PHYL_DROME
ID PHYL_DROME Reviewed; 400 AA.
AC Q27934; C0PV22; Q9V721;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein phyllopod;
GN Name=phyl; ORFNames=CG10108;
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, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=7859287; DOI=10.1016/0092-8674(95)90496-4;
RA Dickson B.J., Dominguez M., Der Straten A., Hafen E.;
RT "Control of Drosophila photoreceptor cell fates by phyllopod, a novel
RT nuclear protein acting downstream of the Raf kinase.";
RL Cell 80:453-462(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Eye imaginal disk;
RX PubMed=7888014; DOI=10.1016/0092-8674(95)90497-2;
RA Chang H.C., Solomon N.M., Wassarman D.A., Karim F.D., Therrien M.,
RA Rubin G.M., Wolff T.;
RT "Phyllopod functions in the fate determination of a subset of
RT photoreceptors in Drosophila.";
RL Cell 80:463-472(1995).
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=Head;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION IN TTK DEGRADATION, AND INTERACTION WITH SINA.
RX PubMed=9267026; DOI=10.1016/s0092-8674(00)80506-1;
RA Tang A.H., Neufeld T.P., Kwan E., Rubin G.M.;
RT "PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal
RT cell fates, by a SINA-dependent mechanism.";
RL Cell 90:459-467(1997).
RN [8]
RP FUNCTION IN TTK DEGRADATION, AND INTERACTION WITH SINA.
RX PubMed=9267027; DOI=10.1016/s0092-8674(00)80507-3;
RA Li S., Li Y., Carthew R.W., Lai Z.-C.;
RT "Photoreceptor cell differentiation requires regulated proteolysis of the
RT transcriptional repressor Tramtrack.";
RL Cell 90:469-478(1997).
RN [9]
RP COMPONENT OF A COMPLEX WITH EBI AND SINA.
RX PubMed=11032805; DOI=10.1093/emboj/19.20.5376;
RA Boulton S.J., Brook A., Staehling-Hampton K., Heitzler P., Dyson N.;
RT "A role for Ebi in neuronal cell cycle control.";
RL EMBO J. 19:5376-5386(2000).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=11526076; DOI=10.1242/dev.128.14.2699;
RA Pi H., Wu H.-J., Chien C.-T.;
RT "A dual function of phyllopod in Drosophila external sensory organ
RT development: cell fate specification of sensory organ precursor and its
RT progeny.";
RL Development 128:2699-2710(2001).
RN [11]
RP FUNCTION IN THE COMPLEX, AND MUTAGENESIS OF 109-GLN-GLU-110;
RP 111-ARG-THR-112; 113-LYS-LEU-114; 115-ARG-PRO-116; 119-MET-VAL-120 AND
RP 121-ARG-PRO-122.
RX PubMed=12215542; DOI=10.1128/mcb.22.19.6854-6865.2002;
RA Li S., Xu C., Carthew R.W.;
RT "Phyllopod acts as an adaptor protein to link the sina ubiquitin ligase to
RT the substrate protein tramtrack.";
RL Mol. Cell. Biol. 22:6854-6865(2002).
RN [12]
RP FUNCTION.
RX PubMed=14602676; DOI=10.1242/dev.00843;
RA Artero R., Furlong E.E., Beckett K., Scott M.P., Baylies M.;
RT "Notch and Ras signaling pathway effector genes expressed in fusion
RT competent and founder cells during Drosophila myogenesis.";
RL Development 130:6257-6272(2003).
CC -!- FUNCTION: Essential adapter component of E3 ubiquitin ligase complexes;
CC involved in R7 photoreceptor cell differentiation, embryonic nervous
CC system, external sensory organ development and specification of
CC particular muscles. E3 ubiquitin ligase complexes mediate
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Required for specification of R7 photoreceptor cell fate in
CC the eye by participating in the ubiquitination and subsequent
CC proteasomal degradation of Tramtrack (ttk), a general inhibitor of
CC photoreceptor differentiation. Acts downstream of Notch signaling to
CC specify the fate of the SOP (sensory organ precursor) cells and their
CC progeny, probably via the sina-mediated proteasomal degradation of ttk.
CC Its restricted pattern of expression, upon Notch and Ras signaling
CC pathways, suggests that it acts as a key determinant in E3 complexes to
CC trigger protein proteolysis in appropriate cells.
CC {ECO:0000269|PubMed:11526076, ECO:0000269|PubMed:12215542,
CC ECO:0000269|PubMed:14602676, ECO:0000269|PubMed:7859287,
CC ECO:0000269|PubMed:7888014, ECO:0000269|PubMed:9267026,
CC ECO:0000269|PubMed:9267027}.
CC -!- SUBUNIT: Component of some E3 complex at least composed of sina, ebi
CC and phyl, required for the degradation of ttk.
CC -!- INTERACTION:
CC Q27934; Q95RJ9: ebi; NbExp=4; IntAct=EBI-77033, EBI-421390;
CC Q27934; P21461: sina; NbExp=11; IntAct=EBI-77033, EBI-77019;
CC Q27934; P42282: ttk; NbExp=10; IntAct=EBI-77033, EBI-77008;
CC Q27934; P61092: Siah1a; Xeno; NbExp=2; IntAct=EBI-77033, EBI-446761;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7859287,
CC ECO:0000269|PubMed:7888014}.
CC -!- TISSUE SPECIFICITY: In embryos, it is ubiquitously present before
CC cellularization. During stages 9-11, it is expressed in neuroblasts and
CC the SOP cells. From stage 12 onward, it decreases, but remains in a
CC subset of PNS cells at stages 12-14. Weakly expressed in wing imaginal
CC disks, in the SOP cells of wing margin bristles, notal macrochaetes,
CC and other sensory organs. In leg disks, it is expressed in the
CC precursors of the femoral chordotonal organs, as well as in external
CC sensory SOP cells. Strongly expressed in the eye-antenna disk, it is
CC specifically expressed in R1, R6 and R7 cells, and not in R3, R3, R4,
CC R5 and R8 cells. {ECO:0000269|PubMed:11526076,
CC ECO:0000269|PubMed:7859287, ECO:0000269|PubMed:7888014}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11526076}.
CC -!- INDUCTION: Activated by the Ras1/MAPK pathway in R1, R6 and R7 cells in
CC the eye. Down-regulated by the Notch pathway.
CC {ECO:0000269|PubMed:11526076}.
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DR EMBL; L38294; AAA66168.1; -; mRNA.
DR EMBL; U19722; AAA65733.1; -; mRNA.
DR EMBL; U19731; AAB60231.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58245.1; -; Genomic_DNA.
DR EMBL; AY075531; AAL68338.1; -; mRNA.
DR EMBL; BT072878; ACN67102.1; -; mRNA.
DR PIR; A55647; A55647.
DR RefSeq; NP_725394.1; NM_166055.2.
DR PDB; 4I7B; X-ray; 3.00 A; B/D=113-125.
DR PDB; 4I7C; X-ray; 2.80 A; B/D=113-125.
DR PDB; 4I7D; X-ray; 2.40 A; B/D=113-125.
DR PDBsum; 4I7B; -.
DR PDBsum; 4I7C; -.
DR PDBsum; 4I7D; -.
DR AlphaFoldDB; Q27934; -.
DR SMR; Q27934; -.
DR BioGRID; 62356; 51.
DR DIP; DIP-29101N; -.
DR ELM; Q27934; -.
DR IntAct; Q27934; 7.
DR STRING; 7227.FBpp0086645; -.
DR PaxDb; Q27934; -.
DR EnsemblMetazoa; FBtr0087516; FBpp0086645; FBgn0013725.
DR GeneID; 36606; -.
DR KEGG; dme:Dmel_CG10108; -.
DR UCSC; CG10108-RA; d. melanogaster.
DR CTD; 36606; -.
DR FlyBase; FBgn0013725; phyl.
DR VEuPathDB; VectorBase:FBgn0013725; -.
DR eggNOG; ENOG502TC95; Eukaryota.
DR HOGENOM; CLU_636589_0_0_1; -.
DR InParanoid; Q27934; -.
DR OMA; SHMGNSV; -.
DR OrthoDB; 1176401at2759; -.
DR PhylomeDB; Q27934; -.
DR BioGRID-ORCS; 36606; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36606; -.
DR PRO; PR:Q27934; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0013725; Expressed in eye disc (Drosophila) and 43 other tissues.
DR Genevisible; Q27934; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:FlyBase.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:FlyBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0035883; P:enteroendocrine cell differentiation; IMP:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:FlyBase.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:FlyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:FlyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR GO; GO:0007462; P:R1/R6 cell fate commitment; IMP:FlyBase.
DR GO; GO:0007465; P:R7 cell fate commitment; IMP:FlyBase.
DR GO; GO:0008052; P:sensory organ boundary specification; IMP:FlyBase.
DR GO; GO:0007423; P:sensory organ development; IMP:CACAO.
DR GO; GO:0016360; P:sensory organ precursor cell fate determination; IMP:FlyBase.
DR GO; GO:0045500; P:sevenless signaling pathway; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR DisProt; DP01122; -.
DR IDEAL; IID50260; -.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Coiled coil; Notch signaling pathway; Nucleus;
KW Reference proteome; Sensory transduction; Ubl conjugation pathway; Vision.
FT CHAIN 1..400
FT /note="Protein phyllopod"
FT /id="PRO_0000058418"
FT REGION 109..127
FT /note="Interaction with sina"
FT REGION 125..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..320
FT /note="Interaction with ttk"
FT REGION 346..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 319..362
FT /evidence="ECO:0000255"
FT COMPBIAS 368..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 109..110
FT /note="QE->AA: Induces a twofold reduction in interaction
FT with sina and impairs ttk degradation."
FT /evidence="ECO:0000269|PubMed:12215542"
FT MUTAGEN 111..112
FT /note="RT->AA: No effect in interaction with sina or ttk
FT degradation."
FT /evidence="ECO:0000269|PubMed:12215542"
FT MUTAGEN 113..114
FT /note="KL->AA: No effect in interaction with sina or ttk
FT degradation."
FT /evidence="ECO:0000269|PubMed:12215542"
FT MUTAGEN 115..116
FT /note="RP->AA: No effect in interaction with sina or ttk
FT degradation."
FT /evidence="ECO:0000269|PubMed:12215542"
FT MUTAGEN 119..120
FT /note="MV->AA: Induces a fourfold reduction in interaction
FT with sina and impairs ttk degradation."
FT /evidence="ECO:0000269|PubMed:12215542"
FT MUTAGEN 121..122
FT /note="RP->AA: Induces a twofold reduction in interaction
FT with sina and impairs ttk degradation."
FT /evidence="ECO:0000269|PubMed:12215542"
FT CONFLICT 127..130
FT /note="Missing (in Ref. 1; AAA66168 and 2; AAA65733)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="Q -> K (in Ref. 2; AAA65733)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="A -> T (in Ref. 2; AAA65733)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="L -> LEEEEE (in Ref. 1; AAA66168 and 2; AAA65733)"
FT /evidence="ECO:0000305"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4I7D"
SQ SEQUENCE 400 AA; 44842 MW; B992F420905407A6 CRC64;
MSTNQQQQAN PSAAVAAPAA SSEYLKRTCL ICGCHTNQTI NIYEPRSGPN IVQLIQAKFK
FQPLNEDKFL CFSCNNWLIN WHSLQAVNSN EAESQSQSPS HMGNSVLQQE RTKLRPVAMV
RPTVRVQPQS QPQLQPQVPI NPTPAPIVYS KRRASRRSAS VSRMSRVLRQ CCVESLRRSP
KKRNQQSVFV CLRPQGQKRS NAICKVECVA PRRKPVERLV KDVAATATPT PVLNTQSTPT
YQRFPQPSVD GKVVAMFRRL GTTLSREEPA AYSAESNPAC SKLPQIMSPL KEAPRWTRDL
DDDEILLEFD TAISEVLPTA RYQVTHEENK ENQQAQEMEL ELEEEEEVDG RAELEVVQEA
EAPLEPQSHH KQGNSHQNSH QASIQLAGLR LPMGLSISLV
