HSPB6_RAT
ID HSPB6_RAT Reviewed; 162 AA.
AC P97541;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Heat shock protein beta-6;
DE Short=HspB6;
DE AltName: Full=Heat shock 20 kDa-like protein p20;
DE Short=Hsp20 {ECO:0000303|PubMed:16385579};
GN Name=Hspb6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Soleus muscle;
RX PubMed=8921906; DOI=10.1016/0378-1119(96)00356-3;
RA Inaguma Y., Hasegawa K., Kato K., Nishida Y.;
RT "cDNA cloning of a 20-kDa protein (p20) highly homologous to small heat
RT shock proteins: developmental and physiological changes in rat hindlimb
RT muscles.";
RL Gene 178:145-150(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-162, AND CHARACTERIZATION.
RC TISSUE=Muscle;
RX PubMed=8195168; DOI=10.1016/s0021-9258(17)36606-1;
RA Kato K., Goto S., Inaguma Y., Hasegawa K., Morishita R., Asano T.;
RT "Purification and characterization of a 20-kDa protein that is highly
RT homologous to alpha B crystallin.";
RL J. Biol. Chem. 269:15302-15309(1994).
RN [3]
RP PHOSPHORYLATION AT SER-16, AND FUNCTION.
RX PubMed=15105294; DOI=10.1161/01.res.0000129179.66631.00;
RA Fan G.C., Chu G., Mitton B., Song Q., Yuan Q., Kranias E.G.;
RT "Small heat-shock protein Hsp20 phosphorylation inhibits beta-agonist-
RT induced cardiac apoptosis.";
RL Circ. Res. 94:1474-1482(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-157, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 65-162, AND HOMODIMER.
RX PubMed=19646995; DOI=10.1016/j.jmb.2009.07.069;
RA Bagneris C., Bateman O.A., Naylor C.E., Cronin N., Boelens W.C., Keep N.H.,
RA Slingsby C.;
RT "Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin
RT and Hsp20.";
RL J. Mol. Biol. 392:1242-1252(2009).
RN [6]
RP TRANSGLUTAMINATION AT GLN-31 AND LYS-162, DEAMIDATION AT GLN-66, AND
RP MUTAGENESIS OF GLN-31.
RX PubMed=16385579; DOI=10.1002/prot.20837;
RA Boros S., Ahrman E., Wunderink L., Kamps B., de Jong W.W., Boelens W.C.,
RA Emanuelsson C.S.;
RT "Site-specific transamidation and deamidation of the small heat-shock
RT protein Hsp20 by tissue transglutaminase.";
RL Proteins 62:1044-1052(2006).
CC -!- FUNCTION: Small heat shock protein which functions as a molecular
CC chaperone probably maintaining denatured proteins in a folding-
CC competent state (By similarity). Seems to have versatile functions in
CC various biological processes (By similarity). Plays a role in
CC regulating muscle function such as smooth muscle vasorelaxation and
CC cardiac myocyte contractility (By similarity). May regulate myocardial
CC angiogenesis implicating KDR (By similarity). Overexpression mediates
CC cardioprotection and angiogenesis after induced damage
CC (PubMed:15105294). Stabilizes monomeric YWHAZ thereby supporting YWHAZ
CC chaperone-like activity (By similarity). {ECO:0000250|UniProtKB:O14558,
CC ECO:0000269|PubMed:15105294}.
CC -!- SUBUNIT: Homodimer (PubMed:19646995). Small heat shock proteins form
CC high molecular mass oligomers containing variable number of monomers;
CC these oligomers display a very flexible quaternary structure easily
CC exchanging their subunits. Heterooligomer with HSPB1; formed through
CC oligomerization of HSPB1:HSBP6 dimers; subunit exchange leads to
CC formation of at least two different heterooligomeric complexes,
CC differing in variable quantities of HSPB1 and HSPB6 homodimers in
CC addition to HSPB1:HSPB6 heterodimers. Heterooligomer with CRYAB; large
CC heterooligomers consist of CRYAB homodimers and HSPB5:HSPB6
CC heterodimers but lacking HSPB6 homodimers. Interacts with BAG3.
CC Interacts (phosphorylated) with YWHAZ. Interacts with PDE4A and PDE4D;
CC required for maintenance of the non-phosphorylated state of HSPB6 under
CC basal conditions. Interacts with KDR. Interacts with PRKD1 (By
CC similarity). {ECO:0000250|UniProtKB:O14558,
CC ECO:0000269|PubMed:19646995}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14558}. Nucleus
CC {ECO:0000250|UniProtKB:O14558}. Secreted
CC {ECO:0000250|UniProtKB:O14558}. Note=Translocates to nuclear foci
CC during heat shock. {ECO:0000250|UniProtKB:O14558}.
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression in muscle
CC tissues. {ECO:0000269|PubMed:8921906}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8195168}.
CC -!- PTM: Phosphorylated at Ser-16 by PKA and probably PKD1K; required to
CC protect cardiomyocytes from apoptosis. {ECO:0000250|UniProtKB:O14558,
CC ECO:0000269|PubMed:15105294}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; D29960; BAA06227.1; -; mRNA.
DR PIR; A53814; A53814.
DR RefSeq; NP_620242.1; NM_138887.1.
DR PDB; 2WJ5; X-ray; 1.12 A; A=65-162.
DR PDBsum; 2WJ5; -.
DR AlphaFoldDB; P97541; -.
DR SMR; P97541; -.
DR BioGRID; 251372; 2.
DR STRING; 10116.ENSRNOP00000028401; -.
DR iPTMnet; P97541; -.
DR PhosphoSitePlus; P97541; -.
DR PaxDb; P97541; -.
DR PRIDE; P97541; -.
DR Ensembl; ENSRNOT00000028401; ENSRNOP00000028401; ENSRNOG00000020922.
DR GeneID; 192245; -.
DR KEGG; rno:192245; -.
DR UCSC; RGD:621554; rat.
DR CTD; 126393; -.
DR RGD; 621554; Hspb6.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000161100; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; P97541; -.
DR OMA; PVQPTWL; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P97541; -.
DR TreeFam; TF105049; -.
DR EvolutionaryTrace; P97541; -.
DR PRO; PR:P97541; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020922; Expressed in heart and 20 other tissues.
DR Genevisible; P97541; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0006937; P:regulation of muscle contraction; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR003090; Alpha-crystallin_N.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR45640; PTHR45640; 1.
DR Pfam; PF00525; Crystallin; 1.
DR Pfam; PF00011; HSP20; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Secreted;
KW Stress response.
FT CHAIN 1..162
FT /note="Heat shock protein beta-6"
FT /id="PRO_0000125940"
FT DOMAIN 56..162
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 1..72
FT /note="Involved in stabilization of the HSPB1:HSBP6
FT heterodimer"
FT /evidence="ECO:0000250|UniProtKB:O14558"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 66
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000269|PubMed:16385579"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 31
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-162)"
FT /evidence="ECO:0000269|PubMed:16385579"
FT CROSSLNK 162
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-31)"
FT /evidence="ECO:0000269|PubMed:16385579"
FT MUTAGEN 31
FT /note="Q->E: Abolished transglutamination."
FT /evidence="ECO:0000269|PubMed:16385579"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2WJ5"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2WJ5"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2WJ5"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:2WJ5"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:2WJ5"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2WJ5"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:2WJ5"
SQ SEQUENCE 162 AA; 17505 MW; 91561D8813EBFC98 CRC64;
MEIRVPVQPS WLRRASAPLP GFSTPGRLFD QRFGEGLLEA ELASLCPAAI APYYLRAPSV
ALPTAQVPTD PGYFSVLLDV KHFSPEEISV KVVGDHVEVH ARHEERPDEH GFIAREFHRR
YRLPPGVDPA AVTSALSPEG VLSIQATPAS AQASLPSPPA AK
