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P47754 (CAZA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-actin-capping protein subunit alpha-2
Alternative name(s):
CapZ alpha-2
Gene names
Name:Capza2
Synonyms:Cappa2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Sequence similarities

Belongs to the F-actin-capping protein alpha subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 286285F-actin-capping protein subunit alpha-2
PRO_0000208628

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue91Phosphoserine By similarity
Modified residue861N6-acetyllysine By similarity
Modified residue971N6-acetyllysine By similarity
Modified residue2731N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P47754 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E706A9BC1830E70B

FASTA28632,967
        10         20         30         40         50         60 
MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD 

        70         80         90        100        110        120 
QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH LRKEATDPRP YEAENAIESW 

       130        140        150        160        170        180 
RTSVETALRA YVKEHYPNGV CTVYGKKVDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT 

       190        200        210        220        230        240 
VTPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ 

       250        260        270        280 
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA 

« Hide

References

« Hide 'large scale' references
[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: 9331217] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
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, 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, MASS SPECTROMETRY.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16741 mRNA. Translation: AAC00567.1.
BC082589 mRNA. Translation: AAH82589.1.
IPIIPI00111265.
RefSeqNP_031630.1. NM_007604.2.
UniGeneMm.392504.

3D structure databases

ProteinModelPortalP47754.
SMRP47754. Positions 8-276.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31382N.
IntActP47754. 8 interactions.
STRINGP47754.

PTM databases

PhosphoSiteP47754.

2D gel databases

REPRODUCTION-2DPAGEP47754.

Proteomic databases

PRIDEP47754.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015877; ENSMUSP00000015877; ENSMUSG00000015733.
GeneID12343.
KEGGmmu:12343.

Organism-specific databases

CTD830.
MGIMGI:106222. Capza2.

Phylogenomic databases

eggNOGroNOG04256.
HOGENOMHBG397839.
HOVERGENHBG050810.
InParanoidP47754.
OMAAIESWRN.
OrthoDBEOG45DWQ0.
PhylomeDBP47754.

Gene expression databases

ArrayExpressP47754.
BgeeP47754.
GenevestigatorP47754.
GermOnlineENSMUSG00000015733. Mus musculus.

Family and domain databases

InterProIPR017865. F-actin_cap_asu_CS.
IPR002189. WASH_F-actin_cap_alpha.
[Graphical view]
KOK10364.
PANTHERPTHR10653. F-actin_cap_A. 1 hit.
PfamPF01267. F-actin_cap_A. 1 hit.
[Graphical view]
PRINTSPR00191. FACTINCAPA.
PROSITEPS00748. F_ACTIN_CAPPING_A_1. 1 hit.
PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280972.
SOURCESearch...

Entry information

Entry nameCAZA2_MOUSE
AccessionPrimary (citable) accession number: P47754
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families