HSPB8_BOVIN
ID HSPB8_BOVIN Reviewed; 196 AA.
AC Q5EAC9; Q3T0Q5;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Heat shock protein beta-8;
DE Short=HspB8;
GN Name=HSPB8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Displays temperature-dependent chaperone activity.
CC {ECO:0000250}.
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 -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; BT020640; AAX08657.1; -; mRNA.
DR EMBL; BC102299; AAI02300.1; -; mRNA.
DR RefSeq; NP_001014955.1; NM_001014955.1.
DR AlphaFoldDB; Q5EAC9; -.
DR SMR; Q5EAC9; -.
DR STRING; 9913.ENSBTAP00000001720; -.
DR PaxDb; Q5EAC9; -.
DR PRIDE; Q5EAC9; -.
DR Ensembl; ENSBTAT00000001720; ENSBTAP00000001720; ENSBTAG00000001303.
DR GeneID; 539524; -.
DR KEGG; bta:539524; -.
DR CTD; 26353; -.
DR VEuPathDB; HostDB:ENSBTAG00000001303; -.
DR VGNC; VGNC:53907; HSPB8.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000160605; -.
DR HOGENOM; CLU_095001_0_1_1; -.
DR InParanoid; Q5EAC9; -.
DR OMA; CVNVQSF; -.
DR OrthoDB; 1187096at2759; -.
DR TreeFam; TF105049; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000001303; Expressed in biceps femoris and 104 other tissues.
DR GO; GO:0101031; C:chaperone complex; IBA:GO_Central.
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:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:1905337; P:positive regulation of aggrephagy; IEA:Ensembl.
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 2: Evidence at transcript 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_0000125944"
FT DOMAIN 74..185
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 1..34
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 COMPBIAS 12..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJY1"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPX0"
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"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK92"
SQ SEQUENCE 196 AA; 21673 MW; 1DA985C698C08EA5 CRC64;
MADGQMPFPC HYTSRRRRDP FRDSPLSSRL LDDGFGMDPF PDDLTASWPD WALPRLSSAW
PGTLRSGMVP RGPTAMTRFG VPAEGRSPPP FPGEPWKVCV NVHSFKPEEL MVKTKDGYVE
VSGKHEEKQQ EGGIVSKNFT KKIQLPAEVD PVTVFASLSP EGLLIIEAPQ VPPYSPFGES
SFNNELPQDG QEVTCT
