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P47757

- CAPZB_MOUSE

UniProt

P47757 - CAPZB_MOUSE

Protein

F-actin-capping protein subunit beta

Gene

Capzb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    F-actin-capping proteins bind in a Ca2+-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Isoform 3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. Plays a role in the regulation of cell morphology and cytoskeletal organization By similarity.By similarity

    GO - Molecular functioni

    1. beta-tubulin binding Source: MGI
    2. protein binding Source: BHF-UCL

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. barbed-end actin filament capping Source: MGI
    3. cell projection organization Source: MGI
    4. cytoskeleton organization Source: UniProtKB
    5. lamellipodium assembly Source: MGI
    6. muscle fiber development Source: MGI
    7. negative regulation of microtubule polymerization Source: MGI
    8. neuron projection development Source: MGI
    9. regulation of cell morphogenesis Source: UniProtKB
    10. regulation of protein kinase C signaling Source: MGI

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-actin-capping protein subunit beta
    Alternative name(s):
    CapZ beta
    Gene namesi
    Name:Capzb
    Synonyms:Cappb1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:104652. Capzb.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity
    Isoform 1 : CytoplasmmyofibrilsarcomereZ line By similarity. Cytoplasmmyofibrilsarcomere By similarity
    Note: In cardiac muscle, isoform 1 is located at Z-disks of sarcomeres while isoform 2 is enriched at intercalated disks.By similarity
    Isoform 3 : Cytoplasmcytoskeletonperinuclear thecacalyx By similarity
    Note: Isoform 3 is located to sperm head cytoskeletal structure tightly associated to the nucleus By similarity. Isoform 3 colocalizes with the alpha subunit in testicular sperm and to the acrosome in elongating and condensing spermatids.By similarity

    GO - Cellular componenti

    1. cortical cytoskeleton Source: MGI
    2. cytoskeletal calyx Source: UniProtKB-SubCell
    3. F-actin capping protein complex Source: MGI
    4. intercalated disc Source: MGI
    5. lamellipodium Source: MGI
    6. membrane Source: MGI
    7. WASH complex Source: UniProtKB
    8. Z disc Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 277276F-actin-capping protein subunit betaPRO_0000204635Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei235 – 2351N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP47757.
    PaxDbiP47757.
    PRIDEiP47757.

    2D gel databases

    REPRODUCTION-2DPAGEP47757.
    UCD-2DPAGEP47757.

    PTM databases

    PhosphoSiteiP47757.

    Expressioni

    Tissue specificityi

    Isoform 3 is testis-specific and is present in round spermatids, but not in pachytene spermatocytes or Sertoli cells.1 Publication

    Developmental stagei

    Isoform 3 is first detected in testis 22 days after birth, coinciding with the first wave of round spermatid development. It is also detected on 30 and 60 days after birth.1 Publication

    Gene expression databases

    ArrayExpressiP47757.
    BgeeiP47757.
    GenevestigatoriP47757.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. Interacts with ARHGAP17 and RCSD1/CAPZIP. Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53 By similarity. Isoform 2 also is a component of dynactin complex from brain, which contains the actin-related protein ARP1.By similarity

    Protein-protein interaction databases

    BioGridi198480. 9 interactions.
    DIPiDIP-31383N.
    IntActiP47757. 7 interactions.
    MINTiMINT-1864831.
    STRINGi10090.ENSMUSP00000030518.

    Structurei

    3D structure databases

    ProteinModelPortaliP47757.
    SMRiP47757. Positions 2-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG291067.
    GeneTreeiENSGT00390000017957.
    HOGENOMiHOG000041208.
    HOVERGENiHBG050789.
    KOiK10365.
    OMAiLMSESIL.
    OrthoDBiEOG7NPFTR.
    PhylomeDBiP47757.
    TreeFamiTF105732.

    Family and domain databases

    InterProiIPR001698. CapZ_beta.
    IPR019771. F-actin_capping_bsu_CS.
    [Graphical view]
    PANTHERiPTHR10619. PTHR10619. 1 hit.
    PfamiPF01115. F_actin_cap_B. 1 hit.
    [Graphical view]
    PRINTSiPR00192. FACTINCAPB.
    PROSITEiPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P47757-1) [UniParc]FASTAAdd to Basket

    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

    MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA    50
    RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA 100
    NNAFDQYRDL YFEGGVSSVY LWDLDHGFAG VILIKKAGDG SKKIKGCWDS 150
    IHVVEVQEKS SGRTAHYKLT STVMLWLQTN KSGSGTMNLG GSLTRQMEKD 200
    ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV NGLRSLDAIP 250
    DNHKFKQLQR ELSQVLTQRQ VYIQPDN 277
    Length:277
    Mass (Da):31,345
    Last modified:January 23, 2007 - v3
    Checksum:iC4409B1F9E014033
    GO
    Isoform 2 (identifier: P47757-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         246-277: LDAIPDNHKFKQLQRELSQVLTQRQVYIQPDN → VQTFADKSKQEALKNDLVEALKRKQQC

    Show »
    Length:272
    Mass (Da):30,629
    Checksum:iE6466A68B1254FD0
    GO
    Isoform 3 (identifier: P47757-4) [UniParc]FASTAAdd to Basket

    Also known as: Capzb3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MHPSRRSLPFPLNCQLVRVGTADYGGASEQ
         246-277: LDAIPDNHKFKQLQRELSQVLTQRQVYIQPDN → VQTFADKSKQEALKNDLVEALKRKQQC

    Show »
    Length:301
    Mass (Da):33,767
    Checksum:i8E3F2CFD4D06B2F0
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MHPSRRSLPFPLNCQLVRVG TADYGGASEQ in isoform 3. 1 PublicationVSP_046517
    Alternative sequencei246 – 27732LDAIP…IQPDN → VQTFADKSKQEALKNDLVEA LKRKQQC in isoform 2 and isoform 3. 2 PublicationsVSP_000768Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10406 mRNA. Translation: AAA52226.1.
    U10407 mRNA. Translation: AAA52227.1.
    FJ692320 mRNA. Translation: ACN43612.1.
    AL807811 Genomic DNA. No translation available.
    CCDSiCCDS18841.1. [P47757-2]
    CCDS18842.1. [P47757-1]
    CCDS71503.1. [P47757-4]
    PIRiB54819.
    RefSeqiNP_001032850.1. NM_001037761.2. [P47757-1]
    NP_001258334.1. NM_001271405.1. [P47757-4]
    NP_033928.1. NM_009798.4. [P47757-2]
    UniGeneiMm.2945.

    Genome annotation databases

    EnsembliENSMUST00000030518; ENSMUSP00000030518; ENSMUSG00000028745. [P47757-4]
    ENSMUST00000102507; ENSMUSP00000099565; ENSMUSG00000028745. [P47757-1]
    ENSMUST00000102508; ENSMUSP00000099566; ENSMUSG00000028745. [P47757-2]
    GeneIDi12345.
    KEGGimmu:12345.
    UCSCiuc008vlv.1. mouse. [P47757-1]
    uc012dnq.1. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10406 mRNA. Translation: AAA52226.1 .
    U10407 mRNA. Translation: AAA52227.1 .
    FJ692320 mRNA. Translation: ACN43612.1 .
    AL807811 Genomic DNA. No translation available.
    CCDSi CCDS18841.1. [P47757-2 ]
    CCDS18842.1. [P47757-1 ]
    CCDS71503.1. [P47757-4 ]
    PIRi B54819.
    RefSeqi NP_001032850.1. NM_001037761.2. [P47757-1 ]
    NP_001258334.1. NM_001271405.1. [P47757-4 ]
    NP_033928.1. NM_009798.4. [P47757-2 ]
    UniGenei Mm.2945.

    3D structure databases

    ProteinModelPortali P47757.
    SMRi P47757. Positions 2-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198480. 9 interactions.
    DIPi DIP-31383N.
    IntActi P47757. 7 interactions.
    MINTi MINT-1864831.
    STRINGi 10090.ENSMUSP00000030518.

    PTM databases

    PhosphoSitei P47757.

    2D gel databases

    REPRODUCTION-2DPAGE P47757.
    UCD-2DPAGE P47757.

    Proteomic databases

    MaxQBi P47757.
    PaxDbi P47757.
    PRIDEi P47757.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030518 ; ENSMUSP00000030518 ; ENSMUSG00000028745 . [P47757-4 ]
    ENSMUST00000102507 ; ENSMUSP00000099565 ; ENSMUSG00000028745 . [P47757-1 ]
    ENSMUST00000102508 ; ENSMUSP00000099566 ; ENSMUSG00000028745 . [P47757-2 ]
    GeneIDi 12345.
    KEGGi mmu:12345.
    UCSCi uc008vlv.1. mouse. [P47757-1 ]
    uc012dnq.1. mouse.

    Organism-specific databases

    CTDi 832.
    MGIi MGI:104652. Capzb.

    Phylogenomic databases

    eggNOGi NOG291067.
    GeneTreei ENSGT00390000017957.
    HOGENOMi HOG000041208.
    HOVERGENi HBG050789.
    KOi K10365.
    OMAi LMSESIL.
    OrthoDBi EOG7NPFTR.
    PhylomeDBi P47757.
    TreeFami TF105732.

    Enzyme and pathway databases

    Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    ChiTaRSi CAPZB. mouse.
    NextBioi 280980.
    PROi P47757.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47757.
    Bgeei P47757.
    Genevestigatori P47757.

    Family and domain databases

    InterProi IPR001698. CapZ_beta.
    IPR019771. F-actin_capping_bsu_CS.
    [Graphical view ]
    PANTHERi PTHR10619. PTHR10619. 1 hit.
    Pfami PF01115. F_actin_cap_B. 1 hit.
    [Graphical view ]
    PRINTSi PR00192. FACTINCAPB.
    PROSITEi PS00231. F_ACTIN_CAPPING_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates."
      Schafer D.A., Korshunova Y.O., Schroer T.A., Cooper J.A.
      J. Cell Biol. 127:453-465(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Skeletal muscle.
    2. "A missense mutation in the Capza3 gene and disruption of F-actin organization in spermatids of repro32 infertile male mice."
      Geyer C.B., Inselman A.L., Sunman J.A., Bornstein S., Handel M.A., Eddy E.M.
      Dev. Biol. 330:142-152(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: CD-1.
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Lubec G., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 79-92 AND 169-181, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Hippocampus.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiCAPZB_MOUSE
    AccessioniPrimary (citable) accession number: P47757
    Secondary accession number(s): A2AMV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3