HSPB8_CANLF
ID HSPB8_CANLF Reviewed; 196 AA.
AC Q8MJ36;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Heat shock protein beta-8;
DE Short=HspB8;
DE AltName: Full=Protein kinase H11;
GN Name=HSPB8;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang L., Depre C.;
RL Submitted (JUN-2002) 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}.
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; AF525493; AAM90297.1; -; mRNA.
DR RefSeq; NP_001003029.1; NM_001003029.1.
DR AlphaFoldDB; Q8MJ36; -.
DR SMR; Q8MJ36; -.
DR STRING; 9612.ENSCAFP00000041782; -.
DR PaxDb; Q8MJ36; -.
DR GeneID; 403553; -.
DR KEGG; cfa:403553; -.
DR CTD; 26353; -.
DR eggNOG; KOG3591; Eukaryota.
DR InParanoid; Q8MJ36; -.
DR OrthoDB; 1187096at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0101031; C:chaperone complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
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_0000252668"
FT DOMAIN 74..185
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 1..35
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 15..29
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; 21760 MW; 977F2BB4F2CD660A CRC64;
MADGQMPFSC HYPSRLRRDP FRDSPLPSRL LDDDFGMDPF PDDLTSSWRN WALPRFSTGW
PGTLRSGMVP RGPTAAARFG VPAEGRSPPP FPGEPWKVCV NVHSFKPEEL MVKTKDGYVE
VSGKHEEKQQ EGGIVSKNFT KKIQLPAEVD PVTVFASLSP EGLLIIEAPQ VPPYSPFGES
NFNNELPQDS QEVTCT
