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P02488 (CRYAA_MACMU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-crystallin A chain
Gene names
Name:CRYAA
OrganismMacaca mulatta (Rhesus macaque) [Reference proteome]
Taxonomic identifier9544 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions By similarity.

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 homodimers and higher homooligomers By similarity.

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.

Post-translational modification

Acetylation at Lys-70 seems to increase chaperone activity By similarity.

Undergoes age-dependent proteolytical cleavage at the C-terminus By similarity.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   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 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 homooligomerization

Inferred from electronic annotation. Source: Ensembl

response to UV-A

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

tubulin complex assembly

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of eye lens

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172Alpha-crystallin A chain
PRO_0000125867

Sites

Metal binding791Zinc 1 By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1021Zinc 2 By similarity
Metal binding1071Zinc 1 By similarity
Metal binding1151Zinc 1 By similarity
Site11Susceptible to oxidation By similarity
Site181Susceptible to oxidation By similarity
Site341Susceptible to oxidation By similarity
Site1381Susceptible to oxidation By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Probable
Modified residue61Deamidated glutamine; partial By similarity
Modified residue211Omega-N-methylated arginine By similarity
Modified residue451Phosphoserine By similarity
Modified residue501Deamidated glutamine; partial By similarity
Modified residue701N6-acetyllysine By similarity
Modified residue901Deamidated glutamine; partial By similarity
Modified residue991N6-acetyllysine By similarity
Modified residue1011Deamidated asparagine; partial By similarity
Modified residue1221Phosphoserine By similarity
Modified residue1231Deamidated asparagine; partial By similarity
Modified residue1471Deamidated glutamine; partial By similarity
Glycosylation1681O-linked (GlcNAc) Ref.3

Experimental info

Sequence conflict153 – 1542TH → HT AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P02488 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 1F7AF9066BEEB2D7

FASTA17219,792
        10         20         30         40         50         60 
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG 

        70         80         90        100        110        120 
ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL 

       130        140        150        160        170 
PSNVDQSALS CSLSADGMLT FSGPKIQTGL DATHERAIPV AREEKPSSAP SS 

« Hide

References

[1]"Primary structures of the alpha-crystallin A chains of seven mammalian species."
de Jong W.W., van der Ouderaa F.J., Versteeg M., Groenewoud G., van Amelsvoort J.M., Bloemendal H.
Eur. J. Biochem. 53:237-242(1975)
Cited for: PROTEIN SEQUENCE.
[2]"A reassessment of mammalian alpha A-crystallin sequences using DNA sequencing: implications for anthropoid affinities of tarsier."
Jaworski C.J.
J. Mol. Evol. 41:901-908(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-162.
[3]"Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin."
Roquemore E.P., Chevrier M.R., Cotter R.J., Hart G.W.
Biochemistry 35:3578-3586(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24061 Genomic DNA. Translation: AAA97563.1.
PIRCYMQAA. A02890.

3D structure databases

ProteinModelPortalP02488.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9544.ENSMMUP00000026679.

PTM databases

UniCarbKBP02488.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG278874.
HOGENOMHOG000233954.
HOVERGENHBG054766.
InParanoidP02488.

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...

Entry information

Entry nameCRYAA_MACMU
AccessionPrimary (citable) accession number: P02488
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 93 of the entry and version 2 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