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P53673

- CRBA4_HUMAN

UniProt

P53673 - CRBA4_HUMAN

Protein

Beta-crystallin A4

Gene

CRYBA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Crystallins are the dominant structural components of the vertebrate eye lens.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei149 – 1491Susceptible to oxidation

    GO - Molecular functioni

    1. structural constituent of eye lens Source: UniProtKB-KW

    GO - Biological processi

    1. camera-type eye development Source: UniProtKB
    2. visual perception Source: UniProtKB

    Keywords - Molecular functioni

    Eye lens protein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-crystallin A4
    Alternative name(s):
    Beta-A4 crystallin
    Gene namesi
    Name:CRYBA4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:2396. CRYBA4.

    Pathology & Biotechi

    Involvement in diseasei

    Cataract 23 (CTRCT23) [MIM:610425]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT23 is a zonular cataract. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti69 – 691L → P in CTRCT23; the patient has cataract and bilateral microphthalmia; the mutation is predicted to disrupt the beta-sheet structure of the protein. 1 Publication
    VAR_029528
    Natural varianti94 – 941F → S in CTRCT23; modeling suggests that this substitution would significantly reduce the intrinsic stability of the crystalline monomer. 1 Publication
    VAR_029529

    Keywords - Diseasei

    Cataract, Disease mutation

    Organism-specific databases

    MIMi610425. phenotype.
    Orphaneti1377. Cataract-microcornea syndrome.
    2543. Microphthalmia - cataract.
    98995. Zonular cataract.
    PharmGKBiPA26910.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 196195Beta-crystallin A4PRO_0000057545Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication

    Keywords - PTMi

    Acetylation, Oxidation

    Proteomic databases

    PaxDbiP53673.
    PRIDEiP53673.

    PTM databases

    PhosphoSiteiP53673.

    Expressioni

    Gene expression databases

    BgeeiP53673.
    CleanExiHS_CRYBA4.
    GenevestigatoriP53673.

    Interactioni

    Subunit structurei

    Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms By similarity.By similarity

    Protein-protein interaction databases

    IntActiP53673. 2 interactions.
    MINTiMINT-5161963.
    STRINGi9606.ENSP00000346805.

    Structurei

    Secondary structure

    1
    196
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 197
    Helixi20 – 223
    Beta strandi23 – 319
    Helixi36 – 394
    Beta strandi46 – 527
    Beta strandi54 – 596
    Helixi60 – 623
    Beta strandi63 – 697
    Beta strandi71 – 744
    Helixi78 – 814
    Beta strandi93 – 964
    Helixi102 – 1043
    Beta strandi106 – 1138
    Beta strandi119 – 1246
    Helixi130 – 1323
    Beta strandi136 – 1383
    Beta strandi141 – 15414
    Turni155 – 1573
    Beta strandi158 – 1658
    Helixi169 – 1713
    Turni176 – 1783
    Beta strandi190 – 1934

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LWKX-ray1.70A8-196[»]
    ProteinModelPortaliP53673.
    SMRiP53673. Positions 8-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53673.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 5140Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini52 – 9847Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini105 – 14642Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini147 – 19549Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 1110N-terminal arm
    Regioni99 – 1046Connecting peptide

    Domaini

    Has a two-domain beta-structure, folded into four very similar Greek key motifs.

    Sequence similaritiesi

    Belongs to the beta/gamma-crystallin family.Curated
    Contains 4 beta/gamma crystallin 'Greek key' domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG39249.
    HOGENOMiHOG000234388.
    HOVERGENiHBG003364.
    InParanoidiP53673.
    OMAiFHVHSGA.
    OrthoDBiEOG7K9K40.
    PhylomeDBiP53673.
    TreeFamiTF331401.

    Family and domain databases

    InterProiIPR001064. Beta/gamma_crystallin.
    IPR011024. G_crystallin-rel.
    [Graphical view]
    PfamiPF00030. Crystall. 2 hits.
    [Graphical view]
    PRINTSiPR01367. BGCRYSTALLIN.
    SMARTiSM00247. XTALbg. 2 hits.
    [Graphical view]
    SUPFAMiSSF49695. SSF49695. 1 hit.
    PROSITEiPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P53673-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLQCTKSAG PWKMVVWDED GFQGRRHEFT AECPSVLELG FETVRSLKVL    50
    SGAWVGFEHA GFQGQQYILE RGEYPSWDAW GGNTAYPAER LTSFRPAACA 100
    NHRDSRLTIF EQENFLGKKG ELSDDYPSLQ AMGWEGNEVG SFHVHSGAWV 150
    CSQFPGYRGF QYVLECDHHS GDYKHFREWG SHAPTFQVQS IRRIQQ 196
    Length:196
    Mass (Da):22,374
    Last modified:January 23, 2007 - v3
    Checksum:i104EC68E3CDE5740
    GO

    Sequence cautioni

    The sequence CAG30310.1 differs from that shown. Reason: Erroneous initiation.

    Mass spectrometryi

    Molecular mass is 22285±3 Da from positions 2 - 196. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361V → M.
    Corresponds to variant rs35520672 [ dbSNP | Ensembl ].
    VAR_033824
    Natural varianti69 – 691L → P in CTRCT23; the patient has cataract and bilateral microphthalmia; the mutation is predicted to disrupt the beta-sheet structure of the protein. 1 Publication
    VAR_029528
    Natural varianti84 – 841T → M.
    Corresponds to variant rs4277 [ dbSNP | Ensembl ].
    VAR_014903
    Natural varianti94 – 941F → S in CTRCT23; modeling suggests that this substitution would significantly reduce the intrinsic stability of the crystalline monomer. 1 Publication
    VAR_029529

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59057 mRNA. Translation: AAC50970.1.
    CR456424 mRNA. Translation: CAG30310.1. Different initiation.
    Z95115 Genomic DNA. Translation: CAI17980.2.
    BC069404 mRNA. Translation: AAH69404.1.
    BC096171 mRNA. Translation: AAH96171.1.
    BC096172 mRNA. Translation: AAH96172.1.
    BC096173 mRNA. Translation: AAH96173.1.
    BC096174 mRNA. Translation: AAH96174.1.
    S67583 Genomic DNA. Translation: AAD13994.1.
    CCDSiCCDS13841.1.
    PIRiI54083.
    RefSeqiNP_001877.1. NM_001886.2.
    UniGeneiHs.57690.

    Genome annotation databases

    EnsembliENST00000354760; ENSP00000346805; ENSG00000196431.
    GeneIDi1413.
    KEGGihsa:1413.
    UCSCiuc003acz.4. human.

    Polymorphism databases

    DMDMi2506318.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59057 mRNA. Translation: AAC50970.1 .
    CR456424 mRNA. Translation: CAG30310.1 . Different initiation.
    Z95115 Genomic DNA. Translation: CAI17980.2 .
    BC069404 mRNA. Translation: AAH69404.1 .
    BC096171 mRNA. Translation: AAH96171.1 .
    BC096172 mRNA. Translation: AAH96172.1 .
    BC096173 mRNA. Translation: AAH96173.1 .
    BC096174 mRNA. Translation: AAH96174.1 .
    S67583 Genomic DNA. Translation: AAD13994.1 .
    CCDSi CCDS13841.1.
    PIRi I54083.
    RefSeqi NP_001877.1. NM_001886.2.
    UniGenei Hs.57690.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LWK X-ray 1.70 A 8-196 [» ]
    ProteinModelPortali P53673.
    SMRi P53673. Positions 8-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P53673. 2 interactions.
    MINTi MINT-5161963.
    STRINGi 9606.ENSP00000346805.

    PTM databases

    PhosphoSitei P53673.

    Polymorphism databases

    DMDMi 2506318.

    Proteomic databases

    PaxDbi P53673.
    PRIDEi P53673.

    Protocols and materials databases

    DNASUi 1413.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354760 ; ENSP00000346805 ; ENSG00000196431 .
    GeneIDi 1413.
    KEGGi hsa:1413.
    UCSCi uc003acz.4. human.

    Organism-specific databases

    CTDi 1413.
    GeneCardsi GC22P027017.
    HGNCi HGNC:2396. CRYBA4.
    MIMi 123631. gene.
    610425. phenotype.
    neXtProti NX_P53673.
    Orphaneti 1377. Cataract-microcornea syndrome.
    2543. Microphthalmia - cataract.
    98995. Zonular cataract.
    PharmGKBi PA26910.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39249.
    HOGENOMi HOG000234388.
    HOVERGENi HBG003364.
    InParanoidi P53673.
    OMAi FHVHSGA.
    OrthoDBi EOG7K9K40.
    PhylomeDBi P53673.
    TreeFami TF331401.

    Miscellaneous databases

    EvolutionaryTracei P53673.
    GeneWikii CRYBA4.
    GenomeRNAii 1413.
    NextBioi 5781.
    PROi P53673.
    SOURCEi Search...

    Gene expression databases

    Bgeei P53673.
    CleanExi HS_CRYBA4.
    Genevestigatori P53673.

    Family and domain databases

    InterProi IPR001064. Beta/gamma_crystallin.
    IPR011024. G_crystallin-rel.
    [Graphical view ]
    Pfami PF00030. Crystall. 2 hits.
    [Graphical view ]
    PRINTSi PR01367. BGCRYSTALLIN.
    SMARTi SM00247. XTALbg. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49695. SSF49695. 1 hit.
    PROSITEi PS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens."
      Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., David L.L.
      J. Biol. Chem. 272:2268-2275(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-25; 159-174 AND 178-192, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, MASS SPECTROMETRY.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Regional fine mapping of the beta crystallin genes on chromosome 22 excludes these genes as physically linked markers for neurofibromatosis type 2."
      Bijlsma E.K., Delattre O., Juyn J.A., Melot T., Westerveld A., Dumanski J.P., Thomas G., Hulsebos T.J.M.
      Genes Chromosomes Cancer 8:112-118(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-194.
    6. Cited for: VARIANTS CTRCT23 PRO-69 AND SER-94.

    Entry informationi

    Entry nameiCRBA4_HUMAN
    AccessioniPrimary (citable) accession number: P53673
    Secondary accession number(s): Q4VB22, Q6ICE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3