COPA_YEAST
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 03-AUG-2022, entry version 200.
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; 632.
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; P53622; -.
DR PRIDE; P53622; -.
DR EnsemblFungi; YDL145C_mRNA; YDL145C; YDL145C.
DR GeneID; 851410; -.
DR KEGG; sce:YDL145C; -.
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; ICAEYIV; -.
DR BioCyc; YEAST:G3O-29542-MON; -.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
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 Gene3D; 2.130.10.10; -; 1.
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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
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; SSF50969; SSF50969; 1.
DR SUPFAM; SSF50978; SSF50978; 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
