TRPV2_HUMAN
ID TRPV2_HUMAN Reviewed; 764 AA.
AC Q9Y5S1; A6NML2; A8K0Z0; Q9Y670;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 2;
DE Short=TrpV2;
DE AltName: Full=Osm-9-like TRP channel 2;
DE Short=OTRPC2;
DE AltName: Full=Vanilloid receptor-like protein 1;
DE Short=VRL-1;
GN Name=TRPV2; Synonyms=VRL;
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], AND FUNCTION.
RC TISSUE=Lymphoblast;
RX PubMed=10201375; DOI=10.1038/18906;
RA Caterina M.J., Rosen T.A., Tominaga M., Brake A.J., Julius D.;
RT "A capsaicin-receptor homologue with a high threshold for noxious heat.";
RL Nature 398:436-441(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoblast;
RA Garcia R.L., Delmas P., Cesare P., England S., Liapi A., Wood J.N.;
RT "Cloning and functional expression of VRL, a vanilloid receptor-like
RT gene.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kelsell R.E.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 69-319, AND ANK REPEATS.
RX PubMed=16882997; DOI=10.1110/ps.062357206;
RA McCleverty C.J., Koesema E., Patapoutian A., Lesley S.A., Kreusch A.;
RT "Crystal structure of the human TRPV2 channel ankyrin repeat domain.";
RL Protein Sci. 15:2201-2206(2006).
CC -!- FUNCTION: Calcium-permeable, non-selective cation channel with an
CC outward rectification. Seems to be regulated, at least in part, by IGF-
CC I, PDGF and neuropeptide head activator. May transduce physical stimuli
CC in mast cells. Activated by temperatures higher than 52 degrees
CC Celsius; is not activated by vanilloids and acidic pH.
CC {ECO:0000269|PubMed:10201375}.
CC -!- SUBUNIT: Homotetramer (Probable). Interacts with a cAMP-dependent
CC protein kinase type II regulatory subunit (PRKAR2A or PRKAR2B) and
CC ACBD3. Interacts with SLC50A1; the interaction probably occurs
CC intracellularly and depends on TRPV2 N-glycosylation (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- INTERACTION:
CC Q9Y5S1; P0DTC2: S; Xeno; NbExp=2; IntAct=EBI-11721896, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Note=Translocates from the cytoplasm to
CC the plasma membrane upon ligand stimulation (By similarity). Identified
CC by mass spectrometry in melanosome fractions from stage I to stage IV.
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated by PKA. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV2 sub-subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TRPV2ID45817ch17p11.html";
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DR EMBL; AF129112; AAD26363.1; -; mRNA.
DR EMBL; AF103906; AAD41724.1; -; mRNA.
DR EMBL; AJ487963; CAD32310.1; -; mRNA.
DR EMBL; AK289705; BAF82394.1; -; mRNA.
DR EMBL; AC093484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471222; EAX04508.1; -; Genomic_DNA.
DR EMBL; BC018926; AAH18926.1; -; mRNA.
DR EMBL; BC051305; AAH51305.1; -; mRNA.
DR CCDS; CCDS32576.1; -.
DR RefSeq; NP_057197.2; NM_016113.4.
DR PDB; 2F37; X-ray; 1.70 A; A/B=69-319.
DR PDBsum; 2F37; -.
DR AlphaFoldDB; Q9Y5S1; -.
DR SMR; Q9Y5S1; -.
DR BioGRID; 119520; 9.
DR IntAct; Q9Y5S1; 29.
DR MINT; Q9Y5S1; -.
DR STRING; 9606.ENSP00000342222; -.
DR BindingDB; Q9Y5S1; -.
DR ChEMBL; CHEMBL5051; -.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB14050; Cannabidivarin.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB11755; Tetrahydrocannabivarin.
DR GuidetoPHARMACOLOGY; 508; -.
DR TCDB; 1.A.4.2.8; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; Q9Y5S1; 1 site.
DR iPTMnet; Q9Y5S1; -.
DR PhosphoSitePlus; Q9Y5S1; -.
DR BioMuta; TRPV2; -.
DR DMDM; 62901477; -.
DR EPD; Q9Y5S1; -.
DR jPOST; Q9Y5S1; -.
DR MassIVE; Q9Y5S1; -.
DR MaxQB; Q9Y5S1; -.
DR PaxDb; Q9Y5S1; -.
DR PeptideAtlas; Q9Y5S1; -.
DR PRIDE; Q9Y5S1; -.
DR ProteomicsDB; 86489; -.
DR Antibodypedia; 13247; 307 antibodies from 36 providers.
DR DNASU; 51393; -.
DR Ensembl; ENST00000338560.12; ENSP00000342222.7; ENSG00000187688.15.
DR GeneID; 51393; -.
DR KEGG; hsa:51393; -.
DR MANE-Select; ENST00000338560.12; ENSP00000342222.7; NM_016113.5; NP_057197.2.
DR UCSC; uc002gpy.3; human.
DR CTD; 51393; -.
DR DisGeNET; 51393; -.
DR GeneCards; TRPV2; -.
DR HGNC; HGNC:18082; TRPV2.
DR HPA; ENSG00000187688; Low tissue specificity.
DR MIM; 606676; gene.
DR neXtProt; NX_Q9Y5S1; -.
DR OpenTargets; ENSG00000187688; -.
DR PharmGKB; PA38292; -.
DR VEuPathDB; HostDB:ENSG00000187688; -.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000158512; -.
DR HOGENOM; CLU_012795_1_1_1; -.
DR InParanoid; Q9Y5S1; -.
DR OMA; TNACILP; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; Q9Y5S1; -.
DR TreeFam; TF314711; -.
DR PathwayCommons; Q9Y5S1; -.
DR Reactome; R-HSA-3295583; TRP channels.
DR SignaLink; Q9Y5S1; -.
DR BioGRID-ORCS; 51393; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; TRPV2; human.
DR EvolutionaryTrace; Q9Y5S1; -.
DR GeneWiki; TRPV2; -.
DR GenomeRNAi; 51393; -.
DR Pharos; Q9Y5S1; Tchem.
DR PRO; PR:Q9Y5S1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y5S1; protein.
DR Bgee; ENSG00000187688; Expressed in granulocyte and 123 other tissues.
DR ExpressionAtlas; Q9Y5S1; baseline and differential.
DR Genevisible; Q9Y5S1; HS.
DR GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0032584; C:growth cone membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005261; F:cation channel activity; IDA:MGI.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0015075; F:ion transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR GO; GO:0009266; P:response to temperature stimulus; IDA:MGI.
DR GO; GO:0007600; P:sensory perception; TAS:ProtInc.
DR Gene3D; 1.25.40.20; -; 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 InterPro; IPR024865; TrpV2.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR PANTHER; PTHR10582:SF5; PTHR10582:SF5; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01768; TRPVRECEPTOR.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Cytoplasm; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..764
FT /note="Transient receptor potential cation channel
FT subfamily V member 2"
FT /id="PRO_0000215342"
FT TOPO_DOM 1..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 572..609
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 72..114
FT /note="ANK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16882997"
FT REPEAT 115..161
FT /note="ANK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16882997"
FT REPEAT 162..207
FT /note="ANK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16882997"
FT REPEAT 208..243
FT /note="ANK 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16882997"
FT REPEAT 244..292
FT /note="ANK 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16882997"
FT REPEAT 293..319
FT /note="ANK 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16882997"
FT REGION 1..388
FT /note="Required for interaction with SLC50A1"
FT /evidence="ECO:0000250"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUD2"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTR1"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTR1"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 17
FT /note="G -> A (in dbSNP:rs3813768)"
FT /id="VAR_024678"
FT VARIANT 764
FT /note="N -> S (in dbSNP:rs8071215)"
FT /id="VAR_059838"
FT CONFLICT 52
FT /note="P -> S (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="A -> V (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="K -> N (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="V -> L (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT CONFLICT 465..466
FT /note="FI -> YT (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT CONFLICT 477..478
FT /note="QA -> HS (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="Q -> L (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="A -> V (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT CONFLICT 535..536
FT /note="LL -> MV (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="L -> V (in Ref. 2; AAD41724)"
FT /evidence="ECO:0000305"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2F37"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2F37"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 260..280
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:2F37"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:2F37"
SQ SEQUENCE 764 AA; 85981 MW; A73E3696E70F91E9 CRC64;
MTSPSSSPVF RLETLDGGQE DGSEADRGKL DFGSGLPPME SQFQGEDRKF APQIRVNLNY
RKGTGASQPD PNRFDRDRLF NAVSRGVPED LAGLPEYLSK TSKYLTDSEY TEGSTGKTCL
MKAVLNLKDG VNACILPLLQ IDRDSGNPQP LVNAQCTDDY YRGHSALHIA IEKRSLQCVK
LLVENGANVH ARACGRFFQK GQGTCFYFGE LPLSLAACTK QWDVVSYLLE NPHQPASLQA
TDSQGNTVLH ALVMISDNSA ENIALVTSMY DGLLQAGARL CPTVQLEDIR NLQDLTPLKL
AAKEGKIEIF RHILQREFSG LSHLSRKFTE WCYGPVRVSL YDLASVDSCE ENSVLEIIAF
HCKSPHRHRM VVLEPLNKLL QAKWDLLIPK FFLNFLCNLI YMFIFTAVAY HQPTLKKQAA
PHLKAEVGNS MLLTGHILIL LGGIYLLVGQ LWYFWRRHVF IWISFIDSYF EILFLFQALL
TVVSQVLCFL AIEWYLPLLV SALVLGWLNL LYYTRGFQHT GIYSVMIQKV ILRDLLRFLL
IYLVFLFGFA VALVSLSQEA WRPEAPTGPN ATESVQPMEG QEDEGNGAQY RGILEASLEL
FKFTIGMGEL AFQEQLHFRG MVLLLLLAYV LLTYILLLNM LIALMSETVN SVATDSWSIW
KLQKAISVLE MENGYWWCRK KQRAGVMLTV GTKPDGSPDE RWCFRVEEVN WASWEQTLPT
LCEDPSGAGV PRTLENPVLA SPPKEDEDGA SEENYVPVQL LQSN
