Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Transient receptor potential cation channel subfamily V member 1  

UniProtKB / Swiss-Prot ID :  TRPV1_RAT

Gene Name (Synonyms) : 
Trpv1, Vr1, Vr1l  

Species :  Rattus norvegicus (Rat). 

Subcellular Localization :  Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell projection, dendritic spine membrane; Multi-pass membrane protein. Note=Mostly, but not exclusively expressed in post-synaptic dendritic spines. 

Protein 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 Ca(2+)-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. 

Transmembrane Topology (topPTM) : TRPV1_RAT 

Protein Sequence MEQRASLDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSEEASPLDCPYEEGGL...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHCCCCCCCCCCCHHHHHHCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
6PhosphoserineEQRASLDSE
CCCCCCCCC
34.59Phosphositeplus
Link-
116PhosphoserineYDRRSIFDA
HCCCHHHHH
28.62Phosphositeplus
Link
116Phosphoserine; by PKA and PKD.YDRRSIFDA
HCCCHHHHH
28.62UniProtKB
Link
144PhosphothreonineKKRLTDSEF
CCCCCCCHH
41.32Phosphositeplus
Link
144Phosphothreonine; by PKA; in vitro.KKRLTDSEF
CCCCCCCHH
41.32UniProtKB
Link
199PhosphotyrosineTDSYYKGQT
CCCCCCCCC
16.76Phosphositeplus
Link
370PhosphothreonineSRKFTEWAY
CCHHHHHHC
33.38Phosphositeplus
Link-
370Phosphothreonine; by PKA; in vitro.SRKFTEWAY
CCHHHHHHC
33.38UniProtKB
Link-
406PhosphothreonineSSSETPNRH
CCCCCCHHH
28.01Phosphositeplus
Link-
502PhosphoserineQRRPSLKSL
HCCCCHHHH
46.77Phosphositeplus
Link-
502Phosphoserine; by PKC/PRKCE.QRRPSLKSL
HCCCCHHHH
46.77UniProtKB
Link-
604N-linked (GlcNAc...).EDGKNNSLP
HCCCCCCCC
49.18UniProtKB
Link-
616S-nitrosocysteineTPHKCRGSA
CCCCCCCCC
5.61dbSNO
Link-
621S-nitrosocysteineRGSACKPGN
CCCCCCCCC
6.14dbSNO
Link-
704PhosphothreonineQRAITILDT
HHHHHHCCC
17.95Phosphositeplus
Link-
704Phosphothreonine.QRAITILDT
HHHHHHCCC
17.95UniProtKB
Link-
774PhosphoserineKRTLSFSLR
CCEEEEEEE
16.51Phosphositeplus
Link-
774Phosphoserine; by PKA; in vitro.KRTLSFSLR
CCEEEEEEE
16.51UniProtKB
Link-
800PhosphoserineLRDASTRDR
ECCCCCCCC
28.41Phosphositeplus
Link-
800Phosphoserine; by PKC/PRKCE andPKC/PRKCZ.LRDASTRDR
ECCCCCCCC
28.41UniProtKB
Link-
820PhosphoserineHYTGSLKPE
ECCCCCCCC
25.97Phosphositeplus
Link-
820Phosphoserine; by PKA; in vitro.HYTGSLKPE
ECCCCCCCC
25.97UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Biochemical characterization of the vanilloid receptor 1 expressed ina 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).
Cited for: SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-604.
Phosphorylation
ReferencePubMed
"cAMP-dependent protein kinase regulates desensitization of thecapsaicin 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).
Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-116; THR-144; THR-370; SER-502;SER-774 AND SER-820.
"Phosphorylation of vanilloid receptor 1 by Ca2+/calmodulin-dependentkinase 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).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-502 AND THR-704, AND MUTAGENESIS OFSER-502 AND THR-704.
"Interaction between protein kinase Cmu and the vanilloid receptortype 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).
Cited for: INTERACTION WITH PRKCM, PHOSPHORYLATION AT SER-116, AND MUTAGENESIS OFSER-116.
"Direct phosphorylation of capsaicin receptor VR1 by protein kinaseCepsilon and identification of two target serine residues.";
Numazaki M., Tominaga T., Toyooka H., Tominaga M.;
J. Biol. Chem. 277:13375-13378(2002).
Cited for: PHOSPHORYLATION AT SER-502 AND SER-800, AND MUTAGENESIS OF SER-502 ANDSER-800.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures