SKI8_YEAST
ID SKI8_YEAST Reviewed; 397 AA.
AC Q02793; D6VTU2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Antiviral protein SKI8;
DE AltName: Full=Superkiller protein 8;
GN Name=SKI8; Synonyms=REC103; OrderedLocusNames=YGL213C;
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 [MRNA].
RX PubMed=8442386; DOI=10.1002/yea.320090106;
RA Matsumoto Y., Sarkar G., Sommer S.S., Wickner R.B.;
RT "A yeast antiviral protein, SKI8, shares a repeated amino acid sequence
RT pattern with beta-subunits of G proteins and several other proteins.";
RL Yeast 9:43-51(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9153757;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<475::aid-yea101>3.0.co;2-0;
RA Feuermann M., Simeonava L., Souciet J.-L., Potier S.;
RT "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII
RT reveals 11 open reading frames: two correspond to new genes.";
RL Yeast 13:475-477(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-245.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [6]
RP FUNCTION.
RX PubMed=6371496; DOI=10.1128/mcb.4.4.761-770.1984;
RA Ridley S.P., Sommer S.S., Wickner R.B.;
RT "Superkiller mutations in Saccharomyces cerevisiae suppress exclusion of M2
RT double-stranded RNA by L-A-HN and confer cold sensitivity in the presence
RT of M and L-A-HN.";
RL Mol. Cell. Biol. 4:761-770(1984).
RN [7]
RP FUNCTION.
RX PubMed=3029964; DOI=10.1016/0042-6822(87)90338-2;
RA Sommer S.S., Wickner R.B.;
RT "Gene disruption indicates that the only essential function of the SKI8
RT chromosomal gene is to protect Saccharomyces cerevisiae from viral
RT cytopathology.";
RL Virology 157:252-256(1987).
RN [8]
RP FUNCTION.
RX PubMed=7739557; DOI=10.1128/mcb.15.5.2763;
RA Masison D.C., Blanc A., Ribas J.C., Carroll K., Sonenberg N., Wickner R.B.;
RT "Decoying the cap- mRNA degradation system by a double-stranded RNA virus
RT and poly(A)- mRNA surveillance by a yeast antiviral system.";
RL Mol. Cell. Biol. 15:2763-2771(1995).
RN [9]
RP FUNCTION.
RX PubMed=9258672; DOI=10.1093/genetics/146.4.1265;
RA Gardiner J.M., Bullard S.A., Chrome C., Malone R.E.;
RT "Molecular and genetic analysis of REC103, an early meiotic recombination
RT gene in yeast.";
RL Genetics 146:1265-1274(1997).
RN [10]
RP FUNCTION.
RX PubMed=9482746; DOI=10.1093/emboj/17.5.1497;
RA Anderson J.S.J., Parker R.P.;
RT "The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA
RT turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases
RT of the exosome complex.";
RL EMBO J. 17:1497-1506(1998).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE SKI COMPLEX.
RX PubMed=10744028; DOI=10.1017/s1355838200991787;
RA Brown J.T., Bai X., Johnson A.W.;
RT "The yeast antiviral proteins Ski2p, Ski3p, and Ski8p exist as a complex in
RT vivo.";
RL RNA 6:449-457(2000).
RN [12]
RP INTERACTION WITH SKI7, AND FUNCTION OF THE SKI COMPLEX.
RX PubMed=11532933; DOI=10.1093/emboj/20.17.4684;
RA Araki Y., Takahashi S., Kobayashi T., Kajiho H., Hoshino S., Katada T.;
RT "Ski7p G protein interacts with the exosome and the Ski complex for 3'-to-
RT 5' mRNA decay in yeast.";
RL EMBO J. 20:4684-4693(2001).
RN [13]
RP FUNCTION OF THE SKI COMPLEX.
RX PubMed=11720286;
RA Brown J.T., Johnson A.W.;
RT "A cis-acting element known to block 3' mRNA degradation enhances
RT expression of polyA-minus mRNA in wild-type yeast cells and phenocopies a
RT ski mutant.";
RL RNA 7:1566-1577(2001).
RN [14]
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 [15]
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 [16]
RP FUNCTION.
RX PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M.,
RA Ahlquist P.;
RT "Systematic, genome-wide identification of host genes affecting replication
RT of a positive-strand RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003).
RN [17]
RP FUNCTION OF THE SKI8-SPO11 COMPLEX.
RX PubMed=15044957; DOI=10.1038/sj.emboj.7600184;
RA Kee K., Protacio R.U., Arora C., Keeney S.;
RT "Spatial organization and dynamics of the association of Rec102 and Rec104
RT with meiotic chromosomes.";
RL EMBO J. 23:1815-1824(2004).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPO11.
RX PubMed=14992724; DOI=10.1016/s1097-2765(04)00063-2;
RA Arora C., Kee K., Maleki S., Keeney S.;
RT "Antiviral protein Ski8 is a direct partner of Spo11 in meiotic DNA break
RT formation, independent of its cytoplasmic role in RNA metabolism.";
RL Mol. Cell 13:549-559(2004).
RN [19]
RP MODELING OF THE SKI COMPLEX 3D-STRUCTURE.
RX PubMed=15044803; DOI=10.1126/science.1092645;
RA Aloy P., Boettcher B., Ceulemans H., Leutwein C., Mellwig C., Fischer S.,
RA Gavin A.-C., Bork P., Superti-Furga G., Serrano L., Russell R.B.;
RT "Structure-based assembly of protein complexes in yeast.";
RL Science 303:2026-2029(2004).
RN [20]
RP FUNCTION, AND INTERACTION WITH SPO11.
RX PubMed=16816949; DOI=10.1007/s00438-006-0143-7;
RA Nag D.K., Pata J.D., Sironi M., Flood D.R., Hart A.M.;
RT "Both conserved and non-conserved regions of Spo11 are essential for
RT meiotic recombination initiation in yeast.";
RL Mol. Genet. Genomics 276:313-321(2006).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=15152089; DOI=10.1110/ps.04704704;
RA Madrona A.Y., Wilson D.K.;
RT "The structure of Ski8p, a protein regulating mRNA degradation:
RT Implications for WD protein structure.";
RL Protein Sci. 13:1557-1565(2004).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=15340168; DOI=10.1110/ps.04856504;
RA Cheng Z., Liu Y., Wang C., Parker R., Song H.;
RT "Crystal structure of Ski8p, a WD-repeat protein with dual roles in mRNA
RT metabolism and meiotic recombination.";
RL Protein Sci. 13:2673-2684(2004).
CC -!- FUNCTION: Involved in double-strand break (DSB) formation during
CC meiotic recombination through stabilization of SPO11 association with
CC meiotic chromosome and helping SPO11 to recruit other DSB proteins like
CC REC102 and REC104 to meiotic chromosomes. Also a component of the SKI
CC complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus
CC propagation by specifically blocking translation of viral mRNAs,
CC perhaps recognizing the absence of CAP or poly(A). Essential for
CC controlling the propagation of M double-stranded RNA (dsRNA) and thus
CC for preventing virus-induced cytopathology.
CC {ECO:0000269|PubMed:10744028, ECO:0000269|PubMed:11532933,
CC ECO:0000269|PubMed:11720286, ECO:0000269|PubMed:14671320,
CC ECO:0000269|PubMed:14992724, ECO:0000269|PubMed:15044957,
CC ECO:0000269|PubMed:16816949, ECO:0000269|PubMed:3029964,
CC ECO:0000269|PubMed:6371496, ECO:0000269|PubMed:7739557,
CC ECO:0000269|PubMed:9258672, ECO:0000269|PubMed:9482746}.
CC -!- SUBUNIT: Component of the SKI complex composed of at least SKI2, SKI3
CC and SKI8. The SKI complex interacts with SKI7, which makes the link
CC between the SKI complex and the exosome in order to perform mRNA
CC degradation. {ECO:0000269|PubMed:10744028, ECO:0000269|PubMed:11532933,
CC ECO:0000269|PubMed:14992724, ECO:0000269|PubMed:16816949}.
CC -!- INTERACTION:
CC Q02793; P35207: SKI2; NbExp=11; IntAct=EBI-17260, EBI-1851;
CC Q02793; P17883: SKI3; NbExp=8; IntAct=EBI-17260, EBI-1861;
CC Q02793; Q08491: SKI7; NbExp=3; IntAct=EBI-17260, EBI-1389;
CC Q02793; P23179: SPO11; NbExp=9; IntAct=EBI-17260, EBI-17705;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome. Note=Relocalizes
CC from the cytoplasm to the nucleus and is recruited to chromosomes by
CC SPO11 during meiotic prophase.
CC -!- MISCELLANEOUS: Present with 1710 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M96058; AAA35050.1; -; mRNA.
DR EMBL; Z72736; CAA96930.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07903.1; -; Genomic_DNA.
DR PIR; S30023; S30023.
DR RefSeq; NP_011302.1; NM_001181078.1.
DR PDB; 1S4U; X-ray; 2.10 A; X=1-397.
DR PDB; 1SQ9; X-ray; 1.90 A; A=1-397.
DR PDB; 4BUJ; X-ray; 3.70 A; C/D/G/H=1-397.
DR PDB; 5MC6; EM; 3.80 A; j/k=1-397.
DR PDBsum; 1S4U; -.
DR PDBsum; 1SQ9; -.
DR PDBsum; 4BUJ; -.
DR PDBsum; 5MC6; -.
DR AlphaFoldDB; Q02793; -.
DR SMR; Q02793; -.
DR BioGRID; 33043; 252.
DR ComplexPortal; CPX-1040; SKI complex.
DR DIP; DIP-1653N; -.
DR IntAct; Q02793; 21.
DR MINT; Q02793; -.
DR STRING; 4932.YGL213C; -.
DR CarbonylDB; Q02793; -.
DR iPTMnet; Q02793; -.
DR MaxQB; Q02793; -.
DR PaxDb; Q02793; -.
DR PRIDE; Q02793; -.
DR EnsemblFungi; YGL213C_mRNA; YGL213C; YGL213C.
DR GeneID; 852659; -.
DR KEGG; sce:YGL213C; -.
DR SGD; S000003181; SKI8.
DR VEuPathDB; FungiDB:YGL213C; -.
DR eggNOG; KOG4155; Eukaryota.
DR GeneTree; ENSGT00940000153533; -.
DR HOGENOM; CLU_065016_0_0_1; -.
DR InParanoid; Q02793; -.
DR OMA; CVCLDRS; -.
DR BioCyc; YEAST:G3O-30690-MON; -.
DR Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR EvolutionaryTrace; Q02793; -.
DR PRO; PR:Q02793; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q02793; protein.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IBA:GO_Central.
DR GO; GO:0000228; C:nuclear chromosome; IDA:SGD.
DR GO; GO:0055087; C:Ski complex; IDA:SGD.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IMP:SGD.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IDA:ComplexPortal.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IMP:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR GO; GO:0065004; P:protein-DNA complex assembly; IMP:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
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; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Chromosome; Cytoplasm; Meiosis; Nucleus;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..397
FT /note="Antiviral protein SKI8"
FT /id="PRO_0000051218"
FT REPEAT 21..42
FT /note="WD 1"
FT REPEAT 67..101
FT /note="WD 2"
FT REPEAT 126..157
FT /note="WD 3"
FT REPEAT 191..213
FT /note="WD 4"
FT REPEAT 238..264
FT /note="WD 5"
FT REPEAT 296..319
FT /note="WD 6"
FT REPEAT 359..392
FT /note="WD 7"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:1SQ9"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:1SQ9"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1SQ9"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1SQ9"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 150..160
FT /evidence="ECO:0007829|PDB:1SQ9"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1SQ9"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:1SQ9"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:1SQ9"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:1SQ9"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:1SQ9"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1SQ9"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:1SQ9"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:1SQ9"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:1SQ9"
FT STRAND 387..394
FT /evidence="ECO:0007829|PDB:1SQ9"
SQ SEQUENCE 397 AA; 44232 MW; C5E7B9D2268F9727 CRC64;
MSKVFIATAN AGKAHDADIF SVSACNSFTV SCSGDGYLKV WDNKLLDNEN PKDKSYSHFV
HKSGLHHVDV LQAIERDAFE LCLVATTSFS GDLLFYRITR EDETKKVIFE KLDLLDSDMK
KHSFWALKWG ASNDRLLSHR LVATDVKGTT YIWKFHPFAD ESNSLTLNWS PTLELQGTVE
SPMTPSQFAT SVDISERGLI ATGFNNGTVQ ISELSTLRPL YNFESQHSMI NNSNSIRSVK
FSPQGSLLAI AHDSNSFGCI TLYETEFGER IGSLSVPTHS SQASLGEFAH SSWVMSLSFN
DSGETLCSAG WDGKLRFWDV KTKERITTLN MHCDDIEIEE DILAVDEHGD SLAEPGVFDV
KFLKKGWRSG MGADLNESLC CVCLDRSIRW FREAGGK
