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Protein

F-actin-capping protein subunit beta

Gene

cpb

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

GO - Molecular functioni

  • actin binding Source: FlyBase
  • protein heterodimerization activity Source: FlyBase

GO - Biological processi

  • actin cytoskeleton organization Source: FlyBase
  • actin filament organization Source: FlyBase
  • barbed-end actin filament capping Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • cell morphogenesis Source: FlyBase
  • cytoplasmic transport, nurse cell to oocyte Source: FlyBase
  • microtubule-based movement Source: FlyBase
  • negative regulation of filopodium assembly Source: FlyBase
  • negative regulation of JNK cascade Source: FlyBase
  • positive regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • regulation of actin filament length Source: FlyBase
  • regulation of lamellipodium assembly Source: FlyBase
  • wing disc development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit beta
Gene namesi
Name:cpb
Synonyms:ANCP-BETA
ORF Names:CG17158
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0011570. cpb.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • dynactin complex Source: FlyBase
  • F-actin capping protein complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 276276F-actin-capping protein subunit betaPRO_0000204639Add
BLAST

Proteomic databases

PaxDbiP48603.
PRIDEiP48603.

Expressioni

Gene expression databases

BgeeiP48603.
ExpressionAtlasiP48603. differential.
GenevisibleiP48603. DM.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.

GO - Molecular functioni

  • actin binding Source: FlyBase
  • protein heterodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi59586. 45 interactions.
DIPiDIP-17681N.
IntActiP48603. 23 interactions.
MINTiMINT-341312.
STRINGi7227.FBpp0077549.

Structurei

3D structure databases

ProteinModelPortaliP48603.
SMRiP48603. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3174. Eukaryota.
ENOG410XQYD. LUCA.
GeneTreeiENSGT00390000017957.
InParanoidiP48603.
KOiK10365.
OMAiFDTYREM.
OrthoDBiEOG7NPFTR.
PhylomeDBiP48603.

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.

P48603-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEMQMDCAL DLMRRLPPQQ IEKNLIDLID LAPDLCEDLL SSVDQPLKIA
60 70 80 90 100
KDKEHGKDYL LCDYNRDGDS YRSPWSNSYY PPLEDGQMPS ERLRKLEIEA
110 120 130 140 150
NYAFDQYREM YYEGGVSSVY LWDLDHGFAA VILIKKAGDG SKMIRGCWDS
160 170 180 190 200
IHVVEVQEKT TGRTAHYKLT STAMLWLQTN KQGSGTMNLG GSLTRQQEQD
210 220 230 240 250
ANVSESSPHI ANIGKMVEEM ENKIRNTLNE IYFGKTKDIV NGLRSTQSLA
260 270
DQRQQAAMKQ DLAAAILRRN VKPESN
Length:276
Mass (Da):31,363
Last modified:February 1, 1996 - v1
Checksum:i512952A1A49629D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35240 mRNA. Translation: AAB38521.1.
AE014134 Genomic DNA. Translation: AAF51349.1.
AY069829 mRNA. Translation: AAL39974.1.
RefSeqiNP_001259877.1. NM_001272948.1.
NP_477005.1. NM_057657.5.
UniGeneiDm.4772.

Genome annotation databases

EnsemblMetazoaiFBtr0077881; FBpp0077549; FBgn0011570.
FBtr0331630; FBpp0304020; FBgn0011570.
GeneIDi33346.
KEGGidme:Dmel_CG17158.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35240 mRNA. Translation: AAB38521.1.
AE014134 Genomic DNA. Translation: AAF51349.1.
AY069829 mRNA. Translation: AAL39974.1.
RefSeqiNP_001259877.1. NM_001272948.1.
NP_477005.1. NM_057657.5.
UniGeneiDm.4772.

3D structure databases

ProteinModelPortaliP48603.
SMRiP48603. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59586. 45 interactions.
DIPiDIP-17681N.
IntActiP48603. 23 interactions.
MINTiMINT-341312.
STRINGi7227.FBpp0077549.

Proteomic databases

PaxDbiP48603.
PRIDEiP48603.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077881; FBpp0077549; FBgn0011570.
FBtr0331630; FBpp0304020; FBgn0011570.
GeneIDi33346.
KEGGidme:Dmel_CG17158.

Organism-specific databases

CTDi33346.
FlyBaseiFBgn0011570. cpb.

Phylogenomic databases

eggNOGiKOG3174. Eukaryota.
ENOG410XQYD. LUCA.
GeneTreeiENSGT00390000017957.
InParanoidiP48603.
KOiK10365.
OMAiFDTYREM.
OrthoDBiEOG7NPFTR.
PhylomeDBiP48603.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii33346.
NextBioi783124.
PROiP48603.

Gene expression databases

BgeeiP48603.
ExpressionAtlasiP48603. differential.
GenevisibleiP48603. DM.

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. "Actin organization, bristle morphology, and viability are affected by actin capping protein mutations in Drosophila."
    Hopmann R., Cooper J.A., Miller K.G.
    J. Cell Biol. 133:1293-1305(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiCAPZB_DROME
AccessioniPrimary (citable) accession number: P48603
Secondary accession number(s): Q9VQ33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.