HSPB1_CANLF
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 03-AUG-2022, entry version 118.
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 STRING; 9612.ENSCAFP00000019945; -.
DR iPTMnet; P42929; -.
DR PaxDb; P42929; -.
DR PRIDE; P42929; -.
DR eggNOG; KOG3591; Eukaryota.
DR InParanoid; P42929; -.
DR Proteomes; UP000002254; 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:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated 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 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 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
