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Protein

Alpha-crystallin A chain

Gene

CRYAA

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 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

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Alpha-crystallin A chainPRO_0000125882Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
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 – 1221Phosphoserine1 Publication
Modified residuei123 – 1231Deamidated asparagine; partialBy similarity
Modified residuei147 – 1471Deamidated glutamine; partialBy similarity
Glycosylationi162 – 1621O-linked (GlcNAc)By similarity

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

iPTMnetiP02493.

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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP02493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP02493.
KOiK09541.

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.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527: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.

P02493-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ
60 70 80 90 100
SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ EDFVEIHGKH
110 120 130 140 150
NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FSGPKVQSGL
160 170
DAGHSERAIP VSREEKPSSA PSS
Length:173
Mass (Da):19,837
Last modified:May 29, 2007 - v3
Checksum:iC12C25369CC327EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701A → V in CAA64668 (PubMed:8814151).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95382 mRNA. Translation: CAA64668.1.
EF187820 mRNA. Translation: ABM74183.1.
PIRiA02896. CYRBAA.
RefSeqiNP_001075875.2. NM_001082406.2.
UniGeneiOcu.6584.

Genome annotation databases

GeneIDi100009294.
KEGGiocu:100009294.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95382 mRNA. Translation: CAA64668.1.
EF187820 mRNA. Translation: ABM74183.1.
PIRiA02896. CYRBAA.
RefSeqiNP_001075875.2. NM_001082406.2.
UniGeneiOcu.6584.

3D structure databases

ProteinModelPortaliP02493.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP02493.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009294.
KEGGiocu:100009294.

Organism-specific databases

CTDi1409.

Phylogenomic databases

HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP02493.
KOiK09541.

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.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527: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]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of rabbit lens alpha-crystallins."
    Parveen R., Smith J.B., Sun Y., Smith D.L.
    J. Protein Chem. 12:93-101(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-122.
    Tissue: Lens.
  2. "Expression of crystallins, Pax6, filensin, CP49, MIP, and MP20 in lens-derived cell lines."
    Krausz E., Augusteyn R.C., Quinlan R.A., Reddan J.R., Russell P., Sax C.M., Graw J.
    Invest. Ophthalmol. Vis. Sci. 37:2120-2128(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lens.
  3. Wistow G.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lens.
  4. "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 OF 2-6 AND 146-150, ACETYLATION AT MET-1.

Entry informationi

Entry nameiCRYAA_RABIT
AccessioniPrimary (citable) accession number: P02493
Secondary accession number(s): A2IBH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 29, 2007
Last modified: January 20, 2016
This is version 112 of the entry and version 3 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.