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Protein

Alpha-crystallin A chain

Gene

CRYAA

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi79Zinc 1By similarity1
Metal bindingi100Zinc 2By similarity1
Metal bindingi102Zinc 2By similarity1
Metal bindingi107Zinc 1By similarity1
Metal bindingi115Zinc 1By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, Eye lens protein
LigandMetal-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
Proteomesi
  • UP000006718 Componenti: Chromosome 3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001258671 – 172Alpha-crystallin A chainAdd BLAST172

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarityCurated1
Modified residuei6Deamidated glutamine; partialBy similarity1
Modified residuei21Omega-N-methylated arginineBy similarity1
Modified residuei45PhosphoserineBy similarity1
Modified residuei50Deamidated glutamine; partialBy similarity1
Modified residuei70N6-acetyllysineBy similarity1
Modified residuei90Deamidated glutamine; partialBy similarity1
Modified residuei99N6-acetyllysineBy similarity1
Modified residuei101Deamidated asparagine; partialBy similarity1
Modified residuei122PhosphoserineBy similarity1
Modified residuei123Deamidated asparagine; partialBy similarity1
Modified residuei147Deamidated glutamine; partialBy similarity1
Glycosylationi168O-linked (GlcNAc) serine1 Publication1

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

GlyConnecti31
iPTMnetiP02488
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
SMRiP02488
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini52 – 163sHSPPROSITE-ProRule annotationAdd BLAST112

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591 Eukaryota
ENOG410YERS LUCA
GeneTreeiENSGT00760000119238
HOGENOMiHOG000233954
HOVERGENiHBG054766
InParanoidiP02488
KOiK09541

Family and domain databases

Gene3Di2.60.40.790, 1 hit
InterProiView protein in InterPro
IPR002068 A-crystallin/Hsp20_dom
IPR001436 Alpha-crystallin/HSP
IPR012274 Alpha-crystallin_A
IPR003090 Alpha-crystallin_N
IPR031107 HSP20
IPR008978 HSP20-like_chaperone
PANTHERiPTHR11527 PTHR11527, 1 hit
PTHR11527:SF36 PTHR11527:SF36, 1 hit
PfamiView protein in Pfam
PF00525 Crystallin, 1 hit
PF00011 HSP20, 1 hit
PIRSFiPIRSF036514 Sm_HSP_B1, 1 hit
PRINTSiPR00299 ACRYSTALLIN
SUPFAMiSSF49764 SSF49764, 1 hit
PROSITEiView protein in PROSITE
PS01031 SHSP, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti153 – 154TH → HT AA sequence (Ref. 1) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24061 Genomic DNA Translation: AAA97563.1
PIRiA02890 CYMQAA
RefSeqiXP_014988287.1, XM_015132801.1
UniGeneiMmu.14836

Genome annotation databases

EnsembliENSMMUT00000058120; ENSMMUP00000056174; ENSMMUG00000020271
GeneIDi722370
KEGGimcc:722370

Similar proteinsi

Entry informationi

Entry nameiCRYAA_MACMU
AccessioniPrimary (citable) accession number: P02488
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: April 25, 2018
This is version 113 of the entry and version 2 of the sequence. See 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

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