Reviewed, UniProtKB/Swiss-Prot O35433 (TRPV1_RAT)

Names and origin

Protein names

Recommended name:
    Transient receptor potential cation channel subfamily V member 1
      Short name=TrpV1
Alternative name(s):
    Osm-9-like TRP channel 1
      Short name=OTRPC1
    Vanilloid receptor 1
    Vanilloid receptor type 1-like
    Capsaicin receptor

Gene names

Name:	Trpv1
Synonyms:	Vr1, Vr1l

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	838 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 endocannabinoids, like anandamide, and bradykinin. Ref.1 Ref.2 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.19
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	Intewracts 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.
Subcellular location	Cell membrane; Multi-pass membrane protein. Ref.7
Tissue specificity	Predominantly expressed in trigeminal and dorsal root sensory ganglia. Isoform 1 and isoform 3 are also expressed in brain and peripheral blood mononuclear cells. Ref.1 Ref.2
Domain	The association domain (AD) is necessary for self-association. Ref.22
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 PKCM and probably PKCZ. Dephosphorylation by calcineurin seems to lead to receptor desensitization and phosphorylation by CAMKII recovers activity. Ref.11 Ref.17 Ref.9 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 family. TrpV subfamily. Contains 6 ANK repeats.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat Transmembrane
Ligand	ATP-binding Calcium Calmodulin-binding Nucleotide-binding
Molecular function	Calcium channel Ionic channel
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	calcium ion transport Inferred from electronic annotation. Source: UniProtKB-KW response to heat Inferred from direct assay. Source: MGI response to pH Inferred from direct assay. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium channel activity Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 838

838

Transient receptor potential cation channel subfamily V member 1

PRO_0000215341

Regions

Topological domain

1 – 432

432

Cytoplasmic Potential

Transmembrane

433 – 453

21

Potential

Topological domain

454 – 476

23

Extracellular Potential

Transmembrane

477 – 497

21

Potential

Topological domain

498 – 510

13

Cytoplasmic Potential

Transmembrane

511 – 531

21

Potential

Topological domain

532 – 535

4

Extracellular Potential

Transmembrane

536 – 556

21

Potential

Topological domain

557 – 579

23

Cytoplasmic Potential

Transmembrane

580 – 600

21

Potential

Topological domain

601 – 658

58

Pore forming Probable

Transmembrane

659 – 679

21

Potential

Topological domain

680 – 838

159

Cytoplasmic Potential

Repeat

110 – 152

43

ANK 1

Repeat

153 – 199

47

ANK 2

Repeat

200 – 246

47

ANK 3

Repeat

247 – 282

36

ANK 4

Repeat

283 – 331

49

ANK 5

Repeat

332 – 358

27

ANK 6

Region

684 – 712

29

AD

Region

767 – 801

35

Interaction with calmodulin

Region

777 – 792

16

Required for PIP2-mediated channel inhibition

Amino acid modifications

Modified residue

116

1

Phosphoserine; by PKA and PKD Ref.11 Ref.20

Modified residue

144

1

Phosphothreonine; by PKA; in vitro Ref.11

Modified residue

370

1

Phosphothreonine; by PKA; in vitro Ref.11

Modified residue

502

1

Phosphoserine Ref.11 Ref.17 Ref.9

Modified residue

704

1

Phosphothreonine Ref.17

Modified residue

774

1

Phosphoserine; by PKA; in vitro Ref.11

Modified residue

800

1

Phosphoserine; by PKC/PRKCZ; in vitro Ref.9

Modified residue

820

1

Phosphoserine; by PKA; in vitro Ref.11

Glycosylation

604

1

N-linked (GlcNAc...) Ref.7

Natural variations

Alternative sequence

1 – 307

307

Missing in isoform 3.

VSP_013431

Alternative sequence

348 – 407

60

Missing in isoform 2 and isoform 3.

VSP_013432

Experimental info

Mutagenesis

114

1

R → E: Abolishes capsaicin-evoked current and binding to resiniferatoxin. Ref.16

Mutagenesis

114

1

Missing: Abolishes sensitivity to acid. Ref.16

Mutagenesis

115

1

R → D: Abolishes capsaicin-evoked current and binding to resiniferatoxin. Ref.16

Mutagenesis

116

1

S → A: Abolishes phosphorylation by PKCM and enhances channel response to capsaicin by PKCM. Ref.20

Mutagenesis

502

1

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. Ref.13 Ref.17 Ref.9

Mutagenesis

511

1

Y → A: Loss of sensitivity to capsaicin. Ref.18

Mutagenesis

547

1

M → L: Reduces binding to resiniferatoxin. Ref.18

Mutagenesis

550

1

T → I: Reduces sensitivity to capsaicin 10-fold; no effect on sensitivity to resiniferatoxin. Reduces binding to resiniferatoxin. Ref.18

Mutagenesis

636

1

E → K: Abolishes channel activity. Restored channel activity; when associated with E-639. Ref.5

Mutagenesis

636

1

E → Q: Slight modification of pore attributes. Ref.5

Mutagenesis

639

1

K → E: Restored channel activity; when associated with K-636. Ref.5

Mutagenesis

644

1

M → Y: Slightly modifies channel permeability. Ref.5

Mutagenesis

646

1

D → N: Strongly reduces the affinity for pore blocker ruthenium red and lowered channel permeability for Mg(2+). Ref.5

Mutagenesis

648

1

E → Q: Minor modification of pore attributes. Ref.5

Mutagenesis

651

1

E → Q: Minor modification of pore attributes. Ref.5

Mutagenesis

704

1

T → A: No effect on PMA-induced enhancement of capsaicin-evoked currents but reduces direct activation by PMA. Ref.13 Ref.17

Mutagenesis

704

1

T → I: Loss of activation by capsaicin and loss of vanilloid binding; when associated with A-502. Ref.13 Ref.17

Mutagenesis

761

1

E → K or Q: Abolishes capsaiin-evoked current and binding to resiniferatoxin. Ref.16

Mutagenesis

761

1

Missing: Abolishes sensitivity to acid. Ref.16

Mutagenesis

785

1

R → Q: Abolishes PLC-mediated channel activity; when associated with Q-788. Ref.14

Mutagenesis

788

1

K → Q: Abolishes PLC-mediated channel activity; when associated with Q-785 or Q-797. Ref.14

Mutagenesis

797

1

R → Q: Abolishes PLC-mediated channel activity; when associated with Q-788. Ref.14

Mutagenesis

800

1

S → A: Largely reduces direct activation of by PMA and PMA-induced currents; no effect on receptor kinase-induced currents. Ref.13 Ref.14 Ref.9

Sequence conflict

18

1

E → D in BAA94307. Ref.3

Sequence conflict

36

1

V → A in AAK83151. Ref.4

Sequence conflict

48

1

R → G in BAA94306. Ref.3

Sequence conflict

51

1

G → W in BAA94306. Ref.3

Sequence conflict

96

1

P → Q in BAA94307. Ref.3

Sequence conflict

179

1

V → I in AAK83151. Ref.4

Sequence conflict

735

1

K → Q in BAA94306. Ref.3

Secondary structure

1

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838

Helix Strand Turn

Details...

Helix

114 – 123

10

Turn

127 – 131

5

Helix

132 – 139

8

Helix

146 – 148

3

Turn

151 – 153

3

Helix

157 – 163

7

Helix

171 – 181

11

Turn

182 – 184

3

Helix

187 – 190

4

Beta strand

196 – 199

4

Helix

204 – 210

7

Helix

214 – 221

8

Turn

222 – 224

3

Helix

234 – 236

3

Helix

251 – 257

7

Helix

261 – 268

8

Helix

287 – 292

6

Helix

299 – 318

20

Helix

325 – 327

3

Helix

336 – 343

8

Helix

346 – 355

10

Turn

356 – 358

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (VR1L1) [UniParc]. Last modified January 1, 1998. Version 1. Checksum: DAFC80B12BDF71BF	FASTA	838	94,948
	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
	Isoform 2 (VR1L2). Checksum: AB7BC5F1721C9010	FASTA	778	88,050
	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 ASSGKIGNRH DMLLVEPLNR 370 380 390 400 410 420 LLQDKWDRFV KRIFYFNFFV YCLYMIIFTA AAYYRPVEGL PPYKLKNTVG DYFRVTGEIL 430 440 450 460 470 480 SVSGGVYFFF RGIQYFLQRR PSLKSLFVDS YSEILFFVQS LFMLVSVVLY FSQRKEYVAS 490 500 510 520 530 540 MVFSLAMGWT NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYLVFLFG FSTAVVTLIE 550 560 570 580 590 600 DGKNNSLPME STPHKCRGSA CKPGNSYNSL YSTCLELFKF TIGMGDLEFT ENYDFKAVFI 610 620 630 640 650 660 ILLLAYVILT YILLLNMLIA LMGETVNKIA QESKNIWKLQ RAITILDTEK SFLKCMRKAF 670 680 690 700 710 720 RSGKLLQVGF TPDGKDDYRW CFRVDEVNWT TWNTNVGIIN EDPGNCEGVK RTLSFSLRSG 730 740 750 760 770 RVSGRNWKNF ALVPLLRDAS TRDRHATQQE EVQLKHYTGS LKPEDAEVFK DSMVPGEK
	Isoform 3 (VR.5'sv). Checksum: DFD8082CA26CA3C6	FASTA	471	54,420
	10 20 30 40 50 60 MYNEILILGA KLHPTLKLEE ITNRKGLTPL ALAASSGKIG NRHDMLLVEP LNRLLQDKWD 70 80 90 100 110 120 RFVKRIFYFN FFVYCLYMII FTAAAYYRPV EGLPPYKLKN TVGDYFRVTG EILSVSGGVY 130 140 150 160 170 180 FFFRGIQYFL QRRPSLKSLF VDSYSEILFF VQSLFMLVSV VLYFSQRKEY VASMVFSLAM 190 200 210 220 230 240 GWTNMLYYTR GFQQMGIYAV MIEKMILRDL CRFMFVYLVF LFGFSTAVVT LIEDGKNNSL 250 260 270 280 290 300 PMESTPHKCR GSACKPGNSY NSLYSTCLEL FKFTIGMGDL EFTENYDFKA VFIILLLAYV 310 320 330 340 350 360 ILTYILLLNM LIALMGETVN KIAQESKNIW KLQRAITILD TEKSFLKCMR KAFRSGKLLQ 370 380 390 400 410 420 VGFTPDGKDD YRWCFRVDEV NWTTWNTNVG IINEDPGNCE GVKRTLSFSL RSGRVSGRNW 430 440 450 460 470 KNFALVPLLR DASTRDRHAT QQEEVQLKHY TGSLKPEDAE VFKDSMVPGE K

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]	"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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00326014.
IPI00389268.
IPI00561075.

PIR

T09054.

RefSeq

NP_114188.1.

UniGene

Rn.3073

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NYJ	X-ray	3.20	A	101-364	[»]
2PNN	X-ray	2.70	A	101-364	[»]

ModBase

Search...

Protein family/group databases

TCDB

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

PTM databases

PhosphoSite

O35433.

Genome annotation databases

Ensembl

ENSRNOG00000019486. Rattus norvegicus. [Contig view]

GeneID

83810.

KEGG

rno:83810.

Organism-specific databases

RGD

628841. Trpv1.

Phylogenomic databases

HOVERGEN

O35433.

Gene expression databases

ArrayExpress

O35433.

GermOnline

ENSRNOG00000019486. Rattus norvegicus.

Family and domain databases

InterPro

IPR002110. ANK.
IPR005821. Ion_trans.
IPR004729. TRP_channel.
IPR008347. Vanilpoid_rcpt.
[Graphical view]

Gene3D

G3DSA:1.25.40.20. ANK. 1 hit.

Pfam

PF00023. Ank. 3 hits.
PF00520. Ion_trans. 1 hit.
[Graphical view]

PRINTS

PR01768. TRPVRECEPTOR.

SMART

SM00248. ANK. 4 hits.
[Graphical view]

TIGRFAMs

TIGR00870. trp. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

616421.

Entry information

Entry name

TRPV1_RAT

Accession

Primary (citable) accession number: O35433
Secondary accession number(s): Q920B3 , Q920B4, Q9JLM0, Q9JM56, Q9JM57

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)