SSB2_YEAST
ID SSB2_YEAST Reviewed; 613 AA.
AC P40150; D6W0Y1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ribosome-associated molecular chaperone SSB2 {ECO:0000303|PubMed:11739779};
DE EC=3.6.4.10;
DE AltName: Full=Heat shock protein SSB2 {ECO:0000303|PubMed:3302682};
DE AltName: Full=Hsp70 chaperone Ssb;
GN Name=SSB2 {ECO:0000303|PubMed:3302682};
GN Synonyms=YG103 {ECO:0000303|PubMed:6761581};
GN OrderedLocusNames=YNL209W {ECO:0000312|SGD:S000005153}; ORFNames=N1333;
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=ATCC 96604 / S288c / FY1679;
RX PubMed=7725799; DOI=10.1002/yea.320101213;
RA Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.;
RT "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries
RT WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8
RT new open reading frames of unknown function.";
RL Yeast 10:1639-1645(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-535.
RX PubMed=6761581; DOI=10.1128/mcb.2.11.1388-1398.1982;
RA Ingolia T.D., Slater M.R., Craig E.A.;
RT "Saccharomyces cerevisiae contains a complex multigene family related to
RT the major heat shock-inducible gene of Drosophila.";
RL Mol. Cell. Biol. 2:1388-1398(1982).
RN [5]
RP PROTEIN SEQUENCE OF 39-49 AND 431-439.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=7737086; DOI=10.1002/elps.1150160124;
RA Norbeck J., Blomberg A.;
RT "Gene linkage of two-dimensional polyacrylamide gel electrophoresis
RT resolved proteins from isogene families in Saccharomyces cerevisiae by
RT microsequencing of in-gel trypsin generated peptides.";
RL Electrophoresis 16:149-156(1995).
RN [6]
RP GENE FAMILY.
RX PubMed=3302682; DOI=10.1128/mcb.7.7.2568-2577.1987;
RA Werner-Washburne M., Stone D.E., Craig E.A.;
RT "Complex interactions among members of an essential subfamily of hsp70
RT genes in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 7:2568-2577(1987).
RN [7]
RP INDUCTION.
RX PubMed=2651414; DOI=10.1128/jb.171.5.2680-2688.1989;
RA Werner-Washburne M., Becker J., Kosic-Smithers J., Craig E.A.;
RT "Yeast Hsp70 RNA levels vary in response to the physiological status of the
RT cell.";
RL J. Bacteriol. 171:2680-2688(1989).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1394434; DOI=10.1016/0092-8674(92)90269-i;
RA Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E.A.;
RT "The translation machinery and 70 kd heat shock protein cooperate in
RT protein synthesis.";
RL Cell 71:97-105(1992).
RN [9]
RP ACETYLATION AT ALA-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9670014; DOI=10.1093/emboj/17.14.3981;
RA Pfund C., Lopez-Hoyo N., Ziegelhoffer T., Schilke B.A., Lopez-Buesa P.,
RA Walter W.A., Wiedmann M., Craig E.A.;
RT "The molecular chaperone Ssb from Saccharomyces cerevisiae is a component
RT of the ribosome-nascent chain complex.";
RL EMBO J. 17:3981-3989(1998).
RN [11]
RP INDUCTION.
RX PubMed=10322015; DOI=10.1128/jb.181.10.3136-3143.1999;
RA Lopez N., Halladay J., Walter W., Craig E.A.;
RT "SSB, encoding a ribosome-associated chaperone, is coordinately regulated
RT with ribosomal protein genes.";
RL J. Bacteriol. 181:3136-3143(1999).
RN [12]
RP FUNCTION.
RX PubMed=11739779; DOI=10.1091/mbc.12.12.3773;
RA Pfund C., Huang P., Lopez-Hoyo N., Craig E.A.;
RT "Divergent functional properties of the ribosome-associated molecular
RT chaperone Ssb compared with other Hsp70s.";
RL Mol. Biol. Cell 12:3773-3782(2001).
RN [13]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11929994; DOI=10.1073/pnas.062048599;
RA Gautschi M., Mun A., Ross S., Rospert S.;
RT "A functional chaperone triad on the yeast ribosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4209-4214(2002).
RN [14]
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 [15]
RP INTERACTION WITH SSE1.
RX PubMed=16219770; DOI=10.1074/jbc.m503615200;
RA Yam A.Y., Albanese V., Lin H.T., Frydman J.;
RT "Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for
RT de novo folding.";
RL J. Biol. Chem. 280:41252-41261(2005).
RN [16]
RP FUNCTION, AND INTERACTION WITH SSE1.
RX PubMed=16221677; DOI=10.1074/jbc.m503614200;
RA Shaner L., Wegele H., Buchner J., Morano K.A.;
RT "The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa
RT and Ssb.";
RL J. Biol. Chem. 280:41262-41269(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, 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).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAC AND SSE1.
RX PubMed=23332755; DOI=10.1016/j.cell.2012.12.001;
RA Willmund F., del Alamo M., Pechmann S., Chen T., Albanese V., Dammer E.B.,
RA Peng J., Frydman J.;
RT "The cotranslational function of ribosome-associated Hsp70 in eukaryotic
RT protein homeostasis.";
RL Cell 152:196-209(2013).
RN [21]
RP SUBUNIT.
RX PubMed=27917864; DOI=10.1038/ncomms13695;
RA Hanebuth M.A., Kityk R., Fries S.J., Jain A., Kriel A., Albanese V.,
RA Frickey T., Peter C., Mayer M.P., Frydman J., Deuerling E.;
RT "Multivalent contacts of the Hsp70 Ssb contribute to its architecture on
RT ribosomes and nascent chain interaction.";
RL Nat. Commun. 7:13695-13695(2016).
CC -!- FUNCTION: Ribosome-bound, Hsp70-type chaperone that assists in the
CC cotranslational folding of newly synthesized proteins in the cytosol.
CC Stimulates folding by interacting with nascent chains, binding to
CC short, largely hydrophobic sequences exposed by unfolded proteins,
CC thereby stabilizing longer, more slowly translated, and aggregation-
CC prone nascent polypeptides and domains that cannot fold stably until
CC fully synthesized. The Hsp70-protein substrate interaction depends on
CC ATP-binding and on allosteric regulation between the NBD and the SBD.
CC The ATP-bound state is characterized by a fast exchange rate of
CC substrate (low affinity state), while in the ADP-bound state exchange
CC is much slower (high affinity state). During the Hsp70 cycle, the
CC chaperone switches between the ATP-bound state (open conformation) and
CC the ADP-bound state (closed conformation) by major conformational
CC rearrangements involving mainly the lid domain. Ssb cooperates with a
CC specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated
CC complex (RAC), which stimulates the ATPase activity of the ribosome-
CC associated pool of Ssbs and switches it to the high affinity substrate
CC binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide
CC exchange factors that cause substrate release.
CC {ECO:0000269|PubMed:11739779, ECO:0000269|PubMed:11929994,
CC ECO:0000269|PubMed:1394434, ECO:0000269|PubMed:16219770,
CC ECO:0000269|PubMed:16221677, ECO:0000269|PubMed:23332755,
CC ECO:0000269|PubMed:9670014}.
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=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:P11484};
CC -!- SUBUNIT: Binds to ribosomes (PubMed:9670014, PubMed:1394434,
CC PubMed:27917864). Binds close to the ribosomal tunnel exit via contacts
CC with both ribosomal proteins RPL35, RPL39 and RPL19, and rRNA (By
CC similarity). Directly interacts with nascent polypeptides. This
CC interaction is dependent on the ribosome-associated complex (RAC)
CC (PubMed:11929994, PubMed:23332755). Interacts with SSE1
CC (PubMed:23332755). {ECO:0000250|UniProtKB:P11484,
CC ECO:0000269|PubMed:11929994, ECO:0000269|PubMed:1394434,
CC ECO:0000269|PubMed:23332755, ECO:0000269|PubMed:27917864,
CC ECO:0000269|PubMed:9670014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23332755,
CC ECO:0000305|PubMed:1394434}. Note=About 50% of the protein is
CC associated with translating ribosomes, but sufficient Ssb exists in the
CC cell for each ribosome to be associated with at least one Ssb molecule.
CC {ECO:0000269|PubMed:1394434, ECO:0000269|PubMed:23332755,
CC ECO:0000269|PubMed:9670014}.
CC -!- INDUCTION: Expression decreases after heat shock or during growth to
CC stationary phase (PubMed:6761581, PubMed:2651414). Up-regulated upon
CC carbon upshift and down-regulated upon amino acid limitation in an
CC HSF1-dependent manner (PubMed:10322015). Interacts with SSE1
CC (PubMed:16219770, PubMed:16221677). Interacts with FES1 (By
CC similarity). {ECO:0000250|UniProtKB:P11484,
CC ECO:0000269|PubMed:10322015, ECO:0000269|PubMed:16219770,
CC ECO:0000269|PubMed:16221677, ECO:0000269|PubMed:2651414,
CC ECO:0000269|PubMed:6761581}.
CC -!- MISCELLANEOUS: Present with 104000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. Ssb-type Hsp70
CC subfamily. {ECO:0000305}.
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DR EMBL; X78898; CAA55498.1; -; Genomic_DNA.
DR EMBL; Z71485; CAA96111.1; -; Genomic_DNA.
DR EMBL; M17586; AAA34693.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10347.1; -; Genomic_DNA.
DR PIR; S50721; S50721.
DR RefSeq; NP_014190.1; NM_001183047.1.
DR AlphaFoldDB; P40150; -.
DR SMR; P40150; -.
DR BioGRID; 35627; 2100.
DR DIP; DIP-7126N; -.
DR IntAct; P40150; 116.
DR MINT; P40150; -.
DR STRING; 4932.YNL209W; -.
DR iPTMnet; P40150; -.
DR COMPLUYEAST-2DPAGE; P40150; -.
DR MaxQB; P40150; -.
DR PaxDb; P40150; -.
DR PRIDE; P40150; -.
DR TopDownProteomics; P40150; -.
DR EnsemblFungi; YNL209W_mRNA; YNL209W; YNL209W.
DR GeneID; 855512; -.
DR KEGG; sce:YNL209W; -.
DR SGD; S000005153; SSB2.
DR VEuPathDB; FungiDB:YNL209W; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000154813; -.
DR HOGENOM; CLU_005965_2_4_1; -.
DR InParanoid; P40150; -.
DR OMA; XATAGNT; -.
DR BioCyc; YEAST:G3O-33215-MON; -.
DR PRO; PR:P40150; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40150; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IDA:SGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; IGI:SGD.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0006450; P:regulation of translational fidelity; IMP:SGD.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IGI:SGD.
DR GO; GO:0006364; P:rRNA processing; IGI:SGD.
DR GO; GO:0006452; P:translational frameshifting; IMP:SGD.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..613
FT /note="Ribosome-associated molecular chaperone SSB2"
FT /id="PRO_0000078390"
FT REGION 2..391
FT /note="Nucleotide binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 392..402
FT /note="Inter-domain linker"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 403..613
FT /note="Substrate binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 516..612
FT /note="Lid domain (SBDalpha)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 601..613
FT /note="Required for interaction with ribosomes"
FT /evidence="ECO:0000269|PubMed:27917864"
FT MOTIF 428..430
FT /note="Contributes to ribosome binding"
FT /evidence="ECO:0000269|PubMed:27917864"
FT MOTIF 574..582
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P11484"
FT BINDING 16..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 205..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 271..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11484"
SQ SEQUENCE 613 AA; 66595 MW; E1040A011346D953 CRC64;
MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPQE RLIGDAAKNQ
AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD GNPVIEVQYL EETKTFSPQE
ISAMVLTKMK EIAEAKIGKK VEKAVITVPA YFNDAQRQAT KDAGAISGLN VLRIINEPTA
AAIAYGLGAG KSEKERHVLI FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL
LEHFKAEFKK KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL
TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ KLLSDFFDGK
QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV APLSLGVGMQ GDIFGIVVPR
NTTVPTIKRR TFTTVSDNQT TVQFPVYQGE RVNCKENTLL GEFDLKNIPM MPAGEPVLEA
IFEVDANGIL KVTAVEKSTG KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH
EARQRLESYV ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV
GLKRVVTKAM SSR
