CAPU_DROME
ID CAPU_DROME Reviewed; 1059 AA.
AC Q24120; Q9VQV8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein cappuccino;
GN Name=capu; ORFNames=CG3399;
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].
RC TISSUE=Ovary;
RX PubMed=7590229; DOI=10.1101/gad.9.20.2482;
RA Emmons S., Phan H., Calley J., Chen W., James B., Manseau L.;
RT "Cappuccino, a Drosophila maternal effect gene required for polarity of the
RT egg and embryo, is related to the vertebrate limb deformity locus.";
RL Genes Dev. 9:2482-2494(1995).
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 INTERACTION WITH WASH.
RX PubMed=19633175; DOI=10.1242/dev.035246;
RA Liu R., Abreu-Blanco M.T., Barry K.C., Linardopoulou E.V., Osborn G.E.,
RA Parkhurst S.M.;
RT "Wash functions downstream of Rho and links linear and branched actin
RT nucleation factors.";
RL Development 136:2849-2860(2009).
RN [5]
RP FUNCTION, INTERACTION WITH SPIR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-1049; ARG-1051 AND ARG-1055.
RX PubMed=21730168; DOI=10.1073/pnas.1105703108;
RA Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W.,
RA Quinlan M.E., Eck M.J.;
RT "Structure and function of the interacting domains of Spire and Fmn-family
RT formins.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011).
CC -!- FUNCTION: Acts as an actin nucleation factor and promotes assembly of
CC actin filaments together with spir. May play a role in intracellular
CC vesicle transport along actin fibers, providing a novel link between
CC actin cytoskeleton dynamics and intracellular transport.
CC {ECO:0000269|PubMed:21730168}.
CC -!- SUBUNIT: Interacts with wash. Interacts with spir.
CC {ECO:0000269|PubMed:19633175, ECO:0000269|PubMed:21730168}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytosol {ECO:0000250}. Membrane {ECO:0000269|PubMed:21730168};
CC Peripheral membrane protein {ECO:0000269|PubMed:21730168}; Cytoplasmic
CC side {ECO:0000269|PubMed:21730168}. Cytoplasmic vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Recruited to membranes via its interaction
CC with spir.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000305}.
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DR EMBL; U34258; AAC46925.1; -; mRNA.
DR EMBL; AE014134; AAF51054.1; -; Genomic_DNA.
DR PIR; T13286; T13286.
DR RefSeq; NP_476966.1; NM_057618.3.
DR AlphaFoldDB; Q24120; -.
DR SMR; Q24120; -.
DR BioGRID; 59814; 11.
DR IntAct; Q24120; 3.
DR STRING; 7227.FBpp0288517; -.
DR PaxDb; Q24120; -.
DR DNASU; 33611; -.
DR EnsemblMetazoa; FBtr0077513; FBpp0077202; FBgn0000256.
DR GeneID; 33611; -.
DR KEGG; dme:Dmel_CG3399; -.
DR UCSC; CG3399-RA; d. melanogaster.
DR CTD; 33611; -.
DR FlyBase; FBgn0000256; capu.
DR VEuPathDB; VectorBase:FBgn0000256; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_006372_0_0_1; -.
DR InParanoid; Q24120; -.
DR OrthoDB; 263102at2759; -.
DR BioGRID-ORCS; 33611; 0 hits in 3 CRISPR screens.
DR ChiTaRS; capu; fly.
DR GenomeRNAi; 33611; -.
DR PRO; PR:Q24120; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000256; Expressed in testis and 32 other tissues.
DR ExpressionAtlas; Q24120; baseline and differential.
DR Genevisible; Q24120; DM.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0030029; P:actin filament-based process; IDA:FlyBase.
DR GO; GO:0045010; P:actin nucleation; IDA:FlyBase.
DR GO; GO:0007304; P:chorion-containing eggshell formation; HMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007315; P:pole plasm assembly; IMP:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; TAS:FlyBase.
DR GO; GO:0007316; P:pole plasm RNA localization; IMP:FlyBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR001265; Formin_Cappuccino_subfam.
DR Pfam; PF02181; FH2; 1.
DR PRINTS; PR00828; FORMIN.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Developmental protein; Membrane; Protein transport; Reference proteome;
KW Stress response; Transport.
FT CHAIN 1..1059
FT /note="Protein cappuccino"
FT /id="PRO_0000194884"
FT DOMAIN 480..560
FT /note="FH1"
FT DOMAIN 585..1032
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 62..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1059
FT /note="Important for interaction with spir"
FT COMPBIAS 62..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1049
FT /note="K->A,D: Abolishes interaction with spir."
FT /evidence="ECO:0000269|PubMed:21730168"
FT MUTAGEN 1051
FT /note="R->A,D: Abolishes interaction with spir."
FT /evidence="ECO:0000269|PubMed:21730168"
FT MUTAGEN 1055
FT /note="R->A,D: Abolishes interaction with spir."
FT /evidence="ECO:0000269|PubMed:21730168"
FT CONFLICT 260
FT /note="S -> C (in Ref. 1; AAC46925)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="S -> T (in Ref. 1; AAC46925)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="T -> S (in Ref. 1; AAC46925)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="E -> K (in Ref. 1; AAC46925)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="H -> P (in Ref. 1; AAC46925)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="Missing (in Ref. 1; AAC46925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1059 AA; 113864 MW; 009B0E24F61B6EA5 CRC64;
MALQLGKKLA QVLGSGAGSP LTPGTMEPCA AGSGSPLANG ELFNVSKAKK VELQNLSSRF
TAAVTQTPPG VTSSTPNESG VTGPAGPLGA TTSSPSLETQ STVIISFKSS QTPVQSQTNS
AASENVEDDT APLPLPPPPP GFGTPTTPLL SSNVLKKVAS FTVEKSSAGN NSSNPPNLCP
TSDETTLLAT PCSSSLTVAT LPPEIAVGAA AGGVAGGAGS RRGSSYVPEK LSFAAYEKFE
GQMLIKWLIS TMQSNPKSSS GDANQELFNT LALQFCNNLK YVGVLKQISN EHLDCGFSPY
EMYQWTHTEQ PTTSLPLTPG KLDKVAAWPF SSTPSGIRAL ESASLASLGA GGVAGSLATI
ATASTASSDN QKTLQQILKK RLLNCTTLAE VHAVVNELLS SVDEPPRRPS KRCVNLTELL
NASEATVYEY NKTGAEGCVK SFTDAETQTE SEDCEGTCKC GQSSTKVSDN ESAKEDGEKP
HAVAPPPPPP PPPLHAFVAP PPPPPPPPPP PPPLANYGAP PPPPPPPPGS GSAPPPPPPA
PIEGGGGIPP PPPPMSASPS KTTISPAPLP DPAEGNWFHR TNTMRKSAVN PPKPMRPLYW
TRIVTSAPPA PRPPSVANST DSTENSGSSP DEPPAANGAD APPTAPPATK EIWTEIEETP
LDNIDEFTEL FSRQAIAPVS KPKELKVKRA KSIKVLDPER SRNVGIIWRS LHVPSSEIEH
AIYHIDTSVV SLEALQHMSN IQATEDELQR IKEAAGGDIP LDHPEQFLLD ISLISMASER
ISCIVFQAEF EESVTLLFRK LETVSQLSQQ LIESEDLKLV FSIILTLGNY MNGGNRQRGQ
ADGFNLDILG KLKDVKSKES HTTLLHFIVR TYIAQRRKEG VHPLEIRLPI PEPADVERAA
QMDFEEVQQQ IFDLNKKFLG CKRTTAKVLA ASRPEIMEPF KSKMEEFVEG ADKSMAKLHQ
SLDECRDLFL ETMRFYHFSP KACTLTLAQC TPDQFFEYWT NFTNDFKDIW KKEITSLLNE
LMKKSKQAQI ESRRNVSTKV EKSGRISLKE RMLMRRSKN
