ID   BNK_DROME               Reviewed;         303 AA.
AC   P40794; Q9VA03;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   02-SEP-2026, entry version 139.
DE   RecName: Full=Protein bottleneck;
GN   Name=bnk; ORFNames=CG1480;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8402919; DOI=10.1016/0092-8674(93)80078-s;
RA   Schejter E.D., Wieschaus E.;
RT   "Bottleneck acts as a regulator of the microfilament network governing
RT   cellularization of the Drosophila embryo.";
RL   Cell 75:373-385(1993).
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).
CC   -!- FUNCTION: Acts as a regulator of the microfilament network governing
CC       cellularization of the embryo. Determines the timing of a key
CC       conformational transition in the cortical microfilament network: the
CC       proper coordination of membrane invagination and basal closure of the
CC       cells. To do this, bnk possibly physically links neighboring
CC       contractile units of the early cycle 14 microfilament network in a
CC       manner that prevents basal constriction until the proper stage has been
CC       reached. Bnk together with nullo and Sry-alpha may provide auxiliary
CC       functions, by acting both to stabilize a large and dynamic
CC       microfilament structure and regulate its functions.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes with
CC       the structural transitions in the microfilament network during
CC       cellularization. Association is observed only when the network assumes
CC       an aligned and tightly apposed hexagonal configuration.
CC   -!- TISSUE SPECIFICITY: Restricted to the blastoderm.
CC   -!- DEVELOPMENTAL STAGE: Observed exclusively in the late syncytial and
CC       cellular blastoderm stages of development. Transcripts are first
CC       detected during nuclear division cycle 11. They reach a strong peak at
CC       cycle 14 and from then on gradually decline until they are no longer
CC       detectable at the end of cellularization.
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DR   EMBL; U01035; AAC46467.1; -; mRNA.
DR   EMBL; AE014297; AAF57125.1; -; Genomic_DNA.
DR   PIR; A49072; A49072.
DR   RefSeq; NP_524604.2; NM_079865.4.
DR   AlphaFoldDB; P40794; -.
DR   SMR; P40794; -.
DR   BioGRID; 68532; 1.
DR   IntAct; P40794; 2.
DR   MINT; P40794; -.
DR   STRING; 7227.FBpp0085116; -.
DR   PaxDb; 7227-FBpp0085116; -.
DR   PeptideAtlas; P40794; -.
DR   DNASU; 43687; -.
DR   EnsemblMetazoa; FBtr0085754; FBpp0085116; FBgn0004389.
DR   GeneID; 43687; -.
DR   KEGG; dme:Dmel_CG1480; -.
DR   UCSC; CG1480-RA; d. melanogaster.
DR   AGR; FB:FBgn0004389; -.
DR   CTD; 43687; -.
DR   FlyBase; FBgn0004389; bnk.
DR   VEuPathDB; VectorBase:FBgn0004389; -.
DR   eggNOG; ENOG502T7TU; Eukaryota.
DR   HOGENOM; CLU_906945_0_0_1; -.
DR   InParanoid; P40794; -.
DR   OMA; QRHAMME; -.
DR   OrthoDB; 8014239at2759; -.
DR   PhylomeDB; P40794; -.
DR   BioGRID-ORCS; 43687; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 43687; -.
DR   PRO; PR:P40794; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0004389; Expressed in copper cell (Drosophila) in digestive tract and 7 other cell types or tissues.
DR   ExpressionAtlas; P40794; baseline.
DR   GO; GO:0005884; C:actin filament; IDA:FlyBase.
DR   GO; GO:0051015; F:actin filament binding; IDA:FlyBase.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:FlyBase.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:FlyBase.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:FlyBase.
DR   GO; GO:0061572; P:actin filament bundle organization; IDA:FlyBase.
DR   GO; GO:0007015; P:actin filament organization; TAS:FlyBase.
DR   GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
DR   GO; GO:0110069; P:syncytial embryo cellularization; IMP:FlyBase.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Developmental protein; Reference proteome.
FT   CHAIN           1..303
FT                   /note="Protein bottleneck"
FT                   /id="PRO_0000064966"
FT   REGION          102..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..138
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..197
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        115
FT                   /note="R -> Q (in Ref. 1; AAC46467)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   303 AA;  33566 MW;  46E337ADC566C23B CRC64;
     MSISTFNFQF YNYKLSPSSP GFGSTASRSS SSCISELEMD IDEDMSAQPT ITSTPKPRFT
     SQLAVELAKT EPGNGISPLR PKLHTAQKRW SMELREKVLE MSKRNNGQEK PQTARQQEQR
     QPQEQPLQQE ELQHQQQEPT VTDKINFFNK LTNTFESGFS KLMPQASSTN NRFIAMLRTA
     RPQNVATTTA NSSTANSFLG SDHSLSGSVT GQVPPPKPKR LSATTAQFAT PHVPAMGVGK
     GGSQRKCSLR RKPSMDKSRA TISRQSSSAS VRTQNHAIME DLSLVVPVRL RIAEYEQRIS
     MSA
//