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UniProtKB - O35433 (TRPV1_RAT)

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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.

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. 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

  • ATP binding Source: UniProtKB
  • 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
  • phosphoprotein binding Source: Ensembl
  • temperature-gated ion channel activity Source: Ensembl
  • transmembrane signaling receptor activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • behavioral response to pain Source: Ensembl
  • 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: 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 by RNA polymerase II 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
View the complete GO annotation on QuickGO ...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
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
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

Show more details

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • phosphoprotein binding Source: Ensembl
View the complete GO annotation on QuickGO ...

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
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
Turni360 – 362Combined sources3
Turni363 – 365Combined sources3
Beta strandi369 – 374Combined sources6
Beta strandi377 – 381Combined sources5
Beta strandi385 – 388Combined sources4
Turni390 – 392Combined sources3
Helixi395 – 400Combined sources6
Turni407 – 411Combined sources5
Helixi412 – 415Combined sources4
Helixi419 – 428Combined sources10
Helixi430 – 453Combined sources24
Beta strandi458 – 461Combined sources4
Helixi469 – 498Combined sources30
Helixi501 – 504Combined sources4
Turni506 – 508Combined sources3
Helixi511 – 531Combined sources21
Helixi537 – 550Combined sources14
Helixi551 – 554Combined sources4
Turni555 – 558Combined sources4
Turni560 – 563Combined sources4
Helixi564 – 574Combined sources11
Helixi576 – 580Combined sources5
Turni581 – 583Combined sources3
Helixi584 – 598Combined sources15
Beta strandi601 – 603Combined sources3
Beta strandi627 – 629Combined sources3
Helixi630 – 641Combined sources12
Beta strandi647 – 649Combined sources3
Helixi656 – 670Combined sources15
Turni671 – 673Combined sources3
Helixi674 – 691Combined sources18
Helixi693 – 712Combined sources20
Helixi716 – 719Combined sources4
Beta strandi732 – 734Combined sources3
Beta strandi743 – 746Combined sources4
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

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

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
IPR004729 TRP_channel
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
TIGRFAMsiTIGR00870 trp, 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

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: June 20, 2018
This is version 162 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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