HSPB1_PIG
ID HSPB1_PIG Reviewed; 207 AA.
AC Q5S1U1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shelden E.A., Mao L.;
RT "Sequence analysis of mammalian small heat shock proteins.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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; AY789513; AAV54182.1; -; mRNA.
DR RefSeq; NP_001007519.1; NM_001007518.1.
DR AlphaFoldDB; Q5S1U1; -.
DR SMR; Q5S1U1; -.
DR STRING; 9823.ENSSSCP00000008215; -.
DR iPTMnet; Q5S1U1; -.
DR PaxDb; Q5S1U1; -.
DR PeptideAtlas; Q5S1U1; -.
DR PRIDE; Q5S1U1; -.
DR GeneID; 493184; -.
DR KEGG; ssc:493184; -.
DR CTD; 3315; -.
DR eggNOG; KOG3591; Eukaryota.
DR HOGENOM; CLU_095001_0_0_1; -.
DR InParanoid; Q5S1U1; -.
DR OMA; EEWAQWF; -.
DR OrthoDB; 1187096at2759; -.
DR TreeFam; TF105049; -.
DR ChiTaRS; HSPB1; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q5S1U1; SS.
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..207
FT /note="Heat shock protein beta-1"
FT /id="PRO_0000125929"
FT DOMAIN 78..186
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 72..207
FT /note="Interaction with TGFB1I1"
FT /evidence="ECO:0000250"
FT REGION 151..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 80
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 84
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT /evidence="ECO:0000250|UniProtKB:P14602"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
SQ SEQUENCE 207 AA; 22942 MW; B2B5E955AAA70D69 CRC64;
MTERRVPFSL LRSPSWDPFR DWYPAHSRLF DQAFGLPRLP EEWSQWLSHS GWPGYVRPLP
PPAIEGPAAV AAPAYSRLLS RQLSSGVSEI QQTADRWRVS LDVNHFAPEE LTVKTKDGVV
EITGKHEERQ DEHGFISRCF TRKYTLPPGV DPTQVSSSLS PEGTLSVEAP LPKPATQSAE
ITIPVTFEAR AQLGGTEAGK SEKPGTK
