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Q9HBA0

- TRPV4_HUMAN

UniProt

Q9HBA0 - TRPV4_HUMAN

Protein

Transient receptor potential cation channel subfamily V member 4

Gene

TRPV4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    Non-selective calcium permeant cation channel probably involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by low pH, citrate and phorbol esters. Increase of intracellular Ca2+ potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism. Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers. Acts as a regulator of intracellular Ca2+ in synoviocytes. Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei192 – 1921ATP1 Publication
    Binding sitei201 – 2011ATP1 Publication
    Binding sitei239 – 2391ATP1 Publication
    Binding sitei248 – 2481ATP1 Publication

    GO - Molecular functioni

    1. actin binding Source: BHF-UCL
    2. actin filament binding Source: BHF-UCL
    3. alpha-tubulin binding Source: BHF-UCL
    4. ATP binding Source: UniProtKB-KW
    5. beta-tubulin binding Source: BHF-UCL
    6. calcium channel activity Source: UniProtKB
    7. calmodulin binding Source: UniProtKB
    8. cation channel activity Source: UniProtKB
    9. microtubule binding Source: BHF-UCL
    10. osmosensor activity Source: Ensembl
    11. protein kinase binding Source: BHF-UCL
    12. protein kinase C binding Source: BHF-UCL
    13. SH2 domain binding Source: BHF-UCL

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: BHF-UCL
    2. actin filament organization Source: BHF-UCL
    3. calcium ion import Source: BHF-UCL
    4. calcium ion transmembrane transport Source: Reactome
    5. calcium ion transport Source: UniProtKB
    6. cell-cell junction assembly Source: UniProtKB
    7. cell death Source: UniProtKB-KW
    8. cellular calcium ion homeostasis Source: UniProtKB
    9. cellular hypotonic response Source: BHF-UCL
    10. cellular response to heat Source: UniProtKB
    11. cellular response to osmotic stress Source: UniProtKB
    12. cell volume homeostasis Source: UniProtKB
    13. cortical microtubule organization Source: BHF-UCL
    14. hyperosmotic salinity response Source: Ensembl
    15. ion transmembrane transport Source: Reactome
    16. microtubule polymerization Source: BHF-UCL
    17. negative regulation of neuron projection development Source: BHF-UCL
    18. osmosensory signaling pathway Source: UniProtKB
    19. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    20. positive regulation of microtubule depolymerization Source: BHF-UCL
    21. regulation of response to osmotic stress Source: Ensembl
    22. response to mechanical stimulus Source: UniProtKB
    23. transmembrane transport Source: Reactome
    24. vasopressin secretion Source: Ensembl

    Keywords - Molecular functioni

    Calcium channel, Ion channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_169333. TRP channels.
    SignaLinkiQ9HBA0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transient receptor potential cation channel subfamily V member 4
    Short name:
    TrpV4
    Alternative name(s):
    Osm-9-like TRP channel 4
    Short name:
    OTRPC4
    Transient receptor potential protein 12
    Short name:
    TRP12
    Vanilloid receptor-like channel 2
    Vanilloid receptor-like protein 2
    Short name:
    VRL-2
    Vanilloid receptor-related osmotically-activated channel
    Short name:
    VR-OAC
    Gene namesi
    Name:TRPV4
    Synonyms:VRL2, VROAC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18083. TRPV4.

    Subcellular locationi

    Cell membrane By similarity; Multi-pass membrane protein By similarity. Cell junctionadherens junction By similarity
    Note: Assembly of the putative homotetramer occurs primarily in the endoplasmic reticulum.3 Publications

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB
    2. cell surface Source: Ensembl
    3. cilium Source: Ensembl
    4. cortical actin cytoskeleton Source: BHF-UCL
    5. cytoplasmic microtubule Source: Ensembl
    6. cytoplasmic vesicle Source: Ensembl
    7. filopodium Source: BHF-UCL
    8. focal adhesion Source: BHF-UCL
    9. growth cone Source: BHF-UCL
    10. integral component of membrane Source: UniProtKB
    11. lamellipodium Source: BHF-UCL
    12. plasma membrane Source: UniProtKB
    13. ruffle membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Brachyolmia 3 (BRAC3) [MIM:113500]: A form of brachyolmia, a clinically and genetically heterogeneous skeletal dysplasia primarily affecting the spine and characterized by a short trunk, short stature, and platyspondyly without significant epiphyseal or metaphyseal changes in the long bones. BRAC3 is an autosomal dominant form with severe scoliosis with or without kyphosis, and flattened irregular cervical vertebrae.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti616 – 6161R → Q in BRAC3; this mutation results in a gain of function and a constitutive activation of the channel. 1 Publication
    VAR_054805
    Natural varianti620 – 6201V → I in BRAC3; this mutation results in a gain of function and a constitutive activation of the channel. 1 Publication
    VAR_054806
    Spondylometaphyseal dysplasia Kozlowski type (SMDK) [MIM:184252]: A form of spondylometaphyseal dysplasia, a group of short stature disorders distinguished by abnormalities in the vertebrae and the metaphyses of the tubular bones. It is characterized by postnatal dwarfism, significant scoliosis and mild metaphyseal abnormalities in the pelvis. The vertebrae exhibit platyspondyly and overfaced pedicles.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti278 – 2781E → K in SMDK. 1 Publication
    VAR_064521
    Natural varianti333 – 3364Missing in SMDK.
    VAR_067992
    Natural varianti333 – 3331D → G in SMDK. 1 Publication
    VAR_062332
    Natural varianti594 – 5941R → H in SMDK and PSTD. 3 Publications
    VAR_062333
    Natural varianti596 – 5961L → P in SMDK. 1 Publication
    VAR_064527
    Natural varianti600 – 6001G → W in SMDK. 1 Publication
    VAR_064528
    Natural varianti625 – 6251M → I in SMDK. 1 Publication
    VAR_064533
    Natural varianti709 – 7091L → M in SMDK. 1 Publication
    VAR_064534
    Natural varianti716 – 7161A → S in SMDK. 1 Publication
    VAR_062334
    Natural varianti777 – 7771C → Y in SMDK. 1 Publication
    VAR_064536
    Natural varianti797 – 7971E → K in MTD and SMDK; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type. 3 Publications
    VAR_064537
    Metatropic dysplasia (MTD) [MIM:156530]: A severe spondyloepimetaphyseal dysplasia characterized by short limbs with limitation and enlargement of joints and usually severe kyphoscoliosis. Radiologic features include severe platyspondyly, severe metaphyseal enlargement and shortening of long bones.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891T → I in MTD; lethal form. 1 Publication
    VAR_064517
    Natural varianti197 – 1971K → R in MTD; lethal form. 1 Publication
    VAR_064519
    Natural varianti199 – 1991L → F in MTD. 1 Publication
    VAR_064520
    Natural varianti295 – 2951T → A in MTD. 1 Publication
    VAR_064522
    Natural varianti331 – 3311I → F in MTD. 2 Publications
    VAR_062331
    Natural varianti331 – 3311I → T in MTD. 1 Publication
    VAR_064523
    Natural varianti342 – 3421V → F in MTD. 1 Publication
    VAR_064524
    Natural varianti471 – 4711Missing in MTD; lethal form. 2 Publications
    VAR_064525
    Natural varianti592 – 5921F → L in MTD. 1 Publication
    VAR_064526
    Natural varianti604 – 6041I → M in MTD; lethal form. 1 Publication
    VAR_064530
    Natural varianti617 – 6171F → L in MTD. 1 Publication
    VAR_064531
    Natural varianti618 – 6181L → P in MTD. 2 Publications
    VAR_064532
    Natural varianti775 – 7751R → K in MTD. 1 Publication
    VAR_064535
    Natural varianti797 – 7971E → K in MTD and SMDK; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type. 3 Publications
    VAR_064537
    Natural varianti799 – 7991P → A in MTD. 1 Publication
    VAR_064538
    Natural varianti799 – 7991P → L in MTD; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type. 4 Publications
    VAR_062335
    Natural varianti799 – 7991P → R in MTD. 1 Publication
    VAR_064539
    Natural varianti799 – 7991P → S in MTD. 1 Publication
    VAR_064540
    Distal spinal muscular atrophy, congenital non-progressive (DSMAC) [MIM:600175]: A clinically variable, neuromuscular disorder characterized by congenital lower motor neuron disorder restricted to the lower part of the body. Clinical manifestations include non-progressive muscular atrophy, thigh muscle atrophy, weak thigh adductors, weak knee and foot extensors, minimal jaw muscle and neck flexor weakness, flexion contractures of knees and pes equinovarus. Tendon reflexes are normal.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti97 – 971P → R in DSMAC; loss of function mutation. 1 Publication
    VAR_067989
    Natural varianti232 – 2321R → C in DSMAC and CMT2C; does not affect channel localization to plasma membrane; results in increased agonist-induced channel activity and increased basal intracellular calcium concentration; causes increased cell death. 2 Publications
    VAR_067990
    Natural varianti269 – 2691R → H in DSMAC and CMT2C; increased agonist-induced channel activity and increased basal intracellular calcium concentration; causes increased cell death. 3 Publications
    VAR_063529
    Charcot-Marie-Tooth disease 2C (CMT2C) [MIM:606071]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti232 – 2321R → C in DSMAC and CMT2C; does not affect channel localization to plasma membrane; results in increased agonist-induced channel activity and increased basal intracellular calcium concentration; causes increased cell death. 2 Publications
    VAR_067990
    Natural varianti269 – 2691R → C in CMT2C. 1 Publication
    VAR_063528
    Natural varianti269 – 2691R → H in DSMAC and CMT2C; increased agonist-induced channel activity and increased basal intracellular calcium concentration; causes increased cell death. 3 Publications
    VAR_063529
    Natural varianti315 – 3151R → W in CMT2C. 2 Publications
    VAR_063541
    Natural varianti316 – 3161R → C in CMT2C and SPSMA. 2 Publications
    VAR_063530
    Natural varianti316 – 3161R → H in CMT2C; does not affect channel localization to plasma membrane; results in increased agonist-induced channel activity and increased basal intracellular calcium concentration; causes increased cell death. 1 Publication
    VAR_067991
    Natural varianti542 – 5421S → Y in CMT2C. 1 Publication
    VAR_067993
    Scapuloperoneal spinal muscular atrophy (SPSMA) [MIM:181405]: A clinically variable neuromuscular disorder characterized by neurogenic scapuloperoneal amyotrophy, laryngeal palsy, congenital absence of muscles, progressive scapuloperoneal atrophy and progressive distal weakness and amyotrophy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti316 – 3161R → C in CMT2C and SPSMA. 2 Publications
    VAR_063530
    Spondyloepiphyseal dysplasia Maroteaux type (SEDM) [MIM:184095]: A clinically variable spondyloepiphyseal dysplasia with manifestations limited to the musculoskeletal system. Clinical features include short stature, brachydactyly, platyspondyly, short and stubby hands and feet, epiphyseal hypoplasia of the large joints, and iliac hypoplasia. Intelligence is normal.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Parastremmatic dwarfism (PSTD) [MIM:168400]: A bone dysplasia characterized by severe dwarfism, kyphoscoliosis, distortion and bowing of the extremities, and contractures of the large joints. Radiographically, the disease is characterized by a combination of decreased bone density, bowing of the long bones, platyspondyly and striking irregularities of endochondral ossification with areas of calcific stippling and streaking in radiolucent epiphyses, metaphyses and apophyses.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti594 – 5941R → H in SMDK and PSTD. 3 Publications
    VAR_062333
    Digital arthropathy-brachydactyly, familial (FDAB) [MIM:606835]: A disorder characterized by irregularities in the proximal articular surfaces of the distal interphalangeal joints of the hand. Individuals appear normal at birth, with no clinical or radiographic evidence of a developmental skeletal dysplasia. The earliest changes appear during the first decade of life. By adulthood, all interphalangeal, metacarpophalangeal, and metatarsophalangeal joints are affected by a deforming, painful osteoarthritis. The remainder of the skeleton is clinically and radiographically unaffected.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti270 – 2701G → V in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists. 1 Publication
    VAR_068498
    Natural varianti271 – 2711R → P in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists. 1 Publication
    VAR_068499
    Natural varianti273 – 2731F → L in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists. 1 Publication
    VAR_068500

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi816 – 8216RLRRDR → ELEEDE: Loss of calmodulin binding; when associated with A-828.
    Mutagenesisi821 – 8244RWSS → AASA: Loss of calmodulin binding.
    Mutagenesisi822 – 8221W → A: Loss of Ca(2+) dependent current potentiation.
    Mutagenesisi824 – 8241S → A: Loss of phosphorylation. 1 Publication
    Mutagenesisi824 – 8241S → D: Up-regulation of its function. 1 Publication
    Mutagenesisi828 – 8281R → A: Loss of calmodulin binding; when associated with 816-ELEEDE-821. 1 Publication

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Dwarfism, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi113500. phenotype.
    156530. phenotype.
    168400. phenotype.
    181405. phenotype.
    184095. phenotype.
    184252. phenotype.
    600175. phenotype.
    606071. phenotype.
    606835. phenotype.
    613508. phenotype.
    Orphaneti93304. Autosomal dominant brachyolmia.
    99937. Autosomal dominant Charcot-Marie-Tooth disease type 2C.
    1216. Autosomal dominant congenital benign spinal muscular atrophy.
    85169. Familial digital arthropathy-brachydactyly.
    2635. Metatropic dysplasia.
    2646. Parastremmatic dwarfism.
    263482. Spondyloepiphyseal dysplasia, Maroteaux type.
    93314. Spondylometaphyseal dysplasia, Kozlowski type.
    PharmGKBiPA38293.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 871871Transient receptor potential cation channel subfamily V member 4PRO_0000215347Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei824 – 8241Phosphoserine; by PKC and PKA1 Publication

    Post-translational modificationi

    Phosphorylation results in enhancement of its channel function.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9HBA0.
    PaxDbiQ9HBA0.
    PRIDEiQ9HBA0.

    PTM databases

    PhosphoSiteiQ9HBA0.

    Expressioni

    Tissue specificityi

    Found in the synoviocytes from patients with (RA) and without (CTR) rheumatoid arthritis (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9HBA0.
    BgeeiQ9HBA0.
    GenevestigatoriQ9HBA0.

    Organism-specific databases

    HPAiHPA007150.

    Interactioni

    Subunit structurei

    Homotetramer Probable. Self-associates in a isoform-specific manner. Isoforms 1/A and 5/D but not isoform 2/B, 4/C and 6/E can oligomerize. Interacts with calmodulin. Interacts with Map7 and Src family Tyr protein kinases LYN, SRC, FYN, HCK, LCK and YES. Interacts with CTNNB1. The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with PACSIN1, PACSIN2 and PACSIN3 (via SH3 domain) By similarity. Part of a complex containing MLC1, AQP4, HEPACAM and ATP1B1.By similarity3 PublicationsCurated

    Protein-protein interaction databases

    BioGridi121883. 12 interactions.
    DIPiDIP-35702N.
    IntActiQ9HBA0. 3 interactions.
    MINTiMINT-4535111.

    Structurei

    Secondary structure

    1
    871
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi151 – 1599
    Helixi164 – 1663
    Helixi169 – 1757
    Helixi183 – 1853
    Beta strandi188 – 1903
    Helixi194 – 2007
    Helixi209 – 22012
    Helixi223 – 2286
    Beta strandi234 – 2396
    Helixi241 – 2477
    Helixi251 – 26010
    Helixi271 – 2733
    Turni276 – 2794
    Helixi288 – 2947
    Helixi298 – 3069
    Helixi324 – 3318
    Helixi336 – 35621
    Beta strandi357 – 3604
    Helixi362 – 3643
    Helixi373 – 3797
    Helixi383 – 39513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DX1X-ray2.85A/B149-397[»]
    4DX2X-ray2.95A/B149-397[»]
    ProteinModelPortaliQ9HBA0.
    SMRiQ9HBA0. Positions 148-755.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 465465CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini487 – 50822ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini530 – 55021CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini572 – 5721ExtracellularSequence Analysis
    Topological domaini594 – 61623CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini712 – 871160CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei648 – 67831Pore-formingCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei466 – 48621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei509 – 52921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei551 – 57121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei573 – 59321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei617 – 63721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei691 – 71121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati237 – 26630ANK 1Add
    BLAST
    Repeati284 – 31330ANK 2Add
    BLAST
    Repeati369 – 39830ANK 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni812 – 83120Interaction with calmodulinAdd
    BLAST

    Sequence similaritiesi

    Contains 3 ANK repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG278734.
    HOVERGENiHBG054085.
    InParanoidiQ9HBA0.
    KOiK04973.
    OMAiEDQTNCT.
    OrthoDBiEOG70S74P.
    PhylomeDBiQ9HBA0.
    TreeFamiTF314711.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR005821. Ion_trans_dom.
    IPR004729. TRP_channel.
    IPR008347. TRPV1-4_channel.
    IPR008348. TRPV4_channel.
    [Graphical view]
    PANTHERiPTHR10582:SF4. PTHR10582:SF4. 1 hit.
    PfamiPF00023. Ank. 1 hit.
    PF00520. Ion_trans. 1 hit.
    [Graphical view]
    PRINTSiPR01768. TRPVRECEPTOR.
    PR01769. VRL2RECEPTOR.
    SMARTiSM00248. ANK. 3 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    TIGRFAMsiTIGR00870. trp. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HBA0-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MADSSEGPRA GPGEVAELPG DESGTPGGEA FPLSSLANLF EGEDGSLSPS    50
    PADASRPAGP GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK 100
    KAPMDSLFDY GTYRHHSSDN KRWRKKIIEK QPQSPKAPAP QPPPILKVFN 150
    RPILFDIVSR GSTADLDGLL PFLLTHKKRL TDEEFREPST GKTCLPKALL 200
    NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT ALHIAIERRC 250
    KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI 300
    VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL 350
    LKCARLFPDS NLEAVLNNDG LSPLMMAAKT GKIGIFQHII RREVTDEDTR 400
    HLSRKFKDWA YGPVYSSLYD LSSLDTCGEE ASVLEILVYN SKIENRHEML 450
    AVEPINELLR DKWRKFGAVS FYINVVSYLC AMVIFTLTAY YQPLEGTPPY 500
    PYRTTVDYLR LAGEVITLFT GVLFFFTNIK DLFMKKCPGV NSLFIDGSFQ 550
    LLYFIYSVLV IVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG 600
    TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVSLLNPCA NMKVCNEDQT 650
    NCTVPTYPSC RDSETFSTFL LDLFKLTIGM GDLEMLSSTK YPVVFIILLV 700
    TYIILTFVLL LNMLIALMGE TVGQVSKESK HIWKLQWATT ILDIERSFPV 750
    FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV DEVNWSHWNQ NLGIINEDPG 800
    KNETYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSNPDE VVVPLDSMGN 850
    PRCDGHQQGY PRKWRTDDAP L 871
    Length:871
    Mass (Da):98,281
    Last modified:April 26, 2005 - v2
    Checksum:iC62056B86C5A6FB6
    GO
    Isoform 2 (identifier: Q9HBA0-2) [UniParc]FASTAAdd to Basket

    Also known as: B, OTRPC4beta

    The sequence of this isoform differs from the canonical sequence as follows:
         385-444: Missing.

    Show »
    Length:811
    Mass (Da):91,261
    Checksum:iA498FF4BBA1CD7A5
    GO
    Isoform 3 (identifier: Q9HBA0-3) [UniParc]FASTAAdd to Basket

    Also known as: TRPV-SV

    The sequence of this isoform differs from the canonical sequence as follows:
         844-871: PLDSMGNPRCDGHQQGYPRKWRTDDAPL → RHLCRVRRKR

    Show »
    Length:853
    Mass (Da):96,449
    Checksum:iEAA07196606AED20
    GO
    Isoform 4 (identifier: Q9HBA0-4) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         239-285: Missing.

    Show »
    Length:824
    Mass (Da):92,904
    Checksum:iEA7AFC7497D14495
    GO
    Isoform 5 (identifier: Q9HBA0-5) [UniParc]FASTAAdd to Basket

    Also known as: D

    The sequence of this isoform differs from the canonical sequence as follows:
         28-61: Missing.

    Show »
    Length:837
    Mass (Da):94,998
    Checksum:i1538A7B2E76C8CDF
    GO
    Isoform 6 (identifier: Q9HBA0-6) [UniParc]FASTAAdd to Basket

    Also known as: E

    The sequence of this isoform differs from the canonical sequence as follows:
         239-285: Missing.
         385-444: Missing.

    Show »
    Length:764
    Mass (Da):85,884
    Checksum:iB1307888F82B0E31
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti385 – 3851I → V in AAG28029. (PubMed:11081638)Curated
    Sequence conflicti452 – 4521V → A in BAC06573. 1 PublicationCurated
    Sequence conflicti781 – 7811D → N in AAG28029. (PubMed:11081638)Curated
    Sequence conflicti820 – 8201D → T in BAB69040. 1 PublicationCurated
    Sequence conflicti861 – 8611P → T in BAC06573. 1 PublicationCurated
    Sequence conflicti867 – 8671D → E in AAG16127. (PubMed:11025659)Curated

    Polymorphismi

    Genetic variations in TRPV4 determine the sodium serum level quantitative trait locus 1 (SSQTL1) [MIMi:613508]. In some populations, variant Pro19Ser has been shown to be significantly associated with hyponatremia defined as serum sodium concentration below or equal to 135 mEq/L.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191P → S Associated with lower sodium concentraions in serum; shows diminished response to hypotonic stress relative to wild-type.
    Corresponds to variant rs3742030 [ dbSNP | Ensembl ].
    VAR_052391
    Natural varianti89 – 891T → I in MTD; lethal form. 1 Publication
    VAR_064517
    Natural varianti97 – 971P → R in DSMAC; loss of function mutation. 1 Publication
    VAR_067989
    Natural varianti183 – 1831E → K Found in a patient with spondyloepiphyseal dysplasia Maroteaux type. 1 Publication
    VAR_064518
    Natural varianti197 – 1971K → R in MTD; lethal form. 1 Publication
    VAR_064519
    Natural varianti199 – 1991L → F in MTD. 1 Publication
    VAR_064520
    Natural varianti232 – 2321R → C in DSMAC and CMT2C; does not affect channel localization to plasma membrane; results in increased agonist-induced channel activity and increased basal intracellular calcium concentration; causes increased cell death. 2 Publications
    VAR_067990
    Natural varianti269 – 2691R → C in CMT2C. 1 Publication
    VAR_063528
    Natural varianti269 – 2691R → H in DSMAC and CMT2C; increased agonist-induced channel activity and increased basal intracellular calcium concentration; causes increased cell death. 3 Publications
    VAR_063529
    Natural varianti270 – 2701G → V in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists. 1 Publication
    VAR_068498
    Natural varianti271 – 2711R → P in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists. 1 Publication
    VAR_068499
    Natural varianti273 – 2731F → L in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists. 1 Publication
    VAR_068500
    Natural varianti278 – 2781E → K in SMDK. 1 Publication
    VAR_064521
    Natural varianti295 – 2951T → A in MTD. 1 Publication
    VAR_064522
    Natural varianti315 – 3151R → W in CMT2C. 2 Publications
    VAR_063541
    Natural varianti316 – 3161R → C in CMT2C and SPSMA. 2 Publications
    VAR_063530
    Natural varianti316 – 3161R → H in CMT2C; does not affect channel localization to plasma membrane; results in increased agonist-induced channel activity and increased basal intracellular calcium concentration; causes increased cell death. 1 Publication
    VAR_067991
    Natural varianti331 – 3311I → F in MTD. 2 Publications
    VAR_062331
    Natural varianti331 – 3311I → T in MTD. 1 Publication
    VAR_064523
    Natural varianti333 – 3364Missing in SMDK.
    VAR_067992
    Natural varianti333 – 3331D → G in SMDK. 1 Publication
    VAR_062332
    Natural varianti342 – 3421V → F in MTD. 1 Publication
    VAR_064524
    Natural varianti471 – 4711Missing in MTD; lethal form. 2 Publications
    VAR_064525
    Natural varianti542 – 5421S → Y in CMT2C. 1 Publication
    VAR_067993
    Natural varianti592 – 5921F → L in MTD. 1 Publication
    VAR_064526
    Natural varianti594 – 5941R → H in SMDK and PSTD. 3 Publications
    VAR_062333
    Natural varianti596 – 5961L → P in SMDK. 1 Publication
    VAR_064527
    Natural varianti600 – 6001G → W in SMDK. 1 Publication
    VAR_064528
    Natural varianti602 – 6021Y → C Found in a patient with spondyloepiphyseal dysplasia Maroteaux type. 1 Publication
    VAR_064529
    Natural varianti604 – 6041I → M in MTD; lethal form. 1 Publication
    VAR_064530
    Natural varianti616 – 6161R → Q in BRAC3; this mutation results in a gain of function and a constitutive activation of the channel. 1 Publication
    VAR_054805
    Natural varianti617 – 6171F → L in MTD. 1 Publication
    VAR_064531
    Natural varianti618 – 6181L → P in MTD. 2 Publications
    VAR_064532
    Natural varianti620 – 6201V → I in BRAC3; this mutation results in a gain of function and a constitutive activation of the channel. 1 Publication
    VAR_054806
    Natural varianti625 – 6251M → I in SMDK. 1 Publication
    VAR_064533
    Natural varianti709 – 7091L → M in SMDK. 1 Publication
    VAR_064534
    Natural varianti716 – 7161A → S in SMDK. 1 Publication
    VAR_062334
    Natural varianti775 – 7751R → K in MTD. 1 Publication
    VAR_064535
    Natural varianti777 – 7771C → Y in SMDK. 1 Publication
    VAR_064536
    Natural varianti797 – 7971E → K in MTD and SMDK; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type. 3 Publications
    VAR_064537
    Natural varianti799 – 7991P → A in MTD. 1 Publication
    VAR_064538
    Natural varianti799 – 7991P → L in MTD; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type. 4 Publications
    VAR_062335
    Natural varianti799 – 7991P → R in MTD. 1 Publication
    VAR_064539
    Natural varianti799 – 7991P → S in MTD. 1 Publication
    VAR_064540

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei28 – 6134Missing in isoform 5. 1 PublicationVSP_026614Add
    BLAST
    Alternative sequencei239 – 28547Missing in isoform 4 and isoform 6. 1 PublicationVSP_026615Add
    BLAST
    Alternative sequencei385 – 44460Missing in isoform 2 and isoform 6. 2 PublicationsVSP_013436Add
    BLAST
    Alternative sequencei844 – 87128PLDSM…DDAPL → RHLCRVRRKR in isoform 3. 1 PublicationVSP_013437Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263523 mRNA. Translation: AAG28029.1.
    AF258465 mRNA. Translation: AAG16127.1.
    AB100308 mRNA. Translation: BAC55864.1.
    AB032427 mRNA. Translation: BAB69040.1.
    AB073669 mRNA. Translation: BAC06573.1.
    AJ296305 mRNA. Translation: CAC82937.1.
    DQ059644 mRNA. Translation: AAZ04918.1.
    DQ059645 mRNA. Translation: AAZ04919.1.
    DQ059646 mRNA. Translation: AAZ04920.1.
    CH471054 Genomic DNA. Translation: EAW97879.1.
    BC117426 mRNA. Translation: AAI17427.1.
    BC143315 mRNA. Translation: AAI43316.1.
    AF279673 mRNA. Translation: AAK69487.1.
    CCDSiCCDS53827.1. [Q9HBA0-6]
    CCDS53828.1. [Q9HBA0-4]
    CCDS53829.1. [Q9HBA0-5]
    CCDS9134.1. [Q9HBA0-1]
    CCDS9135.1. [Q9HBA0-2]
    RefSeqiNP_001170899.1. NM_001177428.1. [Q9HBA0-4]
    NP_001170902.1. NM_001177431.1. [Q9HBA0-5]
    NP_001170904.1. NM_001177433.1. [Q9HBA0-6]
    NP_067638.3. NM_021625.4. [Q9HBA0-1]
    NP_671737.1. NM_147204.2. [Q9HBA0-2]
    XP_005253975.1. XM_005253918.1. [Q9HBA0-1]
    XP_005253976.1. XM_005253919.1. [Q9HBA0-5]
    UniGeneiHs.506713.

    Genome annotation databases

    EnsembliENST00000261740; ENSP00000261740; ENSG00000111199. [Q9HBA0-1]
    ENST00000418703; ENSP00000406191; ENSG00000111199. [Q9HBA0-1]
    ENST00000536838; ENSP00000444336; ENSG00000111199. [Q9HBA0-5]
    ENST00000537083; ENSP00000442738; ENSG00000111199. [Q9HBA0-2]
    ENST00000541794; ENSP00000442167; ENSG00000111199. [Q9HBA0-4]
    ENST00000544971; ENSP00000443611; ENSG00000111199. [Q9HBA0-6]
    GeneIDi59341.
    KEGGihsa:59341.
    UCSCiuc001tpg.2. human. [Q9HBA0-5]
    uc001tph.2. human. [Q9HBA0-4]
    uc001tpi.2. human. [Q9HBA0-6]
    uc001tpj.2. human. [Q9HBA0-1]
    uc021rdp.1. human. [Q9HBA0-2]

    Polymorphism databases

    DMDMi62901470.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263523 mRNA. Translation: AAG28029.1 .
    AF258465 mRNA. Translation: AAG16127.1 .
    AB100308 mRNA. Translation: BAC55864.1 .
    AB032427 mRNA. Translation: BAB69040.1 .
    AB073669 mRNA. Translation: BAC06573.1 .
    AJ296305 mRNA. Translation: CAC82937.1 .
    DQ059644 mRNA. Translation: AAZ04918.1 .
    DQ059645 mRNA. Translation: AAZ04919.1 .
    DQ059646 mRNA. Translation: AAZ04920.1 .
    CH471054 Genomic DNA. Translation: EAW97879.1 .
    BC117426 mRNA. Translation: AAI17427.1 .
    BC143315 mRNA. Translation: AAI43316.1 .
    AF279673 mRNA. Translation: AAK69487.1 .
    CCDSi CCDS53827.1. [Q9HBA0-6 ]
    CCDS53828.1. [Q9HBA0-4 ]
    CCDS53829.1. [Q9HBA0-5 ]
    CCDS9134.1. [Q9HBA0-1 ]
    CCDS9135.1. [Q9HBA0-2 ]
    RefSeqi NP_001170899.1. NM_001177428.1. [Q9HBA0-4 ]
    NP_001170902.1. NM_001177431.1. [Q9HBA0-5 ]
    NP_001170904.1. NM_001177433.1. [Q9HBA0-6 ]
    NP_067638.3. NM_021625.4. [Q9HBA0-1 ]
    NP_671737.1. NM_147204.2. [Q9HBA0-2 ]
    XP_005253975.1. XM_005253918.1. [Q9HBA0-1 ]
    XP_005253976.1. XM_005253919.1. [Q9HBA0-5 ]
    UniGenei Hs.506713.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DX1 X-ray 2.85 A/B 149-397 [» ]
    4DX2 X-ray 2.95 A/B 149-397 [» ]
    ProteinModelPortali Q9HBA0.
    SMRi Q9HBA0. Positions 148-755.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121883. 12 interactions.
    DIPi DIP-35702N.
    IntActi Q9HBA0. 3 interactions.
    MINTi MINT-4535111.

    Chemistry

    BindingDBi Q9HBA0.
    ChEMBLi CHEMBL3119.
    GuidetoPHARMACOLOGYi 510.

    PTM databases

    PhosphoSitei Q9HBA0.

    Polymorphism databases

    DMDMi 62901470.

    Proteomic databases

    MaxQBi Q9HBA0.
    PaxDbi Q9HBA0.
    PRIDEi Q9HBA0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261740 ; ENSP00000261740 ; ENSG00000111199 . [Q9HBA0-1 ]
    ENST00000418703 ; ENSP00000406191 ; ENSG00000111199 . [Q9HBA0-1 ]
    ENST00000536838 ; ENSP00000444336 ; ENSG00000111199 . [Q9HBA0-5 ]
    ENST00000537083 ; ENSP00000442738 ; ENSG00000111199 . [Q9HBA0-2 ]
    ENST00000541794 ; ENSP00000442167 ; ENSG00000111199 . [Q9HBA0-4 ]
    ENST00000544971 ; ENSP00000443611 ; ENSG00000111199 . [Q9HBA0-6 ]
    GeneIDi 59341.
    KEGGi hsa:59341.
    UCSCi uc001tpg.2. human. [Q9HBA0-5 ]
    uc001tph.2. human. [Q9HBA0-4 ]
    uc001tpi.2. human. [Q9HBA0-6 ]
    uc001tpj.2. human. [Q9HBA0-1 ]
    uc021rdp.1. human. [Q9HBA0-2 ]

    Organism-specific databases

    CTDi 59341.
    GeneCardsi GC12M110220.
    GeneReviewsi TRPV4.
    HGNCi HGNC:18083. TRPV4.
    HPAi HPA007150.
    MIMi 113500. phenotype.
    156530. phenotype.
    168400. phenotype.
    181405. phenotype.
    184095. phenotype.
    184252. phenotype.
    600175. phenotype.
    605427. gene.
    606071. phenotype.
    606835. phenotype.
    613508. phenotype.
    neXtProti NX_Q9HBA0.
    Orphaneti 93304. Autosomal dominant brachyolmia.
    99937. Autosomal dominant Charcot-Marie-Tooth disease type 2C.
    1216. Autosomal dominant congenital benign spinal muscular atrophy.
    85169. Familial digital arthropathy-brachydactyly.
    2635. Metatropic dysplasia.
    2646. Parastremmatic dwarfism.
    263482. Spondyloepiphyseal dysplasia, Maroteaux type.
    93314. Spondylometaphyseal dysplasia, Kozlowski type.
    PharmGKBi PA38293.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278734.
    HOVERGENi HBG054085.
    InParanoidi Q9HBA0.
    KOi K04973.
    OMAi EDQTNCT.
    OrthoDBi EOG70S74P.
    PhylomeDBi Q9HBA0.
    TreeFami TF314711.

    Enzyme and pathway databases

    Reactomei REACT_169333. TRP channels.
    SignaLinki Q9HBA0.

    Miscellaneous databases

    GeneWikii TRPV4.
    GenomeRNAii 59341.
    NextBioi 65228.
    PROi Q9HBA0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HBA0.
    Bgeei Q9HBA0.
    Genevestigatori Q9HBA0.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR005821. Ion_trans_dom.
    IPR004729. TRP_channel.
    IPR008347. TRPV1-4_channel.
    IPR008348. TRPV4_channel.
    [Graphical view ]
    PANTHERi PTHR10582:SF4. PTHR10582:SF4. 1 hit.
    Pfami PF00023. Ank. 1 hit.
    PF00520. Ion_trans. 1 hit.
    [Graphical view ]
    PRINTSi PR01768. TRPVRECEPTOR.
    PR01769. VRL2RECEPTOR.
    SMARTi SM00248. ANK. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    TIGRFAMsi TIGR00870. trp. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor."
      Liedtke W.B., Choe Y., Marti-Renom M.A., Bell A.M., Denis C.S., Sali A., Hudspeth A.J., Friedman J.M., Heller S.
      Cell 103:525-535(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity."
      Strotmann R., Harteneck C., Nunnenmacher K., Schultz G., Plant T.D.
      Nat. Cell Biol. 2:695-702(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Tissue: Kidney cortex.
    3. "Impaired pressure sensation in mice lacking TRPV4."
      Suzuki M., Mizuno A., Kodaira K., Imai M.
      J. Biol. Chem. 278:22664-22668(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. "Molecular cloning of a new member of vanilloid receptor channel-like proteins."
      Ishibashi K.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. Kelsell R.E.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. Xu F., Satoh E., Iijima T.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT MTD PRO-618.
      Tissue: Aortic endothelium.
    7. "Human TRPV4 channel splice variants revealed a key role of ankyrin domains in multimerization and trafficking."
      Arniges M., Fernandez-Fernandez J.M., Albrecht N., Schaefer M., Valverde M.A.
      J. Biol. Chem. 281:1580-1586(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6), SUBCELLULAR LOCATION, SELF-ASSOCIATION.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon.
    10. "Cloning of mouse and human vanilloid receptor-like protein 2 (VRL-2)."
      Derst C., Schafer M.K.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-871.
    11. "Ca2+-dependent potentiation of the nonselective cation channel TRPV4 is mediated by a C-terminal calmodulin binding site."
      Strotmann R., Schultz G., Plant T.D.
      J. Biol. Chem. 278:26541-26549(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CALMODULIN, MUTAGENESIS OF 186-ARG--SER-824 AND ARG-828.
    12. "An environmental sensor, TRPV4 is a novel regulator of intracellular Ca2+ in human synoviocytes."
      Itoh Y., Hatano N., Hayashi H., Onozaki K., Miyazawa K., Muraki K.
      Am. J. Physiol. 297:C1082-C1090(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    13. "A loss-of-function nonsynonymous polymorphism in the osmoregulatory TRPV4 gene is associated with human hyponatremia."
      Tian W., Fu Y., Garcia-Elias A., Fernandez-Fernandez J.M., Vicente R., Kramer P.L., Klein R.F., Hitzemann R., Orwoll E.S., Wilmot B., McWeeney S., Valverde M.A., Cohen D.M.
      Proc. Natl. Acad. Sci. U.S.A. 106:14034-14039(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SSQTL1, ASSOCIATION OF VARIANT SER-19 WITH HYPONATREMIA.
    14. "Identification of a Protein Kinase C-dependent phosphorylation site involved in sensitization of TRPV4 channel."
      Peng H., Lewandrowski U., Muller B., Sickmann A., Walz G., Wegierski T.
      Biochem. Biophys. Res. Commun. 391:1721-1725(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-824, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-824.
    15. "Megalencephalic leukoencephalopathy with subcortical cysts protein 1 functionally cooperates with the TRPV4 cation channel to activate the response of astrocytes to osmotic stress: dysregulation by pathological mutations."
      Lanciotti A., Brignone M.S., Molinari P., Visentin S., De Nuccio C., Macchia G., Aiello C., Bertini E., Aloisi F., Petrucci T.C., Ambrosini E.
      Hum. Mol. Genet. 21:2166-2180(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    16. "Structural and biochemical consequences of disease-causing mutations in the ankyrin repeat domain of the human TRPV4 channel."
      Inada H., Procko E., Sotomayor M., Gaudet R.
      Biochemistry 51:6195-6206(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 149-397 ALONE AND IN COMPLEX WITH ATP.
    17. Cited for: VARIANTS BRAC3 GLN-616 AND ILE-620, CHARACTERIZATION OF VARIANTS BRAC3 GLN-616 AND ILE-620.
    18. "Mutations in the gene encoding the calcium-permeable ion channel TRPV4 produce spondylometaphyseal dysplasia, Kozlowski type and metatropic dysplasia."
      Krakow D., Vriens J., Camacho N., Luong P., Deixler H., Funari T.L., Bacino C.A., Irons M.B., Holm I.A., Sadler L., Okenfuss E.B., Janssens A., Voets T., Rimoin D.L., Lachman R.S., Nilius B., Cohn D.H.
      Am. J. Hum. Genet. 84:307-315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SMDK GLY-333; HIS-594 AND SER-716, VARIANTS MTD PHE-331 AND LEU-799.
    19. Cited for: VARIANTS MTD ILE-89; ARG-197; PHE-331; PHE-471 DEL; MET-604; LEU-617; PRO-618; LYS-797 AND LEU-799.
    20. "Spondylo-epiphyseal dysplasia, Maroteaux type (pseudo-Morquio syndrome type 2), and parastremmatic dysplasia are caused by TRPV4 mutations."
      Nishimura G., Dai J., Lausch E., Unger S., Megarbane A., Kitoh H., Kim O.H., Cho T.J., Bedeschi F., Benedicenti F., Mendoza-Londono R., Silengo M., Schmidt-Rimpler M., Spranger J., Zabel B., Ikegawa S., Superti-Furga A.
      Am. J. Med. Genet. A 152:1443-1449(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SEDM, VARIANT PSTD HIS-594, VARIANTS LYS-183; CYS-602; LYS-797 AND LEU-799.
    21. Cited for: VARIANTS MTD PHE-199; ALA-295; THR-331; PHE-342; PHE-471 DEL; LEU-592; LYS-775; ALA-799; SER-799; LEU-799 AND ARG-799, VARIANTS SMDK LYS-278; HIS-594; PRO-596; TRP-600; ILE-625; MET-709; TYR-777 AND LYS-797.
    22. Cited for: VARIANTS CMT2C TRP-315 AND CYS-316, VARIANT DSMAC HIS-269, SUBCELLULAR LOCATION.
    23. "Scapuloperoneal spinal muscular atrophy and CMT2C are allelic disorders caused by alterations in TRPV4."
      Deng H.X., Klein C.J., Yan J., Shi Y., Wu Y., Fecto F., Yau H.J., Yang Y., Zhai H., Siddique N., Hedley-Whyte E.T., Delong R., Martina M., Dyck P.J., Siddique T.
      Nat. Genet. 42:165-169(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT2C HIS-269, VARIANT SPSMA CYS-316, SUBCELLULAR LOCATION.
    24. Cited for: VARIANTS CMT2C CYS-269 AND HIS-269.
    25. "CMT2C with vocal cord paresis associated with short stature and mutations in the TRPV4 gene."
      Chen D.H., Sul Y., Weiss M., Hillel A., Lipe H., Wolff J., Matsushita M., Raskind W., Bird T.
      Neurology 75:1968-1975(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CMT2C TRP-315 AND TYR-542.
    26. Cited for: VARIANTS FDAB VAL-270; PRO-271 AND LEU-273, CHARACTERIZATION OF VARIANTS FDAB VAL-270; PRO-271 AND LEU-273.
    27. "TRPV4 mutations and cytotoxic hypercalcemia in axonal Charcot-Marie-Tooth neuropathies."
      Klein C.J., Shi Y., Fecto F., Donaghy M., Nicholson G., McEntagart M.E., Crosby A.H., Wu Y., Lou H., McEvoy K.M., Siddique T., Deng H.X., Dyck P.J.
      Neurology 76:887-894(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CMT2C CYS-232 AND HIS-316, CHARACTERIZATION OF VARIANTS CMT2C CYS-232; CYS-269; HIS-269 AND HIS-316.
    28. Cited for: VARIANTS DSMAC ARG-97 AND CYS-232, CHARACTERIZATION OF VARIANT DSMAC ARG-97.

    Entry informationi

    Entry nameiTRPV4_HUMAN
    AccessioniPrimary (citable) accession number: Q9HBA0
    Secondary accession number(s): B7ZKQ6
    , Q17R79, Q2Y122, Q2Y123, Q2Y124, Q86YZ6, Q8NDY7, Q8NG64, Q96Q92, Q96RS7, Q9HBC0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3