ID TRPV3_HUMAN Reviewed; 790 AA. AC Q8NET8; Q8NDW7; Q8NET9; Q8NFH2; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 27-MAR-2024, entry version 166. DE RecName: Full=Transient receptor potential cation channel subfamily V member 3; DE Short=TrpV3; DE AltName: Full=Vanilloid receptor-like 3; DE Short=VRL-3; GN Name=TRPV3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, RP INTERACTION WITH TRPV1, AND VARIANTS VAL-25 AND GLY-117. RX PubMed=12077606; DOI=10.1038/nature00894; RA Smith G.D., Gunthorpe M.J., Kelsell R.E., Hayes P.D., Reilly P., Facer P., RA Wright J.E., Jerman J.C., Walhin J.-P., Ooi L., Egerton J., Charles K.J., RA Smart D., Randall A.D., Anand P., Davis J.B.; RT "TRPV3 is a temperature-sensitive vanilloid receptor-like protein."; RL Nature 418:186-190(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=12077604; DOI=10.1038/nature00882; RA Xu H., Ramsey I.S., Kotecha S.A., Moran M.M., Chong J.A., Lawson D., Ge P., RA Lilly J., Silos-Santiago I., Xie Y., DiStefano P.S., Curtis R., RA Clapham D.E.; RT "TRPV3 is a calcium-permeable temperature-sensitive cation channel."; RL Nature 418:181-186(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). RA Poea-Guyon S., Renard S., Chalon P., Kaghad M., Caput D., Besnard F.; RT "Human TRPV3, a new member of the vanilloid receptor family."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION AS NEGATIVE REGULATOR OF HAIR GROWTH, AND TISSUE SPECIFICITY. RX PubMed=21593771; DOI=10.1038/jid.2011.122; RA Borbiro I., Lisztes E., Toth B.I., Czifra G., Olah A., Szollosi A.G., RA Szentandrassy N., Nanasi P.P., Peter Z., Paus R., Kovacs L., Biro T.; RT "Activation of transient receptor potential vanilloid-3 inhibits human hair RT growth."; RL J. Invest. Dermatol. 131:1605-1614(2011). RN [5] RP INVOLVEMENT IN FNEPPK2, VARIANT FNEPPK2 PRO-580, AND CHARACTERIZATION OF RP VARIANT FNEPPK2 PRO-580. RX PubMed=25285920; DOI=10.1038/jid.2014.429; RA He Y., Zeng K., Zhang X., Chen Q., Wu J., Li H., Zhou Y., Glusman G., RA Roach J., Etheridge A., Qing S., Tian Q., Lee I., Tian X., Wang X., Wu Z., RA Hood L., Ding Y., Wang K.; RT "A gain-of-function mutation in TRPV3 causes focal palmoplantar keratoderma RT in a Chinese family."; RL J. Invest. Dermatol. 135:907-909(2015). RN [6] RP VARIANTS OLMS1 SER-573; CYS-573 AND GLY-692, AND CHARACTERIZATION OF RP VARIANTS OLMS1 SER-573; CYS-573 AND GLY-692. RX PubMed=22405088; DOI=10.1016/j.ajhg.2012.02.006; RA Lin Z., Chen Q., Lee M., Cao X., Zhang J., Ma D., Chen L., Hu X., Wang H., RA Wang X., Zhang P., Liu X., Guan L., Tang Y., Yang H., Tu P., Bu D., Zhu X., RA Wang K., Li R., Yang Y.; RT "Exome sequencing reveals mutations in TRPV3 as a cause of Olmsted RT syndrome."; RL Am. J. Hum. Genet. 90:558-564(2012). RN [7] RP VARIANT OLMS1 SER-573. RX PubMed=22835024; DOI=10.1111/j.1365-2133.2012.11115.x; RA Lai-Cheong J.E., Sethuraman G., Ramam M., Stone K., Simpson M.A., RA McGrath J.A.; RT "Recurrent heterozygous missense mutation, p.Gly573Ser, in the TRPV3 gene RT in an Indian boy with sporadic Olmsted syndrome."; RL Br. J. Dermatol. 167:440-442(2012). CC -!- FUNCTION: Putative receptor-activated non-selective calcium permeant CC cation channel. It is activated by innocuous (warm) temperatures and CC shows an increased response at noxious temperatures greater than 39 CC degrees Celsius. Activation exhibits an outward rectification. May CC associate with TRPV1 and may modulate its activity. Is a negative CC regulator of hair growth and cycling: TRPV3-coupled signaling CC suppresses keratinocyte proliferation in hair follicles and induces CC apoptosis and premature hair follicle regression (catagen). CC {ECO:0000269|PubMed:12077604, ECO:0000269|PubMed:12077606, CC ECO:0000269|PubMed:21593771}. CC -!- SUBUNIT: May form a heteromeric channel with TRPV1. Interacts with CC TRPV1. {ECO:0000269|PubMed:12077606}. CC -!- INTERACTION: CC Q8NET8-1; Q8NET8-1: TRPV3; NbExp=2; IntAct=EBI-26518537, EBI-26518537; CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8NET8-1; Sequence=Displayed; CC Name=2; Synonyms=A; CC IsoId=Q8NET8-2; Sequence=VSP_013433; CC Name=3; Synonyms=B; CC IsoId=Q8NET8-3; Sequence=VSP_013434, VSP_013435; CC -!- TISSUE SPECIFICITY: Abundantly expressed in CNS. Widely expressed at CC low levels. Detected in dorsal root ganglion (at protein level). CC Expressed in the keratinocyte layers of the outer root sheath and, to CC lesser extent, to the matrix of the hair follicles (at protein level). CC {ECO:0000269|PubMed:12077604, ECO:0000269|PubMed:12077606, CC ECO:0000269|PubMed:21593771}. CC -!- DISEASE: Olmsted syndrome 1 (OLMS1) [MIM:614594]: An autosomal CC dominant, rare congenital disorder characterized by bilateral CC mutilating palmoplantar keratoderma and periorificial keratotic plaques CC with severe itching at all lesions. Diffuse alopecia, constriction of CC digits, and onychodystrophy have also been reported. Infections and CC squamous cell carcinomas can arise on the keratotic areas. The digital CC constriction may progress to autoamputation of fingers and toes. CC {ECO:0000269|PubMed:22405088, ECO:0000269|PubMed:22835024}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Palmoplantar keratoderma, non-epidermolytic, focal 2 (FNEPPK2) CC [MIM:616400]: A dermatological disorder characterized by non- CC epidermolytic, abnormal thickening of the skin on the palms and soles. CC Focal palmoplantar keratoderma consists of localized areas of CC hyperkeratosis located mainly on pressure points and sites of recurrent CC friction. {ECO:0000269|PubMed:25285920}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV CC subfamily. TRPV3 sub-subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Transient receptor potential cation channel, CC subfamily V, member 3 (TRPV3); Note=Leiden Open Variation Database CC (LOVD); CC URL="https://databases.lovd.nl/shared/genes/TRPV3"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ487035; CAD31711.2; -; mRNA. DR EMBL; AF514998; AAM54027.1; -; mRNA. DR EMBL; AY118267; AAM80558.1; -; mRNA. DR EMBL; AY118268; AAM80559.1; -; mRNA. DR CCDS; CCDS11029.1; -. [Q8NET8-1] DR CCDS; CCDS58500.1; -. [Q8NET8-2] DR RefSeq; NP_659505.1; NM_145068.3. [Q8NET8-1] DR PDB; 6H9J; X-ray; 1.83 A; D=229-250. DR PDB; 6HA6; X-ray; 1.98 A; D=220-246. DR PDB; 6MHO; EM; 3.40 A; A/B/C/D=2-790. DR PDB; 6MHS; EM; 3.20 A; A/B/C/D=2-790. DR PDB; 6MHV; EM; 3.50 A; A/B/C/D=2-790. DR PDB; 6MHW; EM; 4.00 A; A/B/C/D=2-790. DR PDB; 6MHX; EM; 4.00 A; A/B/C/D=2-790. DR PDB; 6OT2; EM; 4.10 A; A/B/C/D=96-790. DR PDB; 6OT5; EM; 3.60 A; A/B/C/D=110-790. DR PDB; 6UW4; EM; 3.10 A; A/B/C/D=1-790. DR PDB; 6UW6; EM; 3.66 A; A/B/C/D=1-790. DR PDB; 6UW8; EM; 4.02 A; A/B/C/D=1-790. DR PDB; 6UW9; EM; 4.33 A; A/B/C/D=1-790. DR PDB; 7QQN; X-ray; 2.45 A; B/D=781-790. DR PDB; 7XJ0; EM; 2.53 A; A/B/C/D=1-790. DR PDB; 7XJ1; EM; 2.93 A; A/B/C/D=1-790. DR PDB; 7XJ2; EM; 3.64 A; A/B/C/D=1-790. DR PDB; 7XJ3; EM; 3.54 A; A/B/C/D=1-790. DR PDB; 8GKA; EM; 2.55 A; A/B/C/D=1-790. DR PDB; 8GKG; EM; 4.38 A; A/B/C/D/E=1-790. DR PDBsum; 6H9J; -. DR PDBsum; 6HA6; -. DR PDBsum; 6MHO; -. DR PDBsum; 6MHS; -. DR PDBsum; 6MHV; -. DR PDBsum; 6MHW; -. DR PDBsum; 6MHX; -. DR PDBsum; 6OT2; -. DR PDBsum; 6OT5; -. DR PDBsum; 6UW4; -. DR PDBsum; 6UW6; -. DR PDBsum; 6UW8; -. DR PDBsum; 6UW9; -. DR PDBsum; 7QQN; -. DR PDBsum; 7XJ0; -. DR PDBsum; 7XJ1; -. DR PDBsum; 7XJ2; -. DR PDBsum; 7XJ3; -. DR PDBsum; 8GKA; -. DR PDBsum; 8GKG; -. DR AlphaFoldDB; Q8NET8; -. DR EMDB; EMD-20192; -. DR EMDB; EMD-20194; -. DR EMDB; EMD-20917; -. DR EMDB; EMD-20918; -. DR EMDB; EMD-20919; -. DR EMDB; EMD-20920; -. DR EMDB; EMD-40181; -. DR EMDB; EMD-40183; -. DR EMDB; EMD-9115; -. DR EMDB; EMD-9117; -. DR EMDB; EMD-9119; -. DR EMDB; EMD-9120; -. DR EMDB; EMD-9121; -. DR SMR; Q8NET8; -. DR BioGRID; 127821; 7. DR STRING; 9606.ENSP00000301365; -. DR BindingDB; Q8NET8; -. DR ChEMBL; CHEMBL5522; -. DR DrugBank; DB11345; (S)-camphor. DR DrugBank; DB01744; Camphor. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB09086; Eugenol. DR DrugBank; DB00825; Levomenthol. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB14011; Nabiximols. DR GuidetoPHARMACOLOGY; 509; -. DR TCDB; 1.A.4.2.9; the transient receptor potential ca2+/cation channel (trp-cc) family. DR iPTMnet; Q8NET8; -. DR PhosphoSitePlus; Q8NET8; -. DR BioMuta; TRPV3; -. DR DMDM; 62901456; -. DR jPOST; Q8NET8; -. DR MassIVE; Q8NET8; -. DR PaxDb; 9606-ENSP00000301365; -. DR PeptideAtlas; Q8NET8; -. DR ABCD; Q8NET8; 2 sequenced antibodies. DR Antibodypedia; 23030; 465 antibodies from 33 providers. DR DNASU; 162514; -. DR Ensembl; ENST00000301365.8; ENSP00000301365.4; ENSG00000167723.15. [Q8NET8-2] DR Ensembl; ENST00000572519.1; ENSP00000460215.1; ENSG00000167723.15. [Q8NET8-3] DR Ensembl; ENST00000576742.6; ENSP00000461518.2; ENSG00000167723.15. [Q8NET8-1] DR GeneID; 162514; -. DR KEGG; hsa:162514; -. DR MANE-Select; ENST00000576742.6; ENSP00000461518.2; NM_145068.4; NP_659505.1. DR UCSC; uc002fvr.4; human. [Q8NET8-1] DR AGR; HGNC:18084; -. DR CTD; 162514; -. DR DisGeNET; 162514; -. DR GeneCards; TRPV3; -. DR HGNC; HGNC:18084; TRPV3. DR HPA; ENSG00000167723; Group enriched (intestine, skeletal muscle, skin). DR MalaCards; TRPV3; -. DR MIM; 607066; gene. DR MIM; 614594; phenotype. DR MIM; 616400; phenotype. DR neXtProt; NX_Q8NET8; -. DR OpenTargets; ENSG00000167723; -. DR Orphanet; 448264; Isolated focal non-epidermolytic palmoplantar keratoderma. DR Orphanet; 659; Mutilating palmoplantar keratoderma with periorificial keratotic plaques. DR PharmGKB; PA38481; -. DR VEuPathDB; HostDB:ENSG00000167723; -. DR eggNOG; KOG3676; Eukaryota. DR GeneTree; ENSGT00940000158281; -. DR HOGENOM; CLU_012795_0_0_1; -. DR InParanoid; Q8NET8; -. DR OMA; GNCEDMD; -. DR OrthoDB; 1003028at2759; -. DR PhylomeDB; Q8NET8; -. DR TreeFam; TF314711; -. DR PathwayCommons; Q8NET8; -. DR Reactome; R-HSA-3295583; TRP channels. DR SIGNOR; Q8NET8; -. DR BioGRID-ORCS; 162514; 108 hits in 1161 CRISPR screens. DR ChiTaRS; TRPV3; human. DR GeneWiki; TRPV3; -. DR GenomeRNAi; 162514; -. DR Pharos; Q8NET8; Tchem. DR PRO; PR:Q8NET8; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q8NET8; Protein. DR Bgee; ENSG00000167723; Expressed in skin of leg and 91 other cell types or tissues. DR ExpressionAtlas; Q8NET8; baseline and differential. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0005262; F:calcium channel activity; TAS:Reactome. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome. DR GO; GO:0042636; P:negative regulation of hair cycle; IMP:UniProtKB. DR GO; GO:0090280; P:positive regulation of calcium ion import; IEA:Ensembl. DR GO; GO:0009266; P:response to temperature stimulus; IEA:Ensembl. DR CDD; cd22194; TRPV3; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR024862; TRPV. DR InterPro; IPR008347; TrpV1-4. DR PANTHER; PTHR10582:SF6; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V MEMBER 3; 1. DR PANTHER; PTHR10582; TRANSIENT RECEPTOR POTENTIAL ION CHANNEL PROTEIN; 1. DR Pfam; PF00023; Ank; 2. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF00520; Ion_trans; 1. DR PRINTS; PR01768; TRPVRECEPTOR. DR SMART; SM00248; ANK; 4. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 2. DR Genevisible; Q8NET8; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ANK repeat; Calcium; Calcium channel; KW Calcium transport; Disease variant; Ion channel; Ion transport; Membrane; KW Palmoplantar keratoderma; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..790 FT /note="Transient receptor potential cation channel FT subfamily V member 3" FT /id="PRO_0000215345" FT TOPO_DOM 1..439 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 440..460 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 461..487 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 488..508 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 509..523 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 524..544 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 545 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 546..566 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 567..589 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 590..610 FT /note="Helical" FT /evidence="ECO:0000255" FT INTRAMEM 621..637 FT /note="Pore-forming" FT /evidence="ECO:0000255" FT TRANSMEM 650..670 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 671..790 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 214..243 FT /note="ANK 1" FT REPEAT 261..291 FT /note="ANK 2" FT REPEAT 340..369 FT /note="ANK 3" FT REGION 15..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 52..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 76..112 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 76..107 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 759 FT /note="T -> TA (in isoform 2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_013433" FT VAR_SEQ 760..765 FT /note="DFNKIQ -> GTVAVR (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_013434" FT VAR_SEQ 766..790 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_013435" FT VARIANT 25 FT /note="I -> V (in dbSNP:rs322965)" FT /evidence="ECO:0000269|PubMed:12077606" FT /id="VAR_052388" FT VARIANT 117 FT /note="R -> G (in dbSNP:rs322937)" FT /evidence="ECO:0000269|PubMed:12077606" FT /id="VAR_052389" FT VARIANT 573 FT /note="G -> C (in OLMS1; gain of function mutation; results FT in constitutive channel activation; dbSNP:rs199473704)" FT /evidence="ECO:0000269|PubMed:22405088" FT /id="VAR_067920" FT VARIANT 573 FT /note="G -> S (in OLMS1; gain of function mutation; results FT in constitutive channel activation; dbSNP:rs199473704)" FT /evidence="ECO:0000269|PubMed:22405088, FT ECO:0000269|PubMed:22835024" FT /id="VAR_067921" FT VARIANT 580 FT /note="Q -> P (in FNEPPK2; gain of function mutation; FT dbSNP:rs786205869)" FT /evidence="ECO:0000269|PubMed:25285920" FT /id="VAR_073832" FT VARIANT 692 FT /note="W -> G (in OLMS1; gain of function mutation; results FT in constitutive channel activation; dbSNP:rs199473705)" FT /evidence="ECO:0000269|PubMed:22405088" FT /id="VAR_067922" FT VARIANT 774 FT /note="T -> I (in dbSNP:rs7212634)" FT /id="VAR_052390" FT CONFLICT 283 FT /note="E -> G (in Ref. 3; AAM80558/AAM80559)" FT /evidence="ECO:0000305" FT HELIX 119..129 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 133..147 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 155..161 FT /evidence="ECO:0007829|PDB:7XJ0" FT TURN 165..168 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 171..177 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 183..196 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 200..204 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 210..213 FT /evidence="ECO:0007829|PDB:7XJ1" FT HELIX 218..224 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 230..235 FT /evidence="ECO:0007829|PDB:6H9J" FT TURN 236..238 FT /evidence="ECO:0007829|PDB:6UW4" FT TURN 248..250 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 253..257 FT /evidence="ECO:0007829|PDB:8GKA" FT HELIX 265..271 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 275..282 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:7XJ1" FT HELIX 299..306 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 310..313 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 332..335 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 344..350 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 354..361 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:8GKA" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:7XJ1" FT STRAND 375..382 FT /evidence="ECO:0007829|PDB:8GKA" FT STRAND 383..391 FT /evidence="ECO:0007829|PDB:7XJ0" FT TURN 393..395 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 396..399 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 403..408 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:7XJ1" FT HELIX 416..419 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 423..435 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 437..460 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 482..506 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 513..519 FT /evidence="ECO:0007829|PDB:8GKA" FT HELIX 521..541 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 547..561 FT /evidence="ECO:0007829|PDB:7XJ0" FT TURN 562..564 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 565..568 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 570..585 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 587..607 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 609..611 FT /evidence="ECO:0007829|PDB:6MHO" FT TURN 617..619 FT /evidence="ECO:0007829|PDB:6MHS" FT STRAND 621..624 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 625..637 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 648..650 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 651..666 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 669..684 FT /evidence="ECO:0007829|PDB:7XJ0" FT TURN 685..687 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 688..706 FT /evidence="ECO:0007829|PDB:7XJ0" FT HELIX 709..715 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 719..723 FT /evidence="ECO:0007829|PDB:8GKA" FT STRAND 724..726 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 729..737 FT /evidence="ECO:0007829|PDB:7XJ0" FT STRAND 787..789 FT /evidence="ECO:0007829|PDB:7QQN" SQ SEQUENCE 790 AA; 90636 MW; 31EB9973C015B611 CRC64; MKAHPKEMVP LMGKRVAAPS GNPAILPEKR PAEITPTKKS AHFFLEIEGF EPNPTVAKTS PPVFSKPMDS NIRQCISGNC DDMDSPQSPQ DDVTETPSNP NSPSAQLAKE EQRRKKRRLK KRIFAAVSEG CVEELVELLV ELQELCRRRH DEDVPDFLMH KLTASDTGKT CLMKALLNIN PNTKEIVRIL LAFAEENDIL GRFINAEYTE EAYEGQTALN IAIERRQGDI AALLIAAGAD VNAHAKGAFF NPKYQHEGFY FGETPLALAA CTNQPEIVQL LMEHEQTDIT SRDSRGNNIL HALVTVAEDF KTQNDFVKRM YDMILLRSGN WELETTRNND GLTPLQLAAK MGKAEILKYI LSREIKEKRL RSLSRKFTDW AYGPVSSSLY DLTNVDTTTD NSVLEITVYN TNIDNRHEML TLEPLHTLLH MKWKKFAKHM FFLSFCFYFF YNITLTLVSY YRPREEEAIP HPLALTHKMG WLQLLGRMFV LIWAMCISVK EGIAIFLLRP SDLQSILSDA WFHFVFFIQA VLVILSVFLY LFAYKEYLAC LVLAMALGWA NMLYYTRGFQ SMGMYSVMIQ KVILHDVLKF LFVYIVFLLG FGVALASLIE KCPKDNKDCS SYGSFSDAVL ELFKLTIGLG DLNIQQNSKY PILFLFLLIT YVILTFVLLL NMLIALMGET VENVSKESER IWRLQRARTI LEFEKMLPEW LRSRFRMGEL CKVAEDDFRL CLRINEVKWT EWKTHVSFLN EDPGPVRRTD FNKIQDSSRN NSKTTLNAFE EVEEFPETSV //