ID OSH2_YEAST Reviewed; 1283 AA. AC Q12451; D6VRX1; P89891; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 200. DE RecName: Full=Oxysterol-binding protein homolog 2 {ECO:0000303|PubMed:11238399}; DE AltName: Full=Oxysterol-binding protein-related protein 2; DE Short=ORP 2; DE Short=OSBP-related protein 2; GN Name=OSH2 {ECO:0000303|PubMed:11238399}; OrderedLocusNames=YDL019C; GN ORFNames=D2845; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP SUBCELLULAR LOCATION. RX PubMed=11408574; DOI=10.1091/mbc.12.6.1633; RA Levine T.P., Munro S.; RT "Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, RT to both the Golgi and the nucleus-vacuole junction."; RL Mol. Biol. Cell 12:1633-1644(2001). RN [4] RP GENETIC ANALYSIS. RX PubMed=11238399; DOI=10.1093/genetics/157.3.1117; RA Beh C.T., Cool L., Phillips J., Rine J.; RT "Overlapping functions of the yeast oxysterol-binding protein homologues."; RL Genetics 157:1117-1140(2001). RN [5] RP DOMAIN FFAT MOTIF, AND SUBCELLULAR LOCATION. RX PubMed=12727870; DOI=10.1093/emboj/cdg201; RA Loewen C.J.R., Roy A., Levine T.P.; RT "A conserved ER targeting motif in three families of lipid binding proteins RT and in Opi1p binds VAP."; RL EMBO J. 22:2025-2035(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP FUNCTION. RX PubMed=15173322; DOI=10.1242/jcs.01157; RA Beh C.T., Rine J.; RT "A role for yeast oxysterol-binding protein homologs in endocytosis and in RT the maintenance of intracellular sterol-lipid distribution."; RL J. Cell Sci. 117:2983-2996(2004). RN [8] RP DOMAIN. RX PubMed=15023338; DOI=10.1016/s1097-2765(04)00083-8; RA Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B., RA Murray D., Emr S.D., Lemmon M.A.; RT "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin RT homology domains."; RL Mol. Cell 13:677-688(2004). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=YAL6B; RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., RA Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling RT pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; THR-488; SER-787 AND RP SER-1151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [13] RP DOMAIN, AND SUBCELLULAR LOCATION. RX PubMed=20008566; DOI=10.1083/jcb.200905007; RA Schulz T.A., Choi M.G., Raychaudhuri S., Mears J.A., Ghirlando R., RA Hinshaw J.E., Prinz W.A.; RT "Lipid-regulated sterol transfer between closely apposed membranes by RT oxysterol-binding protein homologues."; RL J. Cell Biol. 187:889-903(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-451; SER-455; RP SER-458; SER-459; SER-486; SER-512; SER-515; SER-717; THR-783; SER-787 AND RP SER-825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [15] RP FUNCTION. RX PubMed=24213531; DOI=10.1242/jcs.132001; RA Kajiwara K., Ikeda A., Aguilera-Romero A., Castillon G.A., Kagiwada S., RA Hanada K., Riezman H., Muniz M., Funato K.; RT "Osh proteins regulate COPII-mediated vesicular transport of ceramide from RT the endoplasmic reticulum in budding yeast."; RL J. Cell Sci. 127:376-387(2014). CC -!- FUNCTION: Lipid transport protein (LTP) involved in non-vesicular CC transfer of lipids between membranes. Functions in phosphoinositide- CC coupled directional transport of various lipids by carrying the lipid CC molecule in a hydrophobic pocket and transferring it between membranes CC through the cytosol. Involved in maintenance of intracellular sterol CC distribution and homeostasis (PubMed:15173322). Binds and transports CC sterol (PubMed:20008566). Plays a role in the positive regulation of CC vesicular transport of ceramide from the ER to the Golgi, negatively CC regulating COPII-mediated ER export of cargos (PubMed:24213531). CC {ECO:0000269|PubMed:15173322, ECO:0000269|PubMed:20008566, CC ECO:0000269|PubMed:24213531}. CC -!- SUBUNIT: Interacts with SCS2. {ECO:0000305|PubMed:12727870}. CC -!- INTERACTION: CC Q12451; P36006: MYO3; NbExp=3; IntAct=EBI-12621, EBI-11670; CC Q12451; Q04439: MYO5; NbExp=6; IntAct=EBI-12621, EBI-11687; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11408574, CC ECO:0000269|PubMed:12727870, ECO:0000269|PubMed:20008566}; Peripheral CC membrane protein {ECO:0000269|PubMed:11408574, CC ECO:0000269|PubMed:12727870}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:20008566}. Note=Cell periphery, enriched in small CC buds of G1 phase cells and near the bud-neck region of S phase cells. CC Enriched on regions of the ER in close proximity with the plasma CC membrane (PM), which may represent PM-ER membrane contact sites (MCS) CC (PubMed:20008566). {ECO:0000269|PubMed:20008566}. CC -!- DOMAIN: The PH domain strongly binds to phosphoinositides and is CC required for targeting the protein to the membrane. CC {ECO:0000269|PubMed:15023338}. CC -!- DOMAIN: The FFAT (two phenylalanines in an acidic tract) motif is CC required for interaction with SCS2 and proper localization of the CC protein. {ECO:0000269|PubMed:12727870}. CC -!- DOMAIN: The OSBP-related domain (ORD) mediates binding of sterols and CC phospholipids. It displays an incomplete beta-barrel containing a CC central hydrophobic tunnel that can accommodate a single lipid molecule CC with a flexible lid covering the tunnel entrance. The ORD can bind two CC membranes simultaneously. It has at least two membrane-binding CC surfaces; one near the mouth of the lipid-binding pocket and a distal CC site that can bind a second membrane. These structural features CC correlate with the phosphatidylinositol 4-phosphate (PI(4)P)-coupled CC lipid transport optimized in closely apposed membranes, such as CC organelle contact sites. The lipid transfer cycle starts from the CC association of the LTP with a donor membrane, which accompanies CC conformational changes that uncover the ligand-binding pocket. The CC tunnel opening is generally mediated by displacement of the lid CC covering the binding pocket allowing uptake or release of a lipid CC molecule. The LTPs extract the lipid from the membrane by providing a CC hydrophobic environment as well as specific interaction. Dissociation CC from the donor membrane shifts the conformation to a closed form. Then, CC the LTPs loaded with a cargo lipid diffuse through the aqueous phase. CC Lid opening may be induced by the interaction of a hydrophobic side of CC the lid with the target membranes. {ECO:0000305|PubMed:20008566}. CC -!- MISCELLANEOUS: Present with 1069 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the OSBP family. {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; Z74066; CAA98577.1; -; Genomic_DNA. DR EMBL; Z74067; CAA98578.1; -; Genomic_DNA. DR EMBL; Z48432; CAA88340.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11831.1; -; Genomic_DNA. DR PIR; S52500; S52500. DR RefSeq; NP_010265.1; NM_001180078.1. DR AlphaFoldDB; Q12451; -. DR SMR; Q12451; -. DR BioGRID; 32036; 78. DR DIP; DIP-6712N; -. DR ELM; Q12451; -. DR IntAct; Q12451; 8. DR MINT; Q12451; -. DR STRING; 4932.YDL019C; -. DR GlyGen; Q12451; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q12451; -. DR MaxQB; Q12451; -. DR PaxDb; 4932-YDL019C; -. DR PeptideAtlas; Q12451; -. DR TopDownProteomics; Q12451; -. DR EnsemblFungi; YDL019C_mRNA; YDL019C; YDL019C. DR GeneID; 851543; -. DR KEGG; sce:YDL019C; -. DR AGR; SGD:S000002177; -. DR SGD; S000002177; OSH2. DR VEuPathDB; FungiDB:YDL019C; -. DR eggNOG; KOG1737; Eukaryota. DR GeneTree; ENSGT00940000173329; -. DR HOGENOM; CLU_001040_1_1_1; -. DR InParanoid; Q12451; -. DR OMA; SIRQMWE; -. DR OrthoDB; 960at2759; -. DR BioCyc; YEAST:G3O-29448-MONOMER; -. DR Reactome; R-SCE-192105; Synthesis of bile acids and bile salts. DR BioGRID-ORCS; 851543; 2 hits in 10 CRISPR screens. DR PRO; PR:Q12451; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; Q12451; Protein. DR GO; GO:0071944; C:cell periphery; HDA:SGD. DR GO; GO:0005935; C:cellular bud neck; IDA:SGD. DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0005635; C:nuclear envelope; IDA:SGD. DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:SGD. DR GO; GO:0008289; F:lipid binding; IDA:SGD. DR GO; GO:0032934; F:sterol binding; IBA:GO_Central. DR GO; GO:0120015; F:sterol transfer activity; IDA:SGD. DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central. DR GO; GO:0006897; P:endocytosis; IGI:SGD. DR GO; GO:0035621; P:ER to Golgi ceramide transport; IMP:SGD. DR GO; GO:0006887; P:exocytosis; IGI:SGD. DR GO; GO:0030011; P:maintenance of cell polarity; IGI:SGD. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IGI:SGD. DR GO; GO:0015918; P:sterol transport; IDA:SGD. DR CDD; cd13292; PH_Osh1p_Osh2p_yeast; 1. DR Gene3D; 2.40.160.120; -; 1. DR Gene3D; 3.30.70.3490; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR037239; OSBP_sf. DR InterPro; IPR000648; Oxysterol-bd. DR InterPro; IPR018494; Oxysterol-bd_CS. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR10972:SF205; OXYSTEROL-BINDING PROTEIN; 1. DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1. DR Pfam; PF13637; Ank_4; 1. DR Pfam; PF01237; Oxysterol_BP; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00248; ANK; 2. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50297; ANK_REP_REGION; 2. DR PROSITE; PS50088; ANK_REPEAT; 1. DR PROSITE; PS01013; OSBP; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW Acetylation; ANK repeat; Cell membrane; Endoplasmic reticulum; KW Lipid transport; Lipid-binding; Membrane; Phosphoprotein; KW Reference proteome; Repeat; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:15665377" FT CHAIN 2..1283 FT /note="Oxysterol-binding protein homolog 2" FT /id="PRO_0000100388" FT REPEAT 106..134 FT /note="ANK 1" FT REPEAT 206..235 FT /note="ANK 2" FT DOMAIN 289..386 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 504..571 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 702..721 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 767..834 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 897..1268 FT /note="OSBP-related domain (ORD)" FT /evidence="ECO:0000305" FT MOTIF 745..751 FT /note="FFAT" FT COMPBIAS 504..555 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 556..571 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 702..717 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 787..805 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 812..834 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:15665377" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15665377" FT MOD_RES 422 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358, FT ECO:0007744|PubMed:18407956" FT MOD_RES 445 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 451 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 455 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 458 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 459 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 486 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 488 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 512 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 515 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 717 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 783 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 787 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 825 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 1151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" SQ SEQUENCE 1283 AA; 145796 MW; D521957460E7F7C3 CRC64; MSREDLSIAE DLNQVSKPLL KVKLLEVLGQ GDFKHLKALV DNEFQPKDDP SVQQVLNLIL HYAVQVAPIL LIKEIVAHWV DQVGDEKSSS KSDDGIHLDL NYQDENGNTP LHLAAAQSRS DVISFLLSQK SINDCVKNKA HQQPLDMCKD LNVAQMIQLK RDDYFLETVH SLRAAMNKRD FSKLDSIWKN PRNLNLLDIN GIDPETGTTL LYEYSQKKDI EMCQWLLKHG AEATVKDGKG RSPLDLVKNI KLPAKPSNNV TPEIKLKNLL EKNLREQAIV HEDVASSKPP TYKGFLKKWT NFAHGYKLRW FILSGDGNLS YYKDQSHVDR PRGTLKVSTC RLHIDSSEKL NFELLGGITG TTRWRLKGNH PIETTRWVNA IQSAIRFAKD KEILNKKKAV PPSLALKNKS PALISHSKTQ GSLPEASQYY QHTLHKEVIQ PSSVSLYRRP SNNLSVVSSE IQLNDNLTES GKRFVSKMIE NRLDGSKTPV GVHTGSALQR VRSSNTLKSN RSMQSGSGVA SPIDKVPNGA NLSQSNTTTG STASLSDNNY IDNFEGDEAN SDDEEEDLGI NFDRDEEYIK AQYGPYKEKL DMYEQAISIE LSSLIELIEQ EEPSPEVWLT IKKSLINTST IFGKLKDLTY KRDKRLVDMV SKQGDVNNVW VQSVKELEME LSNKTERLAS IDKERRGLKK ILHKKLLESH ATAGNKESLE NDKEQESDTT ASTLGQIAKF ISATKEEDEA SDADEFYDAA ELVDEVTELT EAHPEISTAA APKHAPPPVP NETDNDSQYV QDEKSKIESN VEKTSQKFEK QNNLVTEDEP KTDQSLKNFK AEDKESQVKE KTKEIASSVI GEKTIVAVTT VQKRKEEYLL KEGSYLGYED GIRKRLSMDK DDRPKISLWA VLKSMVGKDM TRMTLPVTFN EPTSLLQRVA EDLEYSELLD QAATFEDSTL RTLYVAAFTA SSYASTTKRV AKPFNPLLGE TFEYSRPDKQ YRFFTEQVSH HPPISATWTE SPRWDFWGES FVDTKFNGRS FNVKHLGLWH IKLRPNDNEK EELYTWKKPN NTVIGILIGN PQVDNHGEVN VVNHTTGDHC KLYFKARGWR SSGAYEITGE VYNKKKQKVW ILGGHWNEAI FAKKVVKDGD LSLEKTRTAA SAGNGPTDDG TKFLIWKAND RPEEPFNLTP FAITLNAPQP HLLPWLPPTD TRLRPDQRAM EDGRYDEAGD EKFRVEEKQR AARRKREENN LEYHPQWFVR DTHPITKAKY WRYTGKYWVK RRDHDLKDCG DIF //