ID A0A2U3VN73_ODORO Unreviewed; 158 AA.
AC A0A2U3VN73;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Heat shock protein beta-6 {ECO:0000313|RefSeq:XP_004396527.1};
GN Name=HSPB6 {ECO:0000313|RefSeq:XP_004396527.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004396527.1};
RN [1] {ECO:0000313|RefSeq:XP_004396527.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Contributes to the transparency and refractive index of the
CC lens. Acts as a chaperone, preventing aggregation of various proteins
CC under a wide range of stress conditions. Required for the correct
CC formation of lens intermediate filaments as part of a complex composed
CC of BFSP1, BFSP2 and CRYAA. {ECO:0000256|ARBA:ARBA00003785}.
CC -!- SUBUNIT: Heteromer composed of three CRYAA and one CRYAB subunits.
CC Inter-subunit bridging via zinc ions enhances stability, which is
CC crucial as there is no protein turn over in the lens. Can also form
CC homodimers and homotetramers (dimers of dimers) which serve as the
CC building blocks of homooligomers (By similarity). Within homooligomers,
CC the zinc-binding motif is created from residues of 3 different
CC molecules. His-100 and Glu-102 from one molecule are ligands of the
CC zinc ion, and His-107 and His-154 residues from additional molecules
CC complete the site with tetrahedral coordination geometry (By
CC similarity). Part of a complex required for lens intermediate filament
CC formation composed of BFSP1, BFSP2 and CRYAA.
CC {ECO:0000256|ARBA:ARBA00025956}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000256|PROSITE-ProRule:PRU00285, ECO:0000256|RuleBase:RU003616}.
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DR RefSeq; XP_004396527.1; XM_004396470.2.
DR AlphaFoldDB; A0A2U3VN73; -.
DR STRING; 9708.A0A2U3VN73; -.
DR GeneID; 101381143; -.
DR KEGG; oro:101381143; -.
DR CTD; 126393; -.
DR InParanoid; A0A2U3VN73; -.
DR OrthoDB; 3014506at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:InterPro.
DR CDD; cd06478; ACD_HspB4-5-6; 1.
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:SF2; HEAT SHOCK PROTEIN BETA-6; 1.
DR PANTHER; PTHR45640; HEAT SHOCK PROTEIN HSP-12.2-RELATED; 1.
DR Pfam; PF00525; Crystallin; 1.
DR Pfam; PF00011; HSP20; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW Stress response {ECO:0000313|RefSeq:XP_004396527.1}.
FT DOMAIN 51..158
FT /note="SHSP"
FT /evidence="ECO:0000259|PROSITE:PS01031"
FT REGION 138..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 158 AA; 17138 MW; 3239D2257127ADE3 CRC64;
MEIPVPVQPS WLRRASAPLP GRLFDQRFGE GLLEAELAAL CPASLAPYYL RAPSVALPTA
QVPTEPGHFS VLLDVKHFSP EEIAVKVVGD HVEVHARHEE RPDEHGYIAR EFHRRYRLPP
GVDPAAVTSA LSPEGVLSIQ AAPTTPQAPL PQPQAAAK
//
