P02488 (CRYAA_MACMU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-crystallin A chain

Cleaved into the following chain:

1. Alpha-crystallin A chain, short form

Gene names

Name:

CRYAA

Organism

Macaca mulatta (Rhesus macaque) [Reference proteome]

Taxonomic identifier

9544 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Cercopithecoidea › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May contribute 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.
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 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.
Sequence similarities	Belongs to the small heat shock protein (HSP20) family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Chaperone Eye lens protein
PTM	Acetylation Glycoprotein Methylation Oxidation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	M phase specific microtubule process Inferred from electronic annotation. Source: Compara actin filament organization Inferred from electronic annotation. Source: Compara apoptotic process involved in morphogenesis Inferred from electronic annotation. Source: Compara embryonic camera-type eye morphogenesis Inferred from electronic annotation. Source: Compara lens fiber cell morphogenesis Inferred from electronic annotation. Source: Compara mitochondrion organization Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of gene expression Inferred from electronic annotation. Source: Compara negative regulation of intracellular transport Inferred from electronic annotation. Source: Compara positive regulation of cell growth Inferred from electronic annotation. Source: Compara positive regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: Compara response to UV-A Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara tubulin complex assembly Inferred from electronic annotation. Source: Compara visual perception Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	metal 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 172	172	Alpha-crystallin A chain		PRO_0000125867
	Chain	1 – 171	171	Alpha-crystallin A chain, short form		PRO_0000226643
	Propeptide	172	1	Removed in short form By similarity		PRO_0000226644
Sites
	Metal binding	79	1	Zinc By similarity
	Metal binding	107	1	Zinc By similarity
	Metal binding	115	1	Zinc By similarity
	Site	18	1	Susceptible to oxidation By similarity
	Site	34	1	Susceptible to oxidation By similarity
	Site	138	1	Susceptible to oxidation By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Probable
	Modified residue	21	1	Omega-N-methylated arginine By similarity
	Modified residue	70	1	N6-acetyllysine By similarity
	Modified residue	99	1	N6-acetyllysine By similarity
	Modified residue	122	1	Phosphoserine By similarity
	Glycosylation	168	1	O-linked (GlcNAc) Ref.3
Experimental info
	Sequence conflict	153 – 154	2	TH → HT AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P02488 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 1F7AF9066BEEB2D7	FASTA	172	19,792
	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

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.
PIR	CYMQAA. A02890.
3D structure databases
ProteinModelPortal	P02488.
ModBase	Search...
Protein-protein interaction databases
STRING	9544.ENSMMUP00000026679.
PTM databases
GlycoSuiteDB	P02488.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG278874.
HOGENOM	HOG000233954.
HOVERGEN	HBG054766.
InParanoid	P02488.
OrthoDB	EOG4F1X4B.
Family and domain databases
InterPro	IPR002068. a-crystallin/Hsp20_dom. IPR001436. Alpha-crystallin/HSP. IPR012274. Alpha-crystallin_A. IPR003090. Alpha-crystallin_N. IPR008978. HSP20-like_chaperone. [Graphical view]
PANTHER	PTHR11527:SF36. PTHR11527:SF36. 1 hit.
Pfam	PF00525. Crystallin. 1 hit. PF00011. HSP20. 1 hit. [Graphical view]
PIRSF	PIRSF036514. Sm_HSP_B1. 1 hit.
PRINTS	PR00299. ACRYSTALLIN.
SUPFAM	SSF49764. HSP20_chap. 1 hit.
PROSITE	PS01031. HSP20. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CRYAA_MACMU

Accession

Primary (citable) accession number: P02488

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program