Q9HBA0 (TRPV4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TRPV4
Synonyms:	VRL2, VROAC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	871 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.11 Ref.12
Subunit structure	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 By similarity. Part of a complex containing MLC1, AQP4, HEPACAM and ATP1B1. Ref.11 Ref.15
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity. Cell junction › adherens junction By similarity. Note: Assembly of the putative homotetramer occurs primarily in the endoplasmic reticulum. Ref.7 Ref.22 Ref.23 Isoform 1: Cell membrane Ref.7 Ref.22 Ref.23. Isoform 5: Cell membrane Ref.7 Ref.22 Ref.23.
Tissue specificity	Found in the synoviocytes from patients with (RA) and without (CTR) rheumatoid arthritis (at protein level). Ref.12
Post-translational modification	Phosphorylation results in enhancement of its channel function.
Polymorphism	Genetic variations in TRPV4 determine the sodium serum level quantitative trait locus 1 (SSQTL1) [MIM: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.
Involvement in disease	Brachyolmia 3 (BRAC3) [MIM:113500]: The brachyolmias constitute a clinically and genetically heterogeneous group of skeletal dysplasias characterized by a short trunk, scoliosis and mild short stature. BRAC3 is an autosomal dominant form with severe kyphoscoliosis and flattened, irregular cervical vertebrae. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.21 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.18 Ref.19 Ref.21 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.28 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 regeneration 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26
Sequence similarities	Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV4 sub-subfamily. [View classification] Contains 3 ANK repeats.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Charcot-Marie-Tooth disease Disease mutation Dwarfism Neurodegeneration Neuropathy
Domain	ANK repeat Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Calmodulin-binding Nucleotide-binding
Molecular function	Calcium channel Ion channel
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton reorganization Inferred from sequence or structural similarity. Source: BHF-UCL actin filament organization Inferred from sequence or structural similarity. Source: BHF-UCL calcium ion import Inferred from sequence or structural similarity. Source: BHF-UCL cell death Inferred from electronic annotation. Source: UniProtKB-KW cell volume homeostasis Traceable author statement Ref.11. Source: UniProtKB cell-cell junction assembly Inferred from sequence or structural similarity. Source: UniProtKB cellular hypotonic response Inferred from sequence or structural similarity. Source: BHF-UCL cortical microtubule organization Inferred from sequence or structural similarity. Source: BHF-UCL elevation of cytosolic calcium ion concentration Inferred from direct assay PubMed 18458941. Source: UniProtKB hyperosmotic salinity response Inferred from electronic annotation. Source: Compara microtubule polymerization Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of neuron projection development Inferred from sequence or structural similarity. Source: BHF-UCL osmosensory signaling pathway Traceable author statement Ref.11. Source: UniProtKB positive regulation of microtubule depolymerization Inferred from sequence or structural similarity. Source: BHF-UCL regulation of response to osmotic stress Inferred from electronic annotation. Source: Compara response to mechanical stimulus Traceable author statement PubMed 15753126. Source: UniProtKB vasopressin secretion Inferred from electronic annotation. Source: Compara
Cellular_component	cilium Inferred from electronic annotation. Source: Compara cortical actin cytoskeleton Inferred from sequence or structural similarity. Source: BHF-UCL cytoplasmic microtubule Inferred from electronic annotation. Source: Compara filopodium Inferred from sequence or structural similarity. Source: BHF-UCL focal adhesion Inferred from sequence or structural similarity. Source: BHF-UCL growth cone Inferred from sequence or structural similarity. Source: BHF-UCL integral to membrane Non-traceable author statement Ref.2. Source: UniProtKB lamellipodium Inferred from sequence or structural similarity. Source: BHF-UCL ruffle membrane Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SH2 domain binding Inferred from sequence or structural similarity. Source: BHF-UCL actin filament binding Inferred from sequence or structural similarity. Source: BHF-UCL alpha-tubulin binding Inferred from sequence or structural similarity. Source: BHF-UCL beta-tubulin binding Inferred from sequence or structural similarity. Source: BHF-UCL calcium channel activity Inferred from direct assay PubMed 18458941. Source: UniProtKB calmodulin binding Inferred from mutant phenotype Ref.11. Source: UniProtKB microtubule binding Inferred from sequence or structural similarity. Source: BHF-UCL osmosensor activity Inferred from electronic annotation. Source: Compara protein kinase C binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9HBA0-1)

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.

Isoform 2 (identifier: Q9HBA0-2)

Also known as: B; OTRPC4beta;

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

Isoform 3 (identifier: Q9HBA0-3)

Also known as: TRPV-SV;

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

Isoform 4 (identifier: Q9HBA0-4)

Also known as: C;

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

Isoform 5 (identifier: Q9HBA0-5)

Also known as: D;

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

Isoform 6 (identifier: Q9HBA0-6)

Also known as: E;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 871

871

Transient receptor potential cation channel subfamily V member 4

PRO_0000215347

Regions

Topological domain

1 – 465

465

Cytoplasmic Potential

Transmembrane

466 – 486

21

Helical; Potential

Topological domain

487 – 508

22

Extracellular Potential

Transmembrane

509 – 529

21

Helical; Potential

Topological domain

530 – 550

21

Cytoplasmic Potential

Transmembrane

551 – 571

21

Helical; Potential

Topological domain

572

1

Extracellular Potential

Transmembrane

573 – 593

21

Helical; Potential

Topological domain

594 – 616

23

Cytoplasmic Potential

Transmembrane

617 – 637

21

Helical; Potential

Intramembrane

648 – 678

31

Pore-forming; Probable

Transmembrane

691 – 711

21

Helical; Potential

Topological domain

712 – 871

160

Cytoplasmic Potential

Repeat

237 – 266

30

ANK 1

Repeat

284 – 313

30

ANK 2

Repeat

369 – 398

30

ANK 3

Region

812 – 831

20

Interaction with calmodulin

Sites

Binding site

192

1

ATP

Binding site

201

1

ATP

Binding site

239

1

ATP

Binding site

248

1

ATP

Amino acid modifications

Modified residue

824

1

Phosphoserine; by PKC and PKA Ref.14

Natural variations

Alternative sequence

28 – 61

34

Missing in isoform 5.

VSP_026614

Alternative sequence

239 – 285

47

Missing in isoform 4 and isoform 6.

VSP_026615

Alternative sequence

385 – 444

60

Missing in isoform 2 and isoform 6.

VSP_013436

Alternative sequence

844 – 871

28

PLDSM…DDAPL → RHLCRVRRKR in isoform 3.

VSP_013437

Natural variant

19

1

P → S Associated with lower sodium concentraions in serum; shows diminished response to hypotonic stress relative to wild-type. Ref.13
Corresponds to variant rs3742030 [ dbSNP | Ensembl ].

VAR_052391

Natural variant

89

1

T → I in MTD; lethal form. Ref.19

VAR_064517

Natural variant

97

1

P → R in DSMAC; loss of function mutation. Ref.28

VAR_067989

Natural variant

183

1

E → K Found in a patient with spondyloepiphyseal dysplasia Maroteaux type. Ref.20

VAR_064518

Natural variant

197

1

K → R in MTD; lethal form. Ref.19

VAR_064519

Natural variant

199

1

L → F in MTD. Ref.21

VAR_064520

Natural variant

232

1

R → 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. Ref.27 Ref.28

VAR_067990

Natural variant

269

1

R → C in CMT2C. Ref.24 Ref.27

VAR_063528

Natural variant

269

1

R → H in DSMAC and CMT2C; increased agonist-induced channel activity and increased basal intracellular calcium concentration; causes increased cell death. Ref.22 Ref.23 Ref.24 Ref.27

VAR_063529

Natural variant

270

1

G → V in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists. Ref.26

VAR_068498

Natural variant

271

1

R → P in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists. Ref.26

VAR_068499

Natural variant

273

1

F → L in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists. Ref.26

VAR_068500

Natural variant

278

1

E → K in SMDK. Ref.21

VAR_064521

Natural variant

295

1

T → A in MTD. Ref.21

VAR_064522

Natural variant

315

1

R → W in CMT2C. Ref.22 Ref.25

VAR_063541

Natural variant

316

1

R → C in CMT2C and SPSMA. Ref.22 Ref.23

VAR_063530

Natural variant

316

1

R → 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. Ref.27

VAR_067991

Natural variant

331

1

I → F in MTD. Ref.18 Ref.19

VAR_062331

Natural variant

331

1

I → T in MTD. Ref.21

VAR_064523

Natural variant

333 – 336

4

Missing in SMDK.

VAR_067992

Natural variant

333

1

D → G in SMDK. Ref.18

VAR_062332

Natural variant

342

1

V → F in MTD. Ref.21

VAR_064524

Natural variant

471

1

Missing in MTD; lethal form. Ref.19 Ref.21

VAR_064525

Natural variant

542

1

S → Y in CMT2C. Ref.25

VAR_067993

Natural variant

592

1

F → L in MTD. Ref.21

VAR_064526

Natural variant

594

1

R → H in SMDK and PSTD. Ref.18 Ref.20 Ref.21

VAR_062333

Natural variant

596

1

L → P in SMDK. Ref.21

VAR_064527

Natural variant

600

1

G → W in SMDK. Ref.21

VAR_064528

Natural variant

602

1

Y → C Found in a patient with spondyloepiphyseal dysplasia Maroteaux type. Ref.20

VAR_064529

Natural variant

604

1

I → M in MTD; lethal form. Ref.19

VAR_064530

Natural variant

616

1

R → Q in BRAC3; this mutation results in a gain of function and a constitutive activation of the channel. Ref.17

VAR_054805

Natural variant

617

1

F → L in MTD. Ref.19

VAR_064531

Natural variant

618

1

L → P in MTD. Ref.6 Ref.19

VAR_064532

Natural variant

620

1

V → I in BRAC3; this mutation results in a gain of function and a constitutive activation of the channel. Ref.17

VAR_054806

Natural variant

625

1

M → I in SMDK. Ref.21

VAR_064533

Natural variant

709

1

L → M in SMDK. Ref.21

VAR_064534

Natural variant

716

1

A → S in SMDK. Ref.18

VAR_062334

Natural variant

775

1

R → K in MTD. Ref.21

VAR_064535

Natural variant

777

1

C → Y in SMDK. Ref.21

VAR_064536

Natural variant

797

1

E → K in MTD and SMDK; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type. Ref.19 Ref.20 Ref.21

VAR_064537

Natural variant

799

1

P → A in MTD. Ref.21

VAR_064538

Natural variant

799

1

P → L in MTD; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type. Ref.18 Ref.19 Ref.20 Ref.21

VAR_062335

Natural variant

799

1

P → R in MTD. Ref.21

VAR_064539

Natural variant

799

1

P → S in MTD. Ref.21

VAR_064540

Experimental info

Mutagenesis

816 – 821

6

RLRRDR → ELEEDE: Loss of calmodulin binding; when associated with A-828.

Mutagenesis

821 – 824

4

RWSS → AASA: Loss of calmodulin binding. Ref.14

Mutagenesis

822

1

W → A: Loss of Ca(2+) dependent current potentiation.

Mutagenesis

824

1

S → A: Loss of phosphorylation. Ref.14

Mutagenesis

824

1

S → D: Up-regulation of its function. Ref.14

Mutagenesis

828

1

R → A: Loss of calmodulin binding; when associated with 816-ELEEDE-821. Ref.11

Sequence conflict

385

1

I → V in AAG28029. Ref.1

Sequence conflict

452

1

V → A in BAC06573. Ref.6

Sequence conflict

781

1

D → N in AAG28029. Ref.1

Sequence conflict

820

1

D → T in BAB69040. Ref.4

Sequence conflict

861

1

P → T in BAC06573. Ref.6

Sequence conflict

867

1

D → E in AAG16127. Ref.2

Secondary structure

1

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871

Helix Strand Turn

Details...

Helix

151 – 159

9

Helix

164 – 166

3

Helix

169 – 175

7

Helix

183 – 185

3

Beta strand

188 – 190

3

Helix

194 – 200

7

Helix

209 – 220

12

Helix

223 – 228

6

Beta strand

234 – 239

6

Helix

241 – 247

7

Helix

251 – 260

10

Helix

271 – 273

3

Turn

276 – 279

4

Helix

288 – 294

7

Helix

298 – 306

9

Helix

324 – 331

8

Helix

336 – 356

21

Beta strand

357 – 360

4

Helix

362 – 364

3

Helix

373 – 379

7

Helix

383 – 395

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) [UniParc]. Last modified April 26, 2005. Version 2. Checksum: C62056B86C5A6FB6	FASTA	871	98,281
	10 20 30 40 50 60 MADSSEGPRA GPGEVAELPG DESGTPGGEA FPLSSLANLF EGEDGSLSPS PADASRPAGP 70 80 90 100 110 120 GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHSSDN 130 140 150 160 170 180 KRWRKKIIEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL PFLLTHKKRL 190 200 210 220 230 240 TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT 250 260 270 280 290 300 ALHIAIERRC KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI 310 320 330 340 350 360 VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL LKCARLFPDS 370 380 390 400 410 420 NLEAVLNNDG LSPLMMAAKT GKIGIFQHII RREVTDEDTR HLSRKFKDWA YGPVYSSLYD 430 440 450 460 470 480 LSSLDTCGEE ASVLEILVYN SKIENRHEML AVEPINELLR DKWRKFGAVS FYINVVSYLC 490 500 510 520 530 540 AMVIFTLTAY YQPLEGTPPY PYRTTVDYLR LAGEVITLFT GVLFFFTNIK DLFMKKCPGV 550 560 570 580 590 600 NSLFIDGSFQ LLYFIYSVLV IVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG 610 620 630 640 650 660 TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVSLLNPCA NMKVCNEDQT NCTVPTYPSC 670 680 690 700 710 720 RDSETFSTFL LDLFKLTIGM GDLEMLSSTK YPVVFIILLV TYIILTFVLL LNMLIALMGE 730 740 750 760 770 780 TVGQVSKESK HIWKLQWATT ILDIERSFPV FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV 790 800 810 820 830 840 DEVNWSHWNQ NLGIINEDPG KNETYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSNPDE 850 860 870 VVVPLDSMGN PRCDGHQQGY PRKWRTDDAP L
	Isoform 2 (B) (OTRPC4beta) [UniParc]. Checksum: A498FF4BBA1CD7A5	FASTA	811	91,261
	10 20 30 40 50 60 MADSSEGPRA GPGEVAELPG DESGTPGGEA FPLSSLANLF EGEDGSLSPS PADASRPAGP 70 80 90 100 110 120 GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHSSDN 130 140 150 160 170 180 KRWRKKIIEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL PFLLTHKKRL 190 200 210 220 230 240 TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT 250 260 270 280 290 300 ALHIAIERRC KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI 310 320 330 340 350 360 VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL LKCARLFPDS 370 380 390 400 410 420 NLEAVLNNDG LSPLMMAAKT GKIGNRHEML AVEPINELLR DKWRKFGAVS FYINVVSYLC 430 440 450 460 470 480 AMVIFTLTAY YQPLEGTPPY PYRTTVDYLR LAGEVITLFT GVLFFFTNIK DLFMKKCPGV 490 500 510 520 530 540 NSLFIDGSFQ LLYFIYSVLV IVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG 550 560 570 580 590 600 TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVSLLNPCA NMKVCNEDQT NCTVPTYPSC 610 620 630 640 650 660 RDSETFSTFL LDLFKLTIGM GDLEMLSSTK YPVVFIILLV TYIILTFVLL LNMLIALMGE 670 680 690 700 710 720 TVGQVSKESK HIWKLQWATT ILDIERSFPV FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV 730 740 750 760 770 780 DEVNWSHWNQ NLGIINEDPG KNETYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSNPDE 790 800 810 VVVPLDSMGN PRCDGHQQGY PRKWRTDDAP L
	Isoform 3 (TRPV-SV) [UniParc]. Checksum: EAA07196606AED20	FASTA	853	96,449
	10 20 30 40 50 60 MADSSEGPRA GPGEVAELPG DESGTPGGEA FPLSSLANLF EGEDGSLSPS PADASRPAGP 70 80 90 100 110 120 GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHSSDN 130 140 150 160 170 180 KRWRKKIIEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL PFLLTHKKRL 190 200 210 220 230 240 TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT 250 260 270 280 290 300 ALHIAIERRC KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI 310 320 330 340 350 360 VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL LKCARLFPDS 370 380 390 400 410 420 NLEAVLNNDG LSPLMMAAKT GKIGIFQHII RREVTDEDTR HLSRKFKDWA YGPVYSSLYD 430 440 450 460 470 480 LSSLDTCGEE ASVLEILVYN SKIENRHEML AVEPINELLR DKWRKFGAVS FYINVVSYLC 490 500 510 520 530 540 AMVIFTLTAY YQPLEGTPPY PYRTTVDYLR LAGEVITLFT GVLFFFTNIK DLFMKKCPGV 550 560 570 580 590 600 NSLFIDGSFQ LLYFIYSVLV IVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG 610 620 630 640 650 660 TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVSLLNPCA NMKVCNEDQT NCTVPTYPSC 670 680 690 700 710 720 RDSETFSTFL LDLFKLTIGM GDLEMLSSTK YPVVFIILLV TYIILTFVLL LNMLIALMGE 730 740 750 760 770 780 TVGQVSKESK HIWKLQWATT ILDIERSFPV FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV 790 800 810 820 830 840 DEVNWSHWNQ NLGIINEDPG KNETYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSNPDE 850 VVVRHLCRVR RKR
	Isoform 4 (C) [UniParc]. Checksum: EA7AFC7497D14495	FASTA	824	92,904
	10 20 30 40 50 60 MADSSEGPRA GPGEVAELPG DESGTPGGEA FPLSSLANLF EGEDGSLSPS PADASRPAGP 70 80 90 100 110 120 GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHSSDN 130 140 150 160 170 180 KRWRKKIIEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL PFLLTHKKRL 190 200 210 220 230 240 TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGEL 250 260 270 280 290 300 PLSLAACTNQ PHIVNYLTEN PHKKADMRRQ DSRGNTVLHA LVAIADNTRE NTKFVTKMYD 310 320 330 340 350 360 LLLLKCARLF PDSNLEAVLN NDGLSPLMMA AKTGKIGIFQ HIIRREVTDE DTRHLSRKFK 370 380 390 400 410 420 DWAYGPVYSS LYDLSSLDTC GEEASVLEIL VYNSKIENRH EMLAVEPINE LLRDKWRKFG 430 440 450 460 470 480 AVSFYINVVS YLCAMVIFTL TAYYQPLEGT PPYPYRTTVD YLRLAGEVIT LFTGVLFFFT 490 500 510 520 530 540 NIKDLFMKKC PGVNSLFIDG SFQLLYFIYS VLVIVSAALY LAGIEAYLAV MVFALVLGWM 550 560 570 580 590 600 NALYFTRGLK LTGTYSIMIQ KILFKDLFRF LLVYLLFMIG YASALVSLLN PCANMKVCNE 610 620 630 640 650 660 DQTNCTVPTY PSCRDSETFS TFLLDLFKLT IGMGDLEMLS STKYPVVFII LLVTYIILTF 670 680 690 700 710 720 VLLLNMLIAL MGETVGQVSK ESKHIWKLQW ATTILDIERS FPVFLRKAFR SGEMVTVGKS 730 740 750 760 770 780 SDGTPDRRWC FRVDEVNWSH WNQNLGIINE DPGKNETYQY YGFSHTVGRL RRDRWSSVVP 790 800 810 820 RVVELNKNSN PDEVVVPLDS MGNPRCDGHQ QGYPRKWRTD DAPL
	Isoform 5 (D) [UniParc]. Checksum: 1538A7B2E76C8CDF	FASTA	837	94,998
	10 20 30 40 50 60 MADSSEGPRA GPGEVAELPG DESGTPGDGR PNLRMKFQGA FRKGVPNPID LLESTLYESS 70 80 90 100 110 120 VVPGPKKAPM DSLFDYGTYR HHSSDNKRWR KKIIEKQPQS PKAPAPQPPP ILKVFNRPIL 130 140 150 160 170 180 FDIVSRGSTA DLDGLLPFLL THKKRLTDEE FREPSTGKTC LPKALLNLSN GRNDTIPVLL 190 200 210 220 230 240 DIAERTGNMR EFINSPFRDI YYRGQTALHI AIERRCKHYV ELLVAQGADV HAQARGRFFQ 250 260 270 280 290 300 PKDEGGYFYF GELPLSLAAC TNQPHIVNYL TENPHKKADM RRQDSRGNTV LHALVAIADN 310 320 330 340 350 360 TRENTKFVTK MYDLLLLKCA RLFPDSNLEA VLNNDGLSPL MMAAKTGKIG IFQHIIRREV 370 380 390 400 410 420 TDEDTRHLSR KFKDWAYGPV YSSLYDLSSL DTCGEEASVL EILVYNSKIE NRHEMLAVEP 430 440 450 460 470 480 INELLRDKWR KFGAVSFYIN VVSYLCAMVI FTLTAYYQPL EGTPPYPYRT TVDYLRLAGE 490 500 510 520 530 540 VITLFTGVLF FFTNIKDLFM KKCPGVNSLF IDGSFQLLYF IYSVLVIVSA ALYLAGIEAY 550 560 570 580 590 600 LAVMVFALVL GWMNALYFTR GLKLTGTYSI MIQKILFKDL FRFLLVYLLF MIGYASALVS 610 620 630 640 650 660 LLNPCANMKV CNEDQTNCTV PTYPSCRDSE TFSTFLLDLF KLTIGMGDLE MLSSTKYPVV 670 680 690 700 710 720 FIILLVTYII LTFVLLLNML IALMGETVGQ VSKESKHIWK LQWATTILDI ERSFPVFLRK 730 740 750 760 770 780 AFRSGEMVTV GKSSDGTPDR RWCFRVDEVN WSHWNQNLGI INEDPGKNET YQYYGFSHTV 790 800 810 820 830 GRLRRDRWSS VVPRVVELNK NSNPDEVVVP LDSMGNPRCD GHQQGYPRKW RTDDAPL
	Isoform 6 (E) [UniParc]. Checksum: B1307888F82B0E31	FASTA	764	85,884
	10 20 30 40 50 60 MADSSEGPRA GPGEVAELPG DESGTPGGEA FPLSSLANLF EGEDGSLSPS PADASRPAGP 70 80 90 100 110 120 GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHSSDN 130 140 150 160 170 180 KRWRKKIIEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL PFLLTHKKRL 190 200 210 220 230 240 TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGEL 250 260 270 280 290 300 PLSLAACTNQ PHIVNYLTEN PHKKADMRRQ DSRGNTVLHA LVAIADNTRE NTKFVTKMYD 310 320 330 340 350 360 LLLLKCARLF PDSNLEAVLN NDGLSPLMMA AKTGKIGNRH EMLAVEPINE LLRDKWRKFG 370 380 390 400 410 420 AVSFYINVVS YLCAMVIFTL TAYYQPLEGT PPYPYRTTVD YLRLAGEVIT LFTGVLFFFT 430 440 450 460 470 480 NIKDLFMKKC PGVNSLFIDG SFQLLYFIYS VLVIVSAALY LAGIEAYLAV MVFALVLGWM 490 500 510 520 530 540 NALYFTRGLK LTGTYSIMIQ KILFKDLFRF LLVYLLFMIG YASALVSLLN PCANMKVCNE 550 560 570 580 590 600 DQTNCTVPTY PSCRDSETFS TFLLDLFKLT IGMGDLEMLS STKYPVVFII LLVTYIILTF 610 620 630 640 650 660 VLLLNMLIAL MGETVGQVSK ESKHIWKLQW ATTILDIERS FPVFLRKAFR SGEMVTVGKS 670 680 690 700 710 720 SDGTPDRRWC FRVDEVNWSH WNQNLGIINE DPGKNETYQY YGFSHTVGRL RRDRWSSVVP 730 740 750 760 RVVELNKNSN PDEVVVPLDS MGNPRCDGHQ QGYPRKWRTD DAPL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, 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]	"Gain-of-function mutations in TRPV4 cause autosomal dominant brachyolmia." Rock M.J., Prenen J., Funari V.A., Funari T.L., Merriman B., Nelson S.F., Lachman R.S., Wilcox W.R., Reyno S., Quadrelli R., Vaglio A., Owsianik G., Janssens A., Voets T., Ikegawa S., Nagai T., Rimoin D.L., Nilius B., Cohn D.H. Nat. Genet. 40:999-1003(2008) [PubMed] [Europe PMC] [Abstract] 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]	"Dominant TRPV4 mutations in nonlethal and lethal metatropic dysplasia." Camacho N., Krakow D., Johnykutty S., Katzman P.J., Pepkowitz S., Vriens J., Nilius B., Boyce B.F., Cohn D.H. Am. J. Med. Genet. A 152:1169-1177(2010) [PubMed] [Europe PMC] [Abstract] 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]	"Novel and recurrent TRPV4 mutations and their association with distinct phenotypes within the TRPV4 dysplasia family." Dai J., Kim O.H., Cho T.J., Schmidt-Rimpler M., Tonoki H., Takikawa K., Haga N., Miyoshi K., Kitoh H., Yoo W.J., Choi I.H., Song H.R., Jin D.K., Kim H.T., Kamasaki H., Bianchi P., Grigelioniene G., Nampoothiri S. , Minagawa M., Miyagawa S.I., Fukao T., Marcelis C., Jansweijer M.C., Hennekam R.C., Bedeschi F., Mustonen A., Jiang Q., Ohashi H., Furuichi T., Unger S., Zabel B., Lausch E., Superti-Furga A., Nishimura G., Ikegawa S. J. Med. Genet. 47:704-709(2010) [PubMed] [Europe PMC] [Abstract] 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]	"Alterations in the ankyrin domain of TRPV4 cause congenital distal SMA, scapuloperoneal SMA and HMSN2C." Auer-Grumbach M., Olschewski A., Papic L., Kremer H., McEntagart M.E., Uhrig S., Fischer C., Frohlich E., Balint Z., Tang B., Strohmaier H., Lochmuller H., Schlotter-Weigel B., Senderek J., Krebs A., Dick K.J., Petty R., Longman C. , Anderson N.E., Padberg G.W., Schelhaas H.J., van Ravenswaaij-Arts C.M., Pieber T.R., Crosby A.H., Guelly C. Nat. Genet. 42:160-164(2010) [PubMed] [Europe PMC] [Abstract] 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]	"Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C." Landoure G., Zdebik A.A., Martinez T.L., Burnett B.G., Stanescu H.C., Inada H., Shi Y., Taye A.A., Kong L., Munns C.H., Choo S.S., Phelps C.B., Paudel R., Houlden H., Ludlow C.L., Caterina M.J., Gaudet R., Kleta R., Fischbeck K.H., Sumner C.J. Nat. Genet. 42:170-174(2010) [PubMed] [Europe PMC] [Abstract] 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]	"Mutations in TRPV4 cause an inherited arthropathy of hands and feet." Lamande S.R., Yuan Y., Gresshoff I.L., Rowley L., Belluoccio D., Kaluarachchi K., Little C.B., Botzenhart E., Zerres K., Amor D.J., Cole W.G., Savarirayan R., McIntyre P., Bateman J.F. Nat. Genet. 43:1142-1146(2011) [PubMed] [Europe PMC] [Abstract] 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]	"TRPV4 mutations in children with congenital distal spinal muscular atrophy." Fiorillo C., Moro F., Brisca G., Astrea G., Nesti C., Balint Z., Olschewski A., Meschini M.C., Guelly C., Auer-Grumbach M., Battini R., Pedemonte M., Romano A., Menchise V., Biancheri R., Santorelli F.M., Bruno C. Neurogenetics 13:195-203(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DSMAC ARG-97 AND CYS-232, CHARACTERIZATION OF VARIANT DSMAC ARG-97.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00168624.
IPI00168926.
IPI00555678.
IPI00657947.
IPI00658012.
IPI00853621.

RefSeq

NP_001170899.1. NM_001177428.1.
NP_001170902.1. NM_001177431.1.
NP_001170904.1. NM_001177433.1.
NP_067638.3. NM_021625.4.
NP_671737.1. NM_147204.2.

UniGene

Hs.506713.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9HBA0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9HBA0. 2 interactions.

PTM databases

PhosphoSite

Q9HBA0.

Polymorphism databases

DMDM

62901470.

Proteomic databases

PaxDb

Q9HBA0.

PRIDE

Q9HBA0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261740; ENSP00000261740; ENSG00000111199.
ENST00000346520; ENSP00000319003; ENSG00000111199.
ENST00000392719; ENSP00000376480; ENSG00000111199.
ENST00000418703; ENSP00000406191; ENSG00000111199.
ENST00000536838; ENSP00000444336; ENSG00000111199.
ENST00000537083; ENSP00000442738; ENSG00000111199.
ENST00000541794; ENSP00000442167; ENSG00000111199.
ENST00000544971; ENSP00000443611; ENSG00000111199.

GeneID

59341.

KEGG

hsa:59341.

UCSC

uc001tpg.2. human.
uc001tph.2. human.
uc001tpi.2. human.
uc001tpj.2. human.
uc021rdp.1. human.

Organism-specific databases

CTD

59341.

GeneCards

GC12M110220.

HGNC

HGNC:18083. TRPV4.

HPA

HPA007150.

MIM

113500. phenotype.
156530. phenotype.
168400. phenotype.
181405. phenotype.
184095. phenotype.
184252. phenotype.
600175. phenotype.
605427. gene.
606071. phenotype.
606835. phenotype.
613508. phenotype.

neXtProt

NX_Q9HBA0.

PharmGKB

PA38293.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG278734.

HOVERGEN

HBG054085.

InParanoid

Q9HBA0.

KO

K04973.

OMA

EDPGKSE.

OrthoDB

EOG4JQ3WW.

PhylomeDB

Q9HBA0.

Gene expression databases

ArrayExpress

Q9HBA0.

Bgee

Q9HBA0.

Genevestigator

Q9HBA0.

GermOnline

ENSG00000111199. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR008348. TRPV4_channel.
IPR024862. TRPV_channel.
[Graphical view]

PANTHER

PTHR10582. PTHR10582. 1 hit.
PTHR10582:SF4. PTHR10582:SF4. 1 hit.

Pfam

PF00023. Ank. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]

PRINTS

PR01768. TRPVRECEPTOR.
PR01769. VRL2RECEPTOR.

SMART

SM00248. ANK. 3 hits.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.

TIGRFAMs

TIGR00870. trp. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9HBA0.

ChEMBL

CHEMBL3119.

GenomeRNAi

59341.

NextBio

65228.

SOURCE

Search...

Entry information

Entry name

TRPV4_HUMAN

Accession

Primary (citable) accession number: Q9HBA0
Secondary accession number(s): B7ZKQ6 , Q17R79, Q2Y122, Q2Y123, Q2Y124, Q86YZ6, Q8NDY7, Q8NG64, Q96Q92, Q96RS7, Q9HBC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.