CRYAB_CHICK
ID CRYAB_CHICK Reviewed; 174 AA.
AC Q05713; Q90657;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alpha-crystallin B chain;
DE AltName: Full=Alpha(B)-crystallin;
GN Name=CRYAB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=1283129; DOI=10.1016/0014-4835(92)90014-j;
RA Sawada K., Agata K., Eguchi G.;
RT "Crystallin gene expression in the process of lentoidogenesis in cultures
RT of chicken lens epithelial cells.";
RL Exp. Eye Res. 55:879-887(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hubbard White Mountain; TISSUE=Testis;
RX PubMed=9099889; DOI=10.1016/s0378-1119(96)00763-9;
RA Macip S., Mezquita C., Mezquita J.;
RT "Alternative transcriptional initiation and alternative use of
RT polyadenylation signals in the alphaB-crystallin gene expressed in
RT different chicken tissues.";
RL Gene 187:253-257(1997).
CC -!- FUNCTION: May contribute to the transparency and refractive index of
CC the lens.
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. {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; S53164; AAB25041.1; -; mRNA.
DR EMBL; U26661; AAB53019.1; -; mRNA.
DR PIR; A49181; A49181.
DR RefSeq; NP_990507.1; NM_205176.1.
DR AlphaFoldDB; Q05713; -.
DR SMR; Q05713; -.
DR STRING; 9031.ENSGALP00000012892; -.
DR PaxDb; Q05713; -.
DR PRIDE; Q05713; -.
DR Ensembl; ENSGALT00000012907; ENSGALP00000012892; ENSGALG00000007945.
DR GeneID; 396089; -.
DR KEGG; gga:396089; -.
DR CTD; 1410; -.
DR VEuPathDB; HostDB:geneid_396089; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000157434; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; Q05713; -.
DR OMA; RPSFMRW; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; Q05713; -.
DR TreeFam; TF105049; -.
DR Reactome; R-GGA-3371571; HSF1-dependent transactivation.
DR PRO; PR:Q05713; -.
DR Proteomes; UP000000539; Chromosome 24.
DR Bgee; ENSGALG00000007945; Expressed in muscle tissue and 9 other tissues.
DR ExpressionAtlas; Q05713; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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; IBA:GO_Central.
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:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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 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 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; Eye lens protein; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..174
FT /note="Alpha-crystallin B chain"
FT /id="PRO_0000125917"
FT DOMAIN 55..163
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 148..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
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"
FT CONFLICT 10
FT /note="I -> V (in Ref. 1; AAB25041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 20034 MW; 931ABA872438EBF6 CRC64;
MDITIHNPLI RRPLFSWLTP SRIFDQIFGE HLQESELLPT SPSLSPFLMR SPFFRMPSWL
ETGLSEMRLE KDKFSVNLDV KHFSPEELKV KVLGDMIEIH GKHEERQDEH GFIAREFSRK
YRIPADVDPL TITSSLSLDG VLTVSAPRKQ SDVPERSIPI TREEKPAIAG SQRK
