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P02488

- CRYAA_MACMU

UniProt

P02488 - CRYAA_MACMU

Protein

Alpha-crystallin A chain

Gene

CRYAA

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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
    Sitei1 – 11Susceptible to oxidationBy similarity
    Sitei18 – 181Susceptible to oxidationBy similarity
    Sitei34 – 341Susceptible to oxidationBy similarity
    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
    Sitei138 – 1381Susceptible to oxidationBy 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. mitochondrion organization Source: Ensembl
    6. negative regulation of apoptotic process Source: Ensembl
    7. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    8. negative regulation of gene expression Source: Ensembl
    9. negative regulation of intracellular transport Source: Ensembl
    10. positive regulation of cell growth Source: Ensembl
    11. positive regulation of protein phosphorylation Source: Ensembl
    12. protein homooligomerization Source: Ensembl
    13. response to hydrogen peroxide Source: Ensembl
    14. response to hypoxia Source: Ensembl
    15. response to UV-A Source: Ensembl
    16. tubulin complex assembly Source: Ensembl
    17. visual perception Source: Ensembl

    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

    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

    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, Oxidation, Phosphoprotein

    PTM databases

    UniCarbKBiP02488.

    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 annotations

    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]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

    P02488-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ    50
    SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH 100
    NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FSGPKIQTGL 150
    DATHERAIPV AREEKPSSAP SS 172
    Length:172
    Mass (Da):19,792
    Last modified:October 1, 1996 - v2
    Checksum:i1F7AF9066BEEB2D7
    GO

    Sequence conflict

    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.

    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 1, 2014
    This is version 94 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

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