HS16B_WHEAT
ID HS16B_WHEAT Reviewed; 151 AA.
AC Q41560;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=16.9 kDa class I heat shock protein 2;
DE AltName: Full=Heat shock protein 16.9B;
GN Name=hsp16.9B;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Mustang; TISSUE=Seedling;
RA Weng J., Wang Z.F., Nguyen H.T.;
RT "Cloning and characterization of cytoplasmic LMW HSP genes from wheat.";
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND HOMODODECAMER.
RX PubMed=11702068; DOI=10.1038/nsb722;
RA van Montfort R.L., Basha E., Friedrich K.L., Slingsby C., Vierling E.;
RT "Crystal structure and assembly of a eukaryotic small heat shock protein.";
RL Nat. Struct. Biol. 8:1025-1030(2001).
CC -!- SUBUNIT: Homododecamer composed of 2 hexameric rings, each consisting
CC of 3 homodimers.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; X64618; CAA45902.1; -; mRNA.
DR PIR; S21600; S21600.
DR PDB; 1GME; X-ray; 2.70 A; A/B/C/D=1-151.
DR PDB; 2BYU; EM; 16.50 A; A/B/C/D/E/F/G/H/I/J/K/L=43-151.
DR PDB; 2H50; EM; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=44-136.
DR PDB; 2H53; EM; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=44-136.
DR PDBsum; 1GME; -.
DR PDBsum; 2BYU; -.
DR PDBsum; 2H50; -.
DR PDBsum; 2H53; -.
DR AlphaFoldDB; Q41560; -.
DR SMR; Q41560; -.
DR PRIDE; Q41560; -.
DR eggNOG; KOG0710; Eukaryota.
DR EvolutionaryTrace; Q41560; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q41560; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043621; F:protein self-association; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051259; P:protein complex oligomerization; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
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; Reference proteome; Stress response.
FT CHAIN 1..151
FT /note="16.9 kDa class I heat shock protein 2"
FT /id="PRO_0000387466"
FT DOMAIN 37..151
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1GME"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:1GME"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1GME"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1GME"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1GME"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1GME"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:1GME"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1GME"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1GME"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1GME"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1GME"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1GME"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1GME"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1GME"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:1GME"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1GME"
SQ SEQUENCE 151 AA; 16867 MW; D12B46720CA8D7E3 CRC64;
MSIVRRTNVF DPFADLWADP FDTFRSIVPA ISGGGSETAA FANARMDWKE TPEAHVFKAD
LPGVKKEEVK VEVEDGNVLV VSGERTKEKE DKNDKWHRVE RSSGKFVRRF RLLEDAKVEE
VKAGLENGVL TVTVPKAEVK KPEVKAIQIS G
