CRYAB_MESAU
ID CRYAB_MESAU Reviewed; 175 AA.
AC P05811;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Alpha-crystallin B chain;
DE AltName: Full=Alpha(B)-crystallin;
GN Name=CRYAB;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3862098; DOI=10.1073/pnas.82.17.5819;
RA Quax-Jeuken Y., Quax W., van Rens G., Khan P.M., Bloemendal H.;
RT "Complete structure of the alpha B-crystallin gene: conservation of the
RT exon-intron distribution in the two nonlinked alpha-crystallin genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5819-5823(1985).
CC -!- FUNCTION: May contribute to the transparency and refractive index of
CC the lens. Has chaperone-like activity, preventing aggregation of
CC various proteins under a wide range of stress conditions. In lens
CC epithelial cells, stabilizes the ATP6V1A protein, preventing its
CC degradation by the proteasome (By similarity).
CC {ECO:0000250|UniProtKB:P23927}.
CC -!- SUBUNIT: Heteromer composed of three CRYAA and one CRYAB subunits.
CC Aggregates with homologous proteins, including the small heat shock
CC protein HSPB1, to form large heteromeric complexes. Inter-subunit
CC bridging via zinc ions enhances stability, which is crucial as there is
CC no protein turn over in the lens. Interacts with HSPBAP1 and TTN/titin.
CC Interacts with TMEM109. Interacts with DES; binds rapidly during early
CC stages of DES filament assembly and a reduced binding seen in the later
CC stages. Interacts with TMED10; the interaction mediates the
CC translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) and thereby secretion. Interacts with
CC ATP6V1A and with MTOR, forming a ternary complex (By similarity).
CC {ECO:0000250|UniProtKB:P02511, ECO:0000250|UniProtKB:P23927}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02511}. Nucleus
CC {ECO:0000250|UniProtKB:P02511}. Secreted
CC {ECO:0000250|UniProtKB:P02511}. Lysosome
CC {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during
CC heat shock and resides in sub-nuclear structures known as SC35 speckles
CC or nuclear splicing speckles. Localizes at the Z-bands and the
CC intercalated disk in cardiomyocytes. Can be secreted; the secretion is
CC dependent on protein unfolding and facilitated by the cargo receptor
CC TMED10; it results in protein translocation from the cytoplasm into the
CC ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed
CC by vesicle entry and secretion. {ECO:0000250|UniProtKB:P02511}.
CC -!- TISSUE SPECIFICITY: Lens as well as other tissues.
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; M12016; AAA37067.1; -; Genomic_DNA.
DR EMBL; M12014; AAA37067.1; JOINED; Genomic_DNA.
DR EMBL; M12015; AAA37067.1; JOINED; Genomic_DNA.
DR RefSeq; XP_012968459.1; XM_013113005.1.
DR AlphaFoldDB; P05811; -.
DR SMR; P05811; -.
DR STRING; 10036.XP_005069569.1; -.
DR GeneID; 101827485; -.
DR CTD; 1410; -.
DR eggNOG; KOG3591; Eukaryota.
DR OrthoDB; 1187096at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0032387; P:negative regulation of intracellular transport; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:Ensembl.
DR CDD; cd06498; ACD_alphaB-crystallin_HspB5; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR037882; ACD_alphaB-crystallin.
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 PIRSF; PIRSF036514; Sm_HSP_B1; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chaperone; Cytoplasm; Eye lens protein; Glycoprotein;
KW Lysosome; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted; Zinc.
FT CHAIN 1..175
FT /note="Alpha-crystallin B chain"
FT /id="PRO_0000125909"
FT DOMAIN 56..164
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 145..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02510, ECO:0000305"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02510"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02510"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02510"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02511"
FT MOD_RES 166
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02511"
FT CARBOHYD 170
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 175 AA; 20075 MW; BD1CC5B291493038 CRC64;
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR PPSFLRAPSW
IDTGLSEMRM EKDRFSVNLD VKHFSPEELK VKVLGDVVEV HGKHEERQDE HGFISREFHR
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QASGPERTIP ITREEKPAVT AAPKK
