HSPB6_BOVIN
ID HSPB6_BOVIN Reviewed; 164 AA.
AC Q148F8; A1A4M7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Heat shock protein beta-6;
DE Short=HspB6;
GN Name=HSPB6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle, and Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=15722443; DOI=10.1110/ps.041020705;
RA Lee S., Carson K., Rice-Ficht A., Good T.;
RT "Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and
RT toxicity.";
RL Protein Sci. 14:593-601(2005).
CC -!- FUNCTION: Small heat shock protein which functions as a molecular
CC chaperone probably maintaining denatured proteins in a folding-
CC competent state. Seems to have versatile functions in various
CC biological processes. Plays a role in regulating muscle function such
CC as smooth muscle vasorelaxation and cardiac myocyte contractility. May
CC regulate myocardial angiogenesis implicating KDR. Overexpression
CC mediates cardioprotection and angiogenesis after induced damage.
CC Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like
CC activity. {ECO:0000250|UniProtKB:O14558, ECO:0000269|PubMed:15722443}.
CC -!- SUBUNIT: Homodimer. Small heat shock proteins form high molecular mass
CC oligomers containing variable number of monomers; these oligomers
CC display a very flexible quaternary structure easily exchanging their
CC subunits. Heterooligomer with HSPB1; formed through oligomerization of
CC HSPB1:HSBP6 dimers; subunit exchange leads to formation of at least two
CC different heterooligomeric complexes, differing in variable quantities
CC of HSPB1 and HSPB6 homodimers in addition to HSPB1:HSPB6 heterodimers.
CC Heterooligomer with CRYAB; large heterooligomers consist of CRYAB
CC homodimers and HSPB5:HSPB6 heterodimers but lacking HSPB6 homodimers.
CC Interacts with BAG3. Interacts (phosphorylated) with YWHAZ. Interacts
CC with PDE4A and PDE4D; required for maintenance of the non-
CC phosphorylated state of HSPB6 under basal conditions. Interacts with
CC KDR. Interacts with PRKD1. {ECO:0000250|UniProtKB:O14558,
CC ECO:0000250|UniProtKB:P97541}.
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 -!- PTM: Phosphorylated at Ser-16 by PKA and probably PKD1K; required to
CC protect cardiomyocytes from apoptosis. {ECO:0000250|UniProtKB:O14558,
CC ECO:0000250|UniProtKB:P97541, ECO:0000250|UniProtKB:Q5EBG6}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; BC118368; AAI18369.1; -; mRNA.
DR EMBL; BC126729; AAI26730.1; -; mRNA.
DR RefSeq; NP_001069495.1; NM_001076027.1.
DR AlphaFoldDB; Q148F8; -.
DR SMR; Q148F8; -.
DR STRING; 9913.ENSBTAP00000024749; -.
DR iPTMnet; Q148F8; -.
DR PaxDb; Q148F8; -.
DR PeptideAtlas; Q148F8; -.
DR PRIDE; Q148F8; -.
DR GeneID; 534551; -.
DR KEGG; bta:534551; -.
DR CTD; 126393; -.
DR eggNOG; KOG3591; Eukaryota.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; Q148F8; -.
DR OrthoDB; 1187096at2759; -.
DR TreeFam; TF105049; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Chaperone; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Secreted; Stress response.
FT CHAIN 1..164
FT /note="Heat shock protein beta-6"
FT /id="PRO_0000252667"
FT DOMAIN 56..163
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:0000250|UniProtKB:O14558"
FT MOD_RES 66
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250|UniProtKB:P97541"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97541"
FT CONFLICT 6
FT /note="S -> P (in Ref. 1; AAI26730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 17469 MW; D632362407A6C9C6 CRC64;
MEIPVSVQPS WLRRASAPLP GLSAPGRLFD QRFGEGLLEA ELAALCPAAL APYYLRAPSV
ALPTAQVSTD PGHFSVLLDV KHFSPEEIAV KVVGDHVEVH ARHEERPDEH GYIAREFHRR
YRLPPGVDPA AVTSALSPEG VLSIQAAPAP AQAPLQSPPG AAAK
