ID   HSP11_PEA               Reviewed;         158 AA.
AC   P19243;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=18.1 kDa class I heat shock protein;
DE   AltName: Full=HSP 18.1;
GN   Name=HSP18.1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2377479; DOI=10.1093/nar/18.14.4274;
RA   Lauzon L.M., Helm K.W., Vierling E.;
RT   "A cDNA clone from Pisum sativum encoding a low molecular weight heat shock
RT   protein.";
RL   Nucleic Acids Res. 18:4274-4274(1990).
CC   -!- SUBUNIT: Forms oligomeric structures.
CC   -!- INTERACTION:
CC       P19243; P19243: HSP18.1; NbExp=3; IntAct=EBI-15802012, EBI-15802012;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M33899; AAA33672.1; -; mRNA.
DR   PDB; 5DS2; X-ray; 1.85 A; A/B/C/D/E/F=50-143.
DR   PDBsum; 5DS2; -.
DR   AlphaFoldDB; P19243; -.
DR   SMR; P19243; -.
DR   DIP; DIP-48960N; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   Pfam; PF00011; HSP20; 1.
DR   SUPFAM; SSF49764; SSF49764; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Stress response.
FT   CHAIN           1..158
FT                   /note="18.1 kDa class I heat shock protein"
FT                   /id="PRO_0000125982"
FT   DOMAIN          44..158
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   STRAND          59..67
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   TURN            82..84
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   STRAND          85..92
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   STRAND          110..118
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:5DS2"
FT   STRAND          136..142
FT                   /evidence="ECO:0007829|PDB:5DS2"
SQ   SEQUENCE   158 AA;  18085 MW;  788BD50547097EB6 CRC64;
     MSLIPSFFSG RRSNVFDPFS LDVWDPLKDF PFSNSSPSAS FPRENPAFVS TRVDWKETPE
     AHVFKADLPG LKKEEVKVEV EDDRVLQISG ERSVEKEDKN DEWHRVERSS GKFLRRFRLP
     ENAKMDKVKA SMENGVLTVT VPKEEIKKAE VKSIEISG