CRYAA_PELLE
ID CRYAA_PELLE Reviewed; 167 AA.
AC P02507;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Alpha-crystallin A chain;
DE Flags: Fragments;
GN Name=CRYAA;
OS Pelophylax lessonae (Pool frog) (Rana lessonae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=45623;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
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. May act as a chaperone, preventing aggregation of various
CC proteins under a wide range of stress conditions.
CC {ECO:0000250|UniProtKB:P02489}.
CC -!- SUBUNIT: Heteropolymer composed of three CRYAA and one CRYAB subunits
CC (By similarity). Inter-subunit bridging via zinc ions enhances
CC stability, which is crucial as there is no protein turn over in the
CC lens. Can also form homodimers and homotetramers (dimers of dimers)
CC which serve as the building blocks of homooligomers (By similarity).
CC Within homooligomers, the zinc-binding motif is created from residues
CC of 3 different molecules. His-94 and Glu-96 from one molecule are
CC ligands of the zinc ion, and His-101 and His-148 residues from
CC additional molecules complete the site with tetrahedral coordination
CC geometry (By 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. {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 PIR; A02910; CYFGAA.
DR AlphaFoldDB; P02507; -.
DR SMR; P02507; -.
DR iPTMnet; P02507; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Eye lens protein;
KW Glycoprotein; Metal-binding; Nucleus; Zinc.
FT CHAIN 1..167
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125901"
FT DOMAIN 47..158
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 143..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 148
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:6723655"
FT CARBOHYD 156
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT NON_CONS 70..71
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 19242 MW; EEDCB4DD6EE5469A CRC64;
MDITIQHPWF KRALGPFYPN RLFDQVFGEG MFDYDLFPFL SSTISPYYRQ SFFRGFLDSG
ISEVRSDRDR VKHFSPEDLT VKILDDFVEI HGKHSERQDD HGYISREFHR RYRLPSNLNE
SSISCSLSAD GILTFSGPKL MSSLDSSHGE RPIPVSREEK PTSAPSS
