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CRYAA_ERIEU
ID   CRYAA_ERIEU             Reviewed;         173 AA.
AC   P82533;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Alpha-crystallin A chain;
GN   Name=CRYAA;
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Lens;
RX   PubMed=6723655; DOI=10.1111/j.1432-1033.1984.tb08167.x;
RA   de Jong W.W., Zweers A., Versteeg M., Nuy-Terwindt E.C.;
RT   "Primary structures of the alpha-crystallin A chains of twenty-eight
RT   mammalian species, chicken and frog.";
RL   Eur. J. Biochem. 141:131-140(1984).
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 (By
CC       similarity). Zinc coordination is achieved at least by His-100, Glu-102
CC       and His-107. His-100 and Glu-102 come from the same molecule within the
CC       oligomer, while His-107 residue is provided by another molecule (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. Can also
CC       form homodimers and homotetramers (dimers of dimers) which serve as the
CC       building blocks of homooligomers. Part of a complex required for lens
CC       intermediate filament formation composed of BFSP1, BFSP2 and CRYAA (By
CC       similarity). {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   AlphaFoldDB; P82533; -.
DR   SMR; P82533; -.
DR   STRING; 9365.XP_007538262.1; -.
DR   eggNOG; KOG3591; Eukaryota.
DR   Proteomes; UP000079721; Unplaced.
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_0000125857"
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   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   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         70
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02489"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02489"
FT   CARBOHYD        162
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   173 AA;  19601 MW;  EB2A85785D442178 CRC64;
     MDVTIQHPWF KRALGPFYPS RLLDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG
     ISEVRSDRDK FVIFLDVKHF SPEDLTVKVL EDFVEIHGKH SERQDDHGYI SREFHRRYRL
     PPSVDQAALS CSLSADGMLT FSGPKVASGL DAGPSERAIP VSREEKPSSA PSS
 
 
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