ID   CRYAA_ASTFA             Reviewed;         173 AA.
AC   O93591;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Alpha-crystallin A chain;
GN   Name=cryaa;
OS   Astyanax fasciatus (Blind cave fish) (Astyanax mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Psalidodon.
OX   NCBI_TaxID=223369;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Spleen;
RX   PubMed=9729440; DOI=10.1016/s0378-1119(98)00346-1;
RA   Behrens M., Wilkens H., Schmale H.;
RT   "Cloning of the alphaA-crystallin genes of a blind cave form and the
RT   epigean form of Astyanax fasciatus: a comparative analysis of structure,
RT   expression and evolutionary conservation.";
RL   Gene 216:319-326(1998).
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. Zinc coordination is achieved at least by His-101, Glu-103 and
CC       His-108. His-101 and Glu-103 come from the same molecule within the
CC       oligomer, while His-108 residue is provided by another molecule (By
CC       similarity). Can also form homodimers and homotetramers (dimers of
CC       dimers) which serve as the building blocks of homooligomers. Part of a
CC       complex required for lens intermediate filament formation composed of
CC       BFSP1, BFSP2 and CRYAA (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; Y11301; CAA72159.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93591; -.
DR   SMR; O93591; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Disulfide bond; Eye lens protein; Metal-binding;
KW   Nucleus; Zinc.
FT   CHAIN           1..173
FT                   /note="Alpha-crystallin A chain"
FT                   /id="PRO_0000125903"
FT   DOMAIN          53..164
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   REGION          143..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        132..143
FT                   /evidence="ECO:0000250|UniProtKB:P02489"
SQ   SEQUENCE   173 AA;  19804 MW;  3076D61255D0FA00 CRC64;
     MDIAIQHPWF RRALGYPSRL FDQFFGEGLF DYDLFPYATS TVSPYYRYSL FRNFLDSSNS
     GMSEVRSDRD KFMVYLDVKH FSPEELNVKV AEDYVEIQGK HGERQDDHGY ISREFHRRYR
     LPSNVDQSAI TCTLSADGQL TICGPKSGGS ESGRGDRSIP VTRDDKTNST PSS