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Protein

F-actin-capping protein subunit alpha-2

Gene

Capza2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-879415. Advanced glycosylation endproduct receptor signaling.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit alpha-2
Alternative name(s):
CapZ alpha-2
Gene namesi
Name:Capza2
Synonyms:Cappa2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:106222. Capza2.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: UniProtKB
  • cortical cytoskeleton Source: MGI
  • extracellular exosome Source: MGI
  • F-actin capping protein complex Source: MGI
  • membrane Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 286285F-actin-capping protein subunit alpha-2PRO_0000208628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei9 – 91PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP47754.
PaxDbiP47754.
PeptideAtlasiP47754.
PRIDEiP47754.

2D gel databases

REPRODUCTION-2DPAGEP47754.

PTM databases

iPTMnetiP47754.
PhosphoSiteiP47754.
SwissPalmiP47754.

Expressioni

Gene expression databases

BgeeiP47754.
ExpressionAtlasiP47754. baseline and differential.
GenevisibleiP47754. MM.

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), WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53. Interacts with RCSD1/CAPZIP (By similarity).By similarity

Protein-protein interaction databases

BioGridi198478. 9 interactions.
DIPiDIP-31382N.
IntActiP47754. 11 interactions.
MINTiMINT-1856708.
STRINGi10090.ENSMUSP00000015877.

Structurei

3D structure databases

ProteinModelPortaliP47754.
SMRiP47754. Positions 9-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0836. Eukaryota.
ENOG410ZAWX. LUCA.
HOGENOMiHOG000036539.
HOVERGENiHBG050810.
InParanoidiP47754.
KOiK10364.
OMAiSHAFSQY.
OrthoDBiEOG71ZP25.
PhylomeDBiP47754.
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]

Sequencei

Sequence statusi: Complete.

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

P47754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA
60 70 80 90 100
AHAFAQYNLD QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH
110 120 130 140 150
LRKEATDPRP YEAENAIESW RTSVETALRA YVKEHYPNGV CTVYGKKVDG
160 170 180 190 200
QQTIIACIES HQFQAKNFWN GRWRSEWKFT VTPSTTQVVG ILKIQVHYYE
210 220 230 240 250
DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ TAISENYQTM
260 270 280
SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
Length:286
Mass (Da):32,967
Last modified:January 23, 2007 - v3
Checksum:iE706A9BC1830E70B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16741 mRNA. Translation: AAC00567.1.
BC082589 mRNA. Translation: AAH82589.1.
CCDSiCCDS19926.1.
RefSeqiNP_031630.1. NM_007604.2.
UniGeneiMm.392504.
Mm.471667.

Genome annotation databases

EnsembliENSMUST00000015877; ENSMUSP00000015877; ENSMUSG00000015733.
GeneIDi12343.
KEGGimmu:12343.
UCSCiuc009azs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16741 mRNA. Translation: AAC00567.1.
BC082589 mRNA. Translation: AAH82589.1.
CCDSiCCDS19926.1.
RefSeqiNP_031630.1. NM_007604.2.
UniGeneiMm.392504.
Mm.471667.

3D structure databases

ProteinModelPortaliP47754.
SMRiP47754. Positions 9-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198478. 9 interactions.
DIPiDIP-31382N.
IntActiP47754. 11 interactions.
MINTiMINT-1856708.
STRINGi10090.ENSMUSP00000015877.

PTM databases

iPTMnetiP47754.
PhosphoSiteiP47754.
SwissPalmiP47754.

2D gel databases

REPRODUCTION-2DPAGEP47754.

Proteomic databases

EPDiP47754.
PaxDbiP47754.
PeptideAtlasiP47754.
PRIDEiP47754.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015877; ENSMUSP00000015877; ENSMUSG00000015733.
GeneIDi12343.
KEGGimmu:12343.
UCSCiuc009azs.1. mouse.

Organism-specific databases

CTDi830.
MGIiMGI:106222. Capza2.

Phylogenomic databases

eggNOGiKOG0836. Eukaryota.
ENOG410ZAWX. LUCA.
HOGENOMiHOG000036539.
HOVERGENiHBG050810.
InParanoidiP47754.
KOiK10364.
OMAiSHAFSQY.
OrthoDBiEOG71ZP25.
PhylomeDBiP47754.
TreeFamiTF314822.

Enzyme and pathway databases

ReactomeiR-MMU-879415. Advanced glycosylation endproduct receptor signaling.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiCapza2. mouse.
PROiP47754.
SOURCEiSearch...

Gene expression databases

BgeeiP47754.
ExpressionAtlasiP47754. baseline and differential.
GenevisibleiP47754. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Muscle.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 20-86 AND 104-129, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic fibroblast.
  4. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-37; 67-86 AND 194-210, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCAZA2_MOUSE
AccessioniPrimary (citable) accession number: P47754
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 139 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.