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   24-JAN-2024, entry version 187.
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="https://atlasgeneticsoncology.org/gene/45817/TRPV2";
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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; 28.
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 ca2+/cation channel (trp-cc) family.
DR   GlyCosmos; Q9Y5S1; 1 site, No reported glycans.
DR   GlyGen; Q9Y5S1; 1 site.
DR   iPTMnet; Q9Y5S1; -.
DR   MetOSite; Q9Y5S1; -.
DR   PhosphoSitePlus; Q9Y5S1; -.
DR   BioMuta; TRPV2; -.
DR   DMDM; 62901477; -.
DR   EPD; Q9Y5S1; -.
DR   jPOST; Q9Y5S1; -.
DR   MassIVE; Q9Y5S1; -.
DR   MaxQB; Q9Y5S1; -.
DR   PaxDb; 9606-ENSP00000342222; -.
DR   PeptideAtlas; Q9Y5S1; -.
DR   ProteomicsDB; 86489; -.
DR   Pumba; Q9Y5S1; -.
DR   Antibodypedia; 13247; 345 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   AGR; HGNC:18082; -.
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; 1003028at2759; -.
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 1162 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 125 other cell types or tissues.
DR   ExpressionAtlas; Q9Y5S1; baseline and differential.
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:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
DR   GO; GO:0005261; F:monoatomic cation channel activity; IDA:MGI.
DR   GO; GO:0005216; F:monoatomic ion channel activity; TAS:ProtInc.
DR   GO; GO:0015075; F:monoatomic ion transmembrane transporter activity; TAS:ProtInc.
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:0009266; P:response to temperature stimulus; IDA:MGI.
DR   GO; GO:0007600; P:sensory perception; TAS:ProtInc.
DR   CDD; cd22197; TRPV2; 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   NCBIfam; TIGR00870; trp; 1.
DR   PANTHER; PTHR10582:SF5; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V MEMBER 2; 1.
DR   PANTHER; PTHR10582; TRANSIENT RECEPTOR POTENTIAL ION CHANNEL PROTEIN; 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; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   Genevisible; Q9Y5S1; HS.
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
//