BNK_DROME
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 03-AUG-2022, entry version 126.
DE RecName: Full=Protein bottleneck;
GN Name=bnk; ORFNames=CG1480;
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.
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; P40794; -.
DR DNASU; 43687; -.
DR EnsemblMetazoa; FBtr0085754; FBpp0085116; FBgn0004389.
DR GeneID; 43687; -.
DR KEGG; dme:Dmel_CG1480; -.
DR UCSC; CG1480-RA; d. melanogaster.
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; HAMMEDL; -.
DR OrthoDB; 1337249at2759; -.
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 seminal fluid secreting gland and 1 other tissue.
DR ExpressionAtlas; P40794; baseline.
DR Genevisible; P40794; DM.
DR GO; GO:0005884; C:actin filament; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 105..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..211
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
