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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}.
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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
 
 
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