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Protein

Transient receptor potential cation channel subfamily V member 1

Gene

Trpv1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca2+-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis.16 Publications
Isoform 3: Does not display channel activity in response to noxious chemical compounds, such as capsaicin and the vanilloid resiniferatoxin. Channel activity is not elicited by mildly acidic extracellular pH, and only slight channel activity is observed in response to noxiuos heat stimuli.1 Publication

Enzyme regulationi

Channel activity is activated via the interaction with PIRT and phosphatidylinositol 4,5-bisphosphate (PIP2). Both PIRT and PIP2 are required to activate channel activity (By similarity). The channel is sensitized by ATP binding. Repeated stimulation with capsaicin gives rise to progressively smaller responses, due to desensitization. This desensitization is triggered by the influx of calcium ions and is inhibited by elevated ATP levels. Ca2+ and CALM displace ATP from its binding site and trigger a conformation change that leads to a closed, desensitized channel. Intracellular PIP2 inhibits desensitization. The double-knot toxin (DkTx) from the Chinese earth tiger tarantula activates the channel and traps it in an open conformation.By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei115ATPCombined sources1
Binding sitei155ATPCombined sources1
Binding sitei160ATPCombined sources1
Binding sitei164ATPCombined sources1
Binding sitei512Agonist1 Publication1
Binding sitei550Agonist1 Publication1
Sitei557Important for agonist binding1 Publication1
Metal bindingi646Calcium; shared with neighboring subunitsBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi199 – 202ATPCombined sources4
Nucleotide bindingi210 – 211ATPCombined sources2

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • calcium channel activity Source: GO_Central
  • calcium-release channel activity Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • cation channel activity Source: RGD
  • cation transmembrane transporter activity Source: MGI
  • chloride channel regulator activity Source: RGD
  • excitatory extracellular ligand-gated ion channel activity Source: UniProtKB
  • extracellular ligand-gated ion channel activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • ligand-gated ion channel activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol binding Source: UniProtKB
  • temperature-gated ion channel activity Source: Ensembl
  • transmembrane signaling receptor activity Source: UniProtKB

GO - Biological processi

  • behavioral response to pain Source: Ensembl
  • calcium ion import into cell Source: UniProtKB
  • calcium ion transmembrane transport Source: UniProtKB
  • calcium ion transport Source: UniProtKB
  • cellular response to acidic pH Source: UniProtKB
  • cellular response to alkaloid Source: UniProtKB
  • cellular response to ATP Source: UniProtKB
  • cellular response to cytokine stimulus Source: UniProtKB
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to heat Source: UniProtKB
  • cellular response to nerve growth factor stimulus Source: RGD
  • cellular response to temperature stimulus Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • detection of chemical stimulus involved in sensory perception of pain Source: Ensembl
  • detection of temperature stimulus involved in sensory perception of pain Source: Ensembl
  • detection of temperature stimulus involved in thermoception Source: Ensembl
  • diet induced thermogenesis Source: Ensembl
  • fever generation Source: Ensembl
  • glutamate secretion Source: RGD
  • inflammatory response Source: RGD
  • lipid metabolic process Source: Ensembl
  • microglial cell activation Source: RGD
  • negative regulation of establishment of blood-brain barrier Source: RGD
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • peptide secretion Source: Ensembl
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of cytosolic calcium ion concentration Source: RGD
  • positive regulation of gastric acid secretion Source: RGD
  • positive regulation of nitric oxide biosynthetic process Source: RGD
  • protein homotetramerization Source: UniProtKB
  • response to capsazepine Source: UniProtKB
  • response to heat Source: MGI
  • response to peptide hormone Source: RGD
  • response to pH Source: MGI
  • sensory perception of mechanical stimulus Source: Ensembl
  • smooth muscle contraction involved in micturition Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Lipid-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-3295583. TRP channels.

Protein family/group databases

TCDBi1.A.4.2.1. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily V member 1
Short name:
TrpV1
Alternative name(s):
Capsaicin receptor
Osm-9-like TRP channel 1
Short name:
OTRPC1
Vanilloid receptor 1
Vanilloid receptor type 1-like
Gene namesi
Name:Trpv1
Synonyms:Vr1, Vr1l
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi628841. Trpv1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 432Cytoplasmic2 PublicationsAdd BLAST432
Transmembranei433 – 453Helical2 PublicationsAdd BLAST21
Topological domaini454 – 471Extracellular2 PublicationsAdd BLAST18
Transmembranei472 – 497Helical2 PublicationsAdd BLAST26
Topological domaini498 – 510Cytoplasmic2 PublicationsAdd BLAST13
Transmembranei511 – 531Helical2 PublicationsAdd BLAST21
Topological domaini532 – 535Extracellular2 Publications4
Transmembranei536 – 556Helical2 PublicationsAdd BLAST21
Topological domaini557 – 571Cytoplasmic2 PublicationsAdd BLAST15
Transmembranei572 – 599Helical2 PublicationsAdd BLAST28
Topological domaini600 – 626Extracellular2 PublicationsAdd BLAST27
Intramembranei627 – 649Pore-forming1 Publication2 PublicationsAdd BLAST23
Transmembranei658 – 686Helical2 PublicationsAdd BLAST29
Topological domaini687 – 838Cytoplasmic2 PublicationsAdd BLAST152

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytosol Source: RGD
  • dendrite Source: RGD
  • dendritic spine membrane Source: UniProtKB-SubCell
  • external side of plasma membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • intrinsic component of plasma membrane Source: UniProtKB
  • membrane Source: MGI
  • neuronal cell body Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic membrane Source: UniProtKB
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi114R → E: Abolishes capsaicin-evoked current and binding to resiniferatoxin. 1 Publication1
Mutagenesisi114Missing : Abolishes sensitivity to acid. 1 Publication1
Mutagenesisi115R → D: Abolishes capsaicin-evoked current and binding to resiniferatoxin. 1 Publication1
Mutagenesisi116S → A: Abolishes phosphorylation by PKCM and enhances channel response to capsaicin by PKCM. 1 Publication1
Mutagenesisi155K → A: Abolishes ATP binding. Abolishes CALM binding. Impairs normal desensitization by repeated exposure to capsaicin. 2 Publications1
Mutagenesisi160K → A: Abolishes ATP binding. Abolishes CALM binding. 1 Publication1
Mutagenesisi199Y → A: Strongly reduces affinity for ATP; when associated with A-202. 1 Publication1
Mutagenesisi202Q → A: Strongly reduces affinity for ATP; when associated with A-199. 1 Publication1
Mutagenesisi502S → A: Largely reduces PMA enhancement of capsaicin-evoked currents, but no effect on direct activation by PMA. Loss of activation by capsaicin and loss of vanilloid binding; when associated with I-704. 3 Publications1
Mutagenesisi511Y → A: Loss of sensitivity to capsaicin. 1 Publication1
Mutagenesisi547M → L: Reduces binding to resiniferatoxin. 1 Publication1
Mutagenesisi550T → I: Reduces sensitivity to capsaicin 10-fold; no effect on sensitivity to resiniferatoxin. Reduces binding to resiniferatoxin. 1 Publication1
Mutagenesisi636E → K: Abolishes channel activity. Restored channel activity; when associated with E-639. 1 Publication1
Mutagenesisi636E → Q: Slight modification of pore attributes. 1 Publication1
Mutagenesisi639K → E: Restored channel activity; when associated with K-636. 1 Publication1
Mutagenesisi644M → Y: Slightly modifies channel permeability. 1 Publication1
Mutagenesisi646D → N: Strongly reduces the affinity for pore blocker ruthenium red and lowered channel permeability for Mg(2+). 1 Publication1
Mutagenesisi648E → Q: Minor modification of pore attributes. 1 Publication1
Mutagenesisi651E → Q: Minor modification of pore attributes. 1 Publication1
Mutagenesisi704T → A: No effect on PMA-induced enhancement of capsaicin-evoked currents but reduces direct activation by PMA. 2 Publications1
Mutagenesisi704T → I: Loss of activation by capsaicin and loss of vanilloid binding; when associated with A-502. 2 Publications1
Mutagenesisi761E → K or Q: Abolishes capsaiin-evoked current and binding to resiniferatoxin. 1 Publication1
Mutagenesisi761Missing : Abolishes sensitivity to acid. 1 Publication1
Mutagenesisi785R → Q: Strongly reduces CALM-binding and abolishes PLC-mediated channel activity; when associated with Q-788. 2 Publications1
Mutagenesisi787W → R: Reduces CALM-binding. Reduces desensitization by repeated exposure to capsaicin. 1 Publication1
Mutagenesisi788K → Q: Strongly reduces CALM-binding and abolishes PLC-mediated channel activity; when associated with Q-785 or Q-797. 2 Publications1
Mutagenesisi797R → Q: Abolishes PLC-mediated channel activity; when associated with Q-788. 1 Publication1
Mutagenesisi800S → A: Largely reduces direct activation of by PMA and PMA-induced currents; no effect on receptor kinase-induced currents. 3 Publications1

Chemistry databases

ChEMBLiCHEMBL5102.
GuidetoPHARMACOLOGYi507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002153411 – 838Transient receptor potential cation channel subfamily V member 1Add BLAST838

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei116Phosphoserine; by PKA and PKD2 Publications1
Modified residuei144Phosphothreonine; by PKA; in vitro1 Publication1
Modified residuei370Phosphothreonine; by PKA; in vitro1 Publication1
Modified residuei502Phosphoserine; by PKC/PRKCE3 Publications1
Glycosylationi604N-linked (GlcNAc...)1 Publication1
Modified residuei704Phosphothreonine1 Publication1
Modified residuei774Phosphoserine; by PKA; in vitro1 Publication1
Modified residuei800Phosphoserine; by PKC/PRKCE and PKC/PRKCZ1 Publication1
Modified residuei820Phosphoserine; by PKA; in vitro1 Publication1

Post-translational modificationi

Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites, probably including Ser-116 as a major phosphorylation site. Phosphorylation by CAMKII seems to regulate binding to vanilloids. Phosphorylated and modulated by PRKCE, PRKCM and probably PRKCZ. Dephosphorylation by calcineurin seems to lead to receptor desensitization and phosphorylation by CAMKII recovers activity.4 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO35433.
PRIDEiO35433.

PTM databases

iPTMnetiO35433.
PhosphoSitePlusiO35433.

Expressioni

Tissue specificityi

Predominantly expressed in trigeminal and dorsal root sensory ganglia. Expressed also in hippocampus, cortex, cerebellum, olfactory bulb, mesencephalon and hindbrain. High expression in the cell bodies and dendrites of neurons in the hippocampus and in the cortex. In the brain detected also in astrocytes and pericytes (at protein level) (PubMed:15857679). Isoform 1 and isoform 3 are expressed in brain and peripheral blood mononuclear cells.3 Publications

Gene expression databases

BgeeiENSRNOG00000019486.
GenevisibleiO35433. RN.

Interactioni

Subunit structurei

Interacts with PIRT (By similarity). Homotetramer (PubMed:15190102, PubMed:24305160, PubMed:24305161, PubMed:27281200). May also form a heteromeric channel with TRPV3 (By similarity). Interacts with CALM, PRKCM and CSK (PubMed:12808128, PubMed:15084474, PubMed:15471852, PubMed:17582331). Interacts with PRKCG and NTRK1, probably by forming a trimeric complex (PubMed:11418861). Interacts with TMEM100 (By similarity).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-2794004,EBI-2794004

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi249845. 1 interactor.
DIPiDIP-56949N.
IntActiO35433. 1 interactor.
MINTiMINT-5117510.
STRINGi10116.ENSRNOP00000026493.

Chemistry databases

BindingDBiO35433.

Structurei

Secondary structure

1838
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi114 – 122Combined sources9
Turni128 – 131Combined sources4
Helixi132 – 138Combined sources7
Helixi146 – 148Combined sources3
Turni151 – 153Combined sources3
Helixi157 – 163Combined sources7
Helixi171 – 182Combined sources12
Helixi186 – 190Combined sources5
Turni197 – 201Combined sources5
Helixi204 – 210Combined sources7
Helixi214 – 222Combined sources9
Helixi234 – 236Combined sources3
Beta strandi240 – 242Combined sources3
Helixi251 – 257Combined sources7
Helixi261 – 269Combined sources9
Helixi287 – 294Combined sources8
Helixi299 – 319Combined sources21
Helixi325 – 327Combined sources3
Helixi336 – 342Combined sources7
Helixi346 – 356Combined sources11
Helixi788 – 792Combined sources5
Helixi793 – 795Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NYJX-ray3.20A101-364[»]
2PNNX-ray2.70A101-364[»]
3J5Pelectron microscopy3.28A/B/C/D111-719[»]
3J5Qelectron microscopy3.80B/D/E/G111-719[»]
3J5Relectron microscopy4.20A/B/C/D111-719[»]
3J9Jelectron microscopy-A/B/C/D111-719[»]
3SUIX-ray1.95B767-801[»]
5IRXelectron microscopy2.95A/B/C/D110-764[»]
5IRZelectron microscopy3.28B/C/D/E110-764[»]
5IS0electron microscopy3.43B/C/D/E110-764[»]
ProteinModelPortaliO35433.
SMRiO35433.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35433.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati110 – 152ANK 1Add BLAST43
Repeati153 – 199ANK 2Add BLAST47
Repeati200 – 246ANK 3Add BLAST47
Repeati247 – 282ANK 4Add BLAST36
Repeati283 – 331ANK 5Add BLAST49
Repeati332 – 358ANK 6Add BLAST27

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni114 – 115Important for channel activation by agonists and heat1 Publication2
Regioni684 – 712ADAdd BLAST29
Regioni767 – 801Interaction with calmodulin1 PublicationAdd BLAST35
Regioni777 – 792Required for PIP2-mediated channel inhibitionAdd BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi643 – 646Selectivity filter1 Publication4

Domaini

The association domain (AD) is necessary for self-association.

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiO35433.
KOiK05222.
OMAiCHRKEYV.
OrthoDBiEOG091G01LY.
PhylomeDBiO35433.
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.
IPR024863. TRPV1_channel.
[Graphical view]
PANTHERiPTHR10582:SF17. PTHR10582:SF17. 2 hits.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
SMARTiSM00248. ANK. 4 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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O35433-1) [UniParc]FASTAAdd to basket
Also known as: VR1L1

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

« Hide

        10         20         30         40         50
MEQRASLDSE ESESPPQENS CLDPPDRDPN CKPPPVKPHI FTTRSRTRLF
60 70 80 90 100
GKGDSEEASP LDCPYEEGGL ASCPIITVSS VLTIQRPGDG PASVRPSSQD
110 120 130 140 150
SVSAGEKPPR LYDRRSIFDA VAQSNCQELE SLLPFLQRSK KRLTDSEFKD
160 170 180 190 200
PETGKTCLLK AMLNLHNGQN DTIALLLDVA RKTDSLKQFV NASYTDSYYK
210 220 230 240 250
GQTALHIAIE RRNMTLVTLL VENGADVQAA ANGDFFKKTK GRPGFYFGEL
260 270 280 290 300
PLSLAACTNQ LAIVKFLLQN SWQPADISAR DSVGNTVLHA LVEVADNTVD
310 320 330 340 350
NTKFVTSMYN EILILGAKLH PTLKLEEITN RKGLTPLALA ASSGKIGVLA
360 370 380 390 400
YILQREIHEP ECRHLSRKFT EWAYGPVHSS LYDLSCIDTC EKNSVLEVIA
410 420 430 440 450
YSSSETPNRH DMLLVEPLNR LLQDKWDRFV KRIFYFNFFV YCLYMIIFTA
460 470 480 490 500
AAYYRPVEGL PPYKLKNTVG DYFRVTGEIL SVSGGVYFFF RGIQYFLQRR
510 520 530 540 550
PSLKSLFVDS YSEILFFVQS LFMLVSVVLY FSQRKEYVAS MVFSLAMGWT
560 570 580 590 600
NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYLVFLFG FSTAVVTLIE
610 620 630 640 650
DGKNNSLPME STPHKCRGSA CKPGNSYNSL YSTCLELFKF TIGMGDLEFT
660 670 680 690 700
ENYDFKAVFI ILLLAYVILT YILLLNMLIA LMGETVNKIA QESKNIWKLQ
710 720 730 740 750
RAITILDTEK SFLKCMRKAF RSGKLLQVGF TPDGKDDYRW CFRVDEVNWT
760 770 780 790 800
TWNTNVGIIN EDPGNCEGVK RTLSFSLRSG RVSGRNWKNF ALVPLLRDAS
810 820 830
TRDRHATQQE EVQLKHYTGS LKPEDAEVFK DSMVPGEK
Length:838
Mass (Da):94,948
Last modified:January 1, 1998 - v1
Checksum:iDAFC80B12BDF71BF
GO
Isoform 2 (identifier: O35433-2) [UniParc]FASTAAdd to basket
Also known as: VR1L2

The sequence of this isoform differs from the canonical sequence as follows:
     348-407: Missing.

Show »
Length:778
Mass (Da):88,050
Checksum:iAB7BC5F1721C9010
GO
Isoform 3 (identifier: O35433-3) [UniParc]FASTAAdd to basket
Also known as: VR.5'sv

The sequence of this isoform differs from the canonical sequence as follows:
     1-307: Missing.
     348-407: Missing.

Note: Inactive.
Show »
Length:471
Mass (Da):54,420
Checksum:iDFD8082CA26CA3C6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18E → D in BAA94307 (PubMed:11578842).Curated1
Sequence conflicti36V → A in AAK83151 (PubMed:11549313).Curated1
Sequence conflicti48R → G in BAA94306 (PubMed:11578842).Curated1
Sequence conflicti51G → W in BAA94306 (PubMed:11578842).Curated1
Sequence conflicti96P → Q in BAA94307 (PubMed:11578842).Curated1
Sequence conflicti179V → I in AAK83151 (PubMed:11549313).Curated1
Sequence conflicti735K → Q in BAA94306 (PubMed:11578842).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0134311 – 307Missing in isoform 3. 1 PublicationAdd BLAST307
Alternative sequenceiVSP_013432348 – 407Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST60

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029310 mRNA. Translation: AAC53398.1.
AF158248 mRNA. Translation: AAF28389.1.
AB041029 mRNA. Translation: BAA94306.1.
AB040873 mRNA. Translation: BAA94307.1.
AF327067 Genomic DNA. Translation: AAK83151.1.
AF327067 Genomic DNA. Translation: AAK83152.1.
PIRiT09054.
RefSeqiNP_114188.1. NM_031982.1. [O35433-1]
UniGeneiRn.3073.

Genome annotation databases

EnsembliENSRNOT00000026456; ENSRNOP00000026456; ENSRNOG00000019486. [O35433-3]
ENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486. [O35433-1]
GeneIDi83810.
KEGGirno:83810.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029310 mRNA. Translation: AAC53398.1.
AF158248 mRNA. Translation: AAF28389.1.
AB041029 mRNA. Translation: BAA94306.1.
AB040873 mRNA. Translation: BAA94307.1.
AF327067 Genomic DNA. Translation: AAK83151.1.
AF327067 Genomic DNA. Translation: AAK83152.1.
PIRiT09054.
RefSeqiNP_114188.1. NM_031982.1. [O35433-1]
UniGeneiRn.3073.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NYJX-ray3.20A101-364[»]
2PNNX-ray2.70A101-364[»]
3J5Pelectron microscopy3.28A/B/C/D111-719[»]
3J5Qelectron microscopy3.80B/D/E/G111-719[»]
3J5Relectron microscopy4.20A/B/C/D111-719[»]
3J9Jelectron microscopy-A/B/C/D111-719[»]
3SUIX-ray1.95B767-801[»]
5IRXelectron microscopy2.95A/B/C/D110-764[»]
5IRZelectron microscopy3.28B/C/D/E110-764[»]
5IS0electron microscopy3.43B/C/D/E110-764[»]
ProteinModelPortaliO35433.
SMRiO35433.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249845. 1 interactor.
DIPiDIP-56949N.
IntActiO35433. 1 interactor.
MINTiMINT-5117510.
STRINGi10116.ENSRNOP00000026493.

Chemistry databases

BindingDBiO35433.
ChEMBLiCHEMBL5102.
GuidetoPHARMACOLOGYi507.

Protein family/group databases

TCDBi1.A.4.2.1. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

iPTMnetiO35433.
PhosphoSitePlusiO35433.

Proteomic databases

PaxDbiO35433.
PRIDEiO35433.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026456; ENSRNOP00000026456; ENSRNOG00000019486. [O35433-3]
ENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486. [O35433-1]
GeneIDi83810.
KEGGirno:83810.

Organism-specific databases

CTDi7442.
RGDi628841. Trpv1.

Phylogenomic databases

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiO35433.
KOiK05222.
OMAiCHRKEYV.
OrthoDBiEOG091G01LY.
PhylomeDBiO35433.
TreeFamiTF314711.

Enzyme and pathway databases

ReactomeiR-RNO-3295583. TRP channels.

Miscellaneous databases

EvolutionaryTraceiO35433.
PROiO35433.

Gene expression databases

BgeeiENSRNOG00000019486.
GenevisibleiO35433. RN.

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.
IPR024863. TRPV1_channel.
[Graphical view]
PANTHERiPTHR10582:SF17. PTHR10582:SF17. 2 hits.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
SMARTiSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRPV1_RAT
AccessioniPrimary (citable) accession number: O35433
Secondary accession number(s): Q920B3
, Q920B4, Q9JLM0, Q9JM56, Q9JM57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Responses evoked by capsaicin, but not by low pH and heat, can be antagonized by capsazepine.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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