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Protein

F-actin-capping protein subunit alpha-1

Gene

Capza1

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

  1. barbed-end actin filament capping Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit alpha-1
Alternative name(s):
CapZ alpha-1
Gene namesi
Name:Capza1
Synonyms:Cappa1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:106227. Capza1.

Subcellular locationi

Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cortical cytoskeleton Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. F-actin capping protein complex Source: MGI
  5. membrane Source: MGI
  6. WASH complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 286285F-actin-capping protein subunit alpha-1PRO_0000208625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei19 – 191N6-acetyllysine1 Publication
Modified residuei97 – 971N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP47753.
PaxDbiP47753.
PRIDEiP47753.

2D gel databases

REPRODUCTION-2DPAGEP47753.

PTM databases

PhosphoSiteiP47753.

Expressioni

Gene expression databases

GenevestigatoriP47753.

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 S100B and S100A (By similarity).By similarity

Protein-protein interaction databases

BioGridi198477. 25 interactions.
IntActiP47753. 23 interactions.
MINTiMINT-1856502.

Structurei

3D structure databases

ProteinModelPortaliP47753.
SMRiP47753. Positions 7-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG261759.
HOVERGENiHBG050810.
InParanoidiP47753.
KOiK10364.
PhylomeDBiP47753.

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.

P47753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA
60 70 80 90 100
AHAFAQYNMD QFTPVKIEGY DDQVLITEHG DLGNSRFLDP RNQISFKFDH
110 120 130 140 150
LRKEASDPQP EDVDGGLKSW RESCDSALRA YVKDHYSNGF CTVYAKTIDG
160 170 180 190 200
QQTIIACIES HQFQPKNFWN GRWRSEWKFT ITPPSAQVVG VLKIQVHYYE
210 220 230 240 250
DGNVQLVSHK DVQDSVTVSN EVQTTKEFIK IIESAENEYQ TAISENYQTM
260 270 280
SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
Length:286
Mass (Da):32,940
Last modified:January 22, 2007 - v4
Checksum:i6FE97BCE5D9B9D3A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221V → I in AAC00566 (PubMed:9331217).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC016232 mRNA. Translation: AAH16232.1.
U16740 mRNA. Translation: AAC00566.1.
CCDSiCCDS38580.1.
RefSeqiNP_033927.2. NM_009797.2.
UniGeneiMm.19142.

Genome annotation databases

GeneIDi12340.
KEGGimmu:12340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC016232 mRNA. Translation: AAH16232.1.
U16740 mRNA. Translation: AAC00566.1.
CCDSiCCDS38580.1.
RefSeqiNP_033927.2. NM_009797.2.
UniGeneiMm.19142.

3D structure databases

ProteinModelPortaliP47753.
SMRiP47753. Positions 7-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198477. 25 interactions.
IntActiP47753. 23 interactions.
MINTiMINT-1856502.

PTM databases

PhosphoSiteiP47753.

2D gel databases

REPRODUCTION-2DPAGEP47753.

Proteomic databases

MaxQBiP47753.
PaxDbiP47753.
PRIDEiP47753.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi12340.
KEGGimmu:12340.

Organism-specific databases

CTDi829.
MGIiMGI:106227. Capza1.

Phylogenomic databases

eggNOGiNOG261759.
HOVERGENiHBG050810.
InParanoidiP47753.
KOiK10364.
PhylomeDBiP47753.

Miscellaneous databases

ChiTaRSiCapza1. mouse.
NextBioi280968.
PROiP47753.
SOURCEiSearch...

Gene expression databases

GenevestigatoriP47753.

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. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-286.
    Tissue: Muscle.
  3. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUN-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 194-210.
    Tissue: Brain.
  4. "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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCAZA1_MOUSE
AccessioniPrimary (citable) accession number: P47753
Secondary accession number(s): Q91YN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1996
Last sequence update: January 22, 2007
Last modified: March 3, 2015
This is version 123 of the entry and version 4 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

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 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.