HSPB8_RAT
ID HSPB8_RAT Reviewed; 196 AA.
AC Q9EPX0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Heat shock protein beta-8;
DE Short=HspB8;
DE AltName: Full=Alpha-crystallin C chain;
DE AltName: Full=Small stress protein-like protein HSP22;
GN Name=Hspb8; Synonyms=Cryac, Hsp22;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP FUNCTION, SUBUNIT, INDUCTION, AND CIRCULAR DICHROISM ANALYSIS.
RC TISSUE=Muscle;
RX PubMed=15030316; DOI=10.1042/bj20031958;
RA Chowdary T.K., Raman B., Ramakrishna T., Rao C.M.;
RT "Mammalian Hsp22 is a heat-inducible small heat shock protein with
RT chaperone-like activity.";
RL Biochem. J. 381:379-387(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-57, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Displays temperature-dependent chaperone activity.
CC {ECO:0000269|PubMed:15030316}.
CC -!- SUBUNIT: Monomer. Interacts with HSPB1 (By similarity). Interacts with
CC DNAJB6 (By similarity). Interacts with BAG3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UJY1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UJY1}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UJY1}. Note=Translocates to nuclear foci
CC during heat shock. {ECO:0000250|UniProtKB:Q9UJY1}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:15030316}.
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; AF314540; AAG34700.1; -; mRNA.
DR EMBL; BC061748; AAH61748.1; -; mRNA.
DR RefSeq; NP_446064.1; NM_053612.2.
DR AlphaFoldDB; Q9EPX0; -.
DR SMR; Q9EPX0; -.
DR BioGRID; 250211; 1.
DR IntAct; Q9EPX0; 1.
DR STRING; 10116.ENSRNOP00000033432; -.
DR iPTMnet; Q9EPX0; -.
DR PhosphoSitePlus; Q9EPX0; -.
DR jPOST; Q9EPX0; -.
DR PaxDb; Q9EPX0; -.
DR PRIDE; Q9EPX0; -.
DR Ensembl; ENSRNOT00000039275; ENSRNOP00000033432; ENSRNOG00000022392.
DR GeneID; 113906; -.
DR KEGG; rno:113906; -.
DR UCSC; RGD:71003; rat.
DR CTD; 26353; -.
DR RGD; 71003; Hspb8.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000160605; -.
DR HOGENOM; CLU_095001_0_1_1; -.
DR InParanoid; Q9EPX0; -.
DR OMA; CVNVQSF; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; Q9EPX0; -.
DR TreeFam; TF105049; -.
DR Reactome; R-RNO-3371571; HSF1-dependent transactivation.
DR PRO; PR:Q9EPX0; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000022392; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q9EPX0; RN.
DR GO; GO:0101031; C:chaperone complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0034620; P:cellular response to unfolded protein; ISO:RGD.
DR GO; GO:1905337; P:positive regulation of aggrephagy; ISO:RGD.
DR CDD; cd06480; ACD_HspB8_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR043254; HSPB8.
DR InterPro; IPR042790; HspB8_ACD.
DR PANTHER; PTHR46906; PTHR46906; 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 Chaperone; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..196
FT /note="Heat shock protein beta-8"
FT /id="PRO_0000125949"
FT DOMAIN 74..185
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJY1"
FT MOD_RES 71
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK92"
FT MOD_RES 78
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK92"
SQ SEQUENCE 196 AA; 21592 MW; 7DF3288BB9846635 CRC64;
MADGQLPFPC SYPSRLRRDP FRDSPLSSRL LDDGFGMDPF PDDLTAPWPE WALPRLSSAW
PGTLRSGMVP RGPTATARFG VPAEGRNPPP FPGEPWKVCV NVHSFKPEEL MVKTKDGYVE
VSGKHEEKQQ EGGIVSKNFT KKIQLPAEVD PVTVFASLSP EGLLIIEAPQ VPPYSPFGES
SFNNELPQDN QEVTCS
