BICC_DROME
ID BICC_DROME Reviewed; 905 AA.
AC Q24009; Q8IP26;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein bicaudal C;
GN Name=BicC; ORFNames=CG4824;
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 TISSUE SPECIFICITY.
RX PubMed=7538070; DOI=10.1002/j.1460-2075.1995.tb07196.x;
RA Mahone M., Saffman E.E., Lasko P.F.;
RT "Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA
RT binding motif of FMR1.";
RL EMBO J. 14:2043-2055(1995).
RN [2]
RP ERRATUM OF PUBMED:7538070, AND SEQUENCE REVISION.
RA Mahone M., Saffman E.E., Lasko P.F.;
RL EMBO J. 16:4152-4152(1997).
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 FUNCTION, RNA-BINDING, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-296.
RX PubMed=9671494; DOI=10.1128/mcb.18.8.4855;
RA Saffman E.E., Styhler S., Rother K., Li W., Richard S., Lasko P.;
RT "Premature translation of oskar in oocytes lacking the RNA-binding protein
RT bicaudal-C.";
RL Mol. Cell. Biol. 18:4855-4862(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557; SER-586; SER-639;
RP SER-642; THR-643; TYR-644; SER-646; SER-666; SER-692; SER-695 AND TYR-696,
RP AND IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: RNA-binding protein that is involved in oogenesis. Required
CC for correct targeting of the migrating anterior follicle cells and the
CC establishment of anterior-posterior polarity in the oocyte. May act as
CC translational repressor of oskar during oogenesis. Function seems to be
CC sensitive to small changes in expression. {ECO:0000269|PubMed:7538070,
CC ECO:0000269|PubMed:9671494}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in ovaries and early embryos.
CC {ECO:0000269|PubMed:7538070}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the devoloping ovary. First
CC detectable at stages 3 and 4 of oogenesis but remains very faint until
CC stage 5, when the protein level increases substantially. In stages 4 to
CC 6 is visible throughout the oocyte cytoplasm but is enriched at the
CC osterior pole of the oocyte. During stages 7 to 9 is abundant in the
CC oocyte cytoplasm, with some enrichment at the anterior of the oocyte
CC and around the oocyte cortex. In stage 10 and in later stages is
CC expressed at high levels in the nurse cells (at protein level).
CC {ECO:0000269|PubMed:9671494}.
CC -!- SIMILARITY: Belongs to the BicC family. {ECO:0000305}.
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DR EMBL; U15928; AAB51692.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10927.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10928.1; -; Genomic_DNA.
DR EMBL; BT023837; AAZ86758.1; -; mRNA.
DR PIR; S55051; S55051.
DR RefSeq; NP_476865.1; NM_057517.3.
DR RefSeq; NP_723948.1; NM_165144.2.
DR RefSeq; NP_723949.1; NM_165145.1.
DR AlphaFoldDB; Q24009; -.
DR SMR; Q24009; -.
DR BioGRID; 60958; 25.
DR IntAct; Q24009; 5.
DR MINT; Q24009; -.
DR STRING; 7227.FBpp0080361; -.
DR iPTMnet; Q24009; -.
DR PaxDb; Q24009; -.
DR EnsemblMetazoa; FBtr0080803; FBpp0080361; FBgn0000182.
DR EnsemblMetazoa; FBtr0080804; FBpp0080362; FBgn0000182.
DR GeneID; 34946; -.
DR KEGG; dme:Dmel_CG4824; -.
DR CTD; 34946; -.
DR FlyBase; FBgn0000182; BicC.
DR VEuPathDB; VectorBase:FBgn0000182; -.
DR eggNOG; KOG2208; Eukaryota.
DR eggNOG; KOG4374; Eukaryota.
DR GeneTree; ENSGT00940000169857; -.
DR HOGENOM; CLU_008040_0_0_1; -.
DR InParanoid; Q24009; -.
DR PhylomeDB; Q24009; -.
DR SignaLink; Q24009; -.
DR BioGRID-ORCS; 34946; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34946; -.
DR PRO; PR:Q24009; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000182; Expressed in ovary and 11 other tissues.
DR ExpressionAtlas; Q24009; baseline.
DR Genevisible; Q24009; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; TAS:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0007319; P:negative regulation of oskar mRNA translation; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; HMP:FlyBase.
DR GO; GO:0007297; P:ovarian follicle cell migration; HMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR CDD; cd09520; SAM_BICC1; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR037974; BICC1_SAM_dom.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF00013; KH_1; 2.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00322; KH; 2.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF54791; SSF54791; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Oogenesis; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..905
FT /note="Protein bicaudal C"
FT /id="PRO_0000267718"
FT DOMAIN 172..239
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 324..392
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 805..868
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 559..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 643
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 644
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 696
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 296
FT /note="G->R: In allele RU-35; bicaudal phenotype; lowers
FT RNA-binding."
FT /evidence="ECO:0000269|PubMed:9671494"
SQ SEQUENCE 905 AA; 97849 MW; 22FC1CD4BB231603 CRC64;
MLSCASFNKL MYPSAADVAK PPMVGLEVEA GSIGSLSSLH ALPSTTSVGS GAPSETQSEI
SSVDSDWSDI RAIAMKLGVQ NPDDLHTERF KVDRQKLEQL IKAESSIEGM NGAEYFFHDI
MNTTDTYVSW PCRLKIGAKS KKDPHVRIVG KVDQVQRAKE RILSSLDSRG TRVIMKMDVS
YTDHSYIIGR GGNNIKRIMD DTHTHIHFPD SNRSNPTEKS NQVSLCGSLE GVERARALVR
LSTPLLISFE MPVMGPNKPQ PDHETPYIKM IETKFNVQVI FSTRPKLHTS LVLVKGSEKE
SAQVRDATQL LINFACESIA SQILVNVQME ISPQHHEIVK GKNNVNLLSI MERTQTKIIF
PDLSDMNVKP LKKSQVTISG RIDDVYLARQ QLLGNLPVAL IFDFPDNHND ASEIMSLNTK
YGVYITLRQK QRQSTLAIVV KGVEKFIDKI YEARQEILRL ATPFVKPEIP DYYFMPKDKD
LNLAYRTQLT ALLAGYVDSP KTPSLLPPSL AGQLTPYANN NHLLLNANGL ATPTGVCAPT
QKYMQLHNSF QQAQNRSMVA GGQSNNGNYL QVPGAVAPPL KPPTVSPRNS CSQNTSGYQS
FSSSTTSLEQ SYPPYAQLPG TVSSTSSSTA GSQNRAHYSP DSTYGSEGGG VGGGGGGGAR
LGRRLSDGVL LGLSNSNGGG GNSGGAHLLP GSAESYRSLH YDLGGNKHSG HRAFDFDMKR
ALGYKAMERT PVAGELRTPT TAWMGMGLSS TSPAPAPLEN GENGAAGGGA SSGWRLPPGL
GSPYGLSATT GLLDATPVNR RMQLAKHKDI QTLLTSLGLE HYIKIFVLNE IDLEVFTTLT
EENLMELGIA AFGARKKLLT AIHTLLANEA ACSTMPSSSS SQNSSSPRFS GSAAPGAERR
PSNQW
