CRYAB_BOVIN
ID CRYAB_BOVIN Reviewed; 175 AA.
AC P02510; O46508; Q3SZQ9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Alpha-crystallin B chain;
DE AltName: Full=Alpha(B)-crystallin;
GN Name=CRYAB; Synonyms=CRYA2;
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 PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=4477528; DOI=10.1111/j.1432-1033.1974.tb03821.x;
RA van der Ouderaa F.J., de Jong W.W., Hilderink A., Bloemendal H.;
RT "The amino-acids sequence of the alphaB2 chain of bovine alpha-
RT crystallin.";
RL Eur. J. Biochem. 49:157-168(1974).
RN [2]
RP SEQUENCE REVISION TO 80.
RA de Jong W.W.;
RL Submitted (NOV-1991) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kelley P.B., Abraham E.C., Zhao H.R., Shroff N.P., Cherian M., Thomas J.J.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-175.
RX PubMed=8114688; DOI=10.1007/bf01674432;
RA Merck K.B., Horwitz J., Kersten M., Overkamp P., Gaestel M., Bloemendal H.,
RA de Jong W.W.;
RT "Comparison of the homologous carboxy-terminal domain and tail of alpha-
RT crystallin and small heat shock protein.";
RL Mol. Biol. Rep. 18:209-215(1993).
RN [6]
RP PHOSPHORYLATION AT SER-45 AND SER-59.
RX PubMed=3579961; DOI=10.1016/0006-291x(87)91457-4;
RA Chiesa R., Gawinowicz-Kolks M.A., Kleiman N.J., Spector A.;
RT "The phosphorylation sites of the B2 chain of bovine alpha-crystallin.";
RL Biochem. Biophys. Res. Commun. 144:1340-1347(1987).
RN [7]
RP PHOSPHORYLATION AT SER-19 AND SER-45.
RX PubMed=2599111; DOI=10.1016/0014-5793(89)81491-7;
RA Voorter C.E.M., de Haard-Hoekman W.A., Roersma E.S., Meyer H.E.,
RA Bloemendal H., de Jong W.W.;
RT "The in vivo phosphorylation sites of bovine alpha B-crystallin.";
RL FEBS Lett. 259:50-52(1989).
RN [8]
RP SEQUENCE REVISION TO 80, AND PHOSPHORYLATION AT SER-19; SER-45 AND SER-59.
RX PubMed=1304359; DOI=10.1002/pro.5560010506;
RA Smith J.B., Sun Y., Smith D.L., Green B.;
RT "Identification of the posttranslational modifications of bovine lens alpha
RT B-crystallins by mass spectrometry.";
RL Protein Sci. 1:601-608(1992).
RN [9]
RP GLYCATION AT LYS-90 AND LYS-92, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=7912928; DOI=10.1006/bbrc.1994.1866;
RA Abraham E.C., Cherian M., Smith J.B.;
RT "Site selectivity in the glycation of alpha A- and alpha B-crystallins by
RT glucose.";
RL Biochem. Biophys. Res. Commun. 201:1451-1456(1994).
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 -!- INTERACTION:
CC P02510; P02470: CRYAA; NbExp=4; IntAct=EBI-7824601, EBI-15796552;
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 -!- PTM: It is not known whether either Lys-90, or Lys-92, or both are
CC glycated.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; AF029793; AAB95323.2; -; mRNA.
DR EMBL; BC102745; AAI02746.1; -; mRNA.
DR PIR; A42446; CYBOAB.
DR RefSeq; NP_776715.1; NM_174290.2.
DR AlphaFoldDB; P02510; -.
DR BMRB; P02510; -.
DR SMR; P02510; -.
DR BioGRID; 159035; 1.
DR DIP; DIP-43761N; -.
DR IntAct; P02510; 1.
DR MINT; P02510; -.
DR STRING; 9913.ENSBTAP00000000556; -.
DR CarbonylDB; P02510; -.
DR GlyConnect; 32; 1 O-Linked glycan (1 site).
DR GlyConnect; 37; 1 O-Linked glycan.
DR GlyConnect; 38; 1 O-Linked glycan.
DR iPTMnet; P02510; -.
DR UCD-2DPAGE; P02510; -.
DR PaxDb; P02510; -.
DR PeptideAtlas; P02510; -.
DR Ensembl; ENSBTAT00000087415; ENSBTAP00000068917; ENSBTAG00000000434.
DR GeneID; 281719; -.
DR KEGG; bta:281719; -.
DR CTD; 1410; -.
DR VEuPathDB; HostDB:ENSBTAG00000000434; -.
DR VGNC; VGNC:27732; CRYAB.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000157434; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; P02510; -.
DR OrthoDB; 1187096at2759; -.
DR TreeFam; TF105049; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000000434; Expressed in gluteus medius and 102 other tissues.
DR ExpressionAtlas; P02510; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
DR GO; GO:0032387; P:negative regulation of intracellular transport; ISS:AgBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Eye lens protein; Glycation; Glycoprotein; Lysosome; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Secreted; Zinc.
FT CHAIN 1..175
FT /note="Alpha-crystallin B chain"
FT /id="PRO_0000125906"
FT DOMAIN 56..164
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 144..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 SITE 72
FT /note="Not glycated"
FT SITE 82
FT /note="Not glycated"
FT SITE 103
FT /note="Not glycated"
FT SITE 121
FT /note="Not glycated"
FT SITE 150
FT /note="Not glycated"
FT SITE 166
FT /note="Not glycated"
FT SITE 174
FT /note="Not glycated"
FT SITE 175
FT /note="Not glycated"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:4477528"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1304359,
FT ECO:0000269|PubMed:2599111"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1304359,
FT ECO:0000269|PubMed:2599111, ECO:0000269|PubMed:3579961"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1304359,
FT ECO:0000269|PubMed:3579961"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02511"
FT MOD_RES 166
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02511"
FT CARBOHYD 90
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:7912928"
FT CARBOHYD 92
FT /note="N-linked (Glc) (glycation) lysine; alternate"
FT /evidence="ECO:0000269|PubMed:7912928"
SQ SEQUENCE 175 AA; 20037 MW; E0CFBBA8D6DE82B2 CRC64;
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPA STSLSPFYLR PPSFLRAPSW
IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
KYRIPADVDP LAITSSLSSD GVLTVNGPRK QASGPERTIP ITREEKPAVT AAPKK
