CRYAA_BOVIN
ID CRYAA_BOVIN Reviewed; 173 AA.
AC P02470;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Alpha-crystallin A chain;
DE Contains:
DE RecName: Full=Alpha-crystallin A(1-172);
DE Contains:
DE RecName: Full=Alpha-crystallin A(1-168);
GN Name=CRYAA; Synonyms=CRYA1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=4770792; DOI=10.1111/j.1432-1033.1973.tb03119.x;
RA van der Ouderaa F.J., de Jong W.W., Bloemendal H.;
RT "The amino-acid sequence of the alphaA2 chain of bovine alpha-crystallin.";
RL Eur. J. Biochem. 39:207-222(1973).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3675580; DOI=10.1016/0006-291x(87)91072-2;
RA Hay R.E., Petrash J.M.;
RT "Nucleotide sequence of a bovine lens alpha A-crystallin cDNA.";
RL Biochem. Biophys. Res. Commun. 148:31-37(1987).
RN [3]
RP PROTEIN SEQUENCE, ACETYLATION AT MET-1, AND PHOSPHORYLATION AT SER-122.
RX PubMed=2042736; DOI=10.1016/0003-2697(91)90050-4;
RA Smith J.B., Thevenon-Emeric G., Simth D.L., Green B.;
RT "Elucidation of the primary structures of proteins by mass spectrometry.";
RL Anal. Biochem. 193:118-124(1991).
RN [4]
RP GLYCOSYLATION AT SER-162.
RX PubMed=1730617; DOI=10.1016/s0021-9258(18)48530-4;
RA Roquemore E.P., Dell A., Morris H.R., Panico M., Reason A.J., Savoy L.-A.,
RA Wistow G.J., Zigler J.S. Jr., Earles B.J., Hart G.W.;
RT "Vertebrate lens alpha-crystallins are modified by O-linked N-
RT acetylglucosamine.";
RL J. Biol. Chem. 267:555-563(1992).
RN [5]
RP GLYCATION AT LYS-11 AND LYS-78, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=7912928; DOI=10.1006/bbrc.1994.1866;
RA Abraham E.C., Cherian M., Smith J.B.;
RT "Site selectivity in the glycation of alpha A- and alpha B-crystallins by
RT glucose.";
RL Biochem. Biophys. Res. Commun. 201:1451-1456(1994).
RN [6]
RP PROTEOLYTIC PROCESSING.
RX PubMed=8529423; DOI=10.3109/02713689508995806;
RA Takemoto L.J.;
RT "Identification of the in vivo truncation sites at the C-terminal region of
RT alpha-A crystallin from aged bovine and human lens.";
RL Curr. Eye Res. 14:837-841(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 59-163 IN COMPLEX WITH ZINC,
RP FUNCTION, AND SUBUNIT.
RX PubMed=20440841; DOI=10.1002/pro.380;
RA Laganowsky A., Benesch J.L., Landau M., Ding L., Sawaya M.R., Cascio D.,
RA Huang Q., Robinson C.V., Horwitz J., Eisenberg D.;
RT "Crystal structures of truncated alphaA and alphaB crystallins reveal
RT structural mechanisms of polydispersity important for eye lens function.";
RL Protein Sci. 19:1031-1043(2010).
CC -!- FUNCTION: Contributes to the transparency and refractive index of the
CC lens (By similarity). Acts as a chaperone, preventing aggregation of
CC various proteins under a wide range of stress conditions
CC (PubMed:20440841). Required for the correct formation of lens
CC intermediate filaments as part of a complex composed of BFSP1, BFSP2
CC and CRYAA (By similarity). {ECO:0000250|UniProtKB:P02489,
CC ECO:0000269|PubMed:20440841}.
CC -!- SUBUNIT: Heteromer composed of three CRYAA and one CRYAB subunits (By
CC similarity). Inter-subunit bridging via zinc ions enhances stability,
CC which is crucial as there is no protein turn over in the lens (By
CC similarity) (PubMed:20440841). Can also form homodimers and
CC homotetramers (dimers of dimers) which serve as the building blocks of
CC homooligomers. Within homooligomers, the zinc-binding motif is created
CC from residues of 3 different molecules. His-100 and Glu-102 from one
CC molecule are ligands of the zinc ion, and His-107 and His-154 residues
CC from additional molecules complete the site with tetrahedral
CC coordination geometry (PubMed:20440841). Part of a complex required for
CC lens intermediate filament formation composed of BFSP1, BFSP2 and CRYAA
CC (By similarity). {ECO:0000250|UniProtKB:P02489,
CC ECO:0000269|PubMed:20440841}.
CC -!- INTERACTION:
CC P02470; P02510: CRYAB; NbExp=4; IntAct=EBI-15796552, EBI-7824601;
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:0000269|PubMed:8529423}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; M26142; AAA30471.1; -; mRNA.
DR PIR; A29656; CYBOA.
DR RefSeq; NP_776714.1; NM_174289.2.
DR PDB; 3L1E; X-ray; 1.15 A; A=59-163.
DR PDB; 3L1F; X-ray; 1.53 A; A=62-163.
DR PDBsum; 3L1E; -.
DR PDBsum; 3L1F; -.
DR AlphaFoldDB; P02470; -.
DR BMRB; P02470; -.
DR SMR; P02470; -.
DR DIP; DIP-58566N; -.
DR IntAct; P02470; 1.
DR STRING; 9913.ENSBTAP00000004073; -.
DR CarbonylDB; P02470; -.
DR GlyConnect; 32; 1 O-Linked glycan (1 site).
DR GlyConnect; 35; 1 O-Linked glycan (1 site).
DR GlyConnect; 36; 1 O-Linked glycan (1 site).
DR iPTMnet; P02470; -.
DR PaxDb; P02470; -.
DR PRIDE; P02470; -.
DR Ensembl; ENSBTAT00000004073; ENSBTAP00000004073; ENSBTAG00000003134.
DR GeneID; 281718; -.
DR KEGG; bta:281718; -.
DR CTD; 1409; -.
DR VEuPathDB; HostDB:ENSBTAG00000003134; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000160159; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; P02470; -.
DR OMA; FRDWWED; -.
DR OrthoDB; 1187096at2759; -.
DR TreeFam; TF105049; -.
DR EvolutionaryTrace; P02470; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000003134; Expressed in pigment epithelium of eye and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA: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; IDA:UniProtKB.
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: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 3D-structure; Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Eye lens protein; Glycation; Glycoprotein; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..173
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125848"
FT CHAIN 1..172
FT /note="Alpha-crystallin A(1-172)"
FT /id="PRO_0000226605"
FT CHAIN 1..168
FT /note="Alpha-crystallin A(1-168)"
FT /id="PRO_0000423502"
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 144..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..163
FT /note="Important for oligomerization"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20440841"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20440841"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:20440841"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:20440841"
FT SITE 70
FT /note="Not glycated"
FT SITE 88
FT /note="Not glycated"
FT SITE 99
FT /note="Not glycated"
FT SITE 145
FT /note="Not glycated"
FT SITE 166
FT /note="Not glycated"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:2042736"
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:0000269|PubMed:2042736"
FT MOD_RES 123
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000250"
FT CARBOHYD 11
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:7912928"
FT CARBOHYD 78
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:7912928"
FT CARBOHYD 162
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:1730617"
FT /id="CAR_000056"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3L1E"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:3L1E"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3L1E"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3L1E"
FT STRAND 93..104
FT /evidence="ECO:0007829|PDB:3L1E"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3L1E"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:3L1E"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3L1E"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:3L1E"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:3L1E"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3L1E"
SQ SEQUENCE 173 AA; 19790 MW; 7796ED1B71864478 CRC64;
MDIAIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG
ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ EDFVEIHGKH NERQDDHGYI SREFHRRYRL
PSNVDQSALS CSLSADGMLT FSGPKIPSGV DAGHSERAIP VSREEKPSSA PSS
