COPB2_YEAST
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 03-AUG-2022, entry version 199.
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}.
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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; 696.
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; P41811; -.
DR PRIDE; P41811; -.
DR EnsemblFungi; YGL137W_mRNA; YGL137W; YGL137W.
DR GeneID; 852740; -.
DR KEGG; sce:YGL137W; -.
DR SGD; S000003105; SEC27.
DR VEuPathDB; FungiDB:YGL137W; -.
DR eggNOG; KOG0276; Eukaryota.
DR GeneTree; ENSGT00900000141083; -.
DR HOGENOM; CLU_005507_1_0_1; -.
DR OMA; NVFWNES; -.
DR BioCyc; YEAST:G3O-30632-MON; -.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
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 Gene3D; 2.130.10.10; -; 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; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF04053; Coatomer_WDAD; 1.
DR Pfam; PF00400; WD40; 4.
DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 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
