BICD_DROME
ID BICD_DROME Reviewed; 782 AA.
AC P16568; Q9VJD5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein bicaudal D;
GN Name=BicD; ORFNames=CG6605;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2590944; DOI=10.1016/0092-8674(89)90611-9;
RA Wharton R.P., Struhl G.;
RT "Structure of the Drosophila BicaudalD protein and its role in localizing
RT the the posterior determinant nanos.";
RL Cell 59:881-892(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=2576013; DOI=10.1101/gad.3.12a.1957;
RA Suter B., Romberg L.M., Steward R.;
RT "Bicaudal-D, a Drosophila gene involved in developmental asymmetry:
RT localized transcript accumulation in ovaries and sequence similarity to
RT myosin heavy chain tail domains.";
RL Genes Dev. 3:1957-1968(1989).
RN [3]
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 [4]
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 [5]
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).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=11546740; DOI=10.1242/dev.128.17.3233;
RA Nakamura A., Amikura R., Hanyu K., Kobayashi S.;
RT "Me31B silences translation of oocyte-localizing RNAs through the formation
RT of cytoplasmic RNP complex during Drosophila oogenesis.";
RL Development 128:3233-3242(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH RAB6.
RX PubMed=17329360; DOI=10.1242/dev.02821;
RA Coutelis J.B., Ephrussi A.;
RT "Rab6 mediates membrane organization and determinant localization during
RT Drosophila oogenesis.";
RL Development 134:1419-1430(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH RAB6.
RX PubMed=17827179; DOI=10.1242/dev.008078;
RA Januschke J., Nicolas E., Compagnon J., Formstecher E., Goud B.,
RA Guichet A.;
RT "Rab6 and the secretory pathway affect oocyte polarity in Drosophila.";
RL Development 134:3419-3425(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-285; SER-288;
RP SER-305; THR-306; SER-310 AND SER-528, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31626769; DOI=10.1016/j.cell.2019.09.022;
RA Hampoelz B., Schwarz A., Ronchi P., Bragulat-Teixidor H., Tischer C.,
RA Gaspar I., Ephrussi A., Schwab Y., Beck M.;
RT "Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.";
RL Cell 179:671-686.E17(2019).
CC -!- FUNCTION: This protein is essential for differentiation. It may play a
CC role in localizing of Nanos (a maternal determinant) activity in
CC oocytes. During oogenesis, plays a specific role, together with Rab6
CC but independently of Sec5, in the polarization of the oocyte
CC microtubule cytoskeleton, in oskar mRNA localization and in the
CC anterodorsal secretion of grk. Plays a role in the biogenesis of
CC annulate lamellae containing nuclear pore complex components
CC (PubMed:31626769). {ECO:0000269|PubMed:17329360,
CC ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:2590944,
CC ECO:0000269|PubMed:31626769}.
CC -!- SUBUNIT: Interacts (via C-terminal domain) with Rab6.
CC {ECO:0000269|PubMed:17329360, ECO:0000269|PubMed:17827179}.
CC -!- INTERACTION:
CC P16568; P29742: Chc; NbExp=5; IntAct=EBI-112159, EBI-160368;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In ovaries, expressed in oocyte and nurse cells.
CC {ECO:0000269|PubMed:2576013}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically
CC (PubMed:2576013). Expressed during oogenesis and throughout development
CC (PubMed:2576013, PubMed:11546740). {ECO:0000269|PubMed:11546740,
CC ECO:0000269|PubMed:2576013}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos show Nanos mislocalization and
CC thus bicaudal development (PubMed:2590944). RNAi-mediated knockdown
CC results in sterility and egg chamber defects including loss of annulate
CC lamellae (PubMed:31626769). {ECO:0000269|PubMed:2590944,
CC ECO:0000269|PubMed:31626769}.
CC -!- SIMILARITY: Belongs to the BicD family. {ECO:0000305}.
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DR EMBL; M31684; AAA28393.1; -; mRNA.
DR EMBL; X51652; CAA35964.1; -; mRNA.
DR EMBL; AE014134; AAF53616.1; -; Genomic_DNA.
DR EMBL; AY069452; AAL39597.1; -; mRNA.
DR PIR; A34219; A34219.
DR RefSeq; NP_001260530.1; NM_001273601.1.
DR RefSeq; NP_724056.1; NM_165220.3.
DR PDB; 4BL6; X-ray; 2.18 A; A/B/C/D=656-745.
DR PDB; 6TZW; X-ray; 2.35 A; A/B=656-745.
DR PDBsum; 4BL6; -.
DR PDBsum; 6TZW; -.
DR AlphaFoldDB; P16568; -.
DR SMR; P16568; -.
DR BioGRID; 61047; 34.
DR DIP; DIP-21297N; -.
DR IntAct; P16568; 15.
DR MINT; P16568; -.
DR STRING; 7227.FBpp0303258; -.
DR iPTMnet; P16568; -.
DR PaxDb; P16568; -.
DR PRIDE; P16568; -.
DR ABCD; P16568; 12 sequenced antibodies.
DR DNASU; 35051; -.
DR EnsemblMetazoa; FBtr0081002; FBpp0080555; FBgn0000183.
DR EnsemblMetazoa; FBtr0330225; FBpp0303258; FBgn0000183.
DR GeneID; 35051; -.
DR KEGG; dme:Dmel_CG6605; -.
DR CTD; 35051; -.
DR FlyBase; FBgn0000183; BicD.
DR VEuPathDB; VectorBase:FBgn0000183; -.
DR eggNOG; KOG0999; Eukaryota.
DR GeneTree; ENSGT00940000154471; -.
DR InParanoid; P16568; -.
DR OMA; ANGECRR; -.
DR OrthoDB; 542877at2759; -.
DR PhylomeDB; P16568; -.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR SignaLink; P16568; -.
DR BioGRID-ORCS; 35051; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35051; -.
DR PRO; PR:P16568; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000183; Expressed in saliva-secreting gland and 59 other tissues.
DR ExpressionAtlas; P16568; baseline and differential.
DR Genevisible; P16568; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032050; F:clathrin heavy chain binding; IPI:FlyBase.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro.
DR GO; GO:0034452; F:dynactin binding; IBA:GO_Central.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0070727; P:cellular macromolecule localization; IMP:FlyBase.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0072393; P:microtubule anchoring at microtubule organizing center; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IDA:FlyBase.
DR GO; GO:0007309; P:oocyte axis specification; TAS:FlyBase.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:0007312; P:oocyte nucleus migration involved in oocyte dorsal/ventral axis specification; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:FlyBase.
DR GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; IMP:FlyBase.
DR GO; GO:0033365; P:protein localization to organelle; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:FlyBase.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0050658; P:RNA transport; IMP:FlyBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IGI:FlyBase.
DR InterPro; IPR018477; BICD.
DR PANTHER; PTHR31233; PTHR31233; 1.
DR Pfam; PF09730; BicD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..782
FT /note="Protein bicaudal D"
FT /id="PRO_0000205361"
FT REGION 699..722
FT /note="Interaction with Rab6"
FT REGION 744..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..263
FT /evidence="ECO:0000255"
FT COILED 319..477
FT /evidence="ECO:0000255"
FT COILED 601..746
FT /evidence="ECO:0000255"
FT COMPBIAS 757..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 296
FT /note="A -> S (in Ref. 1; AAA28393)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="L -> P (in Ref. 1; AAA28393)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="H -> R (in Ref. 1; AAA28393)"
FT /evidence="ECO:0000305"
FT HELIX 664..739
FT /evidence="ECO:0007829|PDB:4BL6"
SQ SEQUENCE 782 AA; 88954 MW; 5A71776171DF58E6 CRC64;
MSSASNNGPS ADQSVQDLQM EVERLTRELD QVSSASAQSA QYGLSLLEEK SALQQKCEEL
ETLYDNTRHE LDITQEALTK FQTSQKVTNK TGIEQEDALL NESAARETSL NLQIFDLENE
LKQLRHELER VRNERDRMLQ ENSDFGRDKS DSEADRLRLK SELKDLKFRE TRMLSEYSEL
EEENISLQKQ VSSLRSSQVE FEGAKHEIRR LTEEVELLNQ QVDELANLKK IAEKQMEEAL
ETLQGEREAK YALKKELDGH LNRESMYHIS NLAYSIRSNM EDNASNNSDG EEENLALKRL
EADLSTELKS PDGTKCDLFS EIHLNELKKL EKQLESMESE KTHLTANLRE AQTSLDKSQN
ELQNFMSRLA LLAAHVDALV QLKKQIDVKE QGKEGGQKKD ELEQQLRALI SQYANWFTLS
AKEIDGLKTD IAELQKGLNY TDATTTLRNE VTNLKNKLLA TEQKSLDLQS DVQTLTHISQ
NAGQSLGSAR STLVALSDDL AQLYHLVCTV NGETPTRVLL DHKTDDMSFE NDSLTAIQSQ
FKSDVFIAKP QIVEDLQGLA DSVEIKKYVD TVSDQIKYLK TAVEHTIDMN KHKIRSEGGD
ALEKVNTEEM EELQEQIVKL KSLLSVKREQ IGTLRNVLKS NKQTAEVALT NLKSKYENEK
IIVSDTMSKL RNELRLLKED AATFSSLRAM FAARCEEYVT QVDDLNRQLE AAEEEKKTLN
QLLRLAVQQK LALTQRLEEM EMDREMRHVR RPMPAQRGTS GKSSFSTRPS SRNPASSNAN
PF
