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P02488

- CRYAA_MACMU

UniProt

P02488 - CRYAA_MACMU

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Protein

Alpha-crystallin A chain

Gene

CRYAA

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Zinc 1By similarity
Metal bindingi100 – 1001Zinc 2By similarity
Metal bindingi102 – 1021Zinc 2By similarity
Metal bindingi107 – 1071Zinc 1By similarity
Metal bindingi115 – 1151Zinc 1By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. structural constituent of eye lens Source: UniProtKB-KW

GO - Biological processi

  1. actin filament organization Source: Ensembl
  2. apoptotic process involved in morphogenesis Source: Ensembl
  3. embryonic camera-type eye morphogenesis Source: Ensembl
  4. lens fiber cell morphogenesis Source: Ensembl
  5. microtubule-based process Source: Ensembl
  6. mitochondrion organization Source: Ensembl
  7. negative regulation of apoptotic process Source: Ensembl
  8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  9. negative regulation of gene expression Source: Ensembl
  10. positive regulation of cell growth Source: Ensembl
  11. positive regulation of protein phosphorylation Source: Ensembl
  12. response to hydrogen peroxide Source: Ensembl
  13. response to hypoxia Source: Ensembl
  14. response to UV-A Source: Ensembl
  15. tubulin complex assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Eye lens protein

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-crystallin A chain
Gene namesi
Name:CRYAA
OrganismiMacaca mulatta (Rhesus macaque)
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
ProteomesiUP000006718: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172Alpha-crystallin A chainPRO_0000125867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCurated
Modified residuei6 – 61Deamidated glutamine; partialBy similarity
Modified residuei21 – 211Omega-N-methylated arginineBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei50 – 501Deamidated glutamine; partialBy similarity
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei90 – 901Deamidated glutamine; partialBy similarity
Modified residuei99 – 991N6-acetyllysineBy similarity
Modified residuei101 – 1011Deamidated asparagine; partialBy similarity
Modified residuei122 – 1221PhosphoserineBy similarity
Modified residuei123 – 1231Deamidated asparagine; partialBy similarity
Modified residuei147 – 1471Deamidated glutamine; partialBy similarity
Glycosylationi168 – 1681O-linked (GlcNAc)1 Publication

Post-translational modificationi

Acetylation at Lys-70 seems to increase chaperone activity.By similarity
Undergoes age-dependent proteolytical cleavage at the C-terminus.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein

PTM databases

UniCarbKBiP02488.

Expressioni

Gene expression databases

ExpressionAtlasiP02488. baseline.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000026679.

Structurei

3D structure databases

ProteinModelPortaliP02488.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG278874.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP02488.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527:SF36. PTHR11527:SF36. 1 hit.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02488-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ
60 70 80 90 100
SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH
110 120 130 140 150
NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FSGPKIQTGL
160 170
DATHERAIPV AREEKPSSAP SS
Length:172
Mass (Da):19,792
Last modified:October 1, 1996 - v2
Checksum:i1F7AF9066BEEB2D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1542TH → HT AA sequence 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U24061 Genomic DNA. Translation: AAA97563.1.
PIRiA02890. CYMQAA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U24061 Genomic DNA. Translation: AAA97563.1 .
PIRi A02890. CYMQAA.

3D structure databases

ProteinModelPortali P02488.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9544.ENSMMUP00000026679.

PTM databases

UniCarbKBi P02488.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG278874.
HOGENOMi HOG000233954.
HOVERGENi HBG054766.
InParanoidi P02488.

Gene expression databases

ExpressionAtlasi P02488. baseline.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
InterProi IPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view ]
PANTHERi PTHR11527:SF36. PTHR11527:SF36. 1 hit.
Pfami PF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSi PR00299. ACRYSTALLIN.
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS01031. HSP20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCRYAA_MACMU
AccessioniPrimary (citable) accession number: P02488
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3