ID   HSPB1_CANLF             Reviewed;         209 AA.
AC   P42929;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 133.
DE   RecName: Full=Heat shock protein beta-1;
DE            Short=HspB1;
DE   AltName: Full=Heat shock 27 kDa protein;
DE            Short=HSP 27;
GN   Name=HSPB1; Synonyms=HSP27;
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].
RC   TISSUE=Colon smooth muscle;
RX   PubMed=7665102; DOI=10.1016/0378-1119(95)00290-m;
RA   Larsen J.K., Gerthoffer W.T., Hickey E., Weber L.A.;
RT   "Cloning and sequencing of a cDNA encoding the canine HSP27 protein.";
RL   Gene 161:305-306(1995).
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. Through its molecular chaperone activity may regulate
CC       numerous biological processes including the phosphorylation and the
CC       axonal transport of neurofilament proteins.
CC       {ECO:0000250|UniProtKB:P04792}.
CC   -!- SUBUNIT: Homooligomer. Homodimer; becomes monomeric upon activation.
CC       Heterooligomer; with HSPB6. Associates with alpha- and beta-tubulin.
CC       Interacts with TGFB1I1. Interacts with CRYAB. Interacts with HSPB8.
CC       Interacts with HSPBAP1. {ECO:0000250|UniProtKB:P04792}.
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   -!- PTM: Phosphorylated upon exposure to protein kinase C activators and
CC       heat shock. Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to
CC       stress dissociates HSPB1 from large small heat-shock protein (sHsps)
CC       oligomers and impairs its chaperone activity and ability to protect
CC       against oxidative stress effectively. Phosphorylation by MAPKAPK5 in
CC       response to PKA stimulation induces F-actin rearrangement.
CC       {ECO:0000250|UniProtKB:P04792}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR   EMBL; U19368; AAA87172.1; -; mRNA.
DR   PIR; JC4244; JC4244.
DR   AlphaFoldDB; P42929; -.
DR   SMR; P42929; -.
DR   FunCoup; P42929; 74.
DR   STRING; 9615.ENSCAFP00000019945; -.
DR   iPTMnet; P42929; -.
DR   PaxDb; 9615-ENSCAFP00000019945; -.
DR   eggNOG; KOG3591; Eukaryota.
DR   InParanoid; P42929; -.
DR   OrthoDB; 10060792at2759; -.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR   CDD; cd06475; ACD_HspB1_like; 1.
DR   FunFam; 2.60.40.790:FF:000024; heat shock protein beta-1; 1.
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:SF7; HEAT SHOCK PROTEIN BETA-1; 1.
DR   PANTHER; PTHR45640; HEAT SHOCK PROTEIN HSP-12.2-RELATED; 1.
DR   Pfam; PF00011; HSP20; 1.
DR   PRINTS; PR00299; ACRYSTALLIN.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           1..209
FT                   /note="Heat shock protein beta-1"
FT                   /id="PRO_0000125925"
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:0000250|UniProtKB:P04792"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42930"
FT   MOD_RES         15
FT                   /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT                   /evidence="ECO:0000250|UniProtKB:P14602"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42930"
FT   MOD_RES         82
FT                   /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT                   /evidence="ECO:0000250|UniProtKB:P04792"
FT   MOD_RES         86
FT                   /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT                   /evidence="ECO:0000250|UniProtKB:P14602"
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"
SQ   SEQUENCE   209 AA;  22939 MW;  7E59F696D8C7F1BD CRC64;
     MTERRVPFSL LRSPSWDPFR DWYPAHSRLF DQAFGLPRLP EEWAQWFGHS GWPGYVRPIP
     PAVEGPAAAA AAAAPAYSRA LSRQLSSGVS EIRQTADRWR VSLDVNHFAP EELTVKTKDG
     VVEITGKHEE RQDEHGYISR RLTPKYTLPP GVDPTLVSSS LSPEGTLTVE APMPKPATQS
     AEITIPVTFE ARAQIGGPEA GKSEQSGAK
//