTPDR RWCFRVDEVN WSHWNQNLGI ISEDPGKSDT YQYYGFSHTV
810 820 830 840 850
GRLRRDRWST VVPRVVELNK SCPTEDVVVP LGTMGTAEAR ERRHGQTPSS

PL
Length:852
Mass (Da):96,282
Last modified:November 30, 2016 - v1
Checksum:i0A799C76C6598845
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47V → G in AAG28026 (PubMed:11081638).Curated1
Sequence conflicti131I → V in AAG28026 (PubMed:11081638).Curated1
Sequence conflicti741V → A in AAG28026 (PubMed:11081638).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF261883 mRNA Translation: AAG28026.1
AADN04000193 Genomic DNA No translation available.
RefSeqiNP_990023.1, NM_204692.1
UniGeneiGga.51246

Genome annotation databases

EnsembliENSGALT00000049402; ENSGALP00000057599; ENSGALG00000036360
GeneIDi395427
KEGGigga:395427

Similar proteinsi

Entry informationi

Entry nameiTRPV4_CHICK
AccessioniPrimary (citable) accession number: A0A1D5PXA5
Secondary accession number(s): Q9DFS3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 28, 2018
Last sequence update: November 30, 2016
Last modified: May 23, 2018
This is version 12 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health