CRYAA_RAT
ID CRYAA_RAT Reviewed; 196 AA.
AC P24623; P02490; P02496; P82532; Q61444;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Alpha-crystallin A chain;
DE Contains:
DE RecName: Full=Alpha-crystallin A(1-168);
DE Contains:
DE RecName: Full=Alpha-crystallin A(1-165);
DE Contains:
DE RecName: Full=Alpha-crystallin A(1-163);
DE Contains:
DE RecName: Full=Alpha-crystallin A(1-162);
DE Contains:
DE RecName: Full=Alpha-crystallin A(1-157);
DE Contains:
DE RecName: Full=Alpha-crystallin A(1-156);
DE Contains:
DE RecName: Full=Alpha-crystallin A(1-151);
GN Name=Cryaa; Synonyms=Crya1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP PROTEIN SEQUENCE (ISOFORMS 1 AND 2).
RX PubMed=2294971; DOI=10.1016/0167-4838(90)90101-k;
RA Hendriks W., Weetink H., Voorter C.E.M., Sander J., Bloemendal H.,
RA de Jong W.W.;
RT "The alternative splicing product alpha Ains-crystallin is structurally
RT equivalent to alpha A and alpha B subunits in the rat alpha-crystallin
RT aggregate.";
RL Biochim. Biophys. Acta 1037:58-65(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Lens;
RX PubMed=8875649; DOI=10.1093/protein/9.8.713;
RA Bhat S.P., Nandy P., Srinivasan A., Cheng D., Sitay A.;
RT "Expression of recombinant alpha Ains-crystallin and not alpha A-crystallin
RT inhibits bacterial growth.";
RL Protein Eng. 9:713-718(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-196 (ISOFORM 2).
RX PubMed=6171772; DOI=10.1093/nar/9.19.4813;
RA Moormann R.J.M., van der Velden H.M.W., Dodemont H.J., Andreoli P.M.,
RA Bloemendal H., Schoenmakers J.G.G.;
RT "An unusually long non-coding region in rat lens alpha-crystallin messenger
RT RNA.";
RL Nucleic Acids Res. 9:4813-4822(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 113-195 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Eye, and Spleen;
RX PubMed=1429679; DOI=10.1016/s0021-9258(18)50096-x;
RA Srinivasan A.N., Nagineni C.N., Bhat S.P.;
RT "Alpha A-crystallin is expressed in non-ocular tissues.";
RL J. Biol. Chem. 267:23337-23341(1992).
RN [5]
RP PROTEIN SEQUENCE OF 2-6; 13-16; 112-115 AND 169-173, AND ACETYLATION AT
RP 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).
RN [6]
RP PRELIMINARY PROTEIN SEQUENCE (ISOFORM 1), AND ACETYLATION AT MET-1.
RX PubMed=699911; DOI=10.1111/j.1432-1033.1978.tb20921.x;
RA Cohen L.H., Westerhuis L.W., de Jong W.W., Bloemendal H.;
RT "Rat alpha-crystallin A chain with an insertion of 22 residues.";
RL Eur. J. Biochem. 89:259-266(1978).
RN [7]
RP PROTEOLYTIC PROCESSING.
RX PubMed=12356833;
RA Thampi P., Hassan A., Smith J.B., Abraham E.C.;
RT "Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in
RT diabetic lenses.";
RL Invest. Ophthalmol. Vis. Sci. 43:3265-3272(2002).
RN [8]
RP FUNCTION, AND PROTEOLYTIC PROCESSING.
RX PubMed=12118077; DOI=10.1074/mcp.m200007-mcp200;
RA Ueda Y., Fukiage C., Shih M., Shearer T.R., David L.L.;
RT "Mass measurements of C-terminally truncated alpha-crystallins from two-
RT dimensional gels identify Lp82 as a major endopeptidase in rat lens.";
RL Mol. Cell. Proteomics 1:357-365(2002).
CC -!- FUNCTION: Contributes to the transparency and refractive index of the
CC lens (By similarity). Acts as a chaperone, preventing aggregation of
CC various proteins under a wide range of stress conditions
CC (PubMed:12118077). Required for the correct formation of lens
CC intermediate filaments as part of a complex composed of BFSP1, BFSP2
CC and CRYAA (By similarity). {ECO:0000250|UniProtKB:P02489,
CC ECO:0000269|PubMed:12118077}.
CC -!- FUNCTION: [Isoform 1]: Inhibits bacterial growth in the lens.
CC {ECO:0000269|PubMed:8875649}.
CC -!- SUBUNIT: Heteropolymer 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 -!- INTERACTION:
CC P24623; P07320: CRYGD; Xeno; NbExp=2; IntAct=EBI-7673244, EBI-7673124;
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=P24623-1; Sequence=Displayed;
CC Name=2; Synonyms=Major;
CC IsoId=P24623-2; Sequence=VSP_011917;
CC -!- TISSUE SPECIFICITY: Highly expressed in eye lens. Also expressed in
CC non-lenticular tissues such as brain, spleen, liver, lung, skin, small
CC intestine and a several epithelial and fibroblast cell lines with
CC highest levels in spleen. {ECO:0000269|PubMed:1429679}.
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 Cleavage by m-calpain produces specifically alpha-crystallin A(1-162),
CC cleavage by Capn3/Lp82 produces specifically alpha-crystallin A(1-168)
CC which is the major truncated form during normal maturation and induced
CC cataract formation. {ECO:0000269|PubMed:12118077,
CC ECO:0000269|PubMed:12356833}.
CC -!- MISCELLANEOUS: Lenses of streptozotocin-induced diabetic rats show
CC increased levels of C-terminal truncated forms.
CC {ECO:0000305|PubMed:12356833}.
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; U47921; AAA93366.1; -; mRNA.
DR EMBL; U47922; AAA93367.1; -; mRNA.
DR EMBL; V01219; CAA24530.1; -; mRNA.
DR EMBL; M96949; AAA40644.1; -; mRNA.
DR EMBL; M96950; AAA40645.1; -; mRNA.
DR PIR; A02892; CYRTA.
DR PIR; A02899; CYRTAM.
DR PIR; S07530; S07530.
DR RefSeq; NP_001276666.1; NM_001289737.1. [P24623-1]
DR RefSeq; NP_036666.2; NM_012534.4. [P24623-2]
DR AlphaFoldDB; P24623; -.
DR SMR; P24623; -.
DR BioGRID; 246457; 1.
DR IntAct; P24623; 1.
DR MINT; P24623; -.
DR STRING; 10116.ENSRNOP00000065714; -.
DR GlyConnect; 34; 1 O-Linked glycan.
DR GlyGen; P24623; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P24623; -.
DR PhosphoSitePlus; P24623; -.
DR PaxDb; P24623; -.
DR DNASU; 24273; -.
DR GeneID; 24273; -.
DR KEGG; rno:24273; -.
DR CTD; 1409; -.
DR RGD; 2413; Cryaa.
DR eggNOG; KOG3591; Eukaryota.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; P24623; -.
DR OMA; FRDWWED; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P24623; -.
DR PRO; PR:P24623; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000047175; Expressed in spleen and 2 other tissues.
DR ExpressionAtlas; P24623; baseline and differential.
DR Genevisible; P24623; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005212; F:structural constituent of eye lens; TAS:RGD.
DR GO; GO:0005198; F:structural molecule activity; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; ISO:RGD.
DR GO; GO:0002088; P:lens development in camera-type eye; IEP:RGD.
DR GO; GO:0070309; P:lens fiber cell morphogenesis; ISO:RGD.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISO:RGD.
DR GO; GO:0007017; P:microtubule-based process; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0032387; P:negative regulation of intracellular transport; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0006457; P:protein folding; IDA:RGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0070141; P:response to UV-A; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007021; P:tubulin complex assembly; ISO:RGD.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
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; Alternative splicing; Chaperone; Cytoplasm;
KW Direct protein sequencing; Eye lens protein; Glycoprotein; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..196
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125883"
FT CHAIN 1..191
FT /note="Alpha-crystallin A(1-168)"
FT /id="PRO_0000423505"
FT CHAIN 1..188
FT /note="Alpha-crystallin A(1-165)"
FT /id="PRO_0000423506"
FT CHAIN 1..186
FT /note="Alpha-crystallin A(1-163)"
FT /id="PRO_0000423507"
FT CHAIN 1..185
FT /note="Alpha-crystallin A(1-162)"
FT /id="PRO_0000423508"
FT CHAIN 1..180
FT /note="Alpha-crystallin A(1-157)"
FT /id="PRO_0000423509"
FT CHAIN 1..179
FT /note="Alpha-crystallin A(1-156)"
FT /id="PRO_0000423510"
FT CHAIN 1..174
FT /note="Alpha-crystallin A(1-151)"
FT /id="PRO_0000423511"
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 168..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:0000269|PubMed:699911, ECO:0000269|Ref.5"
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 146
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000250"
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:0000303|PubMed:1429679,
FT ECO:0000303|PubMed:2294971, ECO:0000303|PubMed:6171772,
FT ECO:0000303|PubMed:8875649"
FT /id="VSP_011917"
FT CONFLICT 147
FT /note="V -> M (in Ref. 4; AAA40645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 22447 MW; D0C0E0DFA82D551C CRC64;
MDVTIQHPWF KRALGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG
ISELMTHMWF VMHQPHAGNP KNNPGKVRSD RDKFVIFLDV KHFSPEDLTV KVLEDFVEIH
GKHNERQDDH GYISREFHRR YRLPSNVDQS ALSCSLSADG MLTFSGPKVQ SGLDAGHSER
AIPVSREEKP SSAPSS
