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";
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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 Genevisible; Q8NET8; HS.
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.
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
//
