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P47755

- CAZA2_HUMAN

UniProt

P47755 - CAZA2_HUMAN

Protein

F-actin-capping protein subunit alpha-2

Gene

CAPZA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (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.

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. actin filament capping Source: UniProtKB-KW
    3. blood coagulation Source: Reactome
    4. cellular component movement Source: ProtInc
    5. innate immune response Source: Reactome
    6. protein complex assembly Source: ProtInc

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-actin-capping protein subunit alpha-2
    Alternative name(s):
    CapZ alpha-2
    Gene namesi
    Name:CAPZA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1490. CAPZA2.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cortical cytoskeleton Source: Ensembl
    3. cytosol Source: Reactome
    4. extracellular region Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. F-actin capping protein complex Source: ProtInc
    7. membrane Source: Ensembl
    8. WASH complex Source: InterPro

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26071.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 286285F-actin-capping protein subunit alpha-2PRO_0000208627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP47755.
    PaxDbiP47755.
    PeptideAtlasiP47755.
    PRIDEiP47755.

    2D gel databases

    DOSAC-COBS-2DPAGEP47755.
    OGPiP47755.
    REPRODUCTION-2DPAGEP47755.

    PTM databases

    PhosphoSiteiP47755.

    Expressioni

    Gene expression databases

    ArrayExpressiP47755.
    BgeeiP47755.
    CleanExiHS_CAPZA2.
    GenevestigatoriP47755.

    Organism-specific databases

    HPAiHPA007470.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53. Interacts with RCSD1/CAPZIP.2 Publications

    Protein-protein interaction databases

    BioGridi107280. 19 interactions.
    IntActiP47755. 14 interactions.
    STRINGi9606.ENSP00000354947.

    Structurei

    3D structure databases

    ProteinModelPortaliP47755.
    SMRiP47755. Positions 8-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG261759.
    HOGENOMiHOG000036539.
    HOVERGENiHBG050810.
    InParanoidiP47755.
    KOiK10364.
    OMAiLDWDKVL.
    PhylomeDBiP47755.
    TreeFamiTF314822.

    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]

    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: P47755-1) [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

    MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA    50
    AHAFAQYNLD QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH 100
    LRKEATDPRP CEVENAVESW RTSVETALRA YVKEHYPNGV CTVYGKKIDG 150
    QQTIIACIES HQFQAKNFWN GRWRSEWKFT ITPSTTQVVG ILKIQVHYYE 200
    DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ TAISENYQTM 250
    SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA 286
    Length:286
    Mass (Da):32,949
    Last modified:January 23, 2007 - v3
    Checksum:iB5E1B617A38E758B
    GO
    Isoform 2 (identifier: P47755-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         143-172: VYGKKIDGQQTIIACIESHQFQAKNFWNGR → EWSLEVRMEVYNHSFNHSSGWHLENSGSLL
         173-286: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:172
    Mass (Da):19,775
    Checksum:iF821EBDB7171C078
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei143 – 17230VYGKK…FWNGR → EWSLEVRMEVYNHSFNHSSG WHLENSGSLL in isoform 2. 1 PublicationVSP_053871Add
    BLAST
    Alternative sequencei173 – 286114Missing in isoform 2. 1 PublicationVSP_053872Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03269 mRNA. Translation: AAA88848.1.
    BT006735 mRNA. Translation: AAP35381.1.
    AK294409 mRNA. Translation: BAG57661.1.
    AC002543 Genomic DNA. Translation: AAC60382.1.
    BC005338 mRNA. Translation: AAH05338.1.
    U03851 mRNA. Translation: AAC00534.1.
    CCDSiCCDS5768.1. [P47755-1]
    PIRiG01229.
    RefSeqiNP_006127.1. NM_006136.2. [P47755-1]
    UniGeneiHs.446123.

    Genome annotation databases

    EnsembliENST00000361183; ENSP00000354947; ENSG00000198898. [P47755-1]
    GeneIDi830.
    KEGGihsa:830.
    UCSCiuc003vil.3. human. [P47755-1]

    Polymorphism databases

    DMDMi1345695.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03269 mRNA. Translation: AAA88848.1 .
    BT006735 mRNA. Translation: AAP35381.1 .
    AK294409 mRNA. Translation: BAG57661.1 .
    AC002543 Genomic DNA. Translation: AAC60382.1 .
    BC005338 mRNA. Translation: AAH05338.1 .
    U03851 mRNA. Translation: AAC00534.1 .
    CCDSi CCDS5768.1. [P47755-1 ]
    PIRi G01229.
    RefSeqi NP_006127.1. NM_006136.2. [P47755-1 ]
    UniGenei Hs.446123.

    3D structure databases

    ProteinModelPortali P47755.
    SMRi P47755. Positions 8-276.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107280. 19 interactions.
    IntActi P47755. 14 interactions.
    STRINGi 9606.ENSP00000354947.

    PTM databases

    PhosphoSitei P47755.

    Polymorphism databases

    DMDMi 1345695.

    2D gel databases

    DOSAC-COBS-2DPAGE P47755.
    OGPi P47755.
    REPRODUCTION-2DPAGE P47755.

    Proteomic databases

    MaxQBi P47755.
    PaxDbi P47755.
    PeptideAtlasi P47755.
    PRIDEi P47755.

    Protocols and materials databases

    DNASUi 830.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361183 ; ENSP00000354947 ; ENSG00000198898 . [P47755-1 ]
    GeneIDi 830.
    KEGGi hsa:830.
    UCSCi uc003vil.3. human. [P47755-1 ]

    Organism-specific databases

    CTDi 830.
    GeneCardsi GC07P116451.
    HGNCi HGNC:1490. CAPZA2.
    HPAi HPA007470.
    MIMi 601571. gene.
    neXtProti NX_P47755.
    PharmGKBi PA26071.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG261759.
    HOGENOMi HOG000036539.
    HOVERGENi HBG050810.
    InParanoidi P47755.
    KOi K10364.
    OMAi LDWDKVL.
    PhylomeDBi P47755.
    TreeFami TF314822.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.

    Miscellaneous databases

    GeneWikii CAPZA2.
    GenomeRNAii 830.
    NextBioi 3418.
    PROi P47755.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47755.
    Bgeei P47755.
    CleanExi HS_CAPZA2.
    Genevestigatori P47755.

    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. "Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families."
      Barron-Casella E.A., Torres M.A., Scherer S.W., Heng H.H.Q., Tsui L.-C., Casella J.F.
      J. Biol. Chem. 270:21472-21479(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Amygdala.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Kidney.
    6. "Vertebrates have conserved capping protein alpha isoforms with specific expression patterns."
      Hart M.C., Korshunova Y.O., Cooper J.A.
      Cell Motil. Cytoskeleton 38:120-132(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-286 (ISOFORM 1).
      Tissue: Pancreas.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-15.
      Tissue: Platelet.
    8. Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15; 20-66; 122-129 AND 179-210, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma and Mammary carcinoma.
    9. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 20-86; 147-166 AND 179-226, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ."
      Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C., Cuenda A., Cohen P.
      Biochem. J. 389:127-135(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RCSD1/CAPZIP, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex."
      Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.
      Dev. Cell 17:712-723(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE WASH COMPLEX.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCAZA2_HUMAN
    AccessioniPrimary (citable) accession number: P47755
    Secondary accession number(s): B4DG50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 135 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3