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P24623

- CRYAA_RAT

UniProt

P24623 - CRYAA_RAT

Protein

Alpha-crystallin A chain

Gene

Cryaa

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    Contributes to the transparency and refractive index of the lens. Isoform 1 is capable of inhibiting bacterial growth in the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1 – 11Susceptible to oxidationBy similarity
    Sitei18 – 181Susceptible to oxidationBy similarity
    Sitei34 – 341Susceptible to oxidationBy similarity
    Metal bindingi102 – 1021Zinc 1By similarity
    Metal bindingi123 – 1231Zinc 2By similarity
    Metal bindingi125 – 1251Zinc 2By similarity
    Metal bindingi130 – 1301Zinc 1By similarity
    Metal bindingi138 – 1381Zinc 1By similarity
    Sitei161 – 1611Susceptible to oxidationBy similarity

    GO - Molecular functioni

    1. identical protein binding Source: RGD
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. structural constituent of eye lens Source: RGD

    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 development in camera-type eye Source: RGD
    5. lens fiber cell morphogenesis 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. negative regulation of intracellular transport Source: Ensembl
    11. positive regulation of cell growth Source: Ensembl
    12. positive regulation of protein phosphorylation Source: Ensembl
    13. protein folding Source: RGD
    14. protein homooligomerization Source: RGD
    15. response to drug Source: RGD
    16. response to glucocorticoid Source: RGD
    17. response to hydrogen peroxide Source: RGD
    18. response to hypoxia Source: Ensembl
    19. response to lead ion Source: RGD
    20. response to UV-A Source: Ensembl
    21. tubulin complex assembly Source: Ensembl
    22. visual perception Source: Ensembl

    Keywords - Molecular functioni

    Chaperone, Eye lens protein

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Gene namesi
    Name:Cryaa
    Synonyms:Crya1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 20

    Organism-specific databases

    RGDi2413. Cryaa.

    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: RGD
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 196196Alpha-crystallin A chainPRO_0000125883Add
    BLAST
    Chaini1 – 191191Alpha-crystallin A(1-168)PRO_0000423505Add
    BLAST
    Chaini1 – 188188Alpha-crystallin A(1-165)PRO_0000423506Add
    BLAST
    Chaini1 – 186186Alpha-crystallin A(1-163)PRO_0000423507Add
    BLAST
    Chaini1 – 185185Alpha-crystallin A(1-162)PRO_0000423508Add
    BLAST
    Chaini1 – 180180Alpha-crystallin A(1-157)PRO_0000423509Add
    BLAST
    Chaini1 – 179179Alpha-crystallin A(1-156)PRO_0000423510Add
    BLAST
    Chaini1 – 174174Alpha-crystallin A(1-151)PRO_0000423511Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei6 – 61Deamidated glutamine; partialBy similarity
    Modified residuei21 – 211Omega-N-methylated arginineBy similarity
    Modified residuei45 – 451PhosphoserineBy similarity
    Modified residuei50 – 501Deamidated glutamine; partialBy similarity
    Modified residuei93 – 931N6-acetyllysineBy similarity
    Modified residuei122 – 1221N6-acetyllysineBy similarity
    Modified residuei124 – 1241Deamidated asparagine; partialBy similarity
    Modified residuei145 – 1451PhosphoserineBy similarity
    Modified residuei146 – 1461Deamidated asparagine; partialBy similarity
    Modified residuei170 – 1701Deamidated glutamine; partialBy similarity
    Glycosylationi185 – 1851O-linked (GlcNAc)By similarity

    Post-translational modificationi

    Acetylation at Lys-93 seems to increase chaperone activity.By similarity
    Undergoes age-dependent proteolytical cleavage at the C-terminus. Cleavage by m-calpain produces specifically alpha-crystallin A(1-162), cleavage by Capn3/Lp82 produces specifically alpha-crystallin A(1-168) which is the major truncated form during normal maturation and induced cataract formation.2 Publications

    Keywords - PTMi

    Acetylation, Glycoprotein, Methylation, Oxidation, Phosphoprotein

    Expressioni

    Tissue specificityi

    Highly expressed in eye lens. Also expressed in non-lenticular tissues such as brain, spleen, liver, lung, skin, small intestine and a several epithelial and fibroblast cell lines with highest levels in spleen.1 Publication

    Gene expression databases

    ArrayExpressiP24623.
    GenevestigatoriP24623.

    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 homooligomers By similarity. Age-dependent C-terminal truncation affects oligomerization. Whereas alpha-crystallin A(1-168) behaves unchanged, specifically alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) show decreased oligomerization.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CRYGDP073202EBI-7673244,EBI-7673124From a different organism.

    Protein-protein interaction databases

    BioGridi246457. 1 interaction.
    IntActiP24623. 1 interaction.
    MINTiMINT-8303018.

    Structurei

    3D structure databases

    ProteinModelPortaliP24623.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    GeneTreeiENSGT00740000115222.
    HOVERGENiHBG054766.
    KOiK09541.
    OMAiGPKVQSG.
    OrthoDBiEOG7WHHBK.
    PhylomeDBiP24623.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P24623-1) [UniParc]FASTAAdd to Basket

    Also known as: Minor, Alpha-A(ins)

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDVTIQHPWF KRALGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ    50
    SLFRTVLDSG ISELMTHMWF VMHQPHAGNP KNNPGKVRSD RDKFVIFLDV 100
    KHFSPEDLTV KVLEDFVEIH GKHNERQDDH GYISREFHRR YRLPSNVDQS 150
    ALSCSLSADG MLTFSGPKVQ SGLDAGHSER AIPVSREEKP SSAPSS 196
    Length:196
    Mass (Da):22,447
    Last modified:March 1, 1992 - v1
    Checksum:iD0C0E0DFA82D551C
    GO
    Isoform 2 (identifier: P24623-2) [UniParc]FASTAAdd to Basket

    Also known as: Major

    The sequence of this isoform differs from the canonical sequence as follows:
         64-86: Missing.

    Show »
    Length:173
    Mass (Da):19,792
    Checksum:iE146E3F488591F93
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471V → M in AAA40645. (PubMed:1429679)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei64 – 8623Missing in isoform 2. 4 PublicationsVSP_011917Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U47921 mRNA. Translation: AAA93366.1.
    U47922 mRNA. Translation: AAA93367.1.
    V01219 mRNA. Translation: CAA24530.1.
    M96949 mRNA. Translation: AAA40644.1.
    M96950 mRNA. Translation: AAA40645.1.
    PIRiA02892. CYRTA.
    A02899. CYRTAM.
    S07530.
    RefSeqiNP_001276666.1. NM_001289737.1. [P24623-1]
    NP_036666.2. NM_012534.4. [P24623-2]
    XP_006256227.1. XM_006256165.1. [P24623-2]
    UniGeneiRn.127769.

    Genome annotation databases

    EnsembliENSRNOT00000071248; ENSRNOP00000067332; ENSRNOG00000047175. [P24623-2]
    ENSRNOT00000075545; ENSRNOP00000065714; ENSRNOG00000047175. [P24623-1]
    GeneIDi24273.
    KEGGirno:24273.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U47921 mRNA. Translation: AAA93366.1 .
    U47922 mRNA. Translation: AAA93367.1 .
    V01219 mRNA. Translation: CAA24530.1 .
    M96949 mRNA. Translation: AAA40644.1 .
    M96950 mRNA. Translation: AAA40645.1 .
    PIRi A02892. CYRTA.
    A02899. CYRTAM.
    S07530.
    RefSeqi NP_001276666.1. NM_001289737.1. [P24623-1 ]
    NP_036666.2. NM_012534.4. [P24623-2 ]
    XP_006256227.1. XM_006256165.1. [P24623-2 ]
    UniGenei Rn.127769.

    3D structure databases

    ProteinModelPortali P24623.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246457. 1 interaction.
    IntActi P24623. 1 interaction.
    MINTi MINT-8303018.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000071248 ; ENSRNOP00000067332 ; ENSRNOG00000047175 . [P24623-2 ]
    ENSRNOT00000075545 ; ENSRNOP00000065714 ; ENSRNOG00000047175 . [P24623-1 ]
    GeneIDi 24273.
    KEGGi rno:24273.

    Organism-specific databases

    CTDi 1409.
    RGDi 2413. Cryaa.

    Phylogenomic databases

    GeneTreei ENSGT00740000115222.
    HOVERGENi HBG054766.
    KOi K09541.
    OMAi GPKVQSG.
    OrthoDBi EOG7WHHBK.
    PhylomeDBi P24623.

    Miscellaneous databases

    NextBioi 602845.
    PROi P24623.

    Gene expression databases

    ArrayExpressi P24623.
    Genevestigatori P24623.

    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. "The alternative splicing product alpha Ains-crystallin is structurally equivalent to alpha A and alpha B subunits in the rat alpha-crystallin aggregate."
      Hendriks W., Weetink H., Voorter C.E.M., Sander J., Bloemendal H., de Jong W.W.
      Biochim. Biophys. Acta 1037:58-65(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (ISOFORMS 1 AND 2).
    2. "Expression of recombinant alpha Ains-crystallin and not alpha A-crystallin inhibits bacterial growth."
      Bhat S.P., Nandy P., Srinivasan A., Cheng D., Sitay A.
      Protein Eng. 9:713-718(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Strain: Sprague-Dawley.
      Tissue: Lens.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-196 (ISOFORM 2).
    4. "Alpha A-crystallin is expressed in non-ocular tissues."
      Srinivasan A.N., Nagineni C.N., Bhat S.P.
      J. Biol. Chem. 267:23337-23341(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 113-195 (ISOFORM 2), TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Eye and Spleen.
    5. "Rat alpha-crystallin A chain with an insertion of 22 residues."
      Cohen L.H., Westerhuis L.W., de Jong W.W., Bloemendal H.
      Eur. J. Biochem. 89:259-266(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE (ISOFORM 1), ACETYLATION AT MET-1.
    6. "Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses."
      Thampi P., Hassan A., Smith J.B., Abraham E.C.
      Invest. Ophthalmol. Vis. Sci. 43:3265-3272(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    7. "Mass measurements of C-terminally truncated alpha-crystallins from two-dimensional gels identify Lp82 as a major endopeptidase in rat lens."
      Ueda Y., Fukiage C., Shih M., Shearer T.R., David L.L.
      Mol. Cell. Proteomics 1:357-365(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.

    Entry informationi

    Entry nameiCRYAA_RAT
    AccessioniPrimary (citable) accession number: P24623
    Secondary accession number(s): P02490
    , P02496, P82532, Q61444
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Lenses of streptozotocin-induced diabetic rats show increased levels of C-terminal truncated forms.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3