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P28495

- CAPZA_YEAST

UniProt

P28495 - CAPZA_YEAST

Protein

F-actin-capping protein subunit alpha

Gene

CAP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 1 (01 Dec 1992)
      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.

    GO - Molecular functioni

    1. actin filament binding Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. barbed-end actin filament capping Source: SGD

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31817-MONOMER.
    ReactomeiREACT_189234. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-actin-capping protein subunit alpha
    Gene namesi
    Name:CAP1
    Ordered Locus Names:YKL007W
    ORF Names:YKL155
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKL007w.
    SGDiS000001490. CAP1.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. actin filament Source: SGD
    3. F-actin capping protein complex Source: SGD
    4. WASH complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 268267F-actin-capping protein subunit alphaPRO_0000208646Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei17 – 171Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP28495.
    PaxDbiP28495.
    PeptideAtlasiP28495.

    Expressioni

    Gene expression databases

    GenevestigatoriP28495.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAP2P135175EBI-4003,EBI-4013

    Protein-protein interaction databases

    BioGridi34125. 91 interactions.
    DIPiDIP-2696N.
    IntActiP28495. 12 interactions.
    MINTiMINT-500609.
    STRINGi4932.YKL007W.

    Structurei

    3D structure databases

    ProteinModelPortaliP28495.
    SMRiP28495. Positions 12-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG261759.
    GeneTreeiENSGT00390000006476.
    HOGENOMiHOG000036539.
    KOiK10364.
    OMAiYGEDHYP.
    OrthoDBiEOG7CZKHC.

    Family and domain databases

    InterProiIPR002189. CapZ_alpha.
    IPR017865. F-actin_cap_asu_CS.
    [Graphical view]
    PANTHERiPTHR10653. PTHR10653. 1 hit.
    PfamiPF01267. F-actin_cap_A. 1 hit.
    [Graphical view]
    PRINTSiPR00191. FACTINCAPA.
    PROSITEiPS00748. F_ACTIN_CAPPING_A_1. 1 hit.
    PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P28495-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSKFEEVI NKIINDSPPG ELREVYDDLI KITSENSKNT ILDAIENYNV    50
    QNCIPIEVNG NSVIISKYNK EGAKFFDPVN SVIFSVNHLE RKGLDIEPYE 100
    FTHAKIEKGQ LKELHDKLHE YLLQSFPGDV SFAVYPVPEE ISKISIIIVS 150
    TKYNPNNFWN GHWRSSYIYD LETRELSGQI STQVHYYEDG NVSFQSGKDI 200
    NQSNVDDVVC TIRDIETNFE NDLDLSFFDL NEKQFKALRR RLPVTRSKIN 250
    WGSAIGSYRL GKNAAEGK 268
    Length:268
    Mass (Da):30,699
    Last modified:December 1, 1992 - v1
    Checksum:i6FBD3130B55B0C5C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S59773 Genomic DNA. Translation: AAC60553.1.
    X61398 Genomic DNA. Translation: CAA43669.1.
    Z28007 Genomic DNA. Translation: CAA81841.1.
    AY558093 Genomic DNA. Translation: AAS56419.1.
    BK006944 Genomic DNA. Translation: DAA09149.1.
    PIRiS30135.
    RefSeqiNP_012918.1. NM_001179573.1.

    Genome annotation databases

    EnsemblFungiiYKL007W; YKL007W; YKL007W.
    GeneIDi853862.
    KEGGisce:YKL007W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S59773 Genomic DNA. Translation: AAC60553.1 .
    X61398 Genomic DNA. Translation: CAA43669.1 .
    Z28007 Genomic DNA. Translation: CAA81841.1 .
    AY558093 Genomic DNA. Translation: AAS56419.1 .
    BK006944 Genomic DNA. Translation: DAA09149.1 .
    PIRi S30135.
    RefSeqi NP_012918.1. NM_001179573.1.

    3D structure databases

    ProteinModelPortali P28495.
    SMRi P28495. Positions 12-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34125. 91 interactions.
    DIPi DIP-2696N.
    IntActi P28495. 12 interactions.
    MINTi MINT-500609.
    STRINGi 4932.YKL007W.

    Proteomic databases

    MaxQBi P28495.
    PaxDbi P28495.
    PeptideAtlasi P28495.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL007W ; YKL007W ; YKL007W .
    GeneIDi 853862.
    KEGGi sce:YKL007W.

    Organism-specific databases

    CYGDi YKL007w.
    SGDi S000001490. CAP1.

    Phylogenomic databases

    eggNOGi NOG261759.
    GeneTreei ENSGT00390000006476.
    HOGENOMi HOG000036539.
    KOi K10364.
    OMAi YGEDHYP.
    OrthoDBi EOG7CZKHC.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31817-MONOMER.
    Reactomei REACT_189234. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    NextBioi 975115.

    Gene expression databases

    Genevestigatori P28495.

    Family and domain databases

    InterProi IPR002189. CapZ_alpha.
    IPR017865. F-actin_cap_asu_CS.
    [Graphical view ]
    PANTHERi PTHR10653. PTHR10653. 1 hit.
    Pfami PF01267. F-actin_cap_A. 1 hit.
    [Graphical view ]
    PRINTSi PR00191. FACTINCAPA.
    PROSITEi PS00748. F_ACTIN_CAPPING_A_1. 1 hit.
    PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Effects of null mutations and overexpression of capping protein on morphogenesis, actin distribution and polarized secretion in yeast."
      Amatruda J.F., Gattermeir D.J., Karpova T.S., Cooper J.A.
      J. Cell Biol. 119:1151-1162(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. "Sequence of a 7.8 kb segment on the left arm of yeast chromosome XI reveals four open reading frames, including the CAP1 gene, an intron-containing gene and a gene encoding a homolog to the mammalian UOG-1 gene."
      Boyer J., Pascolo S., Richard G.-F., Dujon B.
      Yeast 9:279-287(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCAPZA_YEAST
    AccessioniPrimary (citable) accession number: P28495
    Secondary accession number(s): D6VXS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 4380 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3