[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. TISSUE=Spinal ganglion; DOI=10.1038/39807; PubMed=9349813 [NCBI, ExPASy, EBI, Israel, Japan] Caterina M.J., Schumacher M.A., Tominaga M., Rosen T.A., Levine J.D., Julius D.; "The capsaicin receptor: a heat-activated ion channel in the pain pathway."; Nature 389:816-824(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND FUNCTION (ISOFORM 3). STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion, and Trigeminal ganglion; DOI=10.1074/jbc.275.4.2756; PubMed=10644739 [NCBI, ExPASy, EBI, Israel, Japan] Schumacher M.A., Moff I., Sudanagunta S.P., Levine J.D.; "Molecular cloning of an N-terminal splice variant of the capsaicin receptor. Loss of N-terminal domain suggests functional divergence among capsaicin receptor subtypes."; J. Biol. Chem. 275:2756-2762(2000).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). DOI=10.1016/S0304-3940(01)02185-1; PubMed=11578842 [NCBI, ExPASy, EBI, Israel, Japan] Tsutsumi S., Tomioka A., Sudo M., Nakamura A., Shirakura K., Takagishi K., Kohama K.; "Propofol activates vanilloid receptor channels expressed in human embryonic kidney 293 cells."; Neurosci. Lett. 312:45-49(2001).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-468, AND ALTERNATIVE SPLICING. STRAIN=Sprague-Dawley; DOI=10.1006/geno.2001.6582; PubMed=11549313 [NCBI, ExPASy, EBI, Israel, Japan] Xue Q., Yu Y., Trilk S.L., Jong B.E., Schumacher M.A.; "The genomic organization of the gene encoding the vanilloid receptor: evidence for multiple splice variants."; Genomics 76:14-20(2001).
[5]	CHARACTERIZATION OF CHANNEL PORE, AND MUTAGENESIS OF GLU-636; LYS-639; MET-644; ASP-646; GLU-648 AND GLU-651. DOI=10.1074/jbc.M002391200; PubMed=10931826 [NCBI, ExPASy, EBI, Israel, Japan] Garcia-Martinez C., Morenilla-Palao C., Planells-Cases R., Merino J.M., Ferrer-Montiel A.V.; "Identification of an aspartic residue in the P-loop of the vanilloid receptor that modulates pore properties."; J. Biol. Chem. 275:32552-32558(2000).
[6]	FUNCTION. DOI=10.1038/35050121; PubMed=11140687 [NCBI, ExPASy, EBI, Israel, Japan] Premkumar L.S., Ahern G.P.; "Induction of vanilloid receptor channel activity by protein kinase C."; Nature 408:985-990(2000).
[7]	SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-604. DOI=10.1046/j.1432-1033.2001.02500.x; PubMed=11683872 [NCBI, ExPASy, EBI, Israel, Japan] Jahnel R., Dreger M., Gillen C., Bender O., Kurreck J., Hucho F.; "Biochemical characterization of the vanilloid receptor 1 expressed in a dorsal root ganglia derived cell line."; Eur. J. Biochem. 268:5489-5496(2001).
[8]	FUNCTION, AND INTERACTION WITH PRKCG AND NTRK1. DOI=10.1038/35082088; PubMed=11418861 [NCBI, ExPASy, EBI, Israel, Japan] Chuang H.H., Prescott E.D., Kong H., Shields S., Jordt S.E., Basbaum A.I., Chao M.V., Julius D.; "Bradykinin and nerve growth factor release the capsaicin receptor from PtdIns(4,5)P2-mediated inhibition."; Nature 411:957-962(2001).
[9]	PHOSPHORYLATION AT SER-502 AND SER-800, AND MUTAGENESIS OF SER-502 AND SER-800. DOI=10.1074/jbc.C200104200; PubMed=11884385 [NCBI, ExPASy, EBI, Israel, Japan] Numazaki M., Tominaga T., Toyooka H., Tominaga M.; "Direct phosphorylation of capsaicin receptor VR1 by protein kinase Cepsilon and identification of two target serine residues."; J. Biol. Chem. 277:13375-13378(2002).
[10]	FUNCTION. DOI=10.1074/jbc.M201551200; PubMed=12095983 [NCBI, ExPASy, EBI, Israel, Japan] Olah Z., Karai L., Iadarola M.J.; "Protein kinase C(alpha) is required for vanilloid receptor 1 activation. Evidence for multiple signaling pathways."; J. Biol. Chem. 277:35752-35759(2002).
[11]	FUNCTION, AND PHOSPHORYLATION AT SER-116; THR-144; THR-370; SER-502; SER-774 AND SER-820. DOI=10.1016/S0896-6273(02)00802-4; PubMed=12194871 [NCBI, ExPASy, EBI, Israel, Japan] Bhave G., Zhu W., Wang H., Brasier D.J., Oxford G.S., Gereau R.W. IV; "cAMP-dependent protein kinase regulates desensitization of the capsaicin receptor (VR1) by direct phosphorylation."; Neuron 35:721-731(2002).
[12]	FUNCTION, AND INTERACTION WITH CALMODULIN. DOI=10.1073/pnas.1337252100; PubMed=12808128 [NCBI, ExPASy, EBI, Israel, Japan] Numazaki M., Tominaga T., Takeuchi K., Murayama N., Toyooka H., Tominaga M.; "Structural determinant of TRPV1 desensitization interacts with calmodulin."; Proc. Natl. Acad. Sci. U.S.A. 100:8002-8006(2003).
[13]	FUNCTION, AND MUTAGENESIS OF SER-502; THR-704 AND SER-800. DOI=10.1073/pnas.2032100100; PubMed=14523239 [NCBI, ExPASy, EBI, Israel, Japan] Bhave G., Hu H.J., Glauner K.S., Zhu W., Wang H., Brasier D.J., Oxford G.S., Gereau R.W. IV; "Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1)."; Proc. Natl. Acad. Sci. U.S.A. 100:12480-12485(2003).
[14]	FUNCTION, AND MUTAGENESIS OF ARG-785; LYS-788; ARG-797 AND SER-800. DOI=10.1126/science.1083646; PubMed=12764195 [NCBI, ExPASy, EBI, Israel, Japan] Prescott E.D., Julius D.; "A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity."; Science 300:1284-1288(2003).
[15]	INTERACTION WITH CSK. DOI=10.1152/ajpcell.00113.2004; PubMed=15084474 [NCBI, ExPASy, EBI, Israel, Japan] Jin X., Morsy N., Winston J., Pasricha P.J., Garrett K., Akbarali H.I.; "Modulation of TRPV1 by nonreceptor tyrosine kinase, c-Src kinase."; Am. J. Physiol. 287:C558-C563(2004).
[16]	MUTAGENESIS OF ARG-114; ARG-115 AND GLU-761. DOI=10.1074/jbc.M207103200; PubMed=12228246 [NCBI, ExPASy, EBI, Israel, Japan] Jung J., Lee S.Y., Hwang S.W., Cho H., Shin J., Kang Y.S., Kim S., Oh U.; "Agonist recognition sites in the cytosolic tails of vanilloid receptor 1."; J. Biol. Chem. 277:44448-44454(2002).
[17]	FUNCTION, PHOSPHORYLATION AT SER-502 AND THR-704, AND MUTAGENESIS OF SER-502 AND THR-704. DOI=10.1074/jbc.M311448200; PubMed=14630912 [NCBI, ExPASy, EBI, Israel, Japan] Jung J., Shin J.S., Lee S.-Y., Hwang S.W., Koo J., Cho H., Oh U.; "Phosphorylation of vanilloid receptor 1 by Ca2+/calmodulin-dependent kinase II regulates its vanilloid binding."; J. Biol. Chem. 279:7048-7054(2004).
[18]	MUTAGENESIS OF TYR-511; MET-547 AND THR-550. DOI=10.1074/jbc.M312577200; PubMed=14996838 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Molecular determinants of vanilloid sensitivity in TRPV1."; J. Biol. Chem. 279:20283-20295(2004).
[19]	FUNCTION. DOI=10.1074/jbc.M402966200; PubMed=15173182 [NCBI, ExPASy, EBI, Israel, Japan] Hellwig N., Plant T.D., Janson W., Schafer M., Schultz G., Schaefer M.; "TRPV1 acts as proton channel to induce acidification in nociceptive neurons."; J. Biol. Chem. 279:34553-34561(2004).
[20]	INTERACTION WITH PRKCM, PHOSPHORYLATION AT SER-116, AND MUTAGENESIS OF SER-116. DOI=10.1074/jbc.M410331200; PubMed=15471852 [NCBI, ExPASy, EBI, Israel, Japan] Wang Y., Kedei N., Wang M., Wang Q.J., Huppler A.R., Toth A., Tran R., Blumberg P.M.; "Interaction between protein kinase Cmu and the vanilloid receptor type 1."; J. Biol. Chem. 279:53674-53682(2004).
[21]	SUBUNIT. DOI=10.1523/JNEUROSCI.0202-04.2004; PubMed=15190102 [NCBI, ExPASy, EBI, Israel, Japan] Garcia-Sanz N., Fernandez-Carvajal A., Morenilla-Palao C., Planells-Cases R., Fajardo-Sanchez E., Fernandez-Ballester G., Ferrer-Montiel A.; "Identification of a tetramerization domain in the C-terminus of the vanilloid receptor."; J. Neurosci. 24:5307-5314(2004).
[22]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 101-364, ATP-BINDING, AND DOMAINS ANKYRIN REPEATS. DOI=10.1016/j.neuron.2007.05.027; PubMed=17582331 [NCBI, ExPASy, EBI, Israel, Japan] Lishko P.V., Procko E., Jin X., Phelps C.B., Gaudet R.; "The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity."; Neuron 54:905-918(2007).

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 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 endocannabinoids, like anandamide, and bradykinin.
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: 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.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	VR1L1
Isoform ID	O35433-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	VR1L2
Isoform ID	O35433-2
Features which should be applied to build the isoform sequence: VSP_013432.

Name	3
Synonyms	VR.5'sv
Isoform ID	O35433-3
Note: Inactive.
Features which should be applied to build the isoform sequence: VSP_013431, VSP_013432.

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.
DOMAIN: The association domain (AD) is necessary for self-association.
PTM: 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.
MISCELLANEOUS: Responses evoked by capsaicin, but not by low pH and heat, can be antagonized by capsazepine.
SIMILARITY: Belongs to the transient receptor family. TrpV subfamily.
SIMILARITY: Contains 6 ANK repeats.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF029310; AAC53398.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF158248; AAF28389.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB041029; BAA94306.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB040873; BAA94307.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF327067; AAK83151.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF327067; AAK83152.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00326014; -.
IPI00389268; -.
IPI00561075; -.

T09054; T09054.

NP_114188.1; -.

3D structure databases

PDB

2NYJ; X-ray; 3.20 A; A=101-364.	[ExPASy / RCSB / EBI]
2PNN; X-ray; 2.70 A; A=101-364.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2NYJ; -.
2PNN; -.

ModBase

O35433.

Protein family/group databases

TCDB

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

PTM databases

PhosphoSite

O35433; -.

Organism-specific databases

RGD

628841; Trpv1.

Gene expression databases

ArrayExpress

O35433; -.

GermOnline

ENSRNOG00000019486; Rattus norvegicus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005262;	Molecular function: calcium channel activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005516;	Molecular function: calmodulin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006816;	Biological process: calcium ion transport (inferred from electronic annotation from UniProtKB-KW).
GO:0009408;	Biological process: response to heat (inferred from direct assay from MGI).
GO:0009268;	Biological process: response to pH (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR002110; ANK.
IPR005821; Ion_trans.
IPR004729; TRP_channel.
IPR008347; Vanilpoid_rcpt.
Graphical view of domain structure.

Gene3D

G3DSA:1.25.40.20; ANK; 1.

Pfam

PF00023; Ank; 3.
PF00520; Ion_trans; 1.
Pfam graphical view of domain structure.

PRINTS

PR01768; TRPVRECEPTOR.

SMART

SM00248; ANK; 4.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00870; trp; 1.

PROSITE

PS50297; ANK_REP_REGION; 1.
PS50088; ANK_REPEAT; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000019486; Rattus norvegicus. [Contig view]

GeneID

83810; -.

KEGG

rno:83810; -.

Phylogenomic databases

HOVERGEN

O35433; -.

Other

616421; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; ANK repeat; ATP-binding; Calcium; Calcium channel; Calcium transport; Calmodulin-binding; Cell membrane; Glycoprotein; Ion transport; Ionic channel; Membrane; Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 838`	`838`	`Transient receptor potential cation channel subfamily V member 1.`	`PRO_0000215341`
`TOPO_DOM`	`1 432`	`432`	`Cytoplasmic (Potential).`
`TRANSMEM`	`433 453`	`21`	`Potential.`
`TOPO_DOM`	`454 476`	`23`	`Extracellular (Potential).`
`TRANSMEM`	`477 497`	`21`	`Potential.`
`TOPO_DOM`	`498 510`	`13`	`Cytoplasmic (Potential).`
`TRANSMEM`	`511 531`	`21`	`Potential.`
`TOPO_DOM`	`532 535`	`4`	`Extracellular (Potential).`
`TRANSMEM`	`536 556`	`21`	`Potential.`
`TOPO_DOM`	`557 579`	`23`	`Cytoplasmic (Potential).`
`TRANSMEM`	`580 600`	`21`	`Potential.`
`TOPO_DOM`	`601 658`	`58`	`Pore forming (Probable).`
`TRANSMEM`	`659 679`	`21`	`Potential.`
`TOPO_DOM`	`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.`
`MOD_RES`	`116 116`		`Phosphoserine; by PKA and PKD.`
`MOD_RES`	`144 144`		`Phosphothreonine; by PKA; in vitro.`
`MOD_RES`	`370 370`		`Phosphothreonine; by PKA; in vitro.`
`MOD_RES`	`502 502`		`Phosphoserine.`
`MOD_RES`	`704 704`		`Phosphothreonine.`
`MOD_RES`	`774 774`		`Phosphoserine; by PKA; in vitro.`
`MOD_RES`	`800 800`		`Phosphoserine; by PKC/PRKCZ; in vitro.`
`MOD_RES`	`820 820`		`Phosphoserine; by PKA; in vitro.`
`CARBOHYD`	`604 604`		`N-linked (GlcNAc...).`
`VAR_SEQ`	`1 307`		`Missing (in isoform 3).`	`VSP_013431`
`VAR_SEQ`	`348 407`		`Missing (in isoform 2 and isoform 3).`	`VSP_013432`
`MUTAGEN`	`114 114`		`R->E: Abolishes capsaicin-evoked current and binding to resiniferatoxin.`
`MUTAGEN`	`114 114`		`Missing: Abolishes sensitivity to acid.`
`MUTAGEN`	`115 115`		`R->D: Abolishes capsaicin-evoked current and binding to resiniferatoxin.`
`MUTAGEN`	`116 116`		`S->A: Abolishes phosphorylation by PKCM and enhances channel response to capsaicin by PKCM.`
`MUTAGEN`	`502 502`		`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.`
`MUTAGEN`	`511 511`		`Y->A: Loss of sensitivity to capsaicin.`
`MUTAGEN`	`547 547`		`M->L: Reduces binding to resiniferatoxin.`
`MUTAGEN`	`550 550`		`T->I: Reduces sensitivity to capsaicin 10-fold; no effect on sensitivity to resiniferatoxin. Reduces binding to resiniferatoxin.`
`MUTAGEN`	`636 636`		`E->K: Abolishes channel activity. Restored channel activity; when associated with E-639.`
`MUTAGEN`	`636 636`		`E->Q: Slight modification of pore attributes.`
`MUTAGEN`	`639 639`		`K->E: Restored channel activity; when associated with K-636.`
`MUTAGEN`	`644 644`		`M->Y: Slightly modifies channel permeability.`
`MUTAGEN`	`646 646`		`D->N: Strongly reduces the affinity for pore blocker ruthenium red and lowered channel permeability for Mg(2+).`
`MUTAGEN`	`648 648`		`E->Q: Minor modification of pore attributes.`
`MUTAGEN`	`651 651`		`E->Q: Minor modification of pore attributes.`
`MUTAGEN`	`704 704`		`T->A: No effect on PMA-induced enhancement of capsaicin-evoked currents but reduces direct activation by PMA.`
`MUTAGEN`	`704 704`		`T->I: Loss of activation by capsaicin and loss of vanilloid binding; when associated with A-502.`
`MUTAGEN`	`761 761`		`E->K,Q: Abolishes capsaiin-evoked current and binding to resiniferatoxin.`
`MUTAGEN`	`761 761`		`Missing: Abolishes sensitivity to acid.`
`MUTAGEN`	`785 785`		`R->Q: Abolishes PLC-mediated channel activity; when associated with Q-788.`
`MUTAGEN`	`788 788`		`K->Q: Abolishes PLC-mediated channel activity; when associated with Q-785 or Q-797.`
`MUTAGEN`	`797 797`		`R->Q: Abolishes PLC-mediated channel activity; when associated with Q-788.`
`MUTAGEN`	`800 800`		`S->A: Largely reduces direct activation of by PMA and PMA-induced currents; no effect on receptor kinase-induced currents.`
`CONFLICT`	`18 18`		`E -> D (in Ref. 3; BAA94307).`
`CONFLICT`	`36 36`		`V -> A (in Ref. 4; AAK83151).`
`CONFLICT`	`48 48`		`R -> G (in Ref. 3; BAA94306).`
`CONFLICT`	`51 51`		`G -> W (in Ref. 3; BAA94306).`
`CONFLICT`	`96 96`		`P -> Q (in Ref. 3; BAA94307).`
`CONFLICT`	`179 179`		`V -> I (in Ref. 4; AAK83151).`
`CONFLICT`	`735 735`		`K -> Q (in Ref. 3; BAA94306).`
`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`
`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`

Sequence information

Length: 838 AA [This is the length of the unprocessed precursor]

Molecular weight: 94948 Da [This is the MW of the unprocessed precursor]

CRC64: DAFC80B12BDF71BF [This is a checksum on the sequence]

        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

O35433 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools