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P47757 (CAPZB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-actin-capping protein subunit beta
Alternative name(s):
CapZ beta
Gene names
Name:Capzb
Synonyms:Cappb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length277 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. Isoform 3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. Plays a role in the regulation of cell morphology and cytoskeletal organization By similarity.

Subunit structure

Heterodimer of an alpha and a beta subunit. Interacts with ARHGAP17 and RCSD1/CAPZIP. 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 By similarity. Isoform 2 also is a component of dynactin complex from brain, which contains the actin-related protein ARP1.

Subcellular location

Cytoplasmcytoskeleton By similarity Ref.2.

Isoform 1: CytoplasmmyofibrilsarcomereZ line By similarity. Cytoplasmmyofibrilsarcomere By similarity. Note: In cardiac muscle, isoform 1 is located at Z-disks of sarcomeres while isoform 2 is enriched at intercalated disks By similarity. Ref.2

Isoform 3: Cytoplasmcytoskeletonperinuclear thecacalyx By similarity. Note: Isoform 3 is located to sperm head cytoskeletal structure tightly associated to the nucleus By similarity. Isoform 3 colocalizes with the alpha subunit in testicular sperm and to the acrosome in elongating and condensing spermatids. Ref.2

Tissue specificity

Isoform 3 is testis-specific and is present in round spermatids, but not in pachytene spermatocytes or Sertoli cells. Ref.2

Developmental stage

Isoform 3 is first detected in testis 22 days after birth, coinciding with the first wave of round spermatid development. It is also detected on 30 and 60 days after birth. Ref.2

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
   Molecular functionActin capping
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

barbed-end actin filament capping

Inferred from direct assay PubMed 17656356. Source: MGI

cell projection organization

Inferred from mutant phenotype PubMed 15294161. Source: MGI

cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium assembly

Inferred from mutant phenotype PubMed 15294161PubMed 19806181. Source: MGI

muscle fiber development

Inferred from mutant phenotype PubMed 10601341. Source: MGI

negative regulation of microtubule polymerization

Inferred from direct assay PubMed 19806181. Source: MGI

neuron projection development

Inferred from mutant phenotype PubMed 19806181. Source: MGI

regulation of cell morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein kinase C signaling

Inferred from mutant phenotype PubMed 12089068. Source: MGI

   Cellular_componentF-actin capping protein complex

Inferred from direct assay PubMed 11604420. Source: MGI

WASH complex

Inferred from sequence or structural similarity. Source: UniProtKB

Z disc

Inferred from direct assay PubMed 10601341. Source: MGI

cortical cytoskeleton

Inferred from direct assay PubMed 18723693. Source: MGI

cytoskeletal calyx

Inferred from electronic annotation. Source: UniProtKB-SubCell

intercalated disc

Inferred from direct assay PubMed 10601341. Source: MGI

lamellipodium

Inferred from direct assay PubMed 15294161. Source: MGI

membrane

Inferred from direct assay PubMed 18723693. Source: MGI

   Molecular_functionbeta-tubulin binding

Inferred from physical interaction PubMed 19806181. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P47757-1)

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.
Isoform 2 (identifier: P47757-2)

The sequence of this isoform differs from the canonical sequence as follows:
     246-277: LDAIPDNHKFKQLQRELSQVLTQRQVYIQPDN → VQTFADKSKQEALKNDLVEALKRKQQC
Isoform 3 (identifier: P47757-4)

Also known as: Capzb3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHPSRRSLPFPLNCQLVRVGTADYGGASEQ
     246-277: LDAIPDNHKFKQLQRELSQVLTQRQVYIQPDN → VQTFADKSKQEALKNDLVEALKRKQQC

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 277276F-actin-capping protein subunit beta
PRO_0000204635

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue2351N6-acetyllysine Ref.6

Natural variations

Alternative sequence11M → MHPSRRSLPFPLNCQLVRVG TADYGGASEQ in isoform 3.
VSP_046517
Alternative sequence246 – 27732LDAIP…IQPDN → VQTFADKSKQEALKNDLVEA LKRKQQC in isoform 2 and isoform 3.
VSP_000768

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C4409B1F9E014033

FASTA27731,345
        10         20         30         40         50         60 
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL 

        70         80         90        100        110        120 
LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY 

       130        140        150        160        170        180 
LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN 

       190        200        210        220        230        240 
KSGSGTMNLG GSLTRQMEKD ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV 

       250        260        270 
NGLRSLDAIP DNHKFKQLQR ELSQVLTQRQ VYIQPDN 

« Hide

Isoform 2 [UniParc].

Checksum: E6466A68B1254FD0
Show »

FASTA27230,629
Isoform 3 (Capzb3) [UniParc].

Checksum: 8E3F2CFD4D06B2F0
Show »

FASTA30133,767

References

« Hide 'large scale' references
[1]"Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates."
Schafer D.A., Korshunova Y.O., Schroer T.A., Cooper J.A.
J. Cell Biol. 127:453-465(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Skeletal muscle.
[2]"A missense mutation in the Capza3 gene and disruption of F-actin organization in spermatids of repro32 infertile male mice."
Geyer C.B., Inselman A.L., Sunman J.A., Bornstein S., Handel M.A., Eddy E.M.
Dev. Biol. 330:142-152(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: CD-1.
Tissue: Testis.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Lubec G., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 79-92 AND 169-181, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"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(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10406 mRNA. Translation: AAA52226.1.
U10407 mRNA. Translation: AAA52227.1.
FJ692320 mRNA. Translation: ACN43612.1.
AL807811 Genomic DNA. No translation available.
PIRB54819.
RefSeqNP_001032850.1. NM_001037761.2.
NP_001258334.1. NM_001271405.1.
NP_033928.1. NM_009798.4.
UniGeneMm.2945.

3D structure databases

ProteinModelPortalP47757.
SMRP47757. Positions 2-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198480. 7 interactions.
DIPDIP-31383N.
IntActP47757. 7 interactions.
MINTMINT-1864831.
STRING10090.ENSMUSP00000030518.

PTM databases

PhosphoSiteP47757.

2D gel databases

REPRODUCTION-2DPAGEP47757.
UCD-2DPAGEP47757.

Proteomic databases

PaxDbP47757.
PRIDEP47757.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030518; ENSMUSP00000030518; ENSMUSG00000028745. [P47757-4]
ENSMUST00000102507; ENSMUSP00000099565; ENSMUSG00000028745. [P47757-1]
ENSMUST00000102508; ENSMUSP00000099566; ENSMUSG00000028745. [P47757-2]
GeneID12345.
KEGGmmu:12345.
UCSCuc008vlv.1. mouse. [P47757-1]
uc012dnq.1. mouse.

Organism-specific databases

CTD832.
MGIMGI:104652. Capzb.

Phylogenomic databases

eggNOGNOG291067.
GeneTreeENSGT00390000017957.
HOGENOMHOG000041208.
HOVERGENHBG050789.
KOK10365.
OMAFDTYREM.
OrthoDBEOG7NPFTR.
PhylomeDBP47757.
TreeFamTF105732.

Gene expression databases

ArrayExpressP47757.
BgeeP47757.
GenevestigatorP47757.

Family and domain databases

InterProIPR001698. CapZ_beta.
IPR019771. F-actin_capping_bsu_CS.
[Graphical view]
PANTHERPTHR10619. PTHR10619. 1 hit.
PfamPF01115. F_actin_cap_B. 1 hit.
[Graphical view]
PRINTSPR00192. FACTINCAPB.
PROSITEPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAPZB. mouse.
NextBio280980.
PROP47757.
SOURCESearch...

Entry information

Entry nameCAPZB_MOUSE
AccessionPrimary (citable) accession number: P47757
Secondary accession number(s): A2AMV7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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