CRYAA_PROCA
ID CRYAA_PROCA Reviewed; 173 AA.
AC P02499;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-crystallin A chain;
GN Name=CRYAA;
OS Procavia capensis (Rock hyrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Hyracoidea; Procaviidae; Procavia.
OX NCBI_TaxID=9813;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=870070; DOI=10.1016/0005-2795(77)90303-8;
RA de Jong W.W., Nuy-Terwindt E.C., Versteeg M.;
RT "Primary structures of alpha-crystallin A chains of elephant, whale, hyrax
RT and rhinoceros.";
RL Biochim. Biophys. Acta 491:573-580(1977).
CC -!- FUNCTION: Contributes to the transparency and refractive index of the
CC lens. In its oxidized form (absence of intramolecular disulfide bond),
CC acts as a chaperone, preventing aggregation of various proteins under a
CC wide range of stress conditions. Required for the correct formation of
CC lens intermediate filaments as part of a complex composed of BFSP1,
CC BFSP2 and CRYAA. {ECO:0000250|UniProtKB:P02489}.
CC -!- SUBUNIT: Heteromer composed of three CRYAA and one CRYAB subunits.
CC Inter-subunit bridging via zinc ions enhances stability, which is
CC crucial as there is no protein turn over in the lens. Can also form
CC homodimers and homotetramers (dimers of dimers) which serve as the
CC building blocks of homooligomers (By similarity). Within homooligomers,
CC the zinc-binding motif is created from residues of 3 different
CC molecules. His-100 and Glu-102 from one molecule are ligands of the
CC zinc ion, and His-107 and His-154 residues from additional molecules
CC complete the site with tetrahedral coordination geometry (By
CC similarity). Part of a complex required for lens intermediate filament
CC formation composed of BFSP1, BFSP2 and CRYAA (By similarity).
CC {ECO:0000250|UniProtKB:P02470, 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 and resides in sub-nuclear structures known as SC35 speckles
CC or nuclear splicing speckles. {ECO:0000250|UniProtKB:P02489}.
CC -!- PTM: Undergoes age-dependent proteolytical cleavage at the C-terminus.
CC {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 PIR; A02902; CYHXAA.
DR AlphaFoldDB; P02499; -.
DR SMR; P02499; -.
DR iPTMnet; P02499; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR OMA; FRDWWED; -.
DR TreeFam; TF105049; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0032387; P:negative regulation of intracellular transport; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; 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; 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; Chaperone; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Eye lens protein; Glycoprotein; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Zinc.
FT CHAIN 1..173
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125880"
FT DOMAIN 52..162
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 1..63
FT /note="Required for complex formation with BFSP1 and BFSP2"
FT /evidence="ECO:0000250|UniProtKB:P02489"
FT REGION 147..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:870070"
FT MOD_RES 6
FT /note="Deamidated glutamine; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02489"
FT MOD_RES 50
FT /note="Deamidated glutamine; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02489"
FT MOD_RES 101
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT MOD_RES 123
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 147
FT /note="Deamidated glutamine; partial"
FT /evidence="ECO:0000250"
FT CARBOHYD 162
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT DISULFID 131..142
FT /evidence="ECO:0000250|UniProtKB:P02489"
FT VARIANT 55
FT /note="T -> A (in 50% of the molecules)"
SQ SEQUENCE 173 AA; 19822 MW; 96E093F224297228 CRC64;
MDVTIQHPWF KRALGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG
ISEVRSDRDQ FLILLDVKHF SPEDLTVKVL DDFVEIHGKH NERQDDHGYI SREFHRRYRL
PSNVDQSALS CSLSADGMLT FCGPKVQSGM DASHSERAIP VSREEKPSSA PSS
