ID COPB2_YEAST Reviewed; 889 AA. AC P41811; D6VU12; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 207. DE RecName: Full=Coatomer subunit beta'; DE AltName: Full=Beta'-coat protein; DE Short=Beta'-COP; GN Name=SEC27; OrderedLocusNames=YGL137W; ORFNames=G2827; 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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-11. RC STRAIN=RSY255; RX PubMed=7929113; DOI=10.1016/s0021-9258(19)51110-3; RA Duden R., Hosobuchi M., Hamamoto S., Winey M., Byers B., Schekman R.; RT "Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential RT for endoplasmic reticulum-to-Golgi protein traffic."; RL J. Biol. Chem. 269:24486-24495(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8840506; RX DOI=10.1002/(sici)1097-0061(199607)12:9<887::aid-yea971>3.0.co;2-d; RA Escribano V., Eraso P., Portillo F., Mazon M.J.; RT "Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces cerevisiae RT chromosome VII reveals SEC27, SSM1b, a putative S-adenosylmethionine- RT dependent enzyme and six new open reading frames."; RL Yeast 12:887-892(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [4] 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 [5] RP PROTEIN SEQUENCE OF 1-27. RC STRAIN=ATCC 208279 / BJ926; RX PubMed=8405452; DOI=10.1016/0014-5793(93)80487-f; RA Harter C., Draken E., Lottspeich F., Wieland F.T.; RT "Yeast coatomer contains a subunit homologous to mammalian beta'-COP."; RL FEBS Lett. 332:71-73(1993). RN [6] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [7] 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 [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS27. RX PubMed=17101773; DOI=10.1128/mcb.00577-06; RA Gabriely G., Kama R., Gerst J.E.; RT "Involvement of specific COPI subunits in protein sorting from the late RT endosome to the vacuole in yeast."; RL Mol. Cell. Biol. 27:526-540(2007). RN [9] RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY RP 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to CC dilysine motifs and reversibly associates with Golgi non-clathrin- CC coated vesicles, which further mediate biosynthetic protein transport CC from the ER, via the Golgi up to the trans Golgi network. Coatomer CC complex is required for budding from Golgi membranes, and is essential CC for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. CC {ECO:0000269|PubMed:17101773}. CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta, CC beta', gamma, delta, epsilon and zeta subunits. Interacts with the CC ESCRT-0 subunit VPS27. {ECO:0000269|PubMed:17101773}. CC -!- INTERACTION: CC P41811; P53622: COP1; NbExp=17; IntAct=EBI-4898, EBI-4860; CC P41811; P02829: HSP82; NbExp=2; IntAct=EBI-4898, EBI-8659; CC P41811; P40509: SEC28; NbExp=4; IntAct=EBI-4898, EBI-4884; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic CC side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on CC the cytoplasmic side of the Golgi, as well as on the vesicles/buds CC originating from it. {ECO:0000250}. CC -!- MISCELLANEOUS: Present with 129000 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the WD repeat COPB2 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; U11237; AAA61711.1; -; Genomic_DNA. DR EMBL; X92670; CAA63359.1; -; Genomic_DNA. DR EMBL; Z72659; CAA96848.1; -; Genomic_DNA. DR EMBL; BK006941; DAA07973.1; -; Genomic_DNA. DR PIR; B55123; B55123. DR RefSeq; NP_011378.1; NM_001181002.1. DR PDB; 2YNN; X-ray; 1.78 A; A=1-304. DR PDB; 2YNO; X-ray; 1.80 A; A/B=1-304. DR PDB; 2YNP; X-ray; 2.96 A; A=1-604. DR PDB; 4J73; X-ray; 1.44 A; A=1-301. DR PDB; 4J77; X-ray; 1.76 A; A/B=1-301. DR PDB; 4J78; X-ray; 1.48 A; A=1-301. DR PDB; 4J79; X-ray; 1.56 A; A=1-300. DR PDB; 4J81; X-ray; 1.74 A; A/B=1-301. DR PDB; 4J82; X-ray; 1.46 A; A/B=1-301. DR PDB; 4J84; X-ray; 1.47 A; A/B=1-301. DR PDB; 4J86; X-ray; 1.48 A; A/B=1-301. DR PDBsum; 2YNN; -. DR PDBsum; 2YNO; -. DR PDBsum; 2YNP; -. DR PDBsum; 4J73; -. DR PDBsum; 4J77; -. DR PDBsum; 4J78; -. DR PDBsum; 4J79; -. DR PDBsum; 4J81; -. DR PDBsum; 4J82; -. DR PDBsum; 4J84; -. DR PDBsum; 4J86; -. DR AlphaFoldDB; P41811; -. DR SMR; P41811; -. DR BioGRID; 33115; 706. DR ComplexPortal; CPX-1652; COPI vesicle coat complex. DR DIP; DIP-6468N; -. DR IntAct; P41811; 162. DR MINT; P41811; -. DR STRING; 4932.YGL137W; -. DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family. DR iPTMnet; P41811; -. DR MaxQB; P41811; -. DR PaxDb; 4932-YGL137W; -. DR PeptideAtlas; P41811; -. DR EnsemblFungi; YGL137W_mRNA; YGL137W; YGL137W. DR GeneID; 852740; -. DR KEGG; sce:YGL137W; -. DR AGR; SGD:S000003105; -. DR SGD; S000003105; SEC27. DR VEuPathDB; FungiDB:YGL137W; -. DR eggNOG; KOG0276; Eukaryota. DR GeneTree; ENSGT00900000141083; -. DR HOGENOM; CLU_005507_1_0_1; -. DR InParanoid; P41811; -. DR OMA; NVFWNES; -. DR OrthoDB; 20819at2759; -. DR BioCyc; YEAST:G3O-30632-MONOMER; -. DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport. DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR BioGRID-ORCS; 852740; 3 hits in 10 CRISPR screens. DR PRO; PR:P41811; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P41811; Protein. DR GO; GO:0030126; C:COPI vesicle coat; IDA:SGD. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD. DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central. DR GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:SGD. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:SGD. DR CDD; cd22938; Coatomer_WDAD; 1. DR CDD; cd00200; WD40; 1. DR Gene3D; 1.25.40.470; -; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR006692; Coatomer_WD-assoc_reg. DR InterPro; IPR016453; COPB2. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19876; COATOMER; 1. DR PANTHER; PTHR19876:SF2; COATOMER SUBUNIT BETA; 1. DR Pfam; PF04053; Coatomer_WDAD; 1. DR Pfam; PF00400; WD40; 5. DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40 repeat-like; 2. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein; KW Protein transport; Reference proteome; Repeat; Transport; WD repeat. FT CHAIN 1..889 FT /note="Coatomer subunit beta'" FT /id="PRO_0000050918" FT REPEAT 11..41 FT /note="WD 1" FT REPEAT 53..83 FT /note="WD 2" FT REPEAT 95..125 FT /note="WD 3" FT REPEAT 138..169 FT /note="WD 4" FT REPEAT 182..214 FT /note="WD 5" FT REPEAT 226..256 FT /note="WD 6" FT REGION 806..889 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 832..867 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 326 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT STRAND 6..12 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 16..21 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 23..32 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 35..41 FT /evidence="ECO:0007829|PDB:4J73" FT TURN 42..45 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 46..52 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 58..64 FT /evidence="ECO:0007829|PDB:4J73" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:4J73" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 89..94 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 100..105 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 107..116 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:4J73" FT TURN 126..130 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 132..136 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 155..160 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 163..169 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 176..180 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 200..204 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:4J73" FT TURN 215..217 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 220..225 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 231..236 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 238..247 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 252..256 FT /evidence="ECO:0007829|PDB:4J73" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 262..266 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 269..278 FT /evidence="ECO:0007829|PDB:4J73" FT HELIX 283..285 FT /evidence="ECO:0007829|PDB:4J82" FT STRAND 287..291 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 294..299 FT /evidence="ECO:0007829|PDB:4J73" FT STRAND 313..318 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 327..332 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 350..354 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 360..364 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 368..375 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 378..383 FT /evidence="ECO:0007829|PDB:2YNP" FT TURN 384..386 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 389..394 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 396..400 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 404..410 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 416..420 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 423..427 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 442..448 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 453..456 FT /evidence="ECO:0007829|PDB:2YNP" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 463..467 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 471..476 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 480..487 FT /evidence="ECO:0007829|PDB:2YNP" FT TURN 490..493 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 496..502 FT /evidence="ECO:0007829|PDB:2YNP" FT HELIX 504..512 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 518..520 FT /evidence="ECO:0007829|PDB:2YNP" FT HELIX 523..525 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 526..532 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 537..542 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 545..549 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 554..558 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 563..568 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 573..579 FT /evidence="ECO:0007829|PDB:2YNP" FT TURN 580..583 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 584..589 FT /evidence="ECO:0007829|PDB:2YNP" FT STRAND 594..598 FT /evidence="ECO:0007829|PDB:2YNP" SQ SEQUENCE 889 AA; 99445 MW; 6A5E50BBEB02CB58 CRC64; MKLDIKKTFS NRSDRVKGID FHPTEPWVLT TLYSGRVELW NYETQVEVRS IQVTETPVRA GKFIARKNWI IVGSDDFRIR VFNYNTGEKV VDFEAHPDYI RSIAVHPTKP YVLSGSDDLT VKLWNWENNW ALEQTFEGHE HFVMCVAFNP KDPSTFASGC LDRTVKVWSL GQSTPNFTLT TGQERGVNYV DYYPLPDKPY MITASDDLTI KIWDYQTKSC VATLEGHMSN VSFAVFHPTL PIIISGSEDG TLKIWNSSTY KVEKTLNVGL ERSWCIATHP TGRKNYIASG FDNGFTVLSL GNDEPTLSLD PVGKLVWSGG KNAAASDIFT AVIRGNEEVE QDEPLSLQTK ELGSVDVFPQ SLAHSPNGRF VTVVGDGEYV IYTALAWRNK AFGKCQDFVW GPDSNSYALI DETGQIKYYK NFKEVTSWSV PMHSAIDRLF SGALLGVKSD GFVYFFDWDN GTLVRRIDVN AKDVIWSDNG ELVMIVNTNS NGDEASGYTL LFNKDAYLEA ANNGNIDDSE GVDEAFDVLY ELSESITSGK WVGDVFIFTT ATNRLNYFVG GKTYNLAHYT KEMYLLGYLA RDNKVYLADR EVHVYGYEIS LEVLEFQTLT LRGEIEEAIE NVLPNVEGKD SLTKIARFLE GQEYYEEALN ISPDQDQKFE LALKVGQLTL ARDLLTDESA EMKWRALGDA SLQRFNFKLA VEAFTNAHDL ESLFLLHSSF NNKEGLVTLA KDAERAGKFN LAFNAYWIAG DIQGAKDLLI KSQRFSEAAF LGSTYGLGDD AVNDIVTKWK ENLILNGKNT VSERVCGAEG LPGSSSSGDA QPLIDLDSTP APEQADENKE AEVEDSEFKE SNSEAVEAEK KEEEAPQQQQ SEQQPEQGEA VPEPVEEES //