CRYAA_SPAEH
ID CRYAA_SPAEH Reviewed; 196 AA.
AC P15990; Q64211;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alpha-crystallin A chain;
GN Name=CRYAA;
OS Spalax ehrenbergi (Middle East blind mole rat) (Nannospalax ehrenbergi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Spalacidae; Spalacinae; Nannospalax.
OX NCBI_TaxID=30637;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=3474658; DOI=10.1073/pnas.84.15.5320;
RA Hendriks W., Leunissen J., Nevo E., Bloemendal H., de Jong W.W.;
RT "The lens protein alpha A-crystallin of the blind mole rat, Spalax
RT ehrenbergi: evolutionary change and functional constraints.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5320-5324(1987).
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-123 and Glu-125 from one molecule are ligands of the
CC zinc ion, and His-130 and His-177 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Minor, Alpha-A(ins);
CC IsoId=P15990-1; Sequence=Displayed;
CC Name=2; Synonyms=Major;
CC IsoId=P15990-2, Q64211-1;
CC Sequence=VSP_011918;
CC -!- PTM: Acetylation at Lys-93 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 EMBL; M17249; AAA66165.1; -; Genomic_DNA.
DR EMBL; M17249; AAA66166.1; -; Genomic_DNA.
DR EMBL; M17247; AAA66166.1; JOINED; Genomic_DNA.
DR PIR; A28332; A28332.
DR AlphaFoldDB; P15990; -.
DR SMR; P15990; -.
DR PRIDE; P15990; -.
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 PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 3: Inferred from homology;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm; Eye lens protein;
KW Glycoprotein; Metal-binding; Methylation; Nucleus; Phosphoprotein; Zinc.
FT CHAIN 1..196
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125885"
FT DOMAIN 76..185
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 170..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 177
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: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 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02489"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02489"
FT MOD_RES 124
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT MOD_RES 170
FT /note="Deamidated glutamine; partial"
FT /evidence="ECO:0000250"
FT CARBOHYD 185
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 64..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011918"
SQ SEQUENCE 196 AA; 22532 MW; 4D4090D43EB9F906 CRC64;
MDVTIQHPWF KHALGPFYPS RLFDQFFGQG LFEYDLLPFL SSTISPYYRQ TLLRTVLDSC
ISELMTHRWF VPHQPHAGNP ENNPIKVRSD RDKFVIFLDV KHFSPEDLTV KVLEDFVEIH
GKHNERQDDH GYISREFHRR YRLPSSVDQS ALSCSLSADG MLTFSGPKVQ SGLDAGHSER
AIPVSQEEKP SSAPLF
