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UniProtKB - A0A1D5PXA5 (TRPV4_CHICK)
Protein
Transient receptor potential cation channel subfamily V member 4
Gene
TRPV4
Organism
Gallus gallus (Chicken)
Status
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 PublicationsActivity regulationi
ATP binding enhances channel sensitivity to agonists. Ca2+-calmodulin prevents the ATP-mediated increased sensitivity to agonists.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 178 | ATPBy similarity | 1 | |
Binding sitei | 183 | ATPBy similarity | 1 | |
Binding sitei | 187 | ATPBy similarity | 1 | |
Binding sitei | 234 | ATPBy similarity | 1 | |
Binding sitei | 330 | Phosphatidylinositol 4,5-bisphosphateCombined sources1 Publication | 1 | |
Metal bindingi | 668 | Calcium; shared with neighboring subunitsBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 222 – 225 | ATPBy similarity | 4 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- calcium channel activity Source: GO_Central
- calmodulin binding Source: UniProtKB
- cation channel activity Source: UniProtKB
- ion channel activity Source: GO_Central
- lipid binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- actin filament organization Source: GO_Central
- calcium ion import across plasma membrane Source: GO_Central
- cellular calcium ion homeostasis Source: UniProtKB
- osmosensory signaling pathway Source: GO_Central
Keywordsi
Molecular function | Calcium channel, Calmodulin-binding, Ion channel |
Biological process | Calcium transport, Ion transport, Transport |
Ligand | ATP-binding, Calcium, Lipid-binding, Metal-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Transient receptor potential cation channel subfamily V member 4Short name: TrpV4 Alternative name(s): Vanilloid receptor-related osmotically activated channel1 Publication Short name: VR-OAC1 Publication |
Gene namesi | Name:TRPV4 |
Organismi | Gallus gallus (Chicken)Imported |
Taxonomic identifieri | 9031 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Apical cell membrane 2 Publications; Multi-pass membrane protein By similarity
Other locations
- adherens junction By similarity
Plasma Membrane
- apical plasma membrane Source: UniProtKB-SubCell
- integral component of plasma membrane Source: GO_Central
- plasma membrane Source: UniProtKB
Other locations
- adherens junction Source: UniProtKB-SubCell
- cilium Source: GO_Central
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 455 | CytoplasmicBy similarityAdd BLAST | 455 | |
Transmembranei | 456 – 476 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 477 – 493 | ExtracellularBy similarityAdd BLAST | 17 | |
Transmembranei | 494 – 520 | HelicalBy similarityAdd BLAST | 27 | |
Topological domaini | 521 – 533 | CytoplasmicBy similarityAdd BLAST | 13 | |
Transmembranei | 534 – 554 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 555 – 558 | ExtracellularBy similarity | 4 | |
Transmembranei | 559 – 579 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 580 – 594 | CytoplasmicBy similarityAdd BLAST | 15 | |
Transmembranei | 595 – 622 | HelicalBy similarityAdd BLAST | 28 | |
Topological domaini | 623 – 651 | ExtracellularBy similarityAdd BLAST | 29 | |
Intramembranei | 652 – 671 | Pore-formingBy similarityAdd BLAST | 20 | |
Topological domaini | 672 – 679 | ExtracellularBy similarity | 8 | |
Transmembranei | 680 – 708 | HelicalBy similarityAdd BLAST | 29 | |
Topological domaini | 709 – 852 | CytoplasmicBy similarityAdd BLAST | 144 |
Keywords - Cellular componenti
Cell junction, Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 178 | K → A: Strongly decreased affinity for ATP and Ca(2+)-calmodulin. Abolishes ATP-mediated increase in channel sensitivity to agonists. 1 Publication | 1 | |
Mutagenesisi | 183 | K → A: Strongly decreased affinity for ATP and slightly decreased affinity for Ca(2+)-calmodulin. 1 Publication | 1 | |
Mutagenesisi | 205 | K → A: No significant effect on affinity for ATP and Ca(2+)-calmodulin. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000443481 | 1 – 852 | Transient receptor potential cation channel subfamily V member 4Add BLAST | 852 |
Interactioni
Subunit structurei
Homotetramer (By similarity).
Interacts with Ca2+-calmodulin (PubMed:19864432).
By similarity1 PublicationGO - Molecular functioni
- calmodulin binding Source: UniProtKB
Protein-protein interaction databases
STRINGi | 9031.ENSGALP00000008256 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | A0A1D5PXA5 |
SMRi | A0A1D5PXA5 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 223 – 252 | ANK 1Sequence analysisAdd BLAST | 30 | |
Repeati | 270 – 299 | ANK 2Sequence analysisAdd BLAST | 30 | |
Repeati | 355 – 387 | ANK 3Sequence analysisAdd BLAST | 33 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 30 – 51 | DisorderedSequence analysisAdd BLAST | 22 | |
Regioni | 235 – 237 | Phosphatidylinositol 4,5-bisphosphate bindingCombined sources1 Publication | 3 | |
Regioni | 282 – 285 | Phosphatidylinositol 4,5-bisphosphate bindingCombined sources1 Publication | 4 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 665 – 668 | Selectivity filterBy similarity | 4 |
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
Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV4 sub-subfamily. [View classification]Curated
Keywords - Domaini
ANK repeat, Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3676, Eukaryota |
OrthoDBi | 693004at2759 |
Family and domain databases
Gene3Di | 1.25.40.20, 1 hit |
InterProi | View protein in InterPro IPR002110, Ankyrin_rpt IPR036770, Ankyrin_rpt-contain_sf IPR005821, Ion_trans_dom IPR024862, TRPV IPR008347, TrpV1-4 IPR008348, TrpV4 |
PANTHERi | PTHR10582, PTHR10582, 1 hit PTHR10582:SF4, PTHR10582:SF4, 1 hit |
Pfami | View protein in Pfam PF00023, Ank, 1 hit PF00520, Ion_trans, 1 hit |
PRINTSi | PR01768, TRPVRECEPTOR PR01769, VRL2RECEPTOR |
SMARTi | View protein in SMART SM00248, ANK, 3 hits |
SUPFAMi | SSF48403, SSF48403, 1 hit |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 1 hit |
i Sequence
Sequence statusi: Complete.
A0A1D5PXA5-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 47 | V → G in AAG28026 (PubMed:11081638).Curated | 1 | |
Sequence conflicti | 131 | I → V in AAG28026 (PubMed:11081638).Curated | 1 | |
Sequence conflicti | 741 | V → A in AAG28026 (PubMed:11081638).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF261883 mRNA Translation: AAG28026.1 AADN04000193 Genomic DNA No translation available. |
RefSeqi | NP_990023.1, NM_204692.1 |
Genome annotation databases
GeneIDi | 395427 |
KEGGi | gga:395427 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF261883 mRNA Translation: AAG28026.1 AADN04000193 Genomic DNA No translation available. |
RefSeqi | NP_990023.1, NM_204692.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3JXI | X-ray | 2.30 | A/B/C/D | 133-382 | [»] | |
3JXJ | X-ray | 2.80 | A/B | 133-382 | [»] | |
3W9F | X-ray | 1.90 | A/B/C/D | 133-382 | [»] | |
3W9G | X-ray | 2.00 | A/B/C/D | 133-382 | [»] | |
6F55 | NMR | - | B | 121-135 | [»] | |
AlphaFoldDBi | A0A1D5PXA5 | |||||
SMRi | A0A1D5PXA5 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 9031.ENSGALP00000008256 |
Genome annotation databases
GeneIDi | 395427 |
KEGGi | gga:395427 |
Organism-specific databases
CTDi | 59341 |
Phylogenomic databases
eggNOGi | KOG3676, Eukaryota |
OrthoDBi | 693004at2759 |
Miscellaneous databases
PROi | PR:A0A1D5PXA5 |
Family and domain databases
Gene3Di | 1.25.40.20, 1 hit |
InterProi | View protein in InterPro IPR002110, Ankyrin_rpt IPR036770, Ankyrin_rpt-contain_sf IPR005821, Ion_trans_dom IPR024862, TRPV IPR008347, TrpV1-4 IPR008348, TrpV4 |
PANTHERi | PTHR10582, PTHR10582, 1 hit PTHR10582:SF4, PTHR10582:SF4, 1 hit |
Pfami | View protein in Pfam PF00023, Ank, 1 hit PF00520, Ion_trans, 1 hit |
PRINTSi | PR01768, TRPVRECEPTOR PR01769, VRL2RECEPTOR |
SMARTi | View protein in SMART SM00248, ANK, 3 hits |
SUPFAMi | SSF48403, SSF48403, 1 hit |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TRPV4_CHICK | |
Accessioni | A0A1D5PXA5Primary (citable) accession number: A0A1D5PXA5 Secondary accession number(s): Q9DFS3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 28, 2018 |
Last sequence update: | November 30, 2016 | |
Last modified: | May 25, 2022 | |
This is version 36 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families