HSC82_YEAST
ID HSC82_YEAST Reviewed; 705 AA.
AC P15108; D6W010;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=ATP-dependent molecular chaperone HSC82;
DE AltName: Full=82 kDa heat shock cognate protein;
DE AltName: Full=Heat shock protein Hsp90 constitutive isoform;
GN Name=HSC82; OrderedLocusNames=YMR186W; ORFNames=YM8010.16;
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, AND INDUCTION.
RX PubMed=2674684; DOI=10.1128/mcb.9.9.3919-3930.1989;
RA Borkovich K.A., Farrelly F.W., Finkelstein D.B., Taulien J., Lindquist S.;
RT "hsp82 is an essential protein that is required in higher concentrations
RT for growth of cells at higher temperatures.";
RL Mol. Cell. Biol. 9:3919-3930(1989).
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 PROTEIN SEQUENCE OF 2-8.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483834; DOI=10.1002/yea.320110702;
RA Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P.,
RA Perrot M.;
RT "Two-dimensional protein map of Saccharomyces cerevisiae: construction of a
RT gene-protein index.";
RL Yeast 11:601-613(1995).
RN [5]
RP INDUCTION.
RX PubMed=9296388; DOI=10.1242/jcs.110.16.1879;
RA Zarzov P., Boucherie H., Mann C.;
RT "A yeast heat shock transcription factor (Hsf1) mutant is defective in both
RT Hsc82/Hsp82 synthesis and spindle pole body duplication.";
RL J. Cell Sci. 110:1879-1891(1997).
RN [6]
RP FUNCTION, AND INTERACTION WITH CNA2.
RX PubMed=11094077; DOI=10.1128/mcb.20.24.9262-9270.2000;
RA Imai J., Yahara I.;
RT "Role of HSP90 in salt stress tolerance via stabilization and regulation of
RT calcineurin.";
RL Mol. Cell. Biol. 20:9262-9270(2000).
RN [7]
RP MUTAGENESIS OF LEU-453 AND GLU-493.
RX PubMed=12121981; DOI=10.1074/jbc.m203038200;
RA Matsumoto S., Tanaka E., Nemoto T.K., Ono T., Takagi T., Imai J.,
RA Kimura Y., Yahara I., Kobayakawa T., Ayuse T., Oi K., Mizuno A.;
RT "Interaction between the N-terminal and middle regions is essential for the
RT in vivo function of HSP90 molecular chaperone.";
RL J. Biol. Chem. 277:34959-34966(2002).
RN [8]
RP INTERACTION WITH SGT1.
RX PubMed=15340069; DOI=10.1128/mcb.24.18.8069-8079.2004;
RA Bansal P.K., Abdulle R., Kitagawa K.;
RT "Sgt1 associates with Hsp90: an initial step of assembly of the core
RT kinetochore complex.";
RL Mol. Cell. Biol. 24:8069-8079(2004).
RN [9]
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 [10]
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 [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [12]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC in cell cycle control and signal transduction such as CNA2. Undergoes a
CC functional cycle that is linked to its ATPase activity (By similarity).
CC Interacts dynamically with various co-chaperones that modulate its
CC substrate recognition, ATPase cycle and chaperone function. Required
CC for growth at high temperatures. {ECO:0000250,
CC ECO:0000269|PubMed:11094077}.
CC -!- SUBUNIT: Interacts with the co-chaperone SGT1. Interacts directly with
CC the substrate CNA2. Interacts with NAP1. {ECO:0000269|PubMed:11094077,
CC ECO:0000269|PubMed:15340069, ECO:0000269|PubMed:18086883}.
CC -!- INTERACTION:
CC P15108; Q12449: AHA1; NbExp=3; IntAct=EBI-8666, EBI-37072;
CC P15108; P08566: ARO1; NbExp=3; IntAct=EBI-8666, EBI-2883;
CC P15108; P33313: CNS1; NbExp=2; IntAct=EBI-8666, EBI-4806;
CC P15108; P47103: CPR7; NbExp=2; IntAct=EBI-8666, EBI-5436;
CC P15108; P53043: PPT1; NbExp=2; IntAct=EBI-8666, EBI-13796;
CC P15108; P38164: SEA4; NbExp=2; IntAct=EBI-8666, EBI-21365;
CC P15108; Q02821: SRP1; NbExp=2; IntAct=EBI-8666, EBI-1797;
CC P15108; P10591: SSA1; NbExp=2; IntAct=EBI-8666, EBI-8591;
CC P15108; P15705: STI1; NbExp=3; IntAct=EBI-8666, EBI-18418;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
CC -!- INDUCTION: Expressed constitutively at a high level and is moderately
CC induced by high temperatures dependent on transcription factor HSF1.
CC {ECO:0000269|PubMed:2674684, ECO:0000269|PubMed:9296388}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 132053 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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; M26044; AAA02813.1; -; Unassigned_DNA.
DR EMBL; Z49808; CAA89919.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10084.1; -; Genomic_DNA.
DR PIR; S55133; S55133.
DR RefSeq; NP_013911.1; NM_001182692.1.
DR PDB; 6XLB; EM; 3.80 A; A/B=1-705.
DR PDB; 6XLC; EM; 3.66 A; A/B=1-705.
DR PDB; 6XLD; EM; 3.66 A; A/B=1-705.
DR PDB; 6XLE; EM; 2.74 A; A/B=1-705.
DR PDB; 6XLF; EM; 3.15 A; A/B=1-705.
DR PDB; 6XLG; EM; 2.71 A; A/B=1-705.
DR PDB; 6XLH; EM; 2.83 A; A/B=1-705.
DR PDBsum; 6XLB; -.
DR PDBsum; 6XLC; -.
DR PDBsum; 6XLD; -.
DR PDBsum; 6XLE; -.
DR PDBsum; 6XLF; -.
DR PDBsum; 6XLG; -.
DR PDBsum; 6XLH; -.
DR AlphaFoldDB; P15108; -.
DR BMRB; P15108; -.
DR SMR; P15108; -.
DR BioGRID; 35364; 1514.
DR ComplexPortal; CPX-1276; HMC complex.
DR DIP; DIP-1524N; -.
DR IntAct; P15108; 178.
DR MINT; P15108; -.
DR STRING; 4932.YMR186W; -.
DR ChEMBL; CHEMBL4199; -.
DR iPTMnet; P15108; -.
DR SWISS-2DPAGE; P15108; -.
DR MaxQB; P15108; -.
DR PaxDb; P15108; -.
DR PRIDE; P15108; -.
DR TopDownProteomics; P15108; -.
DR EnsemblFungi; YMR186W_mRNA; YMR186W; YMR186W.
DR GeneID; 855224; -.
DR KEGG; sce:YMR186W; -.
DR SGD; S000004798; HSC82.
DR VEuPathDB; FungiDB:YMR186W; -.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P15108; -.
DR OMA; TRMKAEQ; -.
DR BioCyc; YEAST:G3O-32874-MON; -.
DR Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-SCE-203615; eNOS activation.
DR Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-SCE-3371511; HSF1 activation.
DR Reactome; R-SCE-3371571; HSF1-dependent transactivation.
DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-844456; The NLRP3 inflammasome.
DR Reactome; R-SCE-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P15108; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P15108; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:SGD.
DR GO; GO:0043248; P:proteasome assembly; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0070482; P:response to oxygen levels; IC:ComplexPortal.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7483834"
FT CHAIN 2..705
FT /note="ATP-dependent molecular chaperone HSC82"
FT /id="PRO_0000062958"
FT REPEAT 221..225
FT /note="1"
FT REPEAT 226..230
FT /note="2"
FT REPEAT 232..236
FT /note="3"
FT REPEAT 246..250
FT /note="4"
FT REGION 219..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..259
FT /note="4 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly
FT charged region"
FT REGION 675..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 701..705
FT /note="TPR repeat-binding"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 453
FT /note="L->A: Leads to growth defect at 37 degrees Celsius,
FT probably by disrupting the intramolecular interaction of
FT the N-termini with the middle domains; when associated with
FT A-493."
FT /evidence="ECO:0000269|PubMed:12121981"
FT MUTAGEN 493
FT /note="E->A: Leads to growth defect at 37 degrees Celsius,
FT probably by disrupting the intramolecular interaction of
FT the N-termini with the middle domains; when associated with
FT A-453."
FT /evidence="ECO:0000269|PubMed:12121981"
FT CONFLICT 619
FT /note="K -> I (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="L -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6XLE"
FT HELIX 29..49
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6XLG"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:6XLG"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:6XLG"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6XLE"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:6XLE"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:6XLG"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:6XLE"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 385..405
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 407..427
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 453..458
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 484..489
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 501..509
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 515..519
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 530..542
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 544..554
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:6XLE"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:6XLE"
FT HELIX 583..589
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 616..627
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 633..650
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 657..671
FT /evidence="ECO:0007829|PDB:6XLG"
SQ SEQUENCE 705 AA; 80900 MW; DBD41524091B1F9B CRC64;
MAGETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYQAL SDPKQLETEP
DLFIRITPKP EEKVLEIRDS GIGMTKAELI NNLGTIAKSG TKAFMEALSA GADVSMIGQF
GVGFYSLFLV ADRVQVISKN NEDEQYIWES NAGGSFTVTL DEVNERIGRG TVLRLFLKDD
QLEYLEEKRI KEVIKRHSEF VAYPIQLLVT KEVEKEVPIP EEEKKDEEKK DEDDKKPKLE
EVDEEEEEKK PKTKKVKEEV QELEELNKTK PLWTRNPSDI TQEEYNAFYK SISNDWEDPL
YVKHFSVEGQ LEFRAILFIP KRAPFDLFES KKKKNNIKLY VRRVFITDEA EDLIPEWLSF
VKGVVDSEDL PLNLSREMLQ QNKIMKVIRK NIVKKLIEAF NEIAEDSEQF DKFYSAFAKN
IKLGVHEDTQ NRAALAKLLR YNSTKSVDEL TSLTDYVTRM PEHQKNIYYI TGESLKAVEK
SPFLDALKAK NFEVLFLTDP IDEYAFTQLK EFEGKTLVDI TKDFELEETD EEKAEREKEI
KEYEPLTKAL KDILGDQVEK VVVSYKLLDA PAAIRTGQFG WSANMERIMK AQALRDSSMS
SYMSSKKTFE ISPKSPIIKE LKKRVDEGGA QDKTVKDLTN LLFETALLTS GFSLEEPTSF
ASRINRLISL GLNIDEDEET ETAPEASTEA PVEEVPADTE MEEVD
