CRYAA_CHICK
ID CRYAA_CHICK Reviewed; 173 AA.
AC P02504;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Alpha-crystallin A chain;
GN Name=CRYAA;
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 [GENOMIC DNA].
RX PubMed=3678835; DOI=10.1016/0378-1119(87)90135-1;
RA Thompson M.A., Hawkins J.W., Piatigorsky J.;
RT "Complete nucleotide sequence of the chicken alpha A-crystallin gene and
RT its 5' flanking region.";
RL Gene 56:173-184(1987).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=6723655; DOI=10.1111/j.1432-1033.1984.tb08167.x;
RA de Jong W.W., Zweers A., Versteeg M., Nuy-Terwindt E.C.;
RT "Primary structures of the alpha-crystallin A chains of twenty-eight
RT mammalian species, chicken and frog.";
RL Eur. J. Biochem. 141:131-140(1984).
CC -!- FUNCTION: Contributes to the transparency and refractive index of the
CC lens. May act as a chaperone, preventing aggregation of various
CC proteins under a wide range of stress conditions.
CC {ECO:0000250|UniProtKB:P02489}.
CC -!- SUBUNIT: Heteropolymer composed of three CRYAA and one CRYAB subunits
CC (By similarity). Inter-subunit bridging via zinc ions enhances
CC stability, which is crucial as there is no protein turn over in the
CC lens. Can also form homodimers and homotetramers (dimers of dimers)
CC which serve as the building blocks of homooligomers (By similarity).
CC Within homooligomers, the zinc-binding motif is created from residues
CC of 3 different molecules. His-100 and Glu-102 from one molecule are
CC ligands of the zinc ion, and His-107 and His-154 residues from
CC additional molecules complete the site with tetrahedral coordination
CC geometry (By similarity). {ECO:0000250|UniProtKB:P02470,
CC ECO:0000250|UniProtKB:P02489}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02489}. Nucleus
CC {ECO:0000250|UniProtKB:P02489}. Note=Translocates to the nucleus during
CC heat shock. {ECO:0000250|UniProtKB:P02489}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; M17627; AAA48722.1; -; Genomic_DNA.
DR PIR; A27309; CYCHAA.
DR RefSeq; NP_001025968.1; NM_001030797.2.
DR AlphaFoldDB; P02504; -.
DR SMR; P02504; -.
DR STRING; 9031.ENSGALP00000035906; -.
DR iPTMnet; P02504; -.
DR PaxDb; P02504; -.
DR Ensembl; ENSGALT00000064401; ENSGALP00000054560; ENSGALG00000016199.
DR GeneID; 418546; -.
DR KEGG; gga:418546; -.
DR CTD; 1409; -.
DR VEuPathDB; HostDB:geneid_418546; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000160159; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; P02504; -.
DR OMA; FRDWWED; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P02504; -.
DR TreeFam; TF105049; -.
DR PRO; PR:P02504; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000016199; Expressed in testis and 3 other tissues.
DR ExpressionAtlas; P02504; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0070062; C:extracellular exosome; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0042802; F:identical protein binding; ISS:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; ISS:AgBase.
DR GO; GO:0002088; P:lens development in camera-type eye; 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:0051260; P:protein homooligomerization; ISS:AgBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; ISS:AgBase.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR012274; Alpha-crystallin_A.
DR InterPro; IPR003090; Alpha-crystallin_N.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR45640; PTHR45640; 1.
DR PANTHER; PTHR45640:SF14; PTHR45640:SF14; 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; Cytoplasm; Direct protein sequencing; Eye lens protein;
KW Glycoprotein; Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..173
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125893"
FT DOMAIN 52..162
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 142..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:6723655"
FT CARBOHYD 162
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 173 AA; 19787 MW; 327AAFCA3D79B399 CRC64;
MDITIQHPWF KRALGPLIPS RLFDQFFGEG LLEYDLLPLF SSTISPYYRQ SLFRSVLESG
ISEVRSDRDK FTIMLDVKHF SPEDLSVKII DDFVEIHGKH SERQDDHGYI SREFHRRYRL
PANVDQSAIT CSLSSDGMLT FSGPKVPSNM DPSHSERPIP VSREEKPTSA PSS
