ID   HSPB1_POELU             Reviewed;         201 AA.
AC   O13224;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 74.
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;
OS   Poeciliopsis lucida (Desert topminnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poeciliopsis.
OX   NCBI_TaxID=56613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=M61-31;
RX   PubMed=9335145; DOI=10.1093/oxfordjournals.molbev.a025711;
RA   Norris C.E., Brown M.A., Hickey E., Weber L.A., Hightower L.E.;
RT   "Low-molecular-weight heat shock proteins in a desert fish (Poeciliopsis
RT   lucida): homologs of human Hsp27 and Xenopus Hsp30.";
RL   Mol. Biol. Evol. 14:1050-1061(1997).
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:0000250|UniProtKB:P04792}.
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   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR   EMBL; U85501; AAB46593.1; -; mRNA.
DR   AlphaFoldDB; O13224; -.
DR   SMR; O13224; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
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   Chaperone; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..201
FT                   /note="Heat shock protein beta-1"
FT                   /id="PRO_0000125932"
FT   DOMAIN          83..193
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   MOD_RES         15
FT                   /note="Phosphoserine; by PKA and PKC"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   201 AA;  22649 MW;  732AF8E1B56700F6 CRC64;
     MAERRIPFTL QRTPSWDVPD LHQTSRIFDQ AFGLPPVFED FSGFPTTHWP GYMRPSLMTP
     DIMIPQSPMM YHPGHMMAHQ ARALSRQMSS GMSEIKQTQD NWKISLDVPH FSPEELVVKT
     KDGVLEISGK HEERKDEHGF VSRSFTRKYT LPPTANIEKV TSSLSPEGVL TVEAPINKPA
     LEYSETTIPV NVESSGAVAK K