CRYAA_RABIT
ID CRYAA_RABIT Reviewed; 173 AA.
AC P02493; A2IBH4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Alpha-crystallin A chain;
GN Name=CRYAA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-122.
RC TISSUE=Lens;
RX PubMed=8427639; DOI=10.1007/bf01024920;
RA Parveen R., Smith J.B., Sun Y., Smith D.L.;
RT "Primary structure of rabbit lens alpha-crystallins.";
RL J. Protein Chem. 12:93-101(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=8814151;
RA Krausz E., Augusteyn R.C., Quinlan R.A., Reddan J.R., Russell P., Sax C.M.,
RA Graw J.;
RT "Expression of crystallins, Pax6, filensin, CP49, MIP, and MP20 in lens-
RT derived cell lines.";
RL Invest. Ophthalmol. Vis. Sci. 37:2120-2128(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Wistow G.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-5 AND 146-150, 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).
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 (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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X95382; CAA64668.1; -; mRNA.
DR EMBL; EF187820; ABM74183.1; -; mRNA.
DR PIR; A02896; CYRBAA.
DR RefSeq; NP_001075875.2; NM_001082406.2.
DR AlphaFoldDB; P02493; -.
DR SMR; P02493; -.
DR STRING; 9986.ENSOCUP00000024422; -.
DR iPTMnet; P02493; -.
DR Ensembl; ENSOCUT00000003454; ENSOCUP00000002996; ENSOCUG00000003457.
DR GeneID; 100009294; -.
DR KEGG; ocu:100009294; -.
DR CTD; 1409; -.
DR GeneTree; ENSGT00940000160159; -.
DR InParanoid; P02493; -.
DR OrthoDB; 1187096at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000003457; Expressed in embryo and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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 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..173
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125882"
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 145..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:8427639, ECO:0000269|Ref.4"
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:8427639"
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 CONFLICT 170
FT /note="A -> V (in Ref. 2; CAA64668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 173 AA; 19837 MW; C12C25369CC327EA CRC64;
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG
ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ EDFVEIHGKH NERQDDHGYI SREFHRRYRL
PSNVDQSALS CSLSADGMLT FSGPKVQSGL DAGHSERAIP VSREEKPSSA PSS
