CRYAA_SQUAC
ID CRYAA_SQUAC Reviewed; 177 AA.
AC P02509;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Alpha-crystallin A chain;
GN Name=cryaa;
OS Squalus acanthias (Spiny dogfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Squalomorphii; Squaliformes; Squalidae; Squalus.
OX NCBI_TaxID=7797;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=3356684; DOI=10.1016/s0021-9258(18)60691-x;
RA de Jong W.W., Leunissen J.A.M., Leenen P.J.M., Zweers A., Versteeg M.;
RT "Dogfish alpha-crystallin sequences. Comparison with small heat shock
RT proteins and Schistosoma egg antigen.";
RL J. Biol. Chem. 263:5141-5149(1988).
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.
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; A28190; CYDFAA.
DR AlphaFoldDB; P02509; -.
DR SMR; P02509; -.
DR iPTMnet; P02509; -.
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 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; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Eye lens protein; Glycoprotein; Metal-binding; Nucleus; Zinc.
FT CHAIN 1..177
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125905"
FT DOMAIN 52..162
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 146..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:3356684"
FT CARBOHYD 162
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT DISULFID 131..142
FT /evidence="ECO:0000250|UniProtKB:P02489"
SQ SEQUENCE 177 AA; 20680 MW; 652469F3FC603E29 CRC64;
MDLAIQYPWF RRSLGSFYPS RLFDQFFGEG LFDYDLFPFF SSTISPYYRQ SVFRNFLDSG
ISEVRSEKDR FMINLNVKHF SPEELSVKIV DDYVEIHGKH AERQEDQGRV SREFHRTYHL
PSNLNESAIA CSLSNEGLLT LCCPKTRPGD DSNWQDRPIP VSREEKQGTQ PEIRADP
