ID   CRYAA_MACMU             Reviewed;         172 AA.
AC   P02488;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Alpha-crystallin A chain;
GN   Name=CRYAA;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-6; 89-96 AND 146-162, AND ACETYLATION AT MET-1.
RA   de Jong W.W., van der Ouderaa F.J., Versteeg M., Groenewoud G.,
RA   van Amelsvoort J.M., Bloemendal H.;
RT   "Primary structures of the alpha-crystallin A chains of seven mammalian
RT   species.";
RL   Eur. J. Biochem. 53:237-242(1975).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-162.
RX   PubMed=8587135; DOI=10.1007/bf00173170;
RA   Jaworski C.J.;
RT   "A reassessment of mammalian alpha A-crystallin sequences using DNA
RT   sequencing: implications for anthropoid affinities of tarsier.";
RL   J. Mol. Evol. 41:901-908(1995).
RN   [3]
RP   GLYCOSYLATION AT SER-168.
RX   PubMed=8639509; DOI=10.1021/bi951918j;
RA   Roquemore E.P., Chevrier M.R., Cotter R.J., Hart G.W.;
RT   "Dynamic O-GlcNAcylation of the small heat shock protein alpha B-
RT   crystallin.";
RL   Biochemistry 35:3578-3586(1996).
CC   -!- FUNCTION: Contributes to the transparency and refractive index of the
CC       lens. Acts as a chaperone, preventing aggregation of various proteins
CC       under a wide range of stress conditions. Required for the correct
CC       formation of lens intermediate filaments as part of a complex composed
CC       of BFSP1, 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. Within homooligomers, the zinc-
CC       binding motif is created from residues of 3 different molecules. His-
CC       100 and Glu-102 from one molecule are ligands of the zinc ion, and His-
CC       107 and His-154 residues from additional molecules complete the site
CC       with tetrahedral coordination geometry (By similarity). Part of a
CC       complex required for lens intermediate filament formation composed of
CC       BFSP1, BFSP2 and CRYAA. {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 and resides in sub-nuclear structures known as SC35 speckles
CC       or nuclear splicing speckles. {ECO:0000250|UniProtKB:P02489}.
CC   -!- PTM: Acetylation at Lys-70 may increase chaperone activity.
CC       {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   EMBL; U24061; AAA97563.1; -; Genomic_DNA.
DR   PIR; A02890; CYMQAA.
DR   RefSeq; XP_014988287.1; XM_015132801.1.
DR   AlphaFoldDB; P02488; -.
DR   SMR; P02488; -.
DR   STRING; 9544.ENSMMUP00000026679; -.
DR   GlyConnect; 31; 1 O-GlcNAc glycan.
DR   GlyCosmos; P02488; 1 site, 1 glycan.
DR   iPTMnet; P02488; -.
DR   PaxDb; 9544-ENSMMUP00000026679; -.
DR   Ensembl; ENSMMUT00000028514.4; ENSMMUP00000026679.4; ENSMMUG00000020271.4.
DR   GeneID; 722370; -.
DR   KEGG; mcc:722370; -.
DR   CTD; 1409; -.
DR   VEuPathDB; HostDB:ENSMMUG00000020271; -.
DR   eggNOG; KOG3591; Eukaryota.
DR   GeneTree; ENSGT00940000160159; -.
DR   HOGENOM; CLU_095001_5_0_1; -.
DR   InParanoid; P02488; -.
DR   OMA; QQDDHGY; -.
DR   OrthoDB; 3014506at2759; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000020271; Expressed in adult mammalian kidney and 10 other cell types or tissues.
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; IBA:GO_Central.
DR   GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0032387; P:negative regulation of intracellular transport; IEA:Ensembl.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR   CDD; cd06497; ACD_alphaA-crystallin_HspB4; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR   InterPro; IPR003090; Alpha-crystallin_N.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   PANTHER; PTHR45640:SF14; ALPHA-CRYSTALLIN A CHAIN; 1.
DR   PANTHER; PTHR45640; HEAT SHOCK PROTEIN HSP-12.2-RELATED; 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; HSP20-like chaperones; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Eye lens protein; Glycoprotein; Metal-binding; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..172
FT                   /note="Alpha-crystallin A chain"
FT                   /id="PRO_0000125867"
FT   DOMAIN          52..163
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   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|Ref.1"
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         70
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02489"
FT   MOD_RES         90
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        168
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000269|PubMed:8639509"
FT   CONFLICT        153..154
FT                   /note="TH -> HT (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   172 AA;  19792 MW;  1F7AF9066BEEB2D7 CRC64;
     MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG
     ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL
     PSNVDQSALS CSLSADGMLT FSGPKIQTGL DATHERAIPV AREEKPSSAP SS
//