HSPB1_CHICK
ID HSPB1_CHICK Reviewed; 193 AA.
AC Q00649;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Heat shock protein beta-1;
DE Short=HspB1;
DE AltName: Full=25 kDa IAP;
DE AltName: Full=Actin polymerization inhibitor;
DE AltName: Full=Heat shock 25 kDa protein;
DE Short=HSP 25;
DE AltName: Full=Heat shock 27 kDa protein;
DE Short=HSP 27;
GN Name=HSPB1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Gizzard;
RX PubMed=2071672; DOI=10.1083/jcb.114.2.255;
RA Miron T., Vancompernolle K., Vandekerckhove J., Wilchek M., Geiger B.;
RT "A 25-kD inhibitor of actin polymerization is a low molecular mass heat
RT shock protein.";
RL J. Cell Biol. 114:255-261(1991).
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. {ECO:0000269|PubMed:2071672}.
CC -!- SUBUNIT: Homooligomer. Homodimer; becomes monomeric upon activation.
CC Heterooligomer. {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}.
CC -!- TISSUE SPECIFICITY: Smooth, cardiac and skeletal muscle, hardly
CC detectable in fibroblasts or focal contacts.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; X59541; CAA42114.1; -; mRNA.
DR PIR; A39644; A39644.
DR RefSeq; NP_990621.1; NM_205290.1.
DR AlphaFoldDB; Q00649; -.
DR SMR; Q00649; -.
DR BioGRID; 676487; 1.
DR IntAct; Q00649; 1.
DR STRING; 9031.ENSGALP00000039447; -.
DR iPTMnet; Q00649; -.
DR GeneID; 396227; -.
DR KEGG; gga:396227; -.
DR CTD; 3315; -.
DR VEuPathDB; HostDB:geneid_396227; -.
DR eggNOG; KOG3591; Eukaryota.
DR InParanoid; Q00649; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; Q00649; -.
DR PRO; PR:Q00649; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0043292; C:contractile fiber; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005622; C:intracellular anatomical structure; ISS:AgBase.
DR GO; GO:0005739; C:mitochondrion; NAS:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; ISS:AgBase.
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:0005080; F:protein kinase C binding; ISS:AgBase.
DR GO; GO:0008426; F:protein kinase C inhibitor activity; ISS:AgBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; NAS:AgBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:AgBase.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISS:AgBase.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISS:AgBase.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:AgBase.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISS:AgBase.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:AgBase.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:AgBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:AgBase.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
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 Actin capping; Chaperone; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..193
FT /note="Heat shock protein beta-1"
FT /id="PRO_0000125931"
FT DOMAIN 74..182
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 193 AA; 21672 MW; 57C33F9454DA7B0A CRC64;
MAERRVPFTF LTSPSWEPFR DWYHGSRLFD QSFGMPHIPE DWYKWPSGSA WPGYFRLLPS
ESALLPAPGS PYGRALSELS SGISEIRQSA DSWKVTLDVN HFAPEELVVK TKDNIVEITG
KHEEKQDEHG FISRCFTRKY TLPPGVEATA VRSSLSPDGM LTVEAPLPKP AIQSSEITIP
VTVEAKKEEP AKK
