ID SKI7_YEAST Reviewed; 747 AA. AC Q08491; D6W2D9; O00032; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 173. DE RecName: Full=Superkiller protein 7; GN Name=SKI7; OrderedLocusNames=YOR076C; ORFNames=YOR29-27; 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]. RX PubMed=9133743; RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g; RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.; RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the RT presence of two tRNAs and 24 new open reading frames."; RL Yeast 13:379-390(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [3] 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 [4] 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 [5] RP FUNCTION. RX PubMed=10074137; DOI=10.1128/jvi.73.4.2893-2900.1999; RA Benard L., Carroll K., Valle R.C.P., Masison D.C., Wickner R.B.; RT "The ski7 antiviral protein is an EF1-alpha homolog that blocks expression RT of non-Poly(A) mRNA in Saccharomyces cerevisiae."; RL J. Virol. 73:2893-2900(1999). RN [6] RP FUNCTION. RX PubMed=11027292; DOI=10.1128/mcb.20.21.8230-8243.2000; RA van Hoof A., Staples R.R., Baker R.E., Parker R.; RT "Function of the ski4p (Csl4p) and Ski7p proteins in 3'-to-5' degradation RT of mRNA."; RL Mol. Cell. Biol. 20:8230-8243(2000). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH THE EXOSOME RP AND SKI COMPLEXES. 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 [8] RP FUNCTION. RX PubMed=11514438; DOI=10.1093/genetics/158.4.1445; RA He W., Parker R.; RT "The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3' termini from RT partial degradation."; RL Genetics 158:1445-1455(2001). RN [9] RP FUNCTION, AND INTERACTION WITH THE EXOSOME COMPLEX. RX PubMed=11910110; DOI=10.1126/science.1067272; RA van Hoof A., Frischmeyer P.A., Dietz H.C., Parker R.; RT "Exosome-mediated recognition and degradation of mRNAs lacking a RT termination codon."; RL Science 295:2262-2264(2002). RN [10] RP FUNCTION, AND INTERACTION WITH NAM7. RX PubMed=12881429; DOI=10.1093/emboj/cdg374; RA Takahashi S., Araki Y., Sakuno T., Katada T.; RT "Interaction between Ski7p and Upf1p is required for nonsense-mediated 3'- RT to-5' mRNA decay in yeast."; RL EMBO J. 22:3951-3959(2003). RN [11] RP FUNCTION. RX PubMed=12769863; DOI=10.1016/s1097-2765(03)00190-4; RA Mitchell P., Tollervey D.; RT "An NMD pathway in yeast involving accelerated deadenylation and exosome- RT mediated 3'-->5' degradation."; RL Mol. Cell 11:1405-1413(2003). RN [12] 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 [13] 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 [14] RP SUBCELLULAR LOCATION. RX PubMed=12730603; DOI=10.1126/science.1082320; RA Sheth U., Parker R.; RT "Decapping and decay of messenger RNA occur in cytoplasmic processing RT bodies."; RL Science 300:805-808(2003). RN [15] RP FUNCTION. RX PubMed=15933721; DOI=10.1038/sj.emboj.7600636; RA Inada T., Aiba H.; RT "Translation of aberrant mRNAs lacking a termination codon or with a RT shortened 3'-UTR is repressed after initiation in yeast."; RL EMBO J. 24:1584-1595(2005). RN [16] RP INTERACTION WITH SKI3 AND SKI8. RX PubMed=16043509; DOI=10.1261/rna.2060405; RA Wang L., Lewis M.S., Johnson A.W.; RT "Domain interactions within the Ski2/3/8 complex and between the Ski RT complex and Ski7p."; RL RNA 11:1291-1302(2005). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH THE EXOSOME. RX PubMed=17173052; DOI=10.1038/nsmb1184; RA Dziembowski A., Lorentzen E., Conti E., Seraphin B.; RT "A single subunit, Dis3, is essentially responsible for yeast exosome core RT activity."; RL Nat. Struct. Mol. Biol. 14:15-22(2007). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-90, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). CC -!- FUNCTION: Represses the expression of non-poly(A) mRNAs like L-A or M CC viruses and is therefore involved in antiviral system. Mediates CC interactions via its N-terminus between the exosome and the SKI complex CC which operate in the 3'-to-5' mRNA-decay pathway. By interacting with CC NAM7, is also required for nonsense-mediated 3'-to-5' mRNA-decay (NMD). CC May recognize a stalled 80S ribosome at the 3'-end of a nonstop mRNA CC which leads to the recruitment of the exosome and SKI complexes to the CC mRNAs to be degraded. {ECO:0000269|PubMed:10074137, CC ECO:0000269|PubMed:11027292, ECO:0000269|PubMed:11514438, CC ECO:0000269|PubMed:11532933, ECO:0000269|PubMed:11910110, CC ECO:0000269|PubMed:12769863, ECO:0000269|PubMed:12881429, CC ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:15933721, CC ECO:0000269|PubMed:6371496}. CC -!- SUBUNIT: Interacts with the exosome and with the SKI complex composed CC of at least SKI2, SKI3 and SKI8. Interacts directly with SKI3 and SKI8. CC {ECO:0000269|PubMed:11532933, ECO:0000269|PubMed:11910110, CC ECO:0000269|PubMed:12881429, ECO:0000269|PubMed:16043509, CC ECO:0000269|PubMed:17173052}. CC -!- INTERACTION: CC Q08491; P53859: CSL4; NbExp=4; IntAct=EBI-1389, EBI-1731; CC Q08491; P17883: SKI3; NbExp=2; IntAct=EBI-1389, EBI-1861; CC Q08491; Q02793: SKI8; NbExp=3; IntAct=EBI-1389, EBI-17260; CC Q08491; Q92900: UPF1; Xeno; NbExp=2; IntAct=EBI-1389, EBI-373471; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11532933, CC ECO:0000269|PubMed:12730603}. CC -!- DOMAIN: The N-terminal domain (residues 1 to 264) is required and CC sufficient for interaction with the exosome and SKI complexes and for CC 3'-to-5' mRNA degradation. {ECO:0000269|PubMed:11532933}. CC -!- MISCELLANEOUS: Present with 233 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. CC {ECO:0000255|PROSITE-ProRule:PRU01059}. 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; Z70678; CAA94561.1; -; Genomic_DNA. DR EMBL; Z74984; CAA99269.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10855.1; -; Genomic_DNA. DR PIR; S66959; S66959. DR RefSeq; NP_014719.1; NM_001183495.1. DR PDB; 4ZKD; X-ray; 2.18 A; A=254-747. DR PDB; 4ZKE; X-ray; 2.25 A; A=254-747. DR PDB; 5G06; EM; 4.20 A; P=1-747. DR PDB; 5JEA; X-ray; 2.65 A; K=116-225. DR PDB; 8QCA; EM; 2.84 A; E=1-235. DR PDB; 8QCB; EM; 2.80 A; E=1-235. DR PDBsum; 4ZKD; -. DR PDBsum; 4ZKE; -. DR PDBsum; 5G06; -. DR PDBsum; 5JEA; -. DR PDBsum; 8QCA; -. DR PDBsum; 8QCB; -. DR AlphaFoldDB; Q08491; -. DR EMDB; EMD-18326; -. DR EMDB; EMD-18328; -. DR SMR; Q08491; -. DR BioGRID; 34475; 173. DR DIP; DIP-995N; -. DR IntAct; Q08491; 17. DR MINT; Q08491; -. DR STRING; 4932.YOR076C; -. DR iPTMnet; Q08491; -. DR MaxQB; Q08491; -. DR PaxDb; 4932-YOR076C; -. DR PeptideAtlas; Q08491; -. DR EnsemblFungi; YOR076C_mRNA; YOR076C; YOR076C. DR GeneID; 854243; -. DR KEGG; sce:YOR076C; -. DR AGR; SGD:S000005602; -. DR SGD; S000005602; SKI7. DR VEuPathDB; FungiDB:YOR076C; -. DR eggNOG; KOG0458; Eukaryota. DR GeneTree; ENSGT00940000169696; -. DR HOGENOM; CLU_374747_0_0_1; -. DR InParanoid; Q08491; -. DR OMA; FETFSHN; -. DR OrthoDB; 2022804at2759; -. DR BioCyc; YEAST:G3O-33613-MONOMER; -. DR Reactome; R-SCE-156842; Eukaryotic Translation Elongation. DR Reactome; R-SCE-3371511; HSF1 activation. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR Reactome; R-SCE-8876725; Protein methylation. DR BioGRID-ORCS; 854243; 0 hits in 10 CRISPR screens. DR PRO; PR:Q08491; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; Q08491; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005829; C:cytosol; HDA:SGD. DR GO; GO:0005525; F:GTP binding; IDA:SGD. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD. DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central. DR GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD. 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'; IMP:SGD. DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IMP:SGD. DR GO; GO:0030163; P:protein catabolic process; IMP:SGD. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR GO; GO:0006414; P:translational elongation; IBA:GO_Central. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1. DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; GTP-binding; Nonsense-mediated mRNA decay; KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis; KW Reference proteome; Repressor; Translation regulation. FT CHAIN 1..747 FT /note="Superkiller protein 7" FT /id="PRO_0000269648" FT DOMAIN 265..503 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 14..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 89..117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 274..281 FT /note="G1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 331..335 FT /note="G2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 356..359 FT /note="G3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 427..430 FT /note="G4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 467..469 FT /note="G5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT COMPBIAS 32..51 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 274..281 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 356..360 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 427..430 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 88 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT HELIX 121..131 FT /evidence="ECO:0007829|PDB:5JEA" FT HELIX 150..155 FT /evidence="ECO:0007829|PDB:5JEA" FT STRAND 185..189 FT /evidence="ECO:0007829|PDB:5JEA" FT HELIX 197..208 FT /evidence="ECO:0007829|PDB:5JEA" FT HELIX 212..225 FT /evidence="ECO:0007829|PDB:5JEA" FT HELIX 258..262 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 266..273 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 280..290 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 296..305 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 306..309 FT /evidence="ECO:0007829|PDB:4ZKD" FT TURN 311..313 FT /evidence="ECO:0007829|PDB:4ZKE" FT HELIX 318..321 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 325..330 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 337..341 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 350..356 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 361..364 FT /evidence="ECO:0007829|PDB:4ZKD" FT TURN 365..367 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 368..375 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 378..385 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 390..393 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 401..409 FT /evidence="ECO:0007829|PDB:4ZKD" FT TURN 410..415 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 422..427 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 429..432 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 436..452 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 458..460 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 461..465 FT /evidence="ECO:0007829|PDB:4ZKD" FT TURN 468..471 FT /evidence="ECO:0007829|PDB:4ZKD" FT HELIX 504..515 FT /evidence="ECO:0007829|PDB:4ZKD" FT TURN 522..524 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 528..536 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 542..558 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 562..566 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 568..571 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 573..583 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 593..595 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 597..600 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 604..612 FT /evidence="ECO:0007829|PDB:4ZKD" FT TURN 617..619 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 629..632 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 648..660 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 673..678 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 681..691 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 696..698 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 703..710 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 717..722 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 728..732 FT /evidence="ECO:0007829|PDB:4ZKD" FT STRAND 738..744 FT /evidence="ECO:0007829|PDB:4ZKD" SQ SEQUENCE 747 AA; 84779 MW; D93B956D02050BFA CRC64; MSLLEQLARK RIEKSKGLLS ADQSHSTSKS ASLLERLHKN RETKDNNAET KRKDLKTLLA KDKVKRSDFT PNQHSVSLSL KLSALKKSNS DLEKQGKSVT LDSKENELPT KRKSPDDKLN LEESWKAIKE MNHYCFLKND PCINQTDDFA FTNFIIKDKK NSLSTSIPLS SQNSSFLSLK KHNNELLGIF VPCNLPKTTR KVAIENFNRP SPDDIIQSAQ LNAFNEKLEN LNIKSVPKAE KKEPINLQTP PTESIDIHSF IATHPLNLTC LFLGDTNAGK STLLGHLLYD LNEISMSSMR ELQKKSSNLD PSSSNSFKVI LDNTKTEREN GFSMFKKVIQ VENDLLPPSS TLTLIDTPGS IKYFNKETLN SILTFDPEVY VLVIDCNYDS WEKSLDGPNN QIYEILKVIS YLNKNSACKK HLIILLNKAD LISWDKHRLE MIQSELNYVL KENFQWTDAE FQFIPCSGLL GSNLNKTENI TKSKYKSEFD SINYVPEWYE GPTFFSQLYL LVEHNMNKIE TTLEEPFVGT ILQSSVLQPI AEINYVSLKV LINSGYIQSG QTIEIHTQYE DFHYYGIVSR MKNSKQILET NTKNNISVGL NPDILEVLVK IHNTEDFTKK QFHIRKGDII IHSRKTNTLS PNLPNTLKLL ALRLIKLSIQ THALSDPVDL GSELLLYHNL THNAVKLVKI LGTNDISINP NQSLIVEVEI IEPDFALNVI DSKYITNNIV LTSIDHKVIA VGRIACQ //