HSPB1_MOUSE
ID HSPB1_MOUSE Reviewed; 209 AA.
AC P14602;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Heat shock protein beta-1;
DE Short=HspB1;
DE AltName: Full=Growth-related 25 kDa protein;
DE AltName: Full=Heat shock 25 kDa protein;
DE Short=HSP 25;
DE AltName: Full=Heat shock 27 kDa protein;
DE Short=HSP 27;
DE AltName: Full=p25;
GN Name=Hspb1; Synonyms=Hsp25, Hsp27;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RX PubMed=8514194; DOI=10.1016/0378-1119(93)90575-n;
RA Gaestel M., Gotthardt R., Mueller T.;
RT "Structure and organisation of a murine gene encoding small heat-shock
RT protein Hsp25.";
RL Gene 128:279-283(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RX PubMed=8514193; DOI=10.1016/0378-1119(93)90574-m;
RA Froehli E., Aoyama X., Klemenz R.;
RT "Cloning of the mouse hsp25 gene and an extremely conserved hsp25
RT pseudogene.";
RL Gene 128:273-277(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=2645135; DOI=10.1111/j.1432-1033.1989.tb14542.x;
RA Gaestel M., Gross B., Benndorf R., Strauss M., Schunk W.-H., Kraft R.,
RA Otto A., Boehm H., Stahl J., Drabsch H., Bielka H.;
RT "Molecular cloning, sequencing and expression in Escherichia coli of the
RT 25-kDa growth-related protein of Ehrlich ascites tumor and its homology to
RT mammalian stress proteins.";
RL Eur. J. Biochem. 179:209-213(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RC TISSUE=Bone;
RX PubMed=8132504; DOI=10.1016/s0021-9258(17)37131-4;
RA Cooper L.F., Uoshima K.;
RT "Differential estrogenic regulation of small M(r) heat shock protein
RT expression in osteoblasts.";
RL J. Biol. Chem. 269:7869-7873(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION AT SER-15 AND SER-86.
RX PubMed=1860870; DOI=10.1016/s0021-9258(18)98746-6;
RA Gaestel M., Schroeder W., Benndorf R., Lippmann C., Buchner K., Hucho F.,
RA Erdmann V.A., Bielka H.;
RT "Identification of the phosphorylation sites of the murine small heat shock
RT protein hsp25.";
RL J. Biol. Chem. 266:14721-14724(1991).
RN [7]
RP PHOSPHORYLATION AT SER-15 AND SER-86 BY MAPKAPK2.
RX PubMed=1332886; DOI=10.1016/0014-5793(92)81216-9;
RA Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M.;
RT "Identification of MAPKAP kinase 2 as a major enzyme responsible for the
RT phosphorylation of the small mammalian heat shock proteins.";
RL FEBS Lett. 313:307-313(1992).
RN [8]
RP PHOSPHORYLATION BY MAPKAPK2.
RX PubMed=8093612; DOI=10.1016/s0021-9258(18)53882-5;
RA Jakob U., Gaestel M., Engel K., Buchner J.;
RT "Small heat shock proteins are molecular chaperones.";
RL J. Biol. Chem. 268:1517-1520(1993).
RN [9]
RP INTERACTION WITH HSPBAP1.
RX PubMed=10751411; DOI=10.1074/jbc.m001981200;
RA Liu C., Gilmont R.R., Benndorf R., Welsh M.J.;
RT "Identification and characterization of a novel protein from Sertoli cells,
RT PASS1, that associates with mammalian small stress protein hsp27.";
RL J. Biol. Chem. 275:18724-18731(2000).
RN [10]
RP INTERACTION WITH HSPB8.
RX PubMed=11342557; DOI=10.1074/jbc.m103001200;
RA Benndorf R., Sun X., Gilmont R.R., Biederman K.J., Molloy M.P.,
RA Goodmurphy C.W., Cheng H., Andrews P.C., Welsh M.J.;
RT "HSP22, a new member of the small heat shock protein superfamily, interacts
RT with mimic of phosphorylated HSP27 (3DHSP27).";
RL J. Biol. Chem. 276:26753-26761(2001).
RN [11]
RP INTERACTION WITH TGFB1I1.
RX PubMed=11546764; DOI=10.1074/jbc.m103510200;
RA Jia Y., Ransom R.F., Shibanuma M., Liu C., Welsh M.J., Smoyer W.E.;
RT "Identification and characterization of hic-5/ARA55 as an hsp27 binding
RT protein.";
RL J. Biol. Chem. 276:39911-39918(2001).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17661394; DOI=10.1002/dvg.20319;
RA Huang L., Min J.N., Masters S., Mivechi N.F., Moskophidis D.;
RT "Insights into function and regulation of small heat shock protein 25
RT (HSPB1) in a mouse model with targeted gene disruption.";
RL Genesis 45:487-501(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP PHOSPHORYLATION BY MAPKAPK5.
RX PubMed=21575178; DOI=10.1186/1750-2187-6-4;
RA Shiryaev A., Dumitriu G., Moens U.;
RT "Distinct roles of MK2 and MK5 in cAMP/PKA- and stress/p38MAPK-induced heat
RT shock protein 27 phosphorylation.";
RL J. Mol. Signal. 6:4-4(2011).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Small heat shock protein which functions as a molecular
CC chaperone probably maintaining denatured proteins in a folding-
CC competent state. Plays a role in stress resistance and actin
CC organization (PubMed:17661394). Through its molecular chaperone
CC activity may regulate numerous biological processes including the
CC phosphorylation and the axonal transport of neurofilament proteins (By
CC similarity). {ECO:0000250|UniProtKB:P04792,
CC ECO:0000269|PubMed:17661394}.
CC -!- SUBUNIT: Homooligomer. Homodimer; becomes monomeric upon activation.
CC Heterooligomer; with HSPB6. Associates with alpha- and beta-tubulin (By
CC similarity). Interacts with TGFB1I1 (PubMed:11546764). Interacts with
CC CRYAB (By similarity). Interacts with HSPB8 (PubMed:11342557).
CC Interacts with HSPBAP1 (PubMed:10751411).
CC {ECO:0000250|UniProtKB:P04792, ECO:0000269|PubMed:10751411,
CC ECO:0000269|PubMed:11342557, ECO:0000269|PubMed:11546764}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04792}. Nucleus
CC {ECO:0000250|UniProtKB:P04792}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P04792}. Note=Cytoplasmic in interphase cells.
CC Colocalizes with mitotic spindles in mitotic cells. Translocates to the
CC nucleus during heat shock and resides in sub-nuclear structures known
CC as SC35 speckles or nuclear splicing speckles.
CC {ECO:0000250|UniProtKB:P04792}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=A;
CC IsoId=P14602-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P14602-2; Sequence=VSP_002422;
CC Name=C;
CC IsoId=P14602-3; Sequence=VSP_002423;
CC -!- PTM: Phosphorylated upon exposure to protein kinase C activators and
CC heat shock (By similarity). Phosphorylation by MAPKAPK2 and MAPKAPK3 in
CC response to stress dissociates HSPB1 from large small heat-shock
CC protein (sHsps) oligomers and impairs its chaperone activity and
CC ability to protect against oxidative stress effectively.
CC Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-
CC actin rearrangement (PubMed:1332886, PubMed:1860870, PubMed:21575178,
CC PubMed:8093612). {ECO:0000250|UniProtKB:P04792,
CC ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:1860870,
CC ECO:0000269|PubMed:21575178, ECO:0000269|PubMed:8093612}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile with no apparent
CC morphological abnormalities in tissues under physiological conditions.
CC {ECO:0000269|PubMed:17661394}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; X14687; CAA32818.1; -; mRNA.
DR EMBL; X14686; CAB37341.1; -; mRNA.
DR EMBL; L11609; AAA37862.1; -; Genomic_DNA.
DR EMBL; L11608; AAA37862.1; JOINED; Genomic_DNA.
DR EMBL; L07577; AAA37861.1; -; Genomic_DNA.
DR EMBL; U03560; AAA18335.1; -; mRNA.
DR EMBL; U03561; AAA18336.1; -; mRNA.
DR EMBL; U03562; AAA18337.1; -; mRNA.
DR EMBL; BC018257; AAH18257.1; -; mRNA.
DR CCDS; CCDS39320.1; -. [P14602-1]
DR PIR; A53423; A53423.
DR PIR; I49763; JN0679.
DR PIR; S02143; S02143.
DR RefSeq; NP_038588.2; NM_013560.2. [P14602-1]
DR AlphaFoldDB; P14602; -.
DR SMR; P14602; -.
DR BioGRID; 200449; 22.
DR CORUM; P14602; -.
DR IntAct; P14602; 12.
DR MINT; P14602; -.
DR STRING; 10090.ENSMUSP00000005077; -.
DR iPTMnet; P14602; -.
DR PhosphoSitePlus; P14602; -.
DR REPRODUCTION-2DPAGE; IPI00128522; -.
DR REPRODUCTION-2DPAGE; IPI00468068; -.
DR REPRODUCTION-2DPAGE; P14602; -.
DR SWISS-2DPAGE; P14602; -.
DR UCD-2DPAGE; P14602; -.
DR jPOST; P14602; -.
DR MaxQB; P14602; -.
DR PaxDb; P14602; -.
DR PeptideAtlas; P14602; -.
DR PRIDE; P14602; -.
DR ProteomicsDB; 273278; -. [P14602-1]
DR ProteomicsDB; 273279; -. [P14602-2]
DR ProteomicsDB; 273280; -. [P14602-3]
DR Antibodypedia; 603; 3223 antibodies from 54 providers.
DR DNASU; 15507; -.
DR Ensembl; ENSMUST00000005077; ENSMUSP00000005077; ENSMUSG00000004951. [P14602-1]
DR GeneID; 15507; -.
DR KEGG; mmu:15507; -.
DR UCSC; uc008zze.2; mouse. [P14602-1]
DR CTD; 3315; -.
DR MGI; MGI:96240; Hspb1.
DR VEuPathDB; HostDB:ENSMUSG00000004951; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000155882; -.
DR HOGENOM; CLU_095001_0_0_1; -.
DR InParanoid; P14602; -.
DR OMA; EEWAQWF; -.
DR PhylomeDB; P14602; -.
DR TreeFam; TF105049; -.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR BioGRID-ORCS; 15507; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Hspb1; mouse.
DR PRO; PR:P14602; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P14602; protein.
DR Bgee; ENSMUSG00000004951; Expressed in esophagus and 66 other tissues.
DR ExpressionAtlas; P14602; baseline and differential.
DR Genevisible; P14602; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0097512; C:cardiac myofibril; ISO:MGI.
DR GO; GO:0043292; C:contractile fiber; IDA:MGI.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0031674; C:I band; ISO:MGI.
DR GO; GO:0031430; C:M band; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISS:BHF-UCL.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; IDA:BHF-UCL.
DR GO; GO:0008426; F:protein kinase C inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISS:BHF-UCL.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:MGI.
DR GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; ISO:MGI.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISO:MGI.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0006986; P:response to unfolded protein; NAS:BHF-UCL.
DR GO; GO:0009615; P:response to virus; ISS:BHF-UCL.
DR CDD; cd06475; ACD_HspB1_like; 1.
DR DisProt; DP00142; -.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR037876; ACD_HspB1.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR45640; PTHR45640; 1.
DR Pfam; PF00011; HSP20; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..209
FT /note="Heat shock protein beta-1"
FT /id="PRO_0000125928"
FT DOMAIN 80..188
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 74..209
FT /note="Interaction with TGFB1I1"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42930"
FT MOD_RES 15
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3, PKA and PKC"
FT /evidence="ECO:0000269|PubMed:1332886,
FT ECO:0000269|PubMed:1860870"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42930"
FT MOD_RES 86
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3, MAPKAPK5, PKA
FT and PKC"
FT /evidence="ECO:0000269|PubMed:1332886,
FT ECO:0000269|PubMed:1860870, ECO:0007744|PubMed:21183079"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT VAR_SEQ 37..70
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8132504"
FT /id="VSP_002423"
FT VAR_SEQ 61..72
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8132504"
FT /id="VSP_002422"
FT CONFLICT 13
FT /note="S -> T (in Ref. 4; AAA18335/AAA18336/AAA18337)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="E -> G (in Ref. 4; AAA18335)"
FT /evidence="ECO:0000305"
FT CONFLICT 67..68
FT /note="PA -> L (in Ref. 4; AAA18335)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="Missing (in Ref. 3; CAA32818/CAB37341)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..109
FT /note="FA -> VI (in Ref. 3; CAA32818/CAB37341)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="C -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> T (in Ref. 3; CAA32818/CAB37341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 23014 MW; 31BD9FAF4E107C50 CRC64;
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP
AATAEGPAAV TLAAPAFSRA LNRQLSSGVS EIRQTADRWR VSLDVNHFAP EELTVKTKEG
VVEITGKHEE RQDEHGYISR CFTRKYTLPP GVDPTLVSSS LSPEGTLTVE APLPKAVTQS
AEITIPVTFE ARAQIGGPEA GKSEQSGAK
