CRYAA_ANAPL
ID CRYAA_ANAPL Reviewed; 149 AA.
AC O12984;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Alpha-crystallin A chain;
DE Flags: Fragment;
GN Name=CRYAA;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Pekin breed; TISSUE=Lens;
RX PubMed=9126559; DOI=10.1006/mpev.1996.0384;
RA Caspers G.J., Uit de Weerd D., Wattel J., de Jong W.W.;
RT "Alpha-crystallin sequences support a galliform/anseriform clade.";
RL Mol. Phylogenet. Evol. 7:185-188(1997).
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-89 and Glu-91 from one molecule are
CC ligands of the zinc ion, and His-96 and His-143 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; X96592; CAA65410.1; -; mRNA.
DR AlphaFoldDB; O12984; -.
DR SMR; O12984; -.
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 2: Evidence at transcript level;
KW Cytoplasm; Eye lens protein; Metal-binding; Nucleus; Zinc.
FT CHAIN <1..>149
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125892"
FT DOMAIN 41..149
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT NON_TER 1
FT NON_TER 149
SQ SEQUENCE 149 AA; 17017 MW; 35815475430B7290 CRC64;
RALGPLIPSR LFDQFFGEGL LEYDLLPLFS STISPYYRQS LFRSVLESGI SEVRSDRDKF
TIMLDVKHFS PEDLSVKIID DFVEIHGKHS ERQDDHGYIS REFHRRYRLP ANVDQSAITC
SLSGDGMLTF SGPKVPSNMD PTHSERPIP