KU80_YEAST
ID KU80_YEAST Reviewed; 629 AA.
AC Q04437; D6VZS9; Q0P737; Q0P738; Q0P741; Q0P749;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=ATP-dependent DNA helicase II subunit 2;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent DNA helicase II subunit Ku80;
DE AltName: Full=High affinity DNA-binding factor subunit 2;
DE AltName: Full=Yeast Ku80;
GN Name=YKU80; Synonyms=HDF2; OrderedLocusNames=YMR106C; ORFNames=YM9718.05C;
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].
RC STRAIN=DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, DBVPG1853,
RC DBVPG3051, DBVPG6044, DBVPG6763, DBVPG6765, SK1, Y55, and YPS128;
RX PubMed=16951060; DOI=10.1534/genetics.106.062166;
RA Liti G., Barton D.B., Louis E.J.;
RT "Sequence diversity, reproductive isolation and species concepts in
RT Saccharomyces.";
RL Genetics 174:839-850(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 PARTIAL PROTEIN SEQUENCE, FUNCTION IN TELOMERE MAINTENANCE, AND SUBUNIT.
RX PubMed=8910371; DOI=10.1074/jbc.271.44.27765;
RA Feldmann H., Driller L., Meier B., Mages G., Kellermann J.,
RA Winnacker E.-L.;
RT "HDF2, the second subunit of the Ku homologue from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 271:27765-27769(1996).
RN [5]
RP SUBUNIT.
RX PubMed=8509423; DOI=10.1016/s0021-9258(18)31470-4;
RA Feldmann H., Winnacker E.L.;
RT "A putative homologue of the human autoantigen Ku from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 268:12895-12900(1993).
RN [6]
RP FUNCTION IN TELOMERE MAINTENANCE.
RX PubMed=8972848; DOI=10.1093/nar/24.23.4639;
RA Boulton S.J., Jackson S.P.;
RT "Identification of a Saccharomyces cerevisiae Ku80 homologue: roles in DNA
RT double strand break rejoining and in telomeric maintenance.";
RL Nucleic Acids Res. 24:4639-4648(1996).
RN [7]
RP FUNCTION IN TELOMERIC GENE SILENCING.
RX PubMed=9914366; DOI=10.1007/s004120050318;
RA Evans S.K., Sistrunk M.L., Nugent C.I., Lundblad V.;
RT "Telomerase, Ku, and telomeric silencing in Saccharomyces cerevisiae.";
RL Chromosoma 107:352-358(1998).
RN [8]
RP FUNCTION IN TELOMERE MAINTENANCE, AND SUBCELLULAR LOCATION.
RX PubMed=9635192; DOI=10.1016/s0960-9822(98)70252-0;
RA Laroche T., Martin S.G., Gotta M., Gorham H.C., Pryde F.E., Louis E.J.,
RA Gasser S.M.;
RT "Mutation of yeast Ku genes disrupts the subnuclear organization of
RT telomeres.";
RL Curr. Biol. 8:653-656(1998).
RN [9]
RP FUNCTION IN DOUBLE-STRAND DNA REPAIR AND TELOMERE MAINTENANCE.
RX PubMed=9635193; DOI=10.1016/s0960-9822(98)70253-2;
RA Nugent C.I., Bosco G., Ross L.O., Evans S.K., Salinger A.P., Moore J.K.,
RA Haber J.E., Lundblad V.;
RT "Telomere maintenance is dependent on activities required for end repair of
RT double-strand breaks.";
RL Curr. Biol. 8:657-660(1998).
RN [10]
RP FUNCTION IN TELOMERE MAINTENANCE.
RX PubMed=9663392; DOI=10.1016/s0960-9822(98)70325-2;
RA Polotnianka R.M., Li J., Lustig A.J.;
RT "The yeast Ku heterodimer is essential for protection of the telomere
RT against nucleolytic and recombinational activities.";
RL Curr. Biol. 8:831-834(1998).
RN [11]
RP FUNCTION IN CHROMOSOME END PROTECTION AND TELOMERE MAINTENANCE.
RX PubMed=9563951; DOI=10.1126/science.280.5364.741;
RA Gravel S., Larrivee M., Labrecque P., Wellinger R.J.;
RT "Yeast Ku as a regulator of chromosomal DNA end structure.";
RL Science 280:741-744(1998).
RN [12]
RP FUNCTION IN NON-HOMOLOGOUS END JOINING DNA REPAIR.
RX PubMed=10675560; DOI=10.1016/s0014-5793(00)01180-7;
RA de la Torre-Ruiz M., Lowndes N.F.;
RT "The Saccharomyces cerevisiae DNA damage checkpoint is required for
RT efficient repair of double strand breaks by non-homologous end joining.";
RL FEBS Lett. 467:311-315(2000).
RN [13]
RP FUNCTION IN TELOMERASE AND CDC13 TELOMERE RECRUITMENT.
RX PubMed=11046137; DOI=10.1128/mcb.20.22.8397-8408.2000;
RA Grandin N., Damon C., Charbonneau M.;
RT "Cdc13 cooperates with the yeast Ku proteins and Stn1 to regulate
RT telomerase recruitment.";
RL Mol. Cell. Biol. 20:8397-8408(2000).
RN [14]
RP FUNCTION IN TELOMERE RECOMBINATION.
RX PubMed=12138180; DOI=10.1128/mcb.22.16.5679-5687.2002;
RA Tsai Y.-L., Tseng S.-F., Chang S.-H., Lin C.-C., Teng S.-C.;
RT "Involvement of replicative polymerases, Tel1p, Mec1p, Cdc13p, and the Ku
RT complex in telomere-telomere recombination.";
RL Mol. Cell. Biol. 22:5679-5687(2002).
RN [15]
RP FUNCTION IN TELOMERIC REPAIR AND BINDING TO TLC1 STEM LOOP.
RX PubMed=12975323; DOI=10.1101/gad.1125903;
RA Stellwagen A.E., Haimberger Z.W., Veatch J.R., Gottschling D.E.;
RT "Ku interacts with telomerase RNA to promote telomere addition at native
RT and broken chromosome ends.";
RL Genes Dev. 17:2384-2395(2003).
RN [16]
RP FUNCTION IN DOUBLE-STRAND DNA REPAIR AND TELOMERE MAINTENANCE.
RX PubMed=14585978; DOI=10.1128/mcb.23.22.8202-8215.2003;
RA Bertuch A.A., Lundblad V.;
RT "The Ku heterodimer performs separable activities at double-strand breaks
RT and chromosome termini.";
RL Mol. Cell. Biol. 23:8202-8215(2003).
RN [17]
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 [18]
RP FUNCTION IN TELOMERIC SILENCING, AND INTERACTION WITH SIR4.
RX PubMed=14551211; DOI=10.1074/jbc.m306841200;
RA Roy R., Meier B., McAinsh A.D., Feldmann H.M., Jackson S.P.;
RT "Separation-of-function mutants of yeast Ku80 reveal a Yku80p-Sir4p
RT interaction involved in telomeric silencing.";
RL J. Biol. Chem. 279:86-94(2004).
RN [19]
RP FUNCTION IN MATING-TYPE SWITCHING.
RX PubMed=16166630; DOI=10.1128/mcb.25.19.8476-8485.2005;
RA Ruan C., Workman J.L., Simpson R.T.;
RT "The DNA repair protein yKu80 regulates the function of recombination
RT enhancer during yeast mating type switching.";
RL Mol. Cell. Biol. 25:8476-8485(2005).
CC -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase.
CC Involved in non-homologous end joining (NHEJ) DNA double strand break
CC repair. DNA-binding is sequence-independent but has a high affinity to
CC nicks in double-stranded DNA and to the ends of duplex DNA. Binds to
CC naturally occurring chromosomal ends, and therefore provides
CC chromosomal end protection. Appears to have a role in recruitment of
CC telomerase and CDC13 to the telomere and the subsequent telomere
CC elongation. Required also for telomere recombination to repair
CC telomeric ends in the absence of telomerase. KU70, of the KU70/KU80
CC heterodimer, binds to the stem loop of TLC1, the RNA component of
CC telomerase. Involved in telomere maintenance. Interacts with telomeric
CC repeats and subtelomeric sequences thereby controlling telomere length
CC and protecting against subtelomeric rearrangement. Maintains telomeric
CC chromatin, which is involved in silencing the expression of genes
CC located at the telomere. Required for mating-type switching.
CC {ECO:0000269|PubMed:10675560, ECO:0000269|PubMed:11046137,
CC ECO:0000269|PubMed:12138180, ECO:0000269|PubMed:12975323,
CC ECO:0000269|PubMed:14551211, ECO:0000269|PubMed:14585978,
CC ECO:0000269|PubMed:16166630, ECO:0000269|PubMed:8910371,
CC ECO:0000269|PubMed:8972848, ECO:0000269|PubMed:9563951,
CC ECO:0000269|PubMed:9635192, ECO:0000269|PubMed:9635193,
CC ECO:0000269|PubMed:9663392, ECO:0000269|PubMed:9914366}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Heterodimer of YKU70/HDF1 and YKU80/HDF2. Interacts with SIR4.
CC {ECO:0000269|PubMed:14551211, ECO:0000269|PubMed:8509423,
CC ECO:0000269|PubMed:8910371}.
CC -!- INTERACTION:
CC Q04437; P22336: RFA1; NbExp=2; IntAct=EBI-8224, EBI-14971;
CC Q04437; P11978: SIR4; NbExp=2; IntAct=EBI-8224, EBI-17237;
CC Q04437; Q12306: SMT3; NbExp=2; IntAct=EBI-8224, EBI-17490;
CC Q04437; P32807: YKU70; NbExp=2; IntAct=EBI-8224, EBI-8214;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9635192}. Chromosome,
CC telomere {ECO:0000269|PubMed:9635192}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ku80 family. {ECO:0000305}.
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DR EMBL; AM296333; CAL35984.1; -; Genomic_DNA.
DR EMBL; AM296334; CAL35983.1; -; Genomic_DNA.
DR EMBL; AM296335; CAL35982.1; -; Genomic_DNA.
DR EMBL; AM296336; CAL35981.1; -; Genomic_DNA.
DR EMBL; AM296337; CAL35980.1; -; Genomic_DNA.
DR EMBL; AM296338; CAL35979.1; -; Genomic_DNA.
DR EMBL; AM296339; CAL35978.1; -; Genomic_DNA.
DR EMBL; AM296340; CAL35977.1; -; Genomic_DNA.
DR EMBL; AM296341; CAL35976.1; -; Genomic_DNA.
DR EMBL; AM296342; CAL35975.1; -; Genomic_DNA.
DR EMBL; AM296343; CAL35974.1; -; Genomic_DNA.
DR EMBL; AM296344; CAL35973.1; -; Genomic_DNA.
DR EMBL; AM296345; CAL35972.1; -; Genomic_DNA.
DR EMBL; Z49702; CAA89742.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10003.1; -; Genomic_DNA.
DR PIR; S54567; S54567.
DR RefSeq; NP_013824.1; NM_001182606.1.
DR PDB; 5Y58; X-ray; 2.80 A; B/D/F=2-629.
DR PDB; 5Y59; X-ray; 2.40 A; B=2-200.
DR PDBsum; 5Y58; -.
DR PDBsum; 5Y59; -.
DR AlphaFoldDB; Q04437; -.
DR SMR; Q04437; -.
DR BioGRID; 35281; 298.
DR ComplexPortal; CPX-1732; Ku70:Ku80 complex.
DR DIP; DIP-2757N; -.
DR IntAct; Q04437; 115.
DR MINT; Q04437; -.
DR STRING; 4932.YMR106C; -.
DR MaxQB; Q04437; -.
DR PaxDb; Q04437; -.
DR PRIDE; Q04437; -.
DR EnsemblFungi; YMR106C_mRNA; YMR106C; YMR106C.
DR GeneID; 855132; -.
DR KEGG; sce:YMR106C; -.
DR SGD; S000004712; YKU80.
DR VEuPathDB; FungiDB:YMR106C; -.
DR eggNOG; KOG2326; Eukaryota.
DR GeneTree; ENSGT00940000153239; -.
DR HOGENOM; CLU_029650_0_0_1; -.
DR InParanoid; Q04437; -.
DR OMA; SEVQMCV; -.
DR BioCyc; YEAST:G3O-32803-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:Q04437; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04437; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IMP:SGD.
DR GO; GO:0043564; C:Ku70:Ku80 complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0070034; F:telomerase RNA binding; IDA:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0071480; P:cellular response to gamma radiation; IBA:GO_Central.
DR GO; GO:0071481; P:cellular response to X-ray; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0007535; P:donor selection; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0097695; P:establishment of protein-containing complex localization to telomere; IMP:SGD.
DR GO; GO:0034502; P:protein localization to chromosome; IGI:SGD.
DR GO; GO:0000725; P:recombinational repair; IC:ComplexPortal.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR CDD; cd00873; KU80; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR024193; Ku80.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR PIRSF; PIRSF016570; Ku80; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromosome; Direct protein sequencing;
KW DNA damage; DNA recombination; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..629
FT /note="ATP-dependent DNA helicase II subunit 2"
FT /id="PRO_0000084339"
FT DOMAIN 254..476
FT /note="Ku"
FT REGION 608..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 149
FT /note="L -> V (in strain: DBVPG6044, SK1 and YPS128)"
FT VARIANT 301
FT /note="S -> L (in strain: DBVPG1853)"
FT VARIANT 349
FT /note="N -> D (in strain: DBVPG6044, SK1 and YPS128)"
FT VARIANT 499
FT /note="G -> D (in strain: DBVPG1853)"
FT VARIANT 518
FT /note="E -> A (in strain: DBVPG6044, SK1 and YPS128)"
FT VARIANT 528
FT /note="T -> A (in strain: DBVPG1853)"
FT VARIANT 585
FT /note="I -> S (in strain: DBVPG6763)"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:5Y59"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:5Y59"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:5Y59"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:5Y59"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:5Y59"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:5Y59"
FT HELIX 77..94
FT /evidence="ECO:0007829|PDB:5Y59"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:5Y59"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:5Y59"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:5Y59"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:5Y59"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:5Y59"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:5Y59"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5Y59"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 239..250
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 277..287
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 328..333
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 341..349
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:5Y58"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 374..389
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 392..399
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 407..418
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 426..436
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:5Y58"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 467..480
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:5Y58"
FT TURN 514..518
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 529..545
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:5Y58"
FT HELIX 577..583
FT /evidence="ECO:0007829|PDB:5Y58"
SQ SEQUENCE 629 AA; 71241 MW; 58126164EE375643 CRC64;
MSSESTTFIV DVSPSMMKNN NVSKSMAYLE YTLLNKSKKS RKTDWISCYL ANCPVSENSQ
EIPNVFQIQS FLAPVTTTAT IGFIKRLKQY CDQHSHDSSN EGLQSMIQCL LVVSLDIKQQ
FQARKILKQI VVFTDNLDDL DITDEEIDLL TEELSTRIIL IDCGKDTQEE RKKSNWLKLV
EAIPNSRIYN MNELLVEITS PATSVVKPVR VFSGELRLGA DILSTQTSNP SGSMQDENCL
CIKVEAFPAT KAVSGLNRKT AVEVEDSQKK ERYVGVKSII EYEIHNEGNK KNVSEDDQSG
SSYIPVTISK DSVTKAYRYG ADYVVLPSVL VDQTVYESFP GLDLRGFLNR EALPRYFLTS
ESSFITADTR LGCQSDLMAF SALVDVMLEN RKIAVARYVS KKDSEVNMCA LCPVLIEHSN
INSEKKFVKS LTLCRLPFAE DERVTDFPKL LDRTTTSGVP LKKETDGHQI DELMEQFVDS
MDTDELPEIP LGNYYQPIGE VTTDTTLPLP SLNKDQEENK KDPLRIPTVF VYRQQQVLLE
WIHQLMINDS REFEIPELPD SLKNKISPYT HKKFDSTKLV EVLGIKKVDK LKLDSELKTE
LEREKIPDLE TLLKRGEQHS RGSPNNSNN
