CRYAA_TRASE
ID CRYAA_TRASE Reviewed; 149 AA.
AC Q91517;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Alpha-crystallin A chain;
DE Flags: Fragment;
GN Name=CRYAA;
OS Trachemys scripta elegans (Red-eared slider turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Emydidae; Trachemys.
OX NCBI_TaxID=31138;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=8662010; DOI=10.1007/bf02352288;
RA Caspers G.J., Reinders G.J., Leunissen J.A.M., Wattel J., de Jong W.W.;
RT "Protein sequences indicate that turtles branched off from the amniote tree
RT after mammals.";
RL J. Mol. Evol. 42:580-586(1996).
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 (By similarity). Zinc coordination is achieved at least by His-89,
CC Glu-91 and His-96. His-83 and Glu-85 come from the same molecule within
CC the oligomer, while His-90 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 (By
CC 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; U31938; AAB08829.1; -; mRNA.
DR AlphaFoldDB; Q91517; -.
DR SMR; Q91517; -.
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_0000125898"
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 NON_TER 1
FT NON_TER 149
SQ SEQUENCE 149 AA; 17214 MW; B6F8BC4F36968C5C CRC64;
RALGPLFPSR LFDQYLGEGL FDYDLLPFFS STISPYYRHS LFRTVLESGI SEVRSDRDKF
TILLDVKHFS PEDLSVKIMD DFVEIHGKHN ERQDDHGYIS REFHRRYRLP SNVDQSAITC
SLSADGMLTF SGPKVQSNMD TSYSERPIP
