CRYAA_MOUSE
ID CRYAA_MOUSE Reviewed; 196 AA.
AC P24622; P02490; P02496; P82532; Q61444; Q6LEL4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Alpha-crystallin A chain;
GN Name=Cryaa; Synonyms=Crya1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=6187470; DOI=10.1016/0092-8674(83)90056-9;
RA King C.R., Piatigorsky J.;
RT "Alternative RNA splicing of the murine alpha A-crystallin gene: protein-
RT coding information within an intron.";
RL Cell 32:707-712(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-196 (ISOFORM 2).
RX PubMed=7156978; DOI=10.1126/science.7156978;
RA King C.R., Shinohara T., Piatigorsky J.;
RT "Alpha A-crystallin messenger RNA of the mouse lens: more noncoding than
RT coding sequences.";
RL Science 215:985-987(1982).
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: Heteropolymer 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-123 and Glu-125 from one molecule are ligands of the
CC zinc ion, and His-130 and His-177 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Minor, Alpha-A(ins);
CC IsoId=P24622-1; Sequence=Displayed;
CC Name=2; Synonyms=Major;
CC IsoId=P24622-2; Sequence=VSP_011916;
CC -!- PTM: Acetylation at Lys-93 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 -!- MISCELLANEOUS: [Isoform 1]: Constitutes approximately 10% of the total
CC alpha-A-crystallin in the lens.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; V00730; CAA24108.2; -; Genomic_DNA.
DR EMBL; V00730; CAA24109.2; -; Genomic_DNA.
DR EMBL; J00375; AAA37469.1; -; Genomic_DNA.
DR EMBL; J00375; AAA37470.1; -; Genomic_DNA.
DR EMBL; J00376; AAA37471.1; -; mRNA.
DR CCDS; CCDS37551.1; -. [P24622-1]
DR CCDS; CCDS89061.1; -. [P24622-2]
DR PIR; A02893; CYMSA.
DR PIR; B18860; B18860.
DR RefSeq; NP_038529.1; NM_013501.3. [P24622-1]
DR AlphaFoldDB; P24622; -.
DR SMR; P24622; -.
DR STRING; 10090.ENSMUSP00000019192; -.
DR GlyGen; P24622; 1 site.
DR iPTMnet; P24622; -.
DR PhosphoSitePlus; P24622; -.
DR PaxDb; P24622; -.
DR PRIDE; P24622; -.
DR ProteomicsDB; 285337; -. [P24622-1]
DR ProteomicsDB; 285338; -. [P24622-2]
DR DNASU; 12954; -.
DR Ensembl; ENSMUST00000019192; ENSMUSP00000019192; ENSMUSG00000024041. [P24622-1]
DR Ensembl; ENSMUST00000228716; ENSMUSP00000154747; ENSMUSG00000024041. [P24622-2]
DR GeneID; 12954; -.
DR KEGG; mmu:12954; -.
DR UCSC; uc008bvp.2; mouse. [P24622-1]
DR CTD; 1409; -.
DR MGI; MGI:88515; Cryaa.
DR VEuPathDB; HostDB:ENSMUSG00000024041; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000160159; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; P24622; -.
DR OMA; FRDWWED; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P24622; -.
DR TreeFam; TF105049; -.
DR BioGRID-ORCS; 12954; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Cryaa; mouse.
DR PRO; PR:P24622; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P24622; protein.
DR Bgee; ENSMUSG00000024041; Expressed in lens of camera-type eye and 53 other tissues.
DR ExpressionAtlas; P24622; baseline and differential.
DR Genevisible; P24622; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005212; F:structural constituent of eye lens; TAS:MGI.
DR GO; GO:0005198; F:structural molecule activity; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IGI:MGI.
DR GO; GO:0043010; P:camera-type eye development; IGI:MGI.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:0070309; P:lens fiber cell morphogenesis; IMP:MGI.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0007017; P:microtubule-based process; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IGI:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0032387; P:negative regulation of intracellular transport; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0070141; P:response to UV-A; IMP:MGI.
DR GO; GO:0007021; P:tubulin complex assembly; IMP:MGI.
DR GO; GO:0007601; P:visual perception; ISO:MGI.
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 PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm; Eye lens protein;
KW Glycoprotein; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..196
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125872"
FT DOMAIN 76..185
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 168..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 177
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:0000250|UniProtKB:P02474, ECO:0000305"
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 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02489"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02489"
FT MOD_RES 124
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT MOD_RES 146
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 170
FT /note="Deamidated glutamine; partial"
FT /evidence="ECO:0000250"
FT CARBOHYD 185
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 64..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7156978"
FT /id="VSP_011916"
SQ SEQUENCE 196 AA; 22489 MW; A6063BB21EEB8E78 CRC64;
MDVTIQHPWF KRALGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG
ISELMTHMWF VMHQPHAGNP KNNPVKVRSD RDKFVIFLDV KHFSPEDLTV KVLEDFVEIH
GKHNERQDDH GYISREFHRR YRLPSNVDQS ALSCSLSADG MLTFSGPKVQ SGLDAGHSER
AIPVSREEKP SSAPSS
