ID ITPR3_MOUSE Reviewed; 2670 AA. AC P70227; Q5DWM4; Q8CED5; Q91Z08; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 3. DT 14-OCT-2015, entry version 135. DE RecName: Full=Inositol 1,4,5-trisphosphate receptor type 3; DE AltName: Full=IP3 receptor isoform 3; DE Short=IP3R 3; DE Short=InsP3R3; DE AltName: Full=Type 3 inositol 1,4,5-trisphosphate receptor; DE Short=Type 3 InsP3 receptor; GN Name=Itpr3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP LYS-507 AND ARG-510. RC STRAIN=C57BL/6J; TISSUE=Lung; RX PubMed=15632133; DOI=10.1074/jbc.M413824200; RA Iwai M., Tateishi Y., Hattori M., Mizutani A., Nakamura T., RA Futatsugi A., Inoue T., Furuichi T., Michikawa T., Mikoshiba K.; RT "Molecular cloning of mouse type 2 and type 3 inositol 1,4,5- RT trisphosphate receptors and identification of a novel type 2 receptor RT splice variant."; RL J. Biol. Chem. 280:10305-10317(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1857-2670. RC STRAIN=C57BL/6J; TISSUE=Skin; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2181-2670. RC STRAIN=FVB/N; TISSUE=Mammary tumor; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2406-2609. RC TISSUE=Placenta; RX PubMed=1374893; DOI=10.1073/pnas.89.10.4265; RA Ross C.A., Danoff S.K., Schell M.J., Snyder S.H., Ullrich A.; RT "Three additional inositol 1,4,5-trisphosphate receptors: molecular RT cloning and differential localization in brain and peripheral RT tissues."; RL Proc. Natl. Acad. Sci. U.S.A. 89:4265-4269(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2433-2629. RC STRAIN=C3H; TISSUE=Embryo; RX PubMed=9065779; RA De Smedt H., Missiaen L., Parys J.B., Henning R.H., Sienaert I., RA Vanlingen S., Gijsens A., Himpens B., Casteels R.; RT "Isoform diversity of the inositol trisphosphate receptor in cell RT types of mouse origin."; RL Biochem. J. 322:575-583(1997). RN [6] RP INTERACTION WITH SIGMAR1. RX PubMed=11149946; DOI=10.1073/pnas.98.2.491; RA Hayashi T., Su T.-P.; RT "Regulating ankyrin dynamics: roles of sigma-1 receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 98:491-496(2001). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916; SER-934; SER-1832 RP AND SER-2669, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; 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 RT expression."; RL Cell 143:1174-1189(2010). RN [9] RP INTERACTION WITH LRMP. RX PubMed=20071408; DOI=10.1093/chemse/bjp097; RA Shindo Y., Kim M.R., Miura H., Yuuki T., Kanda T., Hino A., RA Kusakabe Y.; RT "Lrmp/Jaw1 is expressed in sweet, bitter, and umami receptor- RT expressing cells."; RL Chem. Senses 35:171-177(2010). RN [10] RP FUNCTION, AND MUTAGENESIS OF TRP-168. RX PubMed=20813840; DOI=10.1074/jbc.M110.140129; RA Yamazaki H., Chan J., Ikura M., Michikawa T., Mikoshiba K.; RT "Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor RT mediates functional coupling between ligand binding and channel RT opening."; RL J. Biol. Chem. 285:36081-36091(2010). RN [11] RP FUNCTION, INTERACTION WITH PML AND AKT1, PHOSPHORYLATION, AND RP SUBCELLULAR LOCATION. RX PubMed=21030605; DOI=10.1126/science.1189157; RA Giorgi C., Ito K., Lin H.K., Santangelo C., Wieckowski M.R., RA Lebiedzinska M., Bononi A., Bonora M., Duszynski J., Bernardi R., RA Rizzuto R., Tacchetti C., Pinton P., Pandolfi P.P.; RT "PML regulates apoptosis at endoplasmic reticulum by modulating RT calcium release."; RL Science 330:1247-1251(2010). RN [12] RP INTERACTION WITH TESPA1. RX PubMed=23650607; DOI=10.1016/j.fob.2012.08.005; RA Matsuzaki H., Fujimoto T., Ota T., Ogawa M., Tsunoda T., Doi K., RA Hamabashiri M., Tanaka M., Shirasawa S.; RT "Tespa1 is a novel inositol 1,4,5-trisphosphate receptor binding RT protein in T and B lymphocytes."; RL FEBS Open Bio 2:255-259(2012). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-224. RX PubMed=20843799; DOI=10.1074/jbc.M110.140160; RA Chan J., Yamazaki H., Ishiyama N., Seo M.D., Mal T.K., Michikawa T., RA Mikoshiba K., Ikura M.; RT "Structural studies of inositol 1,4,5-trisphosphate receptor: coupling RT ligand binding to channel gating."; RL J. Biol. Chem. 285:36092-36099(2010). CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second CC messenger that mediates the release of intracellular calcium. CC {ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:21030605}. CC -!- SUBUNIT: Homotetramer. Interacts with TRPC1, TRPC3, TRPC4. CC Interacts with TRPV4 (By similarity). Interacts with SIGMAR1 CC (PubMed:11149946). Interacts with AKT1 and PML (PubMed:21030605). CC Interacts with LRMP (via coiled-coil domain) (PubMed:20071408). CC Interacts with CABP1 (By similarity). Interacts with TMBIM4/LFG4 CC (By similarity). Interacts with CEMIP (By similarity). Interacts CC with TESPA1 (PubMed:23650607). Interacts with TMEM203 (By CC similarity). {ECO:0000250|UniProtKB:Q14573, CC ECO:0000269|PubMed:11149946, ECO:0000269|PubMed:20071408, CC ECO:0000269|PubMed:21030605, ECO:0000269|PubMed:23650607}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:15632133, ECO:0000269|PubMed:21030605}; Multi- CC pass membrane protein {ECO:0000269|PubMed:15632133, CC ECO:0000269|PubMed:21030605}. CC -!- DOMAIN: The receptor contains a calcium channel in its C-terminal CC extremity. Its large N-terminal cytoplasmic region has the ligand- CC binding site in the N-terminus and modulatory sites in the middle CC portion immediately upstream of the channel region. CC -!- PTM: Phosphorylated on tyrosine residues (By similarity). CC Phosphorylated by AKT1 on serine and/or threonine residues. CC {ECO:0000250, ECO:0000269|PubMed:21030605}. CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}. CC -!- SIMILARITY: Contains 5 MIR domains. {ECO:0000255|PROSITE- CC ProRule:PRU00131}. 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; AB182289; BAD90683.1; -; mRNA. DR EMBL; AK028491; BAC25977.1; -; mRNA. DR EMBL; BC010323; AAH10323.1; -; mRNA. DR EMBL; M90088; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; Z71174; CAA94862.1; -; mRNA. DR CCDS; CCDS28560.1; -. DR RefSeq; NP_542120.2; NM_080553.3. DR UniGene; Mm.458106; -. DR PDB; 3JRR; X-ray; 1.90 A; A/B=1-224. DR PDBsum; 3JRR; -. DR ProteinModelPortal; P70227; -. DR SMR; P70227; 4-579. DR BioGrid; 200849; 4. DR IntAct; P70227; 2. DR STRING; 10090.ENSMUSP00000038150; -. DR GuidetoPHARMACOLOGY; 745; -. DR PhosphoSite; P70227; -. DR MaxQB; P70227; -. DR PaxDb; P70227; -. DR PRIDE; P70227; -. DR Ensembl; ENSMUST00000049308; ENSMUSP00000038150; ENSMUSG00000042644. DR GeneID; 16440; -. DR KEGG; mmu:16440; -. DR UCSC; uc008bfi.2; mouse. DR CTD; 3710; -. DR MGI; MGI:96624; Itpr3. DR eggNOG; NOG280601; -. DR GeneTree; ENSGT00760000119152; -. DR HOGENOM; HOG000007660; -. DR HOVERGEN; HBG052158; -. DR InParanoid; P70227; -. DR KO; K04960; -. DR OMA; FVHELFY; -. DR OrthoDB; EOG76HQ0M; -. DR PhylomeDB; P70227; -. DR TreeFam; TF312815; -. DR Reactome; R-MMU-112043; PLC beta mediated events. DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis. DR Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels. DR Reactome; R-MMU-1489509; DAG and IP3 signaling. DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis. DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization. DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-MMU-4086398; Ca2+ pathway. DR Reactome; R-MMU-422356; Regulation of insulin secretion. DR Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation. DR Reactome; R-MMU-5607763; CLEC7A (Dectin-1) induces NFAT activation. DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. DR ChiTaRS; Itpr3; mouse. DR EvolutionaryTrace; P70227; -. DR NextBio; 289691; -. DR PRO; PR:P70227; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; P70227; -. DR CleanEx; MM_ITPR3; -. DR Genevisible; P70227; MM. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0005730; C:nucleolus; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0043235; C:receptor complex; ISO:MGI. DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:MGI. DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB. DR GO; GO:0005218; F:intracellular ligand-gated calcium channel activity; IDA:UniProtKB. DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI. DR GO; GO:0006816; P:calcium ion transport; IDA:MGI. DR GO; GO:0060402; P:calcium ion transport into cytosol; IDA:UniProtKB. DR GO; GO:0048016; P:inositol phosphate-mediated signaling; ISO:MGI. DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI. DR GO; GO:0007613; P:memory; IMP:MGI. DR GO; GO:0051592; P:response to calcium ion; ISO:MGI. DR GO; GO:0050913; P:sensory perception of bitter taste; IMP:MGI. DR GO; GO:0050916; P:sensory perception of sweet taste; IMP:MGI. DR GO; GO:0050917; P:sensory perception of umami taste; IMP:MGI. DR Gene3D; 1.25.10.30; -; 2. DR InterPro; IPR014821; Ins145_P3_rcpt. DR InterPro; IPR000493; InsP3_rcpt-bd. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR016093; MIR_motif. DR InterPro; IPR013662; RIH_assoc-dom. DR InterPro; IPR000699; RIH_dom. DR InterPro; IPR015925; Ryanodine_recept-rel. DR PANTHER; PTHR13715; PTHR13715; 1. DR Pfam; PF08709; Ins145_P3_rec; 1. DR Pfam; PF00520; Ion_trans; 1. DR Pfam; PF02815; MIR; 1. DR Pfam; PF08454; RIH_assoc; 1. DR Pfam; PF01365; RYDR_ITPR; 2. DR PRINTS; PR00779; INSP3RECEPTR. DR SMART; SM00472; MIR; 4. DR SUPFAM; SSF100909; SSF100909; 2. DR SUPFAM; SSF82109; SSF82109; 2. DR PROSITE; PS50919; MIR; 5. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Calcium channel; Calcium transport; KW Complete proteome; Endoplasmic reticulum; Ion channel; Ion transport; KW Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 2670 Inositol 1,4,5-trisphosphate receptor FT type 3. FT /FTId=PRO_0000153929. FT TOPO_DOM 1 2233 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 2234 2254 Helical. {ECO:0000255}. FT TOPO_DOM 2255 2262 Extracellular. {ECO:0000255}. FT TRANSMEM 2263 2283 Helical. {ECO:0000255}. FT TOPO_DOM 2284 2292 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 2293 2310 Helical. {ECO:0000255}. FT TOPO_DOM 2311 2324 Extracellular. {ECO:0000255}. FT TRANSMEM 2325 2345 Helical. {ECO:0000255}. FT TOPO_DOM 2346 2367 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 2368 2388 Helical. {ECO:0000255}. FT TOPO_DOM 2389 2495 Extracellular. {ECO:0000255}. FT TRANSMEM 2496 2516 Helical. {ECO:0000255}. FT TOPO_DOM 2517 2670 Cytoplasmic. {ECO:0000255}. FT DOMAIN 113 173 MIR 1. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT DOMAIN 174 224 MIR 2. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT DOMAIN 232 288 MIR 3. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT DOMAIN 295 372 MIR 4. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT DOMAIN 378 434 MIR 5. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT REGION 266 270 Inositol 1,4,5-trisphosphate binding. FT REGION 507 510 Inositol 1,4,5-trisphosphate binding. FT REGION 567 569 Inositol 1,4,5-trisphosphate binding. FT MOD_RES 916 916 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 934 934 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 1152 1152 Phosphoserine. FT {ECO:0000269|PubMed:21030605}. FT MOD_RES 1813 1813 Phosphoserine. FT {ECO:0000250|UniProtKB:Q14573}. FT MOD_RES 1832 1832 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 2582 2582 Phosphotyrosine. {ECO:0000255}. FT MOD_RES 2669 2669 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MUTAGEN 168 168 W->A: Loss of calcium flux. FT {ECO:0000269|PubMed:20813840}. FT MUTAGEN 507 507 K->A: Loss of binding activity. FT {ECO:0000269|PubMed:15632133}. FT MUTAGEN 510 510 R->A: Loss of binding activity. FT {ECO:0000269|PubMed:15632133}. FT CONFLICT 2406 2413 SRASPLGM -> FPPSRARR (in Ref. 4). FT {ECO:0000305}. FT CONFLICT 2430 2430 D -> E (in Ref. 4; M90088). FT {ECO:0000305}. FT CONFLICT 2447 2447 P -> L (in Ref. 4; M90088). FT {ECO:0000305}. FT CONFLICT 2605 2609 RAMSL -> LGSTS (in Ref. 4; M90088). FT {ECO:0000305}. FT STRAND 13 29 {ECO:0000244|PDB:3JRR}. FT STRAND 35 38 {ECO:0000244|PDB:3JRR}. FT HELIX 40 42 {ECO:0000244|PDB:3JRR}. FT STRAND 45 47 {ECO:0000244|PDB:3JRR}. FT HELIX 52 55 {ECO:0000244|PDB:3JRR}. FT STRAND 57 60 {ECO:0000244|PDB:3JRR}. FT HELIX 66 74 {ECO:0000244|PDB:3JRR}. FT HELIX 84 110 {ECO:0000244|PDB:3JRR}. FT TURN 111 113 {ECO:0000244|PDB:3JRR}. FT STRAND 121 126 {ECO:0000244|PDB:3JRR}. FT TURN 127 130 {ECO:0000244|PDB:3JRR}. FT STRAND 131 140 {ECO:0000244|PDB:3JRR}. FT STRAND 142 144 {ECO:0000244|PDB:3JRR}. FT STRAND 147 155 {ECO:0000244|PDB:3JRR}. FT HELIX 158 160 {ECO:0000244|PDB:3JRR}. FT STRAND 162 166 {ECO:0000244|PDB:3JRR}. FT STRAND 182 187 {ECO:0000244|PDB:3JRR}. FT TURN 188 190 {ECO:0000244|PDB:3JRR}. FT STRAND 194 201 {ECO:0000244|PDB:3JRR}. FT STRAND 204 214 {ECO:0000244|PDB:3JRR}. FT STRAND 218 223 {ECO:0000244|PDB:3JRR}. SQ SEQUENCE 2670 AA; 304275 MW; 9B5BA808B195C58F CRC64; MNEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK KFRDCLFKVC PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME QKQNDTENKK VHGDVVKYGS VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV TLDATGNEGS WLFIQPFWKL RSNGDNVVVG DKVILNPVNA GQPLHASNYE LSDNAGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV VRLFHAEQEK FLTCDEYRGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW NGLYRFKHLA TGNYLAAEEN PSYKGDVSDP KAAGLGAQGR TGRRNAGEKI KYRLVAVPHG NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS TNAPIDVEEE RPIRLMLGTC PTKEDKEAFA IVSVPVSEIR DLDFANDASS MLASAVEKLN EGFISQNDRR FVIQLLEDLV FFVSDVPNNG QNVLDIMVTK PNRERQKLMR EQNILKQIFG ILKAPFRDKG GEGPLVRLEE LSDQKNAPYQ YMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NRIAIPVTQE LICKCVLDPK NSDILIQTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDRN NEHHEKSVRQ LAQEARAGNA HDENVLSYYR YQLKLFARMC LDRQYLAIDE ISKQLGVELL FLCMADEMLP FDLRASFCHL MLHVHVDRDP QELVTPVKFA RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ASTMEFVEDY LNNVVSEAVP FANDEKNILT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCIQAPAA MLQAYEEPGG KNVRRSIQGV GHMMSTMVLS RKQSVFGASS LPAGVGVPEQ LDRSKFEDNE HTVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE VFPMQDSGAD GTAPAFDSST ATMNLDRIGE QAEAMFGVGK TSSMLEVDDE GGRMFLRVLL HLTMHDYPSL VSGALQLLFK HFSQRQEAMH TFKQVQLLIS AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSVKGEEVE AGATKDKKER PSDEEGFLQP HGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM DAHKVMLDLL QIPYDKSDNK MLEILRYTHQ FLQKFCAGNP GNQALLHKHL QLFLTPGLLE AETMQHIFLN NYQLCSEISE PVLQHFVHLL ATHGRHVQYL DFLHTVIKAE GKYVKKCQDM IMTELTNAGD DVVVFYNDKA SLAHLLDMMK AARDGVEDHS PLMYHISLVD LLAACAEGKN VYTEIKCTSL LPLEDVVTVV THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL FENFTLDMAL VCNKREKRLS DPTLEKYVLT VVLDTISAFF SSPFSENSTS LQTHQTIVVQ LLQSTTRLLE CPWLQQQHKG SVEACVRTLA MVAKSRAILL PMDLDAHMSA LLSSGGSCSA AAQRSAANYK TATRTFPRVI PTANQWDYKN IIEKLQDIIM ALEERLKPLV QAELSVLVDM LHWPELLFPE GSEAYQRCES GGFLSKLIRH TKGLMESEEK LCVKVLRTLQ QMLLKKSKFG DRGNQLRKML LQNYLQNRKS GARGELTDPT GSGLDQDWSA IAATQCRLDK EGATKLVCDL ITSTKNEKIF QESIGLAIRL LDGGNTEIQK SFYNLMTSDK KSERFFKVLH DRMKRAQQET KSTVAVNMSD LGSQPREDRE PADPATKGRV SSFSMPSSSR YLLGLGLHRG HDMSERAQNN EMGTSVLIMR PILRFLQLLC ENHNRDLQNF LRCQNNKTNY NLVCETLQFL DIMCGSTTGG LGLLGLYINE DNVGLVIQTL ETLTEYCQGP CHENQTCIVT HESNGIDIIT ALILNDISPL CKYRMDLVLQ LKDNASKLLL ALMESRHDSE NAERILISLR PQELVDVIKK AYLQEEEREN SEVSPREVGH NIYILALQLS RHNKQLQHLL KPVRRIQEEE AEGISSMLSL NNKQLSQMLK SSAPAQEEEE DPLAYYENHT SQIEIVRQDR SMEQIVFPVP AICQFLTEET KHRLFTTTEQ DEQGSKVSDF FDQSSFLHNE MEWQRRLRSM PLIYWFSRRM TLWGSISFNL AVFINIIIAF FYPYVEGAST GVLGSPLISL LFWILICFSI AALFTKRYSV RPLIVALILR SIYYLGIGPT LNILGALNLT NKIVFVVSFV GNRGTFIRGY KAMVMDMEFL YHVGYILTSV LGLFAHELFY SILLFDLIYR EETLFNVIKS VTRNGRSILL TALLALILVY LFSIVGFLFL KDDFILEVDR LPGNHSRASP LGMPHGAATF MGTCSGDKMD CVSEVSVPEI LEEDEEPDST ERACDTLLMC IVTVMNHGLR NGGGVGDILR KPSKDESLFP ARVVYDLLFF FIVIIIVLNL IFGVIIDTFA DLRSEKQKKE EILKTTCFIC GLERDKFDNK TVSFEEHIKL EHNMWNYLYF IVLVRVKNKT DYTGPESYVA QMIKNKNLDW FPRMRAMSLV SGEGEGEQNE IRILQEKLGS TMKLVSHLTS QLNELKEQMT EQRKRRQRLG FVDVQNCMSR //