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Protein

Transient receptor potential cation channel subfamily V member 1

Gene

Trpv1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Activity 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. The Scolopendra mutilans RhTx toxin potentiates the heat activation pathway mediated by this channel by binding to the charge-rich outer pore region (in an activated state) (By similarity).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

GO - Biological processi

Keywordsi

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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi628841 Trpv1

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 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

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...) asparagine1 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 Expressed in 8 organ(s), highest expression level in adult mammalian kidney
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 the Scolopendra mutilans RhTx toxin (By similarity). Interacts with the spider Tau-theraphotoxin-Hs1a (PubMed:27281200). Interacts with TMEM100 (By similarity).By similarity9 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi249845, 2 interactors
DIPiDIP-56949N
IntActiO35433, 1 interactor
MINTiO35433
STRINGi10116.ENSRNOP00000026493

Chemistry databases

BindingDBiO35433

Structurei

Secondary structure

1838
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

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

Family and domain databases

CDDicd00204 ANK, 2 hits
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR005821 Ion_trans_dom
IPR024862 TRPV
IPR024863 TRPV1
IPR008347 TRPV1-4_channel
PANTHERiPTHR10582 PTHR10582, 1 hit
PTHR10582:SF17 PTHR10582:SF17, 1 hit
PfamiView protein in Pfam
PF12796 Ank_2, 1 hit
PF00520 Ion_trans, 1 hit
PRINTSiPR01768 TRPVRECEPTOR
SMARTiView protein in SMART
SM00248 ANK, 4 hits
SUPFAMiSSF48403 SSF48403, 1 hit
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 1 hit

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

EnsembliENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486 [O35433-1]
GeneIDi83810
KEGGirno:83810

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

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, 2 interactors
DIPiDIP-56949N
IntActiO35433, 1 interactor
MINTiO35433
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

EnsembliENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486 [O35433-1]
GeneIDi83810
KEGGirno:83810

Organism-specific databases

CTDi7442
RGDi628841 Trpv1

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-RNO-3295583 TRP channels

Miscellaneous databases

EvolutionaryTraceiO35433
PROiPR:O35433

Gene expression databases

BgeeiENSRNOG00000019486 Expressed in 8 organ(s), highest expression level in adult mammalian kidney
GenevisibleiO35433 RN

Family and domain databases

CDDicd00204 ANK, 2 hits
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR005821 Ion_trans_dom
IPR024862 TRPV
IPR024863 TRPV1
IPR008347 TRPV1-4_channel
PANTHERiPTHR10582 PTHR10582, 1 hit
PTHR10582:SF17 PTHR10582:SF17, 1 hit
PfamiView protein in Pfam
PF12796 Ank_2, 1 hit
PF00520 Ion_trans, 1 hit
PRINTSiPR01768 TRPVRECEPTOR
SMARTiView protein in SMART
SM00248 ANK, 4 hits
SUPFAMiSSF48403 SSF48403, 1 hit
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTRPV1_RAT
AccessioniPrimary (citable) accession number: O35433
Secondary accession number(s): Q920B3
, Q920B4, Q9JLM0, Q9JM56, Q9JM57
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 1, 1998
Last modified: November 7, 2018
This is version 164 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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