CRYAA_MACMU
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 03-AUG-2022, entry version 132.
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-Linked glycan.
DR iPTMnet; P02488; -.
DR Ensembl; ENSMMUT00000028514; ENSMMUP00000026679; ENSMMUG00000020271.
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 OrthoDB; 1187096at2759; -.
DR Proteomes; UP000006718; Chromosome 3.
DR Bgee; ENSMMUG00000020271; Expressed in adult mammalian kidney and 10 other 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 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 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
