ABRU_DROME
ID ABRU_DROME Reviewed; 904 AA.
AC Q24174; E1JHF4; Q86NP4; Q9VKI1;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein abrupt;
DE AltName: Full=Protein clueless;
GN Name=ab; Synonyms=clu; ORFNames=CG43860;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-585.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=7498790; DOI=10.1101/gad.9.23.2936;
RA Hu S., Fambrough D., Atashi J.R., Goodman C.S., Crews S.T.;
RT "The Drosophila abrupt gene encodes a BTB-zinc finger regulatory protein
RT that controls the specificity of neuromuscular connections.";
RL Genes Dev. 9:2936-2948(1995).
RN [2] {ECO:0000305}
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, AND ALTERNATIVE SPLICING.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15363392; DOI=10.1016/j.neuron.2004.08.016;
RA Sugimura K., Satoh D., Estes P., Crews S., Uemura T.;
RT "Development of morphological diversity of dendrites in Drosophila by the
RT BTB-zinc finger protein abrupt.";
RL Neuron 43:809-822(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; SER-837; SER-846;
RP SER-868; SER-889 AND SER-896, 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: Expression is vital for development; may be involved in
CC transcriptional regulation. In embryos, muscle specific expression is
CC required for segmental nerve b (SNb) motoneuron target recognition
CC within ventral longitudinal muscles. Has a role in establishing and
CC maintaining embryonic muscle attachments, adult sensory cell formation
CC (macrochaetae) and morphogenesis of adult appendages (legs, antenna
CC aristae and male external genitalia). Has a role in the morphogenesis
CC of the class I dendritic neurons: selective expression of ab in class I
CC da neurons plays a pivotal role in forming dendritic arbors, which are
CC characteristic of the class I cells. The development of more complex
CC arbors of class II-IV neurons depends on the absence of ab.
CC {ECO:0000269|PubMed:15363392, ECO:0000269|PubMed:7498790}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=Long;
CC IsoId=Q24174-1; Sequence=Displayed;
CC Name=B; Synonyms=Short, D, F;
CC IsoId=Q24174-2; Sequence=VSP_006823;
CC Name=C;
CC IsoId=Q24174-3; Sequence=VSP_047504;
CC -!- TISSUE SPECIFICITY: Expressed in CNS midline cells during embryonic
CC stages 9-13. Expression also seen in cells of the stomagastric nervous
CC system. Segmentally repeated stripes of ectodermal expression appear at
CC stage 11 that become uniform by stage 12 and throughout embryogenesis.
CC Expressed at variable levels in somatic muscles from stage 16 and in
CC all imaginal disks during larval development. Expression is seen in da
CC neurons that grow in two-dimensional dendrites underneath the epidermis
CC during late embryonic, larval, and pupal stages.
CC {ECO:0000269|PubMed:15363392, ECO:0000269|PubMed:7498790}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit disrupts to motoneuron guidance and
CC connectivity. Loss of ab in class I neurons results in malformation of
CC their typical comb-like arbor patterns and generation of supernumerary
CC branch terminals. {ECO:0000269|PubMed:7498790}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U43733; AAA86639.1; -; mRNA.
DR EMBL; AE014134; AAF53087.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10774.1; -; Genomic_DNA.
DR EMBL; AE014134; ACZ94239.1; -; Genomic_DNA.
DR EMBL; AE014134; AGB92914.1; -; Genomic_DNA.
DR EMBL; BT001583; AAN71338.1; -; mRNA.
DR EMBL; BT003807; AAO41490.1; -; mRNA.
DR RefSeq; NP_001162952.1; NM_001169481.2. [Q24174-2]
DR RefSeq; NP_001260379.1; NM_001273450.1. [Q24174-2]
DR RefSeq; NP_476562.1; NM_057214.5. [Q24174-1]
DR RefSeq; NP_476563.1; NM_057215.5. [Q24174-2]
DR AlphaFoldDB; Q24174; -.
DR SMR; Q24174; -.
DR BioGRID; 60620; 17.
DR DIP; DIP-19247N; -.
DR IntAct; Q24174; 2.
DR STRING; 7227.FBpp0304816; -.
DR iPTMnet; Q24174; -.
DR PaxDb; Q24174; -.
DR PRIDE; Q24174; -.
DR DNASU; 34560; -.
DR EnsemblMetazoa; FBtr0332557; FBpp0304815; FBgn0264442. [Q24174-2]
DR EnsemblMetazoa; FBtr0332558; FBpp0304816; FBgn0264442. [Q24174-1]
DR EnsemblMetazoa; FBtr0332560; FBpp0304818; FBgn0264442. [Q24174-2]
DR EnsemblMetazoa; FBtr0332562; FBpp0304820; FBgn0264442. [Q24174-2]
DR GeneID; 34560; -.
DR KEGG; dme:Dmel_CG43860; -.
DR UCSC; CG4807-RA; d. melanogaster. [Q24174-1]
DR CTD; 34560; -.
DR FlyBase; FBgn0264442; ab.
DR VEuPathDB; VectorBase:FBgn0264442; -.
DR eggNOG; ENOG502RR0V; Eukaryota.
DR GeneTree; ENSGT00530000064321; -.
DR HOGENOM; CLU_007430_0_0_1; -.
DR InParanoid; Q24174; -.
DR OMA; MSQEHAA; -.
DR PhylomeDB; Q24174; -.
DR SignaLink; Q24174; -.
DR BioGRID-ORCS; 34560; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34560; -.
DR PRO; PR:Q24174; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0264442; Expressed in wing disc and 31 other tissues.
DR ExpressionAtlas; Q24174; baseline and differential.
DR Genevisible; Q24174; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016198; P:axon choice point recognition; TAS:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0016203; P:muscle attachment; IMP:UniProtKB.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0007423; P:sensory organ development; IMP:UniProtKB.
DR GO; GO:0008039; P:synaptic target recognition; IMP:UniProtKB.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..904
FT /note="Protein abrupt"
FT /id="PRO_0000046907"
FT DOMAIN 103..168
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037,
FT ECO:0000305"
FT ZN_FING 544..567
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 573..596
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..535
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_047504"
FT VAR_SEQ 356..365
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_006823"
FT MUTAGEN 585
FT /note="R->C: In allele AB-CLU2; lethal."
FT /evidence="ECO:0000269|PubMed:7498790"
FT CONFLICT 264
FT /note="H -> P (in Ref. 4; AAN71338)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="S -> T (in Ref. 1; AAA86639)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="N -> D (in Ref. 4; AAN71338)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 95093 MW; 9DF8F4EDDF8E5CF7 CRC64;
MTESTQLQTA ENNNAGVVKM EPPPPATSSV SVSAAAAAHA LSSLSSLTMA ATGSALSPAT
PPPSLNLSHQ QQQHQQHYAL KWNDFQSSIL SSFRHLRDEE DFVDVTLACD ERSFTAHKVV
LSACSPYFRR LLKANPCEHP IVILRDVRCD DVENLLSFMY NGEVNVSHEQ LPDFLKTAHL
LQIRGLADVN GGYPYSKALS AALSHNSSNN NNNNSSSNNS LSNNNNNNNN NAESSNHNKI
SSYLSPNQTS AACNNSSNSN SNNHSSSHNN SSSNNISGSL NSSLNSPFSA PQIPPPVTAS
SAAAAAAAAA SLTAAVAAAA AATAASAGSS SSAASGQTSG TPAIQELKAS SAASPVRNPN
PNPSKASSSN HWDMGEMEGS RKSHLTPPPQ KRIKSADLFR AQHGISPERL LLDREFPVAG
QHPLTRNRSG RDTSKDRERN LELRESLLGQ ALENSNGQQA NPKHELGQSA GEDSNSSDTE
PSDRGDGQHD GTLDGIDNQR SHSFPNAFLG LQGIPGLLPG PSGINSDFVS RRSLEMRVRA
TDPRPCPKCG KIYRSAHTLR THLEDKHTVC PGYRCVLCGT VAKSRNSLHS HMSRQHRGIS
TKDLPVLPMP SAFDPELASR LLAKAGVKIS PAELRARASP TGGSGSSGGG GGGGSSQAKL
DLSNASGGPM DDAEDSDDDP EDLTTGNGLY GMGGSSSDLS RYHESLLSNF GHARMRNEAA
AVAATAAALG QPKDLGVQLP NSNAPGQSLL DTYLQFITEN TFGMGMSQEQ AAAAALRAKM
AQLNAMGHSL DNLPPGLLPG QFDLSKLAAG NPAFGQSGPG LTIEPIMRHE QAAGNLSPNR
PLALNSGGRM MGHDEMAEND GDMRREGSEP MDLGLDNNQS GSNHEVANSD AEENYSEDEG
VHNT