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Protein

F-actin-capping protein subunit beta

Gene

cap-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 - Molecular functioni

  • actin filament binding Source: WormBase

GO - Biological processi

  • actin cytoskeleton organization Source: WormBase
  • barbed-end actin filament capping Source: InterPro
  • embryonic axis specification Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-CEL-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit beta
Gene namesi
Name:cap-2
ORF Names:M106.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiM106.5; CE01608; WBGene00000293; cap-2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: WormBase
  • dynactin complex Source: WormBase
  • F-actin capping protein complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270F-actin-capping protein subunit betaPRO_0000204637Add
BLAST

Proteomic databases

EPDiP34686.
PaxDbiP34686.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.

GO - Molecular functioni

  • actin filament binding Source: WormBase

Protein-protein interaction databases

BioGridi39983. 4 interactions.
DIPiDIP-26957N.
IntActiP34686. 1 interaction.
MINTiMINT-1095007.
STRINGi6239.M106.5.1.

Structurei

3D structure databases

ProteinModelPortaliP34686.
SMRiP34686. Positions 4-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3174. Eukaryota.
ENOG410XQYD. LUCA.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
InParanoidiP34686.
KOiK10365.
OMAiFDTYREM.
OrthoDBiEOG7NPFTR.
PhylomeDBiP34686.

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]

Sequencei

Sequence statusi: Complete.

P34686-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEQQLDCAL DLMRRLPPQH CDKNLTDLID LCPHLVDDLL STIDQPLKIA
60 70 80 90 100
ADRETGKQYL LCDYNRDGDS YRSPWSNTYD PPLEDGQLPS EKRRKMEIEA
110 120 130 140 150
NAAFESYRDL YFEGGVSSVY FWDLDNGGFA GIVLIKKEGD GAKNITGCWD
160 170 180 190 200
SIHVIEITER ARQAHYKLTS TIMLWLQTNK SSSGVMNLGG SLTRQHEMDA
210 220 230 240 250
PINDQNTHLA NMGRMIEDQE SKMRLTINEI YFGKTKKVMS DLRSTEKQSE
260 270
LEKQDEIVRE LNNAMANRGN
Length:270
Mass (Da):30,786
Last modified:February 1, 1994 - v1
Checksum:i8EB7BC108233CDC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18806 Genomic DNA. Translation: CAA79270.1.
Z18854 mRNA. Translation: CAA79306.1.
Z46935 Genomic DNA. Translation: CAA87051.1.
PIRiB47734.
RefSeqiNP_496336.1. NM_063935.6.
UniGeneiCel.18252.

Genome annotation databases

EnsemblMetazoaiM106.5; M106.5; WBGene00000293.
GeneIDi174673.
KEGGicel:CELE_M106.5.
UCSCiM106.5.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18806 Genomic DNA. Translation: CAA79270.1.
Z18854 mRNA. Translation: CAA79306.1.
Z46935 Genomic DNA. Translation: CAA87051.1.
PIRiB47734.
RefSeqiNP_496336.1. NM_063935.6.
UniGeneiCel.18252.

3D structure databases

ProteinModelPortaliP34686.
SMRiP34686. Positions 4-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi39983. 4 interactions.
DIPiDIP-26957N.
IntActiP34686. 1 interaction.
MINTiMINT-1095007.
STRINGi6239.M106.5.1.

Proteomic databases

EPDiP34686.
PaxDbiP34686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiM106.5; M106.5; WBGene00000293.
GeneIDi174673.
KEGGicel:CELE_M106.5.
UCSCiM106.5.1. c. elegans.

Organism-specific databases

CTDi174673.
WormBaseiM106.5; CE01608; WBGene00000293; cap-2.

Phylogenomic databases

eggNOGiKOG3174. Eukaryota.
ENOG410XQYD. LUCA.
GeneTreeiENSGT00390000017957.
HOGENOMiHOG000041208.
InParanoidiP34686.
KOiK10365.
OMAiFDTYREM.
OrthoDBiEOG7NPFTR.
PhylomeDBiP34686.

Enzyme and pathway databases

ReactomeiR-CEL-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

PROiP34686.

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. "The alpha and beta subunits of nematode actin capping protein function in yeast."
    Waddle J.A., Cooper J.A., Waterston R.H.
    Mol. Biol. Cell 4:907-917(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: Bristol N2.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiCAPZB_CAEEL
AccessioniPrimary (citable) accession number: P34686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 8, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.