UniProtKB - O35433 (TRPV1_RAT)
Transient receptor potential cation channel subfamily V member 1
Trpv1
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 PublicationsDoes 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 PublicationMiscellaneous
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 115 | ATPCombined sources | 1 | |
Binding sitei | 155 | ATPCombined sources | 1 | |
Binding sitei | 160 | ATPCombined sources | 1 | |
Binding sitei | 164 | ATPCombined sources | 1 | |
Binding sitei | 550 | Resiniferatoxin; agonistCombined sources1 Publication | 1 | |
Binding sitei | 557 | Resiniferatoxin; agonistCombined sources1 Publication | 1 | |
Metal bindingi | 646 | Calcium; shared with neighboring subunitsBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 199 – 202 | ATPCombined sources | 4 | |
Nucleotide bindingi | 210 – 211 | ATPCombined sources | 2 |
GO - Molecular functioni
- ATP binding Source: UniProtKB
- calcium channel activity Source: RGD
- 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
- ion channel activity Source: GO_Central
- ligand-gated ion channel activity Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- phosphatidylinositol binding Source: UniProtKB
- phosphoprotein binding Source: RGD
- temperature-gated ion channel activity Source: RGD
- transmembrane signaling receptor activity Source: UniProtKB
GO - Biological processi
- behavioral response to pain Source: RGD
- calcium ion import across plasma membrane 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: RGD
- detection of temperature stimulus involved in sensory perception of pain Source: RGD
- detection of temperature stimulus involved in thermoception Source: RGD
- diet induced thermogenesis Source: RGD
- fever generation Source: RGD
- glutamate secretion Source: RGD
- inflammatory response Source: RGD
- ion transmembrane transport Source: RGD
- lipid metabolic process Source: RGD
- microglial cell activation Source: RGD
- negative regulation of establishment of blood-brain barrier Source: RGD
- negative regulation of heart rate Source: RGD
- negative regulation of mitochondrial membrane potential Source: RGD
- negative regulation of systemic arterial blood pressure Source: RGD
- negative regulation of transcription by RNA polymerase II Source: RGD
- peptide secretion Source: RGD
- 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 organonitrogen compound Source: RGD
- response to pain Source: RGD
- response to peptide hormone Source: RGD
- response to pH Source: MGI
- sensory perception of mechanical stimulus Source: RGD
- sensory perception of pain Source: RGD
- smooth muscle contraction involved in micturition Source: RGD
- temperature homeostasis Source: RGD
- thermoception Source: RGD
- urinary bladder smooth muscle contraction Source: RGD
Keywordsi
Molecular function | Calcium channel, Calmodulin-binding, Ion channel |
Biological process | Calcium transport, Ion transport, Transport |
Ligand | ATP-binding, Calcium, Lipid-binding, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-RNO-3295583, TRP channels |
Protein family/group databases
TCDBi | 1.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 1Short 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 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 628841, Trpv1 |
Subcellular locationi
Plasma membrane
- postsynaptic cell membrane 1 Publication; Multi-pass membrane protein Curated
- dendritic spine membrane 1 Publication; Multi-pass membrane protein Curated
- Cell membrane 3 Publications; Multi-pass membrane protein 3 Publications
Note: Mostly, but not exclusively expressed in postsynaptic dendritic spines.1 Publication
Cytosol
- cytosol Source: RGD
Mitochondrion
- mitochondrion Source: RGD
Plasma Membrane
- dendritic spine membrane Source: UniProtKB-SubCell
- external side of plasma membrane Source: UniProtKB
- integral component of plasma membrane Source: UniProtKB
- intrinsic component of plasma membrane Source: UniProtKB
- plasma membrane Source: RGD
- postsynaptic membrane Source: UniProtKB
Other locations
- dendrite Source: RGD
- integral component of membrane Source: UniProtKB
- membrane Source: MGI
- neuron projection Source: RGD
- neuronal cell body Source: RGD
- synapse Source: RGD
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 432 | Cytoplasmic2 PublicationsAdd BLAST | 432 | |
Transmembranei | 433 – 453 | Helical2 PublicationsAdd BLAST | 21 | |
Topological domaini | 454 – 471 | Extracellular2 PublicationsAdd BLAST | 18 | |
Transmembranei | 472 – 497 | Helical2 PublicationsAdd BLAST | 26 | |
Topological domaini | 498 – 510 | Cytoplasmic2 PublicationsAdd BLAST | 13 | |
Transmembranei | 511 – 531 | Helical2 PublicationsAdd BLAST | 21 | |
Topological domaini | 532 – 535 | Extracellular2 Publications | 4 | |
Transmembranei | 536 – 556 | Helical2 PublicationsAdd BLAST | 21 | |
Topological domaini | 557 – 571 | Cytoplasmic2 PublicationsAdd BLAST | 15 | |
Transmembranei | 572 – 599 | Helical2 PublicationsAdd BLAST | 28 | |
Topological domaini | 600 – 626 | Extracellular2 PublicationsAdd BLAST | 27 | |
Intramembranei | 627 – 649 | Pore-forming1 Publication2 PublicationsAdd BLAST | 23 | |
Transmembranei | 658 – 686 | Helical2 PublicationsAdd BLAST | 29 | |
Topological domaini | 687 – 838 | Cytoplasmic2 PublicationsAdd BLAST | 152 |
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, SynapsePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 114 | R → E: Abolishes capsaicin-evoked current and binding to resiniferatoxin. 1 Publication | 1 | |
Mutagenesisi | 114 | Missing : Abolishes sensitivity to acid. 1 Publication | 1 | |
Mutagenesisi | 115 | R → D: Abolishes capsaicin-evoked current and binding to resiniferatoxin. 1 Publication | 1 | |
Mutagenesisi | 116 | S → A: Abolishes phosphorylation by PKCM and enhances channel response to capsaicin by PKCM. 1 Publication | 1 | |
Mutagenesisi | 155 | K → A: Abolishes ATP binding. Abolishes CALM binding. Impairs normal desensitization by repeated exposure to capsaicin. 2 Publications | 1 | |
Mutagenesisi | 160 | K → A: Abolishes ATP binding. Abolishes CALM binding. 1 Publication | 1 | |
Mutagenesisi | 199 | Y → A: Strongly reduces affinity for ATP; when associated with A-202. 1 Publication | 1 | |
Mutagenesisi | 202 | Q → A: Strongly reduces affinity for ATP; when associated with A-199. 1 Publication | 1 | |
Mutagenesisi | 502 | S → 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 Publications | 1 | |
Mutagenesisi | 511 | Y → A: Loss of sensitivity to capsaicin. 1 Publication | 1 | |
Mutagenesisi | 547 | M → L: Reduces binding to resiniferatoxin. 1 Publication | 1 | |
Mutagenesisi | 550 | T → I: Reduces sensitivity to capsaicin 10-fold; no effect on sensitivity to resiniferatoxin. Reduces binding to resiniferatoxin. 1 Publication | 1 | |
Mutagenesisi | 636 | E → K: Abolishes channel activity. Restored channel activity; when associated with E-639. 1 Publication | 1 | |
Mutagenesisi | 636 | E → Q: Slight modification of pore attributes. 1 Publication | 1 | |
Mutagenesisi | 639 | K → E: Restored channel activity; when associated with K-636. 1 Publication | 1 | |
Mutagenesisi | 644 | M → Y: Slightly modifies channel permeability. 1 Publication | 1 | |
Mutagenesisi | 646 | D → N: Strongly reduces the affinity for pore blocker ruthenium red and lowered channel permeability for Mg(2+). 1 Publication | 1 | |
Mutagenesisi | 648 | E → Q: Minor modification of pore attributes. 1 Publication | 1 | |
Mutagenesisi | 651 | E → Q: Minor modification of pore attributes. 1 Publication | 1 | |
Mutagenesisi | 704 | T → A: No effect on PMA-induced enhancement of capsaicin-evoked currents but reduces direct activation by PMA. 2 Publications | 1 | |
Mutagenesisi | 704 | T → I: Loss of activation by capsaicin and loss of vanilloid binding; when associated with A-502. 2 Publications | 1 | |
Mutagenesisi | 761 | E → K or Q: Abolishes capsaiin-evoked current and binding to resiniferatoxin. 1 Publication | 1 | |
Mutagenesisi | 761 | Missing : Abolishes sensitivity to acid. 1 Publication | 1 | |
Mutagenesisi | 785 | R → Q: Strongly reduces CALM-binding and abolishes PLC-mediated channel activity; when associated with Q-788. 2 Publications | 1 | |
Mutagenesisi | 787 | W → R: Reduces CALM-binding. Reduces desensitization by repeated exposure to capsaicin. 1 Publication | 1 | |
Mutagenesisi | 788 | K → Q: Strongly reduces CALM-binding and abolishes PLC-mediated channel activity; when associated with Q-785 or Q-797. 2 Publications | 1 | |
Mutagenesisi | 797 | R → Q: Abolishes PLC-mediated channel activity; when associated with Q-788. 1 Publication | 1 | |
Mutagenesisi | 800 | S → A: Largely reduces direct activation of by PMA and PMA-induced currents; no effect on receptor kinase-induced currents. 3 Publications | 1 |
Chemistry databases
ChEMBLi | CHEMBL5102 |
DrugCentrali | O35433 |
GuidetoPHARMACOLOGYi | 507 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000215341 | 1 – 838 | Transient receptor potential cation channel subfamily V member 1Add BLAST | 838 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 116 | Phosphoserine; by PKA and PKD2 Publications | 1 | |
Modified residuei | 144 | Phosphothreonine; by PKA; in vitro1 Publication | 1 | |
Modified residuei | 370 | Phosphothreonine; by PKA; in vitro1 Publication | 1 | |
Modified residuei | 502 | Phosphoserine; by PKC/PRKCE3 Publications | 1 | |
Glycosylationi | 604 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Modified residuei | 704 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 774 | Phosphoserine; by PKA; in vitro1 Publication | 1 | |
Modified residuei | 800 | Phosphoserine; by PKC/PRKCE and PKC/PRKCZ1 Publication | 1 | |
Modified residuei | 820 | Phosphoserine; by PKA; in vitro1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Glycoprotein, PhosphoproteinProteomic databases
PaxDbi | O35433 |
PTM databases
GlyGeni | O35433, 1 site |
iPTMneti | O35433 |
PhosphoSitePlusi | O35433 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSRNOG00000019486, Expressed in adult mammalian kidney and 19 other tissues |
Genevisiblei | O35433, 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).
Interacts with PACS2 (By similarity).
By similarity9 PublicationsBinary interactionsi
O35433
With | #Exp. | IntAct |
---|---|---|
itself | 11 | EBI-2794004,EBI-2794004 |
P0CH43 from Cyriopagopus schmidti. | 2 | EBI-2794004,EBI-2793994 |
Trpv1 - isoform 1 [O35433-1]
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-15703031,EBI-15703031 |
GO - Molecular functioni
- calmodulin binding Source: UniProtKB
- identical protein binding Source: IntAct
- phosphoprotein binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 249845, 3 interactors |
DIPi | DIP-56949N |
IntActi | O35433, 3 interactors |
MINTi | O35433 |
STRINGi | 10116.ENSRNOP00000026493 |
Chemistry databases
BindingDBi | O35433 |
Structurei
Secondary structure
3D structure databases
SMRi | O35433 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O35433 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 110 – 152 | ANK 1Add BLAST | 43 | |
Repeati | 153 – 199 | ANK 2Add BLAST | 47 | |
Repeati | 200 – 246 | ANK 3Add BLAST | 47 | |
Repeati | 247 – 282 | ANK 4Add BLAST | 36 | |
Repeati | 283 – 331 | ANK 5Add BLAST | 49 | |
Repeati | 332 – 358 | ANK 6Add BLAST | 27 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 63 | DisorderedSequence analysisAdd BLAST | 63 | |
Regioni | 86 – 109 | DisorderedSequence analysisAdd BLAST | 24 | |
Regioni | 511 – 512 | Resiniferatoxin binding; agonistCombined sources1 Publication | 2 | |
Regioni | 684 – 712 | ADAdd BLAST | 29 | |
Regioni | 767 – 801 | Interaction with calmodulin1 PublicationAdd BLAST | 35 | |
Regioni | 777 – 792 | Required for PIP2-mediated channel inhibitionAdd BLAST | 16 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 643 – 646 | Selectivity filter1 Publication | 4 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 86 – 104 | Polar residuesSequence analysisAdd BLAST | 19 |
Domaini
Sequence similaritiesi
Keywords - Domaini
ANK repeat, Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3676, Eukaryota |
GeneTreei | ENSGT00940000160870 |
HOGENOMi | CLU_012795_1_0_1 |
InParanoidi | O35433 |
OMAi | YLHQNMK |
OrthoDBi | 693004at2759 |
PhylomeDBi | O35433 |
TreeFami | TF314711 |
Family and domain databases
Gene3Di | 1.25.40.20, 1 hit |
InterProi | View protein in InterPro IPR002110, Ankyrin_rpt IPR036770, Ankyrin_rpt-contain_sf IPR005821, Ion_trans_dom IPR024862, TRPV IPR024863, TRPV1 IPR008347, TRPV1-4_channel |
PANTHERi | PTHR10582, PTHR10582, 1 hit PTHR10582:SF17, PTHR10582:SF17, 1 hit |
Pfami | View protein in Pfam PF12796, Ank_2, 1 hit PF00520, Ion_trans, 1 hit |
PRINTSi | PR01768, TRPVRECEPTOR |
SMARTi | View protein in SMART SM00248, ANK, 4 hits |
SUPFAMi | SSF48403, SSF48403, 1 hit |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 1 hit |
s (3)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 18 | E → D in BAA94307 (PubMed:11578842).Curated | 1 | |
Sequence conflicti | 36 | V → A in AAK83151 (PubMed:11549313).Curated | 1 | |
Sequence conflicti | 48 | R → G in BAA94306 (PubMed:11578842).Curated | 1 | |
Sequence conflicti | 51 | G → W in BAA94306 (PubMed:11578842).Curated | 1 | |
Sequence conflicti | 96 | P → Q in BAA94307 (PubMed:11578842).Curated | 1 | |
Sequence conflicti | 179 | V → I in AAK83151 (PubMed:11549313).Curated | 1 | |
Sequence conflicti | 735 | K → Q in BAA94306 (PubMed:11578842).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_013431 | 1 – 307 | Missing in isoform 3. 1 PublicationAdd BLAST | 307 | |
Alternative sequenceiVSP_013432 | 348 – 407 | Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST | 60 |
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 |
PIRi | T09054 |
RefSeqi | NP_114188.1, NM_031982.1 [O35433-1] |
Genome annotation databases
Ensembli | ENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486 [O35433-1] |
GeneIDi | 83810 |
KEGGi | rno:83810 |
Keywords - Coding sequence diversityi
Alternative splicingSimilar 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 |
PIRi | T09054 |
RefSeqi | NP_114188.1, NM_031982.1 [O35433-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2NYJ | X-ray | 3.20 | A | 101-364 | [»] | |
2PNN | X-ray | 2.70 | A | 101-364 | [»] | |
3J5P | electron microscopy | 3.28 | A/B/C/D | 111-719 | [»] | |
3J5Q | electron microscopy | 3.80 | B/D/E/G | 111-719 | [»] | |
3J5R | electron microscopy | 4.20 | A/B/C/D | 111-719 | [»] | |
3J9J | electron microscopy | - | A/B/C/D | 111-719 | [»] | |
3SUI | X-ray | 1.95 | B | 767-801 | [»] | |
5IRX | electron microscopy | 2.95 | A/B/C/D | 110-764 | [»] | |
5IRZ | electron microscopy | 3.28 | B/C/D/E | 110-764 | [»] | |
5IS0 | electron microscopy | 3.43 | B/C/D/E | 110-764 | [»] | |
7L2H | electron microscopy | 2.63 | A/B/C/D | 2-838 | [»] | |
7L2I | electron microscopy | 3.70 | A/B/C/D | 2-838 | [»] | |
7L2J | electron microscopy | 3.66 | A/B/C/D | 2-838 | [»] | |
7L2K | electron microscopy | 3.89 | A/B/C/D | 2-838 | [»] | |
7L2L | electron microscopy | 3.42 | A/B/C/D | 2-838 | [»] | |
7L2M | electron microscopy | 3.84 | A/B/C/D | 2-838 | [»] | |
7L2N | electron microscopy | 3.09 | A/B/C/D | 2-838 | [»] | |
7L2O | electron microscopy | 3.64 | A/B/C/D | 2-838 | [»] | |
7L2P | electron microscopy | 2.60 | A/B/C/D | 110-764 | [»] | |
7L2R | electron microscopy | 3.30 | A/B/C/D | 110-764 | [»] | |
7L2S | electron microscopy | 2.71 | A/B/C/D | 110-764 | [»] | |
7L2T | electron microscopy | 3.08 | A/B/C/D | 110-764 | [»] | |
7L2U | electron microscopy | 3.47 | A/B/C/D | 110-764 | [»] | |
7L2V | electron microscopy | 3.64 | A/B/C/D | 110-764 | [»] | |
7L2W | electron microscopy | 3.16 | A/B/C/D | 110-764 | [»] | |
7L2X | electron microscopy | 3.26 | A/B/C/D | 110-764 | [»] | |
7LP9 | electron microscopy | 2.63 | A/B/C/D | 1-838 | [»] | |
7LPA | electron microscopy | 3.37 | A/B/C/D | 1-838 | [»] | |
7LPB | electron microscopy | 3.54 | A/B/C/D | 1-838 | [»] | |
7LPC | electron microscopy | 3.06 | A/B/C/D | 1-838 | [»] | |
7LPD | electron microscopy | 3.55 | A/B/C/D | 1-838 | [»] | |
7LPE | electron microscopy | 3.72 | A/B/C/D | 1-838 | [»] | |
7MZ5 | electron microscopy | 2.76 | A/B/C/D | 2-838 | [»] | |
7MZ6 | electron microscopy | 2.91 | A/B/C/D | 110-764 | [»] | |
7MZ7 | electron microscopy | 3.35 | A/B/C/D | 110-764 | [»] | |
7MZ9 | electron microscopy | 3.18 | A/B/C/D | 110-764 | [»] | |
7MZA | electron microscopy | 3.46 | A/B/C/D | 110-764 | [»] | |
7MZB | electron microscopy | 3.72 | A/B/C/D | 110-764 | [»] | |
7MZC | electron microscopy | 3.03 | A/B/C/D | 110-764 | [»] | |
7MZD | electron microscopy | 2.90 | A/B/C/D | 110-764 | [»] | |
7MZE | electron microscopy | 3.42 | A/B/C/D | 110-764 | [»] | |
SMRi | O35433 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 249845, 3 interactors |
DIPi | DIP-56949N |
IntActi | O35433, 3 interactors |
MINTi | O35433 |
STRINGi | 10116.ENSRNOP00000026493 |
Chemistry databases
BindingDBi | O35433 |
ChEMBLi | CHEMBL5102 |
DrugCentrali | O35433 |
GuidetoPHARMACOLOGYi | 507 |
Protein family/group databases
TCDBi | 1.A.4.2.1, the transient receptor potential ca(2+) channel (trp-cc) family |
PTM databases
GlyGeni | O35433, 1 site |
iPTMneti | O35433 |
PhosphoSitePlusi | O35433 |
Proteomic databases
PaxDbi | O35433 |
Protocols and materials databases
ABCDi | O35433, 2 sequenced antibodies |
Genome annotation databases
Ensembli | ENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486 [O35433-1] |
GeneIDi | 83810 |
KEGGi | rno:83810 |
Organism-specific databases
CTDi | 7442 |
RGDi | 628841, Trpv1 |
Phylogenomic databases
eggNOGi | KOG3676, Eukaryota |
GeneTreei | ENSGT00940000160870 |
HOGENOMi | CLU_012795_1_0_1 |
InParanoidi | O35433 |
OMAi | YLHQNMK |
OrthoDBi | 693004at2759 |
PhylomeDBi | O35433 |
TreeFami | TF314711 |
Enzyme and pathway databases
Reactomei | R-RNO-3295583, TRP channels |
Miscellaneous databases
EvolutionaryTracei | O35433 |
PROi | PR:O35433 |
Gene expression databases
Bgeei | ENSRNOG00000019486, Expressed in adult mammalian kidney and 19 other tissues |
Genevisiblei | O35433, RN |
Family and domain databases
Gene3Di | 1.25.40.20, 1 hit |
InterProi | View protein in InterPro IPR002110, Ankyrin_rpt IPR036770, Ankyrin_rpt-contain_sf IPR005821, Ion_trans_dom IPR024862, TRPV IPR024863, TRPV1 IPR008347, TRPV1-4_channel |
PANTHERi | PTHR10582, PTHR10582, 1 hit PTHR10582:SF17, PTHR10582:SF17, 1 hit |
Pfami | View protein in Pfam PF12796, Ank_2, 1 hit PF00520, Ion_trans, 1 hit |
PRINTSi | PR01768, TRPVRECEPTOR |
SMARTi | View protein in SMART SM00248, ANK, 4 hits |
SUPFAMi | SSF48403, SSF48403, 1 hit |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TRPV1_RAT | |
Accessioni | O35433Primary (citable) accession number: O35433 Secondary accession number(s): Q920B3 Q9JM57 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 10, 2005 |
Last sequence update: | January 1, 1998 | |
Last modified: | February 23, 2022 | |
This is version 182 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families