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O35433 (TRPV1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:Trpv1
Synonyms:Vr1, Vr1l
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length838 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor-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. May be 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 accubens by affecting AMPA receptors endocytosis. Ref.1 Ref.2 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.24

Enzyme regulation

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.

Subunit structure

Interacts with PIRT By similarity. Self-associates. Probably homotetramer. May also form a heteromeric channel with TRPV3. Interacts with calmodulin, PRKCM and CSK. Interacts with PRKCG and NTRK1, probably by forming a trimeric complex. Ref.8 Ref.12 Ref.15 Ref.20 Ref.21

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell projectiondendritic spine membrane; Multi-pass membrane protein. Note: Mostly, but not exclusively expressed in post-synaptic dendritic spines. Ref.7 Ref.22

Tissue specificity

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. Isoform 1 and isoform 3 are expressed in brain and peripheral blood mononuclear cells. Ref.1 Ref.2 Ref.22

Domain

The association domain (AD) is necessary for self-association. Ref.23

Post-translational modification

Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites, probably including Ser-116 as a major phosphorylation site. Phoshphorylation 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. Ref.9 Ref.11 Ref.17 Ref.20

Miscellaneous

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

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV1 sub-subfamily. [View classification]

Contains 6 ANK repeats.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainANK repeat
Repeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Calmodulin-binding
Nucleotide-binding
   Molecular functionCalcium channel
Ionic channel
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular response to growth factor stimulus

Inferred from expression pattern. Source: RGD

cellular response to temperature stimulus

Inferred from expression pattern. Source: RGD

elevation of cytosolic calcium ion concentration

Inferred from direct assay. Source: RGD

glutamate secretion

Inferred from direct assay. Source: RGD

microglial cell activation

Inferred from mutant phenotype. Source: RGD

negative regulation of establishment of blood-brain barrier

Inferred from mutant phenotype. Source: RGD

positive regulation of apoptotic process

Inferred from mutant phenotype. Source: RGD

positive regulation of gastric acid secretion

Inferred from mutant phenotype. Source: RGD

positive regulation of nitric oxide biosynthetic process

Inferred from mutant phenotype. Source: RGD

response to heat

Inferred from direct assay. Source: MGI

response to pH

Inferred from direct assay. Source: MGI

response to peptide hormone stimulus

Inferred from expression pattern. Source: RGD

   Cellular componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Inferred from direct assay. Source: RGD

dendritic spine membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuronal cell body

Inferred from direct assay Ref.22. Source: RGD

postsynaptic membrane

Inferred from direct assay Ref.22. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin binding

Inferred from electronic annotation. Source: UniProtKB-KW

chloride channel regulator activity

Inferred from direct assay. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O35433-1)

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.
Isoform 2 (identifier: O35433-2)

Also known as: VR1L2;

The sequence of this isoform differs from the canonical sequence as follows:
     348-407: Missing.
Isoform 3 (identifier: O35433-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 838838Transient receptor potential cation channel subfamily V member 1
PRO_0000215341

Regions

Topological domain1 – 432432Cytoplasmic Potential
Transmembrane433 – 45321Helical; Potential
Topological domain454 – 47623Extracellular Potential
Transmembrane477 – 49721Helical; Potential
Topological domain498 – 51013Cytoplasmic Potential
Transmembrane511 – 53121Helical; Potential
Topological domain532 – 5354Extracellular Potential
Transmembrane536 – 55621Helical; Potential
Topological domain557 – 57923Cytoplasmic Potential
Transmembrane580 – 60021Helical; Potential
Intramembrane611 – 64636Pore-forming; Probable
Transmembrane659 – 67921Helical; Potential
Topological domain680 – 838159Cytoplasmic Potential
Repeat110 – 15243ANK 1
Repeat153 – 19947ANK 2
Repeat200 – 24647ANK 3
Repeat247 – 28236ANK 4
Repeat283 – 33149ANK 5
Repeat332 – 35827ANK 6
Region684 – 71229AD
Region767 – 80135Interaction with calmodulin
Region777 – 79216Required for PIP2-mediated channel inhibition

Amino acid modifications

Modified residue1161Phosphoserine; by PKA and PKD Ref.11 Ref.20
Modified residue1441Phosphothreonine; by PKA; in vitro Ref.11
Modified residue3701Phosphothreonine; by PKA; in vitro Ref.11
Modified residue5021Phosphoserine; by PKC/PRKCE Ref.9 Ref.11 Ref.17
Modified residue7041Phosphothreonine Ref.17
Modified residue7741Phosphoserine; by PKA; in vitro Ref.11
Modified residue8001Phosphoserine; by PKC/PRKCE and PKC/PRKCZ Ref.9
Modified residue8201Phosphoserine; by PKA; in vitro Ref.11
Glycosylation6041N-linked (GlcNAc...) Ref.7

Natural variations

Alternative sequence1 – 307307Missing in isoform 3.
VSP_013431
Alternative sequence348 – 40760Missing in isoform 2 and isoform 3.
VSP_013432

Experimental info

Mutagenesis1141R → E: Abolishes capsaicin-evoked current and binding to resiniferatoxin. Ref.16
Mutagenesis1141Missing: Abolishes sensitivity to acid. Ref.16
Mutagenesis1151R → D: Abolishes capsaicin-evoked current and binding to resiniferatoxin. Ref.16
Mutagenesis1161S → A: Abolishes phosphorylation by PKCM and enhances channel response to capsaicin by PKCM. Ref.20
Mutagenesis5021S → 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. Ref.9 Ref.13 Ref.17
Mutagenesis5111Y → A: Loss of sensitivity to capsaicin. Ref.18
Mutagenesis5471M → L: Reduces binding to resiniferatoxin. Ref.18
Mutagenesis5501T → I: Reduces sensitivity to capsaicin 10-fold; no effect on sensitivity to resiniferatoxin. Reduces binding to resiniferatoxin. Ref.18
Mutagenesis6361E → K: Abolishes channel activity. Restored channel activity; when associated with E-639. Ref.5
Mutagenesis6361E → Q: Slight modification of pore attributes. Ref.5
Mutagenesis6391K → E: Restored channel activity; when associated with K-636. Ref.5
Mutagenesis6441M → Y: Slightly modifies channel permeability. Ref.5
Mutagenesis6461D → N: Strongly reduces the affinity for pore blocker ruthenium red and lowered channel permeability for Mg(2+). Ref.5
Mutagenesis6481E → Q: Minor modification of pore attributes. Ref.5
Mutagenesis6511E → Q: Minor modification of pore attributes. Ref.5
Mutagenesis7041T → A: No effect on PMA-induced enhancement of capsaicin-evoked currents but reduces direct activation by PMA. Ref.13 Ref.17
Mutagenesis7041T → I: Loss of activation by capsaicin and loss of vanilloid binding; when associated with A-502. Ref.13 Ref.17
Mutagenesis7611E → K or Q: Abolishes capsaiin-evoked current and binding to resiniferatoxin. Ref.16
Mutagenesis7611Missing: Abolishes sensitivity to acid. Ref.16
Mutagenesis7851R → Q: Abolishes PLC-mediated channel activity; when associated with Q-788. Ref.14
Mutagenesis7881K → Q: Abolishes PLC-mediated channel activity; when associated with Q-785 or Q-797. Ref.14
Mutagenesis7971R → Q: Abolishes PLC-mediated channel activity; when associated with Q-788. Ref.14
Mutagenesis8001S → A: Largely reduces direct activation of by PMA and PMA-induced currents; no effect on receptor kinase-induced currents. Ref.9 Ref.13 Ref.14
Sequence conflict181E → D in BAA94307. Ref.3
Sequence conflict361V → A in AAK83151. Ref.4
Sequence conflict481R → G in BAA94306. Ref.3
Sequence conflict511G → W in BAA94306. Ref.3
Sequence conflict961P → Q in BAA94307. Ref.3
Sequence conflict1791V → I in AAK83151. Ref.4
Sequence conflict7351K → Q in BAA94306. Ref.3

Secondary structure

......................................... 838
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (VR1L1) [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DAFC80B12BDF71BF

FASTA83894,948
        10         20         30         40         50         60 
MEQRASLDSE ESESPPQENS CLDPPDRDPN CKPPPVKPHI FTTRSRTRLF GKGDSEEASP 

        70         80         90        100        110        120 
LDCPYEEGGL ASCPIITVSS VLTIQRPGDG PASVRPSSQD SVSAGEKPPR LYDRRSIFDA 

       130        140        150        160        170        180 
VAQSNCQELE SLLPFLQRSK KRLTDSEFKD PETGKTCLLK AMLNLHNGQN DTIALLLDVA 

       190        200        210        220        230        240 
RKTDSLKQFV NASYTDSYYK GQTALHIAIE RRNMTLVTLL VENGADVQAA ANGDFFKKTK 

       250        260        270        280        290        300 
GRPGFYFGEL PLSLAACTNQ LAIVKFLLQN SWQPADISAR DSVGNTVLHA LVEVADNTVD 

       310        320        330        340        350        360 
NTKFVTSMYN EILILGAKLH PTLKLEEITN RKGLTPLALA ASSGKIGVLA YILQREIHEP 

       370        380        390        400        410        420 
ECRHLSRKFT EWAYGPVHSS LYDLSCIDTC EKNSVLEVIA YSSSETPNRH DMLLVEPLNR 

       430        440        450        460        470        480 
LLQDKWDRFV KRIFYFNFFV YCLYMIIFTA AAYYRPVEGL PPYKLKNTVG DYFRVTGEIL 

       490        500        510        520        530        540 
SVSGGVYFFF RGIQYFLQRR PSLKSLFVDS YSEILFFVQS LFMLVSVVLY FSQRKEYVAS 

       550        560        570        580        590        600 
MVFSLAMGWT NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYLVFLFG FSTAVVTLIE 

       610        620        630        640        650        660 
DGKNNSLPME STPHKCRGSA CKPGNSYNSL YSTCLELFKF TIGMGDLEFT ENYDFKAVFI 

       670        680        690        700        710        720 
ILLLAYVILT YILLLNMLIA LMGETVNKIA QESKNIWKLQ RAITILDTEK SFLKCMRKAF 

       730        740        750        760        770        780 
RSGKLLQVGF TPDGKDDYRW CFRVDEVNWT TWNTNVGIIN EDPGNCEGVK RTLSFSLRSG 

       790        800        810        820        830 
RVSGRNWKNF ALVPLLRDAS TRDRHATQQE EVQLKHYTGS LKPEDAEVFK DSMVPGEK 

« Hide

Isoform 2 (VR1L2) [UniParc].

Checksum: AB7BC5F1721C9010
Show »

FASTA77888,050
Isoform 3 (VR.5'sv) [UniParc].

Checksum: DFD8082CA26CA3C6
Show »

FASTA47154,420

References

[1]"The capsaicin receptor: a heat-activated ion channel in the pain pathway."
Caterina M.J., Schumacher M.A., Tominaga M., Rosen T.A., Levine J.D., Julius D.
Nature 389:816-824(1997) [PubMed: 9349813] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Spinal ganglion.
[2]"Molecular cloning of an N-terminal splice variant of the capsaicin receptor. Loss of N-terminal domain suggests functional divergence among capsaicin receptor subtypes."
Schumacher M.A., Moff I., Sudanagunta S.P., Levine J.D.
J. Biol. Chem. 275:2756-2762(2000) [PubMed: 10644739] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, FUNCTION (ISOFORM 3).
Strain: Sprague-Dawley.
Tissue: Spinal ganglion and Trigeminal ganglion.
[3]"Propofol activates vanilloid receptor channels expressed in human embryonic kidney 293 cells."
Tsutsumi S., Tomioka A., Sudo M., Nakamura A., Shirakura K., Takagishi K., Kohama K.
Neurosci. Lett. 312:45-49(2001) [PubMed: 11578842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[4]"The genomic organization of the gene encoding the vanilloid receptor: evidence for multiple splice variants."
Xue Q., Yu Y., Trilk S.L., Jong B.E., Schumacher M.A.
Genomics 76:14-20(2001) [PubMed: 11549313] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-468, ALTERNATIVE SPLICING.
Strain: Sprague-Dawley.
[5]"Identification of an aspartic residue in the P-loop of the vanilloid receptor that modulates pore properties."
Garcia-Martinez C., Morenilla-Palao C., Planells-Cases R., Merino J.M., Ferrer-Montiel A.V.
J. Biol. Chem. 275:32552-32558(2000) [PubMed: 10931826] [Abstract]
Cited for: CHARACTERIZATION OF CHANNEL PORE, MUTAGENESIS OF GLU-636; LYS-639; MET-644; ASP-646; GLU-648 AND GLU-651.
[6]"Induction of vanilloid receptor channel activity by protein kinase C."
Premkumar L.S., Ahern G.P.
Nature 408:985-990(2000) [PubMed: 11140687] [Abstract]
Cited for: FUNCTION.
[7]"Biochemical characterization of the vanilloid receptor 1 expressed in a dorsal root ganglia derived cell line."
Jahnel R., Dreger M., Gillen C., Bender O., Kurreck J., Hucho F.
Eur. J. Biochem. 268:5489-5496(2001) [PubMed: 11683872] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-604.
[8]"Bradykinin and nerve growth factor release the capsaicin receptor from PtdIns(4,5)P2-mediated inhibition."
Chuang H.H., Prescott E.D., Kong H., Shields S., Jordt S.E., Basbaum A.I., Chao M.V., Julius D.
Nature 411:957-962(2001) [PubMed: 11418861] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRKCG AND NTRK1.
[9]"Direct phosphorylation of capsaicin receptor VR1 by protein kinase Cepsilon and identification of two target serine residues."
Numazaki M., Tominaga T., Toyooka H., Tominaga M.
J. Biol. Chem. 277:13375-13378(2002) [PubMed: 11884385] [Abstract]
Cited for: PHOSPHORYLATION AT SER-502 AND SER-800, MUTAGENESIS OF SER-502 AND SER-800.
[10]"Protein kinase C(alpha) is required for vanilloid receptor 1 activation. Evidence for multiple signaling pathways."
Olah Z., Karai L., Iadarola M.J.
J. Biol. Chem. 277:35752-35759(2002) [PubMed: 12095983] [Abstract]
Cited for: FUNCTION.
[11]"cAMP-dependent protein kinase regulates desensitization of the capsaicin receptor (VR1) by direct phosphorylation."
Bhave G., Zhu W., Wang H., Brasier D.J., Oxford G.S., Gereau R.W. IV
Neuron 35:721-731(2002) [PubMed: 12194871] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-116; THR-144; THR-370; SER-502; SER-774 AND SER-820.
[12]"Structural determinant of TRPV1 desensitization interacts with calmodulin."
Numazaki M., Tominaga T., Takeuchi K., Murayama N., Toyooka H., Tominaga M.
Proc. Natl. Acad. Sci. U.S.A. 100:8002-8006(2003) [PubMed: 12808128] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CALMODULIN.
[13]"Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1)."
Bhave G., Hu H.J., Glauner K.S., Zhu W., Wang H., Brasier D.J., Oxford G.S., Gereau R.W. IV
Proc. Natl. Acad. Sci. U.S.A. 100:12480-12485(2003) [PubMed: 14523239] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-502; THR-704 AND SER-800.
[14]"A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity."
Prescott E.D., Julius D.
Science 300:1284-1288(2003) [PubMed: 12764195] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-785; LYS-788; ARG-797 AND SER-800.
[15]"Modulation of TRPV1 by nonreceptor tyrosine kinase, c-Src kinase."
Jin X., Morsy N., Winston J., Pasricha P.J., Garrett K., Akbarali H.I.
Am. J. Physiol. 287:C558-C563(2004) [PubMed: 15084474] [Abstract]
Cited for: INTERACTION WITH CSK.
[16]"Agonist recognition sites in the cytosolic tails of vanilloid receptor 1."
Jung J., Lee S.Y., Hwang S.W., Cho H., Shin J., Kang Y.S., Kim S., Oh U.
J. Biol. Chem. 277:44448-44454(2002) [PubMed: 12228246] [Abstract]
Cited for: MUTAGENESIS OF ARG-114; ARG-115 AND GLU-761.
[17]"Phosphorylation of vanilloid receptor 1 by Ca2+/calmodulin-dependent kinase II regulates its vanilloid binding."
Jung J., Shin J.S., Lee S.-Y., Hwang S.W., Koo J., Cho H., Oh U.
J. Biol. Chem. 279:7048-7054(2004) [PubMed: 14630912] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-502 AND THR-704, MUTAGENESIS OF SER-502 AND THR-704.
[18]"Molecular determinants of vanilloid sensitivity in TRPV1."
Gavva N.R., Klionsky L., Qu Y., Shi L., Tamir R., Edenson S., Zhang T.J., Viswanadhan V.N., Toth A., Pearce L.V., Vanderah T.W., Porreca F., Blumberg P.M., Lile J., Sun Y., Wild K., Louis J.C., Treanor J.J.
J. Biol. Chem. 279:20283-20295(2004) [PubMed: 14996838] [Abstract]
Cited for: MUTAGENESIS OF TYR-511; MET-547 AND THR-550.
[19]"TRPV1 acts as proton channel to induce acidification in nociceptive neurons."
Hellwig N., Plant T.D., Janson W., Schafer M., Schultz G., Schaefer M.
J. Biol. Chem. 279:34553-34561(2004) [PubMed: 15173182] [Abstract]
Cited for: FUNCTION.
[20]"Interaction between protein kinase Cmu and the vanilloid receptor type 1."
Wang Y., Kedei N., Wang M., Wang Q.J., Huppler A.R., Toth A., Tran R., Blumberg P.M.
J. Biol. Chem. 279:53674-53682(2004) [PubMed: 15471852] [Abstract]
Cited for: INTERACTION WITH PRKCM, PHOSPHORYLATION AT SER-116, MUTAGENESIS OF SER-116.
[21]"Identification of a tetramerization domain in the C-terminus of the vanilloid receptor."
Garcia-Sanz N., Fernandez-Carvajal A., Morenilla-Palao C., Planells-Cases R., Fajardo-Sanchez E., Fernandez-Ballester G., Ferrer-Montiel A.
J. Neurosci. 24:5307-5314(2004) [PubMed: 15190102] [Abstract]
Cited for: SUBUNIT.
[22]"Expression and distribution of vanilloid receptor 1 (TRPV1) in the adult rat brain."
Toth A., Boczan J., Kedei N., Lizanecz E., Bagi Z., Papp Z., Edes I., Csiba L., Blumberg P.M.
Brain Res. Mol. Brain Res. 135:162-168(2005) [PubMed: 15857679] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[23]"The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity."
Lishko P.V., Procko E., Jin X., Phelps C.B., Gaudet R.
Neuron 54:905-918(2007) [PubMed: 17582331] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 101-364, ATP-BINDING, DOMAINS ANKYRIN REPEATS.
[24]"TRPV1 activation by endogenous anandamide triggers postsynaptic long-term depression in dentate gyrus."
Chavez A.E., Chiu C.Q., Castillo P.E.
Nat. Neurosci. 13:1511-1518(2010) [PubMed: 21076423] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00326014.
IPI00389268.
IPI00561075.
PIRT09054.
RefSeqNP_114188.1. NM_031982.1.
UniGeneRn.3073.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NYJX-ray3.20A101-364[»]
2PNNX-ray2.70A101-364[»]
ProteinModelPortalO35433.
SMRO35433. Positions 111-358.
ModBaseSearch...

Protein-protein interaction databases

IntActO35433. 1 interaction.
STRINGO35433.

Protein family/group databases

TCDB1.A.4.2.1. transient receptor potential Ca2+ channel (TRP-CC) family.

PTM databases

PhosphoSiteO35433.

Proteomic databases

PRIDEO35433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026456; ENSRNOP00000026456; ENSRNOG00000019486.
ENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486.
GeneID83810.
KEGGrno:83810.
UCSCAF029310. rat.
NM_031982. rat.

Organism-specific databases

CTD7442.
RGD628841. Trpv1.

Phylogenomic databases

eggNOGroNOG04377.
GeneTreeENSGT00550000074425.
HOVERGENHBG054085.
InParanoidO35433.
OrthoDBEOG48WC1B.

Gene expression databases

ArrayExpressO35433.
GenevestigatorO35433.
GermOnlineENSRNOG00000019486. Rattus norvegicus.

Family and domain databases

InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024862. TRPV_channel.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
KOK05222.
PANTHERPTHR10582. PTHR10582. 1 hit.
PfamPF00023. Ank. 2 hits.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR01768. TRPVRECEPTOR.
SMARTSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMSSF48403. ANK. 1 hit.
TIGRFAMsTIGR00870. Trp. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616421.

Entry information

Entry nameTRPV1_RAT
AccessionPrimary (citable) accession number: O35433
Secondary accession number(s): Q920B3 expand/collapse secondary AC list , Q920B4, Q9JLM0, Q9JM56, Q9JM57
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families