SKI7_YEAST
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 03-AUG-2022, entry version 168.
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}.
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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 PDBsum; 4ZKD; -.
DR PDBsum; 4ZKE; -.
DR PDBsum; 5G06; -.
DR PDBsum; 5JEA; -.
DR AlphaFoldDB; Q08491; -.
DR SMR; Q08491; -.
DR BioGRID; 34475; 166.
DR DIP; DIP-995N; -.
DR IntAct; Q08491; 17.
DR MINT; Q08491; -.
DR STRING; 4932.YOR076C; -.
DR iPTMnet; Q08491; -.
DR MaxQB; Q08491; -.
DR PaxDb; Q08491; -.
DR PRIDE; Q08491; -.
DR EnsemblFungi; YOR076C_mRNA; YOR076C; YOR076C.
DR GeneID; 854243; -.
DR KEGG; sce:YOR076C; -.
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 BioCyc; YEAST:G3O-33613-MON; -.
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 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; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR Pfam; PF00009; GTP_EFTU; 1.
DR SUPFAM; SSF52540; SSF52540; 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
