ID   COPA_YEAST              Reviewed;        1201 AA.
AC   P53622; D6VRK3; Q07595;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=Coatomer subunit alpha;
DE   AltName: Full=Alpha-coat protein;
DE            Short=Alpha-COP;
DE   AltName: Full=Retrieval from endoplasmic reticulum protein 1;
DE   AltName: Full=Secretory protein 22;
DE   AltName: Full=Suppressor of osmo-sensitivity 1;
GN   Name=COP1; Synonyms=RET1, SEC33, SOO1; OrderedLocusNames=YDL145C;
GN   ORFNames=D1578;
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 1-20.
RC   STRAIN=PC70;
RX   PubMed=8001155; DOI=10.1016/0092-8674(94)90011-6;
RA   Letourneur F., Gaynor E.C., Hennecke S., Demolliere C., Durden R.,
RA   Emr S.D., Riezman H., Cosson P.;
RT   "Coatomer is essential for retrieval of dilysine-tagged proteins to the
RT   endoplasmic reticulum.";
RL   Cell 79:1199-1207(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=RS453;
RX   PubMed=7724544; DOI=10.1073/pnas.92.8.3229;
RA   Gerich B., Orci L., Tschochner H., Lottspeich F., Ravazolla M., Amherdt M.,
RA   Wieland F., Harter C.;
RT   "Non-clathrin-coat protein alpha is a conserved subunit of coatomer and in
RT   Saccharomyces cerevisiae is essential for growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3229-3233(1995).
RN   [3]
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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 799-1201.
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8972581;
RX   DOI=10.1002/(sici)1097-0061(199612)12:15%3c1587::aid-yea46%3e3.0.co;2-6;
RA   Delaveau T.T.D., Blugeon C., Jacq C., Perea J.;
RT   "Analysis of a 23 kb region on the left arm of yeast chromosome IV.";
RL   Yeast 12:1587-1592(1996).
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   INTERACTION WITH KEI1.
RX   PubMed=19726565; DOI=10.1091/mbc.e09-03-0235;
RA   Sato K., Noda Y., Yoda K.;
RT   "Kei1: a novel subunit of inositolphosphorylceramide synthase, essential
RT   for its enzyme activity and Golgi localization.";
RL   Mol. Biol. Cell 20:4444-4457(2009).
RN   [11]
RP   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   [12]
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. Interacts with KEI1 (via C-terminal region).
CC       {ECO:0000269|PubMed:17101773, ECO:0000269|PubMed:19726565}.
CC   -!- INTERACTION:
CC       P53622; P41811: SEC27; NbExp=17; IntAct=EBI-4860, EBI-4898;
CC       P53622; P40509: SEC28; NbExp=11; IntAct=EBI-4860, EBI-4884;
CC       P53622; P33767: WBP1; NbExp=3; IntAct=EBI-4860, EBI-12658;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral
CC       membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC       Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side
CC       of the Golgi, as well as on the vesicles/buds originating from it.
CC   -!- MISCELLANEOUS: Present with 15200 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z46617; CAA86588.1; -; Genomic_DNA.
DR   EMBL; X83754; CAA58712.1; -; Genomic_DNA.
DR   EMBL; Z74193; CAA98719.1; -; Genomic_DNA.
DR   EMBL; Z74192; CAA98718.1; -; Genomic_DNA.
DR   EMBL; X97751; CAA66346.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11713.1; -; Genomic_DNA.
DR   PIR; S67692; ERBYA.
DR   RefSeq; NP_010136.1; NM_001180205.1.
DR   PDB; 3MKQ; X-ray; 2.50 A; B/D/F=642-818.
DR   PDB; 3MV2; X-ray; 2.90 A; A/C/E=900-1201.
DR   PDB; 3MV3; X-ray; 3.25 A; A/C/E=900-1201.
DR   PDB; 6U3W; X-ray; 2.39 A; A=899-1201.
DR   PDBsum; 3MKQ; -.
DR   PDBsum; 3MV2; -.
DR   PDBsum; 3MV3; -.
DR   PDBsum; 6U3W; -.
DR   AlphaFoldDB; P53622; -.
DR   SMR; P53622; -.
DR   BioGRID; 31916; 653.
DR   ComplexPortal; CPX-1652; COPI vesicle coat complex.
DR   DIP; DIP-2582N; -.
DR   IntAct; P53622; 73.
DR   MINT; P53622; -.
DR   STRING; 4932.YDL145C; -.
DR   TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR   CarbonylDB; P53622; -.
DR   iPTMnet; P53622; -.
DR   MaxQB; P53622; -.
DR   PaxDb; 4932-YDL145C; -.
DR   PeptideAtlas; P53622; -.
DR   EnsemblFungi; YDL145C_mRNA; YDL145C; YDL145C.
DR   GeneID; 851410; -.
DR   KEGG; sce:YDL145C; -.
DR   AGR; SGD:S000002304; -.
DR   SGD; S000002304; COP1.
DR   VEuPathDB; FungiDB:YDL145C; -.
DR   eggNOG; KOG0292; Eukaryota.
DR   GeneTree; ENSGT00940000155451; -.
DR   HOGENOM; CLU_007565_1_0_1; -.
DR   InParanoid; P53622; -.
DR   OMA; EMTYQKQ; -.
DR   OrthoDB; 20819at2759; -.
DR   BioCyc; YEAST:G3O-29542-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; 851410; 6 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P53622; -.
DR   PRO; PR:P53622; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P53622; 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:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:SGD.
DR   CDD; cd22948; Coatomer_WDAD_alpha; 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; IPR047312; Coatomer_alpha_WD-assoc_reg.
DR   InterPro; IPR016391; Coatomer_asu.
DR   InterPro; IPR010714; Coatomer_asu_C.
DR   InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19876; COATOMER; 1.
DR   PANTHER; PTHR19876:SF1; COATOMER SUBUNIT ALPHA; 1.
DR   Pfam; PF04053; Coatomer_WDAD; 1.
DR   Pfam; PF06957; COPI_C; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
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; Protein transport;
KW   Reference proteome; Repeat; Transport; WD repeat.
FT   CHAIN           1..1201
FT                   /note="Coatomer subunit alpha"
FT                   /id="PRO_0000050910"
FT   REPEAT          9..39
FT                   /note="WD 1"
FT   REPEAT          51..81
FT                   /note="WD 2"
FT   REPEAT          93..123
FT                   /note="WD 3"
FT   REPEAT          135..165
FT                   /note="WD 4"
FT   REPEAT          207..237
FT                   /note="WD 5"
FT   REPEAT          251..281
FT                   /note="WD 6"
FT   REGION          842..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        753
FT                   /note="F -> L (in Ref. 1; CAA86588 and 2; CAA58712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        905
FT                   /note="I -> T (in Ref. 1; CAA86588 and 2; CAA58712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1006
FT                   /note="P -> L (in Ref. 1; CAA86588 and 2; CAA58712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1027..1028
FT                   /note="DA -> NT (in Ref. 1; CAA86588 and 2; CAA58712)"
FT                   /evidence="ECO:0000305"
FT   HELIX           649..658
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           662..672
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           675..687
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           691..700
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           704..714
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           717..729
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           733..743
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           746..755
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           759..768
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           772..781
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           786..788
FT                   /evidence="ECO:0007829|PDB:3MKQ"
FT   HELIX           900..907
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           911..917
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           920..931
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           937..939
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           940..949
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          951..954
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          957..961
FT                   /evidence="ECO:0007829|PDB:3MV3"
FT   STRAND          964..967
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          969..971
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          973..975
FT                   /evidence="ECO:0007829|PDB:3MV2"
FT   HELIX           977..979
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           987..1002
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           1006..1021
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          1025..1027
FT                   /evidence="ECO:0007829|PDB:3MV3"
FT   HELIX           1028..1055
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   TURN            1059..1061
FT                   /evidence="ECO:0007829|PDB:3MV3"
FT   HELIX           1062..1072
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           1079..1095
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           1099..1110
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           1117..1132
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          1135..1137
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          1147..1149
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   TURN            1151..1153
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          1156..1158
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          1163..1165
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   TURN            1167..1169
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          1172..1174
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           1175..1177
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          1179..1181
FT                   /evidence="ECO:0007829|PDB:3MV3"
FT   TURN            1183..1185
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          1186..1189
FT                   /evidence="ECO:0007829|PDB:6U3W"
SQ   SEQUENCE   1201 AA;  135607 MW;  D3589073106F5570 CRC64;
     MKMLTKFESK STRAKGIAFH PSRPWVLVAL FSSTIQLWDY RMGTLLHRFE DHEGPVRGLD
     FHPTQPIFVS AGDDYTIKVW SLDTNKCLYT LTGHLDYVRT VFFHRELPWI ISASDDQTIR
     IWNWQNRKEI ACLTGHNHFV MCAQFHPTDD LIVSASLDET IRIWDISGLR KRHSAPGTSS
     FEEQMSAQQN LLDGSLGDCV VKFILEGHTR GVNWASFHPT LPLIVSGSDD RQVKLWRMSA
     TKAWEVDTCR GHTNNVDSVI FHPHQNLIIS VGEDKTLRVW DLDKRTPVKQ FKRENDRFWL
     IAAHPHINLF GAAHDSGIMV FKLDRERPCS FIHQNQLFFV NAEKQIQSFN FQKRVASLPY
     ASLKGIGQPW DAFRSISYNP SQHSVLVNEA NGKFALVILP KQPVGAVEPT SVTQDTGNFA
     TFVGRNRFVV YNKNTESVEV RSLENKVTRN IKVEETVRTI VAAGPGSVLV IHPREVILYD
     VQQGKKVSQL AVKNVKYVSW SLDGQYVALM SKHTITLATK KLELINSMHE TIRIKSAAWD
     ETGVLIYSTL NHIRYSLLNG DRGIIKTLEK TLYITKVQGK LVYCLNREGE IEILTIDPTE
     YRFKKALVNK NFPEVLRLIK DSNLVGQNII SYLQKSGYPE IALQFVQDPH IRFDLALEYG
     NLDVALDEAK KLNDSSTWER LIQEALAQGN ASLAEMIYQT QHSFDKLSFL YLVTGDVNKL
     SKMQNIAQTR EDFGSMLLNT FYNNSTKERS SIFAEGGSLP LAYAVAKANG DEAAASAFLE
     QAEVDEQDVT LPDQMDASNF VQRPVISKPL EKWPLKEAEL SYFEKAVLGQ IDDLTIDDET
     PAVNTTQEQE EPLGEENFND EDIGEDEGAW DLGDEDLDVG EELPEEVEQG EITSPAQEVE
     TAIWIKNSKL PAVLVAAGAF DAAVQALSKQ VGVVKLEPLK KYFTNIYEGC RTYIPSTPCE
     LPAQLGYVRA YDDTVSEDQI LPYVPGLDVV NEKMNEGYKN FKLNKPDIAI ECFREAIYRI
     TLLMVDDAED EKLAHKILET AREYILGLSI ELERRSLKEG NTVRMLELAA YFTKAKLSPI
     HRTNALQVAM SQHFKHKNFL QASYFAGEFL KIISSGPRAE QARKIKNKAD SMASDAIPID
     FDPYAKFDIC AATYKPIYED TPSVSDPLTG SKYVITEKDK IDRIAMISKI GAPASGLRIR
     V
//