ID TRPV2_MOUSE Reviewed; 756 AA. AC Q9WTR1; Q99K71; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 24-JAN-2024, entry version 173. DE RecName: Full=Transient receptor potential cation channel subfamily V member 2; DE Short=TrpV2; DE AltName: Full=Growth factor-regulated calcium channel; DE Short=GRC; DE AltName: Full=Osm-9-like TRP channel 2; DE Short=OTRPC2; GN Name=Trpv2; Synonyms=Grc; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND GLYCOSYLATION. RC STRAIN=C57BL/6J; TISSUE=Spleen; RX PubMed=10559903; DOI=10.1038/11086; RA Kanzaki M., Zhang Y.-Q., Mashima H., Li L., Shibata H., Kojima I.; RT "Translocation of a calcium-permeable cation channel induced by insulin- RT like growth factor-I."; RL Nat. Cell Biol. 1:165-170(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; 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 [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11707512; DOI=10.1242/jcs.114.20.3599; RA Boels K., Glassmeier G., Herrmann D., Riedel I.B., Hampe W., Kojima I., RA Schwarz J.R., Schaller H.C.; RT "The neuropeptide head activator induces activation and translocation of RT the growth-factor-regulated Ca(2+)-permeable channel GRC."; RL J. Cell Sci. 114:3599-3606(2001). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-755, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-743, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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:10559903, ECO:0000269|PubMed:11707512}. 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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC Cytoplasm. Melanosome {ECO:0000250}. Note=Translocates from the CC cytoplasm to the plasma membrane upon ligand stimulation. CC -!- TISSUE SPECIFICITY: Abundantly expressed in spleen, placenta, skeleton CC muscle, lung and brain. {ECO:0000269|PubMed:10559903}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10559903}. 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 --------------------------------------------------------------------------- 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; AB021665; BAA78478.1; -; mRNA. DR EMBL; AK089004; BAC40695.1; -; mRNA. DR EMBL; AL596181; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005415; AAH05415.1; -; mRNA. DR CCDS; CCDS24827.1; -. DR RefSeq; NP_035836.2; NM_011706.2. DR RefSeq; XP_006533228.1; XM_006533165.2. DR RefSeq; XP_011247273.1; XM_011248971.1. DR PDB; 7XEM; EM; 3.17 A; A/B/C/D=1-756. DR PDB; 7XEO; EM; 2.89 A; A/B/C/D=1-756. DR PDB; 7XER; EM; 2.47 A; A/B/C/D=1-756. DR PDB; 7XEU; EM; 2.77 A; A/B/C/D=1-756. DR PDB; 7XEV; EM; 3.27 A; A/B/C/D=1-756. DR PDB; 7XEW; EM; 2.59 A; A/B/C/D=1-756. DR PDB; 7YEP; EM; 2.83 A; A/B/C/D=1-756. DR PDBsum; 7XEM; -. DR PDBsum; 7XEO; -. DR PDBsum; 7XER; -. DR PDBsum; 7XEU; -. DR PDBsum; 7XEV; -. DR PDBsum; 7XEW; -. DR PDBsum; 7YEP; -. DR AlphaFoldDB; Q9WTR1; -. DR EMDB; EMD-33156; -. DR EMDB; EMD-33157; -. DR EMDB; EMD-33158; -. DR EMDB; EMD-33159; -. DR EMDB; EMD-33160; -. DR EMDB; EMD-33161; -. DR EMDB; EMD-33774; -. DR SMR; Q9WTR1; -. DR BioGRID; 204537; 2. DR IntAct; Q9WTR1; 2. DR MINT; Q9WTR1; -. DR STRING; 10090.ENSMUSP00000018651; -. DR BindingDB; Q9WTR1; -. DR ChEMBL; CHEMBL4523498; -. DR GuidetoPHARMACOLOGY; 508; -. DR TCDB; 1.A.4.2.4; the transient receptor potential ca2+/cation channel (trp-cc) family. DR GlyCosmos; Q9WTR1; 1 site, No reported glycans. DR GlyGen; Q9WTR1; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9WTR1; -. DR MetOSite; Q9WTR1; -. DR PhosphoSitePlus; Q9WTR1; -. DR SwissPalm; Q9WTR1; -. DR EPD; Q9WTR1; -. DR jPOST; Q9WTR1; -. DR MaxQB; Q9WTR1; -. DR PaxDb; 10090-ENSMUSP00000018651; -. DR PeptideAtlas; Q9WTR1; -. DR ProteomicsDB; 258986; -. DR Antibodypedia; 13247; 345 antibodies from 36 providers. DR DNASU; 22368; -. DR Ensembl; ENSMUST00000018651.14; ENSMUSP00000018651.8; ENSMUSG00000018507.17. DR Ensembl; ENSMUST00000102643.2; ENSMUSP00000099703.2; ENSMUSG00000018507.17. DR GeneID; 22368; -. DR KEGG; mmu:22368; -. DR UCSC; uc007jjh.1; mouse. DR AGR; MGI:1341836; -. DR CTD; 51393; -. DR MGI; MGI:1341836; Trpv2. DR VEuPathDB; HostDB:ENSMUSG00000018507; -. DR eggNOG; KOG3676; Eukaryota. DR GeneTree; ENSGT00940000158512; -. DR HOGENOM; CLU_012795_1_1_1; -. DR InParanoid; Q9WTR1; -. DR OMA; TNACILP; -. DR OrthoDB; 1003028at2759; -. DR PhylomeDB; Q9WTR1; -. DR TreeFam; TF314711; -. DR Reactome; R-MMU-3295583; TRP channels. DR BioGRID-ORCS; 22368; 4 hits in 77 CRISPR screens. DR PRO; PR:Q9WTR1; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q9WTR1; Protein. DR Bgee; ENSMUSG00000018507; Expressed in placenta labyrinth and 151 other cell types or tissues. DR GO; GO:0030424; C:axon; IDA:DFLAT. DR GO; GO:0044295; C:axonal growth cone; IDA:DFLAT. DR GO; GO:0044297; C:cell body; IDA:DFLAT. DR GO; GO:0009986; C:cell surface; IDA:DFLAT. DR GO; GO:0012505; C:endomembrane system; ISO:MGI. DR GO; GO:0032584; C:growth cone membrane; IDA:DFLAT. DR GO; GO:0030027; C:lamellipodium; ISO:MGI. 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; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0005261; F:monoatomic cation channel activity; IDA:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI. DR GO; GO:0045773; P:positive regulation of axon extension; IMP:DFLAT. DR GO; GO:0090280; P:positive regulation of calcium ion import; IMP:DFLAT. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab. DR GO; GO:0009266; P:response to temperature stimulus; ISO:MGI. 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; Q9WTR1; MM. 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..756 FT /note="Transient receptor potential cation channel FT subfamily V member 2" FT /id="PRO_0000215343" FT TOPO_DOM 1..387 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 388..408 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 409..428 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 429..449 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 450..455 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 456..476 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 477..490 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 491..511 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 512..532 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 533..553 FT /note="Helical" FT /evidence="ECO:0000255" FT INTRAMEM 568..604 FT /note="Pore-forming" FT /evidence="ECO:0000255" FT TRANSMEM 617..637 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 638..756 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 68..110 FT /note="ANK 1" FT REPEAT 111..157 FT /note="ANK 2" FT REPEAT 158..203 FT /note="ANK 3" FT REPEAT 204..239 FT /note="ANK 4" FT REPEAT 240..288 FT /note="ANK 5" FT REPEAT 289..315 FT /note="ANK 6" FT REGION 1..385 FT /note="Required for interaction with SLC50A1" FT /evidence="ECO:0000250" FT REGION 1..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 559..583 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 719..756 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 77 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WUD2" FT MOD_RES 743 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 755 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT CARBOHYD 567 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 565 FT /note="D -> N (in Ref. 1; BAA78478)" FT /evidence="ECO:0000305" FT HELIX 72..81 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 90..96 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 101..105 FT /evidence="ECO:0007829|PDB:7XER" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 115..120 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:7XEW" FT HELIX 131..140 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 162..168 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 172..180 FT /evidence="ECO:0007829|PDB:7XER" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 208..214 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 218..225 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:7XEW" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:7XEM" FT HELIX 244..250 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 256..276 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:7XEW" FT STRAND 288..290 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 293..299 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 304..310 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:7XEU" FT STRAND 323..326 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 333..339 FT /evidence="ECO:0007829|PDB:7XER" FT TURN 341..343 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 351..357 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 364..368 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 371..383 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 385..407 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 424..453 FT /evidence="ECO:0007829|PDB:7XER" FT TURN 454..456 FT /evidence="ECO:0007829|PDB:7XER" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 462..464 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 468..487 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 492..510 FT /evidence="ECO:0007829|PDB:7XER" FT TURN 511..513 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 515..530 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 533..552 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 553..557 FT /evidence="ECO:0007829|PDB:7YEP" FT HELIX 588..599 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 609..612 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 614..628 FT /evidence="ECO:0007829|PDB:7XER" FT TURN 629..631 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 632..646 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 648..667 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 671..673 FT /evidence="ECO:0007829|PDB:7XEV" FT STRAND 681..685 FT /evidence="ECO:0007829|PDB:7XER" FT STRAND 690..693 FT /evidence="ECO:0007829|PDB:7XEW" FT STRAND 696..705 FT /evidence="ECO:0007829|PDB:7XER" FT HELIX 707..712 FT /evidence="ECO:0007829|PDB:7XER" SQ SEQUENCE 756 AA; 85965 MW; C0E537AB2C86E1A8 CRC64; MTSASNPPAF RLETSDGDEE GSAEVNKGKN EPPPMESPFQ GEDRNFSPQI KVNLNYRKGL GPSQQDPNRF DRDRLFSVVS RGVPEELTGL LEYLRRTSKY LTDSAYTEGS TGKTCLMKAV LNLQDGVNAC ILPLLQIDRD SGNPQPLVNA QCTDEFYRGH SALHIAIEKR SLWCVKLLVE NGANVHIRAC GRFFQKHQGT CFYFGELPLS LAACTKQWDV VTYLLENPHQ PASLEATDSL GNTVLHALVM IADNSPENSA LVIHMYDSLL QMGARLCPTV QLEDICNHQG LTPLKLAAKE GKIEIFRHIL QREFSGLYQP LSRKFTEWCY GPVRVSLYDL SSVDSWEKNS VLEIIAFHCK SPHRHRMVVL EPLNKLLQEK WDRLIPRFFF NFACYLVYMI IFTIVAYHQP SLEQPAIPSS KATFGDSMLL LGHILILLGG IYLLLGQLWY FWRRRLFIWI SFMDSYFEIL FLVQALLTVL SQVLRFVETE WYLPLLVSSL VLGWLNLLYY TRGFQHTGIY SVMIQKVILR DLLRFLLVYL VFLFGFAVAL VSLSREARSP KAPEDSNTTV TEKPTLGQEE EPVPYGGILD ASLELFKFTI GMGELAFQEQ LRFRGVVLLL LLAYVLLTYV LLLNMLIALM SETVNSVATD SWSIWKLQKA ISVLEMENGY WWCRRKRHRA GRLLKVGTKG DGIPDERWCF RVEEVNWAAW EKTLPTLSED PSGAGITGYK KNPTSKPGKN SASEEDHLPL QVLQSH //