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Protein

F-actin-capping protein subunit beta

Gene

Capzb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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. 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).By similarity

GO - Molecular functioni

  1. beta-tubulin binding Source: MGI

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. barbed-end actin filament capping Source: MGI
  3. cell morphogenesis Source: GO_Central
  4. cell projection organization Source: MGI
  5. cytoskeleton organization Source: UniProtKB
  6. lamellipodium assembly Source: MGI
  7. muscle fiber development Source: MGI
  8. negative regulation of filopodium assembly Source: GO_Central
  9. negative regulation of microtubule polymerization Source: MGI
  10. neuron projection development Source: MGI
  11. regulation of cell morphogenesis Source: UniProtKB
  12. regulation of lamellipodium assembly Source: GO_Central
  13. regulation of protein kinase C signaling Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit beta
Alternative name(s):
CapZ beta
Gene namesi
Name:Capzb
Synonyms:Cappb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:104652. Capzb.

Subcellular locationi

Cytoplasmcytoskeleton By similarity
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
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.By similarity

GO - Cellular componenti

  1. actin cortical patch Source: GO_Central
  2. actin filament Source: GO_Central
  3. cortical cytoskeleton Source: MGI
  4. cytoskeletal calyx Source: UniProtKB-SubCell
  5. extracellular vesicular exosome Source: MGI
  6. F-actin capping protein complex Source: MGI
  7. intercalated disc Source: MGI
  8. lamellipodium Source: MGI
  9. membrane Source: MGI
  10. WASH complex Source: UniProtKB
  11. Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 277276F-actin-capping protein subunit betaPRO_0000204635Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei235 – 2351N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP47757.
PaxDbiP47757.
PRIDEiP47757.

2D gel databases

REPRODUCTION-2DPAGEP47757.
UCD-2DPAGEP47757.

PTM databases

PhosphoSiteiP47757.

Expressioni

Tissue specificityi

Isoform 3 is testis-specific and is present in round spermatids, but not in pachytene spermatocytes or Sertoli cells.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiP47757.
ExpressionAtlasiP47757. baseline and differential.
GenevestigatoriP47757.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

BioGridi198480. 9 interactions.
DIPiDIP-31383N.
IntActiP47757. 7 interactions.
MINTiMINT-1864831.
STRINGi10090.ENSMUSP00000030518.

Structurei

3D structure databases

ProteinModelPortaliP47757.
SMRiP47757. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG291067.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
HOVERGENiHBG050789.
InParanoidiP47757.
KOiK10365.
OMAiREFLCCD.
OrthoDBiEOG7NPFTR.
PhylomeDBiP47757.
TreeFamiTF105732.

Family and domain databases

InterProiIPR001698. CAPZB.
IPR019771. F-actin_capping_bsu_CS.
[Graphical view]
PANTHERiPTHR10619. PTHR10619. 1 hit.
PfamiPF01115. F_actin_cap_B. 1 hit.
[Graphical view]
PRINTSiPR00192. FACTINCAPB.
PROSITEiPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P47757-1) [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

        10         20         30         40         50
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA
60 70 80 90 100
RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA
110 120 130 140 150
NNAFDQYRDL YFEGGVSSVY LWDLDHGFAG VILIKKAGDG SKKIKGCWDS
160 170 180 190 200
IHVVEVQEKS SGRTAHYKLT STVMLWLQTN KSGSGTMNLG GSLTRQMEKD
210 220 230 240 250
ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV NGLRSLDAIP
260 270
DNHKFKQLQR ELSQVLTQRQ VYIQPDN
Length:277
Mass (Da):31,345
Last modified:January 23, 2007 - v3
Checksum:iC4409B1F9E014033
GO
Isoform 2 (identifier: P47757-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:272
Mass (Da):30,629
Checksum:iE6466A68B1254FD0
GO
Isoform 3 (identifier: P47757-4) [UniParc]FASTAAdd to Basket

Also known as: Capzb3

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

Show »
Length:301
Mass (Da):33,767
Checksum:i8E3F2CFD4D06B2F0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MHPSRRSLPFPLNCQLVRVG TADYGGASEQ in isoform 3. 1 PublicationVSP_046517
Alternative sequencei246 – 27732LDAIP…IQPDN → VQTFADKSKQEALKNDLVEA LKRKQQC in isoform 2 and isoform 3. 2 PublicationsVSP_000768Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10406 mRNA. Translation: AAA52226.1.
U10407 mRNA. Translation: AAA52227.1.
FJ692320 mRNA. Translation: ACN43612.1.
AL807811 Genomic DNA. No translation available.
CCDSiCCDS18841.1. [P47757-2]
CCDS18842.1. [P47757-1]
CCDS71503.1. [P47757-4]
PIRiB54819.
RefSeqiNP_001032850.1. NM_001037761.2. [P47757-1]
NP_001258334.1. NM_001271405.1. [P47757-4]
NP_033928.1. NM_009798.4. [P47757-2]
UniGeneiMm.2945.

Genome annotation databases

EnsembliENSMUST00000030518; ENSMUSP00000030518; ENSMUSG00000028745. [P47757-4]
ENSMUST00000102507; ENSMUSP00000099565; ENSMUSG00000028745. [P47757-1]
ENSMUST00000102508; ENSMUSP00000099566; ENSMUSG00000028745. [P47757-2]
GeneIDi12345.
KEGGimmu:12345.
UCSCiuc008vlv.1. mouse. [P47757-1]
uc012dnq.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10406 mRNA. Translation: AAA52226.1.
U10407 mRNA. Translation: AAA52227.1.
FJ692320 mRNA. Translation: ACN43612.1.
AL807811 Genomic DNA. No translation available.
CCDSiCCDS18841.1. [P47757-2]
CCDS18842.1. [P47757-1]
CCDS71503.1. [P47757-4]
PIRiB54819.
RefSeqiNP_001032850.1. NM_001037761.2. [P47757-1]
NP_001258334.1. NM_001271405.1. [P47757-4]
NP_033928.1. NM_009798.4. [P47757-2]
UniGeneiMm.2945.

3D structure databases

ProteinModelPortaliP47757.
SMRiP47757. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198480. 9 interactions.
DIPiDIP-31383N.
IntActiP47757. 7 interactions.
MINTiMINT-1864831.
STRINGi10090.ENSMUSP00000030518.

PTM databases

PhosphoSiteiP47757.

2D gel databases

REPRODUCTION-2DPAGEP47757.
UCD-2DPAGEP47757.

Proteomic databases

MaxQBiP47757.
PaxDbiP47757.
PRIDEiP47757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030518; ENSMUSP00000030518; ENSMUSG00000028745. [P47757-4]
ENSMUST00000102507; ENSMUSP00000099565; ENSMUSG00000028745. [P47757-1]
ENSMUST00000102508; ENSMUSP00000099566; ENSMUSG00000028745. [P47757-2]
GeneIDi12345.
KEGGimmu:12345.
UCSCiuc008vlv.1. mouse. [P47757-1]
uc012dnq.1. mouse.

Organism-specific databases

CTDi832.
MGIiMGI:104652. Capzb.

Phylogenomic databases

eggNOGiNOG291067.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
HOVERGENiHBG050789.
InParanoidiP47757.
KOiK10365.
OMAiREFLCCD.
OrthoDBiEOG7NPFTR.
PhylomeDBiP47757.
TreeFamiTF105732.

Enzyme and pathway databases

ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiCapzb. mouse.
NextBioi280980.
PROiP47757.
SOURCEiSearch...

Gene expression databases

BgeeiP47757.
ExpressionAtlasiP47757. baseline and differential.
GenevestigatoriP47757.

Family and domain databases

InterProiIPR001698. CAPZB.
IPR019771. F-actin_capping_bsu_CS.
[Graphical view]
PANTHERiPTHR10619. PTHR10619. 1 hit.
PfamiPF01115. F_actin_cap_B. 1 hit.
[Graphical view]
PRINTSiPR00192. FACTINCAPB.
PROSITEiPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiCAPZB_MOUSE
AccessioniPrimary (citable) accession number: P47757
Secondary accession number(s): A2AMV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 131 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

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.