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P24623 (CRYAA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to the transparency and refractive index of the lens. Isoform 1 is capable of inhibiting bacterial growth in the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity.

Subunit structure

Heteropolymer composed of three CRYAA and one CRYAB subunits. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Can also form homooligomers By similarity. Age-dependent C-terminal truncation affects oligomerization. Whereas alpha-crystallin A(1-168) behaves unchanged, specifically alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) show decreased oligomerization.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles By similarity.

Tissue specificity

Highly expressed in eye lens. Also expressed in non-lenticular tissues such as brain, spleen, liver, lung, skin, small intestine and a several epithelial and fibroblast cell lines with highest levels in spleen. Ref.4

Post-translational modification

Acetylation at Lys-93 seems to increase chaperone activity By similarity.

Undergoes age-dependent proteolytical cleavage at the C-terminus. Cleavage by m-calpain produces specifically alpha-crystallin A(1-162), cleavage by Capn3/Lp82 produces specifically alpha-crystallin A(1-168) which is the major truncated form during normal maturation and induced cataract formation.

Miscellaneous

Lenses of streptozotocin-induced diabetic rats show increased levels of C-terminal truncated forms (Ref.6).

Sequence similarities

Belongs to the small heat shock protein (HSP20) family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
Zinc
   Molecular functionChaperone
Eye lens protein
   PTMAcetylation
Glycoprotein
Methylation
Oxidation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Inferred from electronic annotation. Source: Ensembl

apoptotic process involved in morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

lens development in camera-type eye

Inferred from expression pattern PubMed 8187157. Source: RGD

lens fiber cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of intracellular transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from direct assay PubMed 11598124. Source: RGD

protein homooligomerization

Inferred from direct assay PubMed 14529298. Source: RGD

response to UV-A

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from expression pattern PubMed 11851352. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 18626730. Source: RGD

response to hydrogen peroxide

Inferred from direct assay PubMed 7556464. Source: RGD

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to lead ion

Inferred from expression pattern PubMed 15905016. Source: RGD

tubulin complex assembly

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11851352. Source: RGD

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionidentical protein binding

Inferred from direct assay PubMed 14529298. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of eye lens

Traceable author statement Ref.4. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CRYGDP073202EBI-7673244,EBI-7673124From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P24623-1)

Also known as: Minor; Alpha-A(ins);

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P24623-2)

Also known as: Major;

The sequence of this isoform differs from the canonical sequence as follows:
     64-86: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196Alpha-crystallin A chain
PRO_0000125883
Chain1 – 191191Alpha-crystallin A(1-168)
PRO_0000423505
Chain1 – 188188Alpha-crystallin A(1-165)
PRO_0000423506
Chain1 – 186186Alpha-crystallin A(1-163)
PRO_0000423507
Chain1 – 185185Alpha-crystallin A(1-162)
PRO_0000423508
Chain1 – 180180Alpha-crystallin A(1-157)
PRO_0000423509
Chain1 – 179179Alpha-crystallin A(1-156)
PRO_0000423510
Chain1 – 174174Alpha-crystallin A(1-151)
PRO_0000423511

Sites

Metal binding1021Zinc 1 By similarity
Metal binding1231Zinc 2 By similarity
Metal binding1251Zinc 2 By similarity
Metal binding1301Zinc 1 By similarity
Metal binding1381Zinc 1 By similarity
Site11Susceptible to oxidation By similarity
Site181Susceptible to oxidation By similarity
Site341Susceptible to oxidation By similarity
Site1611Susceptible to oxidation By similarity

Amino acid modifications

Modified residue11N-acetylmethionine
Modified residue61Deamidated glutamine; partial By similarity
Modified residue211Omega-N-methylated arginine By similarity
Modified residue451Phosphoserine By similarity
Modified residue501Deamidated glutamine; partial By similarity
Modified residue931N6-acetyllysine By similarity
Modified residue1221N6-acetyllysine By similarity
Modified residue1241Deamidated asparagine; partial By similarity
Modified residue1451Phosphoserine By similarity
Modified residue1461Deamidated asparagine; partial By similarity
Modified residue1701Deamidated glutamine; partial By similarity
Glycosylation1851O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence64 – 8623Missing in isoform 2.
VSP_011917

Experimental info

Sequence conflict1471V → M in AAA40645. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Minor) (Alpha-A(ins)) [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: D0C0E0DFA82D551C

FASTA19622,447
        10         20         30         40         50         60 
MDVTIQHPWF KRALGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG 

        70         80         90        100        110        120 
ISELMTHMWF VMHQPHAGNP KNNPGKVRSD RDKFVIFLDV KHFSPEDLTV KVLEDFVEIH 

       130        140        150        160        170        180 
GKHNERQDDH GYISREFHRR YRLPSNVDQS ALSCSLSADG MLTFSGPKVQ SGLDAGHSER 

       190 
AIPVSREEKP SSAPSS 

« Hide

Isoform 2 (Major) [UniParc].

Checksum: E146E3F488591F93
Show »

FASTA17319,792

References

[1]"The alternative splicing product alpha Ains-crystallin is structurally equivalent to alpha A and alpha B subunits in the rat alpha-crystallin aggregate."
Hendriks W., Weetink H., Voorter C.E.M., Sander J., Bloemendal H., de Jong W.W.
Biochim. Biophys. Acta 1037:58-65(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (ISOFORMS 1 AND 2).
[2]"Expression of recombinant alpha Ains-crystallin and not alpha A-crystallin inhibits bacterial growth."
Bhat S.P., Nandy P., Srinivasan A., Cheng D., Sitay A.
Protein Eng. 9:713-718(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Strain: Sprague-Dawley.
Tissue: Lens.
[3]"An unusually long non-coding region in rat lens alpha-crystallin messenger RNA."
Moormann R.J.M., van der Velden H.M.W., Dodemont H.J., Andreoli P.M., Bloemendal H., Schoenmakers J.G.G.
Nucleic Acids Res. 9:4813-4822(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-196 (ISOFORM 2).
[4]"Alpha A-crystallin is expressed in non-ocular tissues."
Srinivasan A.N., Nagineni C.N., Bhat S.P.
J. Biol. Chem. 267:23337-23341(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 113-195 (ISOFORM 2), TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Eye and Spleen.
[5]"Rat alpha-crystallin A chain with an insertion of 22 residues."
Cohen L.H., Westerhuis L.W., de Jong W.W., Bloemendal H.
Eur. J. Biochem. 89:259-266(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE (ISOFORM 1).
[6]"Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses."
Thampi P., Hassan A., Smith J.B., Abraham E.C.
Invest. Ophthalmol. Vis. Sci. 43:3265-3272(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[7]"Mass measurements of C-terminally truncated alpha-crystallins from two-dimensional gels identify Lp82 as a major endopeptidase in rat lens."
Ueda Y., Fukiage C., Shih M., Shearer T.R., David L.L.
Mol. Cell. Proteomics 1:357-365(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U47921 mRNA. Translation: AAA93366.1.
U47922 mRNA. Translation: AAA93367.1.
V01219 mRNA. Translation: CAA24530.1.
M96949 mRNA. Translation: AAA40644.1.
M96950 mRNA. Translation: AAA40645.1.
PIRCYRTA. A02892.
CYRTAM. A02899.
S07530.
RefSeqNP_036666.2. NM_012534.4.
XP_006256227.1. XM_006256165.1.
UniGeneRn.127769.

3D structure databases

ProteinModelPortalP24623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246457. 1 interaction.
IntActP24623. 1 interaction.
MINTMINT-8303018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000071248; ENSRNOP00000067332; ENSRNOG00000047175. [P24623-2]
ENSRNOT00000075545; ENSRNOP00000065714; ENSRNOG00000047175. [P24623-1]
GeneID24273.
KEGGrno:24273.

Organism-specific databases

CTD1409.
RGD2413. Cryaa.

Phylogenomic databases

GeneTreeENSGT00740000115222.
HOVERGENHBG054766.
KOK09541.
OMAGPKVQSG.
OrthoDBEOG7WHHBK.
PhylomeDBP24623.

Gene expression databases

ArrayExpressP24623.
GenevestigatorP24623.

Family and domain databases

Gene3D2.60.40.790. 1 hit.
InterProIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERPTHR11527:SF36. PTHR11527:SF36. 1 hit.
PfamPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSPR00299. ACRYSTALLIN.
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio602845.
PROP24623.

Entry information

Entry nameCRYAA_RAT
AccessionPrimary (citable) accession number: P24623
Secondary accession number(s): P02490 expand/collapse secondary AC list , P02496, P82532, Q61444
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families