CAPZB_DROME
ID CAPZB_DROME Reviewed; 276 AA.
AC P48603; Q9VQ33;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=F-actin-capping protein subunit beta;
GN Name=cpb; Synonyms=ANCP-BETA; ORFNames=CG17158;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8682865; DOI=10.1083/jcb.133.6.1293;
RA Hopmann R., Cooper J.A., Miller K.G.;
RT "Actin organization, bristle morphology, and viability are affected by
RT actin capping protein mutations in Drosophila.";
RL J. Cell Biol. 133:1293-1305(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner
CC to the fast growing ends of actin filaments (barbed end) thereby
CC blocking the exchange of subunits at these ends. Unlike other capping
CC proteins (such as gelsolin and severin), these proteins do not sever
CC actin filaments. {ECO:0000269|PubMed:8682865}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U35240; AAB38521.1; -; mRNA.
DR EMBL; AE014134; AAF51349.1; -; Genomic_DNA.
DR EMBL; AY069829; AAL39974.1; -; mRNA.
DR RefSeq; NP_001259877.1; NM_001272948.1.
DR RefSeq; NP_477005.1; NM_057657.5.
DR AlphaFoldDB; P48603; -.
DR SMR; P48603; -.
DR BioGRID; 59586; 56.
DR DIP; DIP-17681N; -.
DR IntAct; P48603; 23.
DR STRING; 7227.FBpp0077549; -.
DR PaxDb; P48603; -.
DR PRIDE; P48603; -.
DR DNASU; 33346; -.
DR EnsemblMetazoa; FBtr0077881; FBpp0077549; FBgn0011570.
DR EnsemblMetazoa; FBtr0331630; FBpp0304020; FBgn0011570.
DR GeneID; 33346; -.
DR KEGG; dme:Dmel_CG17158; -.
DR CTD; 33346; -.
DR FlyBase; FBgn0011570; cpb.
DR VEuPathDB; VectorBase:FBgn0011570; -.
DR eggNOG; KOG3174; Eukaryota.
DR GeneTree; ENSGT00390000017957; -.
DR HOGENOM; CLU_045864_1_1_1; -.
DR InParanoid; P48603; -.
DR OMA; MIEDMEI; -.
DR OrthoDB; 1076134at2759; -.
DR PhylomeDB; P48603; -.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9035034; RHOF GTPase cycle.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P48603; -.
DR BioGRID-ORCS; 33346; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33346; -.
DR PRO; PR:P48603; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011570; Expressed in saliva-secreting gland and 30 other tissues.
DR ExpressionAtlas; P48603; baseline and differential.
DR Genevisible; P48603; DM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005869; C:dynactin complex; ISS:FlyBase.
DR GO; GO:0008290; C:F-actin capping protein complex; IDA:FlyBase.
DR GO; GO:0071203; C:WASH complex; ISS:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IC:FlyBase.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IGI:FlyBase.
DR GO; GO:0140591; P:nuclear envelope budding; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0030832; P:regulation of actin filament length; IMP:FlyBase.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR Gene3D; 1.20.58.570; -; 1.
DR Gene3D; 3.90.1150.210; -; 1.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR001698; CAPZB.
DR InterPro; IPR043175; CAPZB_N.
DR InterPro; IPR019771; F-actin_capping_bsu_CS.
DR PANTHER; PTHR10619; PTHR10619; 1.
DR Pfam; PF01115; F_actin_cap_B; 1.
DR PRINTS; PR00192; FACTINCAPB.
DR SUPFAM; SSF90096; SSF90096; 1.
DR PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE 2: Evidence at transcript level;
KW Actin capping; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..276
FT /note="F-actin-capping protein subunit beta"
FT /id="PRO_0000204639"
SQ SEQUENCE 276 AA; 31363 MW; 512952A1A49629D3 CRC64;
MSEMQMDCAL DLMRRLPPQQ IEKNLIDLID LAPDLCEDLL SSVDQPLKIA KDKEHGKDYL
LCDYNRDGDS YRSPWSNSYY PPLEDGQMPS ERLRKLEIEA NYAFDQYREM YYEGGVSSVY
LWDLDHGFAA VILIKKAGDG SKMIRGCWDS IHVVEVQEKT TGRTAHYKLT STAMLWLQTN
KQGSGTMNLG GSLTRQQEQD ANVSESSPHI ANIGKMVEEM ENKIRNTLNE IYFGKTKDIV
NGLRSTQSLA DQRQQAAMKQ DLAAAILRRN VKPESN
