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Q27934 (PHYL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phyllopod
Gene names
Name:phyl
ORF Names:CG10108
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential adapter component of E3 ubiquitin ligase complexes; involved in R7 photoreceptor cell differentiation, embryonic nervous system, external sensory organ development and specification of particular muscles. E3 ubiquitin ligase complexes mediate ubiquitination and subsequent proteasomal degradation of target proteins. Required for specification of R7 photoreceptor cell fate in the eye by participating in the ubiquitination and subsequent proteasomal degradation of Tramtrack (ttk), a general inhibitor of photoreceptor differentiation. Acts downstream of Notch signaling to specify the fate of the SOP (sensory organ precursor) cells and their progeny, probably via the sina-mediated proteasomal degradation of ttk. Its restricted pattern of expression, upon Notch and Ras signaling pathways, suggests that it acts as a key determinant in E3 complexes to trigger protein proteolysis in appropriate cells. Ref.1 Ref.2 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12

Subunit structure

Component of some E3 complex at least composed of sina, ebi and phyl, required for the degradation of ttk.

Subcellular location

Nucleus Ref.1 Ref.2.

Tissue specificity

In embryos, it is ubiquitously present before cellularization. During stages 9-11, it is expressed in neuroblasts and the SOP cells. From stage 12 onward, it decreases, but remains in a subset of PNS cells at stages 12-14. Weakly expressed in wing imaginal disks, in the SOP cells of wing margin bristles, notal macrochaetes, and other sensory organs. In leg disks, it is expressed in the precursors of the femoral chordotonal organs, as well as in external sensory SOP cells. Strongly expressed in the eye-antenna disk, it is specifically expressed in R1, R6 and R7 cells, and not in R3, R3, R4, R5 and R8 cells. Ref.1 Ref.2 Ref.10

Developmental stage

Expressed both maternally and zygotically. Ref.10

Induction

Activated by the Ras1/MAPK pathway in R1, R6 and R7 cells in the eye. Down-regulated by the Notch pathway. Ref.10

Ontologies

Keywords
   Biological processCell cycle
Notch signaling pathway
Sensory transduction
Ubl conjugation pathway
Vision
   Cellular componentNucleus
   DomainCoiled coil
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processNotch signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

R1/R6 cell fate commitment

Inferred from mutant phenotype Ref.1. Source: FlyBase

R7 cell development

Traceable author statement. Source: FlyBase

R7 cell fate commitment

Inferred from mutant phenotype Ref.1. Source: FlyBase

Ras protein signal transduction

Inferred from genetic interaction Ref.2. Source: FlyBase

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

peripheral nervous system development

Inferred from mutant phenotype Ref.2. Source: FlyBase

proteasomal protein catabolic process

Inferred from direct assay. Source: FlyBase

regulation of Notch signaling pathway

Inferred from direct assay. Source: FlyBase

regulation of Wnt receptor signaling pathway

Inferred from direct assay. Source: FlyBase

sensory organ precursor cell fate determination

Inferred from mutant phenotype Ref.10. Source: FlyBase

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from direct assay Ref.1. Source: FlyBase

ubiquitin ligase complex

Inferred from direct assay Ref.11. Source: FlyBase

   Molecular functionbinding, bridging

Inferred from direct assay. Source: FlyBase

protein self-association

Inferred from physical interaction Ref.11. Source: FlyBase

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Protein phyllopod
PRO_0000058418

Regions

Region109 – 12719Interaction with sina
Region241 – 32080Interaction with ttk
Coiled coil319 – 36244 Potential

Experimental info

Mutagenesis109 – 1102QE → AA: Induces a twofold reduction in interaction with sina and impairs ttk degradation. Ref.11
Mutagenesis111 – 1122RT → AA: No effect in interaction with sina or ttk degradation. Ref.11
Mutagenesis113 – 1142KL → AA: No effect in interaction with sina or ttk degradation. Ref.11
Mutagenesis115 – 1162RP → AA: No effect in interaction with sina or ttk degradation. Ref.11
Mutagenesis119 – 1202MV → AA: Induces a fourfold reduction in interaction with sina and impairs ttk degradation. Ref.11
Mutagenesis121 – 1222RP → AA: Induces a twofold reduction in interaction with sina and impairs ttk degradation. Ref.11
Sequence conflict127 – 1304Missing in AAA66168. Ref.1
Sequence conflict127 – 1304Missing in AAA65733. Ref.2
Sequence conflict2361Q → K in AAA65733. Ref.2
Sequence conflict2931A → T in AAA65733. Ref.2
Sequence conflict3421L → LEEEEE in AAA66168. Ref.1
Sequence conflict3421L → LEEEEE in AAA65733. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q27934 [UniParc].

Last modified April 26, 2004. Version 2.
Checksum: B992F420905407A6

FASTA40044,842
        10         20         30         40         50         60 
MSTNQQQQAN PSAAVAAPAA SSEYLKRTCL ICGCHTNQTI NIYEPRSGPN IVQLIQAKFK 

        70         80         90        100        110        120 
FQPLNEDKFL CFSCNNWLIN WHSLQAVNSN EAESQSQSPS HMGNSVLQQE RTKLRPVAMV 

       130        140        150        160        170        180 
RPTVRVQPQS QPQLQPQVPI NPTPAPIVYS KRRASRRSAS VSRMSRVLRQ CCVESLRRSP 

       190        200        210        220        230        240 
KKRNQQSVFV CLRPQGQKRS NAICKVECVA PRRKPVERLV KDVAATATPT PVLNTQSTPT 

       250        260        270        280        290        300 
YQRFPQPSVD GKVVAMFRRL GTTLSREEPA AYSAESNPAC SKLPQIMSPL KEAPRWTRDL 

       310        320        330        340        350        360 
DDDEILLEFD TAISEVLPTA RYQVTHEENK ENQQAQEMEL ELEEEEEVDG RAELEVVQEA 

       370        380        390        400 
EAPLEPQSHH KQGNSHQNSH QASIQLAGLR LPMGLSISLV 

« Hide

References

« Hide 'large scale' references
[1]"Control of Drosophila photoreceptor cell fates by phyllopod, a novel nuclear protein acting downstream of the Raf kinase."
Dickson B.J., Dominguez M., Der Straten A., Hafen E.
Cell 80:453-462(1995) [PubMed: 7859287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Phyllopod functions in the fate determination of a subset of photoreceptors in Drosophila."
Chang H.C., Solomon N.M., Wassarman D.A., Karim F.D., Therrien M., Rubin G.M., Wolff T.
Cell 80:463-472(1995) [PubMed: 7888014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: Canton-S.
Tissue: Eye imaginal disk.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[6]Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
[7]"PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism."
Tang A.H., Neufeld T.P., Kwan E., Rubin G.M.
Cell 90:459-467(1997) [PubMed: 9267026] [Abstract]
Cited for: FUNCTION IN TTK DEGRADATION, INTERACTION WITH SINA.
[8]"Photoreceptor cell differentiation requires regulated proteolysis of the transcriptional repressor Tramtrack."
Li S., Li Y., Carthew R.W., Lai Z.-C.
Cell 90:469-478(1997) [PubMed: 9267027] [Abstract]
Cited for: FUNCTION IN TTK DEGRADATION, INTERACTION WITH SINA.
[9]"A role for Ebi in neuronal cell cycle control."
Boulton S.J., Brook A., Staehling-Hampton K., Heitzler P., Dyson N.
EMBO J. 19:5376-5386(2000) [PubMed: 11032805] [Abstract]
Cited for: COMPONENT OF A COMPLEX WITH EBI AND SINA.
[10]"A dual function of phyllopod in Drosophila external sensory organ development: cell fate specification of sensory organ precursor and its progeny."
Pi H., Wu H.-J., Chien C.-T.
Development 128:2699-2710(2001) [PubMed: 11526076] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
[11]"Phyllopod acts as an adaptor protein to link the sina ubiquitin ligase to the substrate protein tramtrack."
Li S., Xu C., Carthew R.W.
Mol. Cell. Biol. 22:6854-6865(2002) [PubMed: 12215542] [Abstract]
Cited for: FUNCTION IN THE COMPLEX, MUTAGENESIS OF 109-GLN-GLU-110; 111-ARG-THR-112; 113-LYS-LEU-114; 115-ARG-PRO-116; 119-MET-VAL-120 AND 121-ARG-PRO-122.
[12]"Notch and Ras signaling pathway effector genes expressed in fusion competent and founder cells during Drosophila myogenesis."
Artero R., Furlong E.E., Beckett K., Scott M.P., Baylies M.
Development 130:6257-6272(2003) [PubMed: 14602676] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L38294 mRNA. Translation: AAA66168.1.
U19722 mRNA. Translation: AAA65733.1.
U19731 Genomic DNA. Translation: AAB60231.1.
AE013599 Genomic DNA. Translation: AAF58245.1.
AY075531 mRNA. Translation: AAL68338.1.
BT072878 mRNA. Translation: ACN67102.1.
PIRA55647.
RefSeqNP_725394.1. NM_166055.1.
UniGeneDm.5449.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29101N.
IntActQ27934. 8 interactions.
MINTMINT-282993.
STRINGQ27934.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087516; FBpp0086645; FBgn0013725.
GeneID36606.
KEGGdme:Dmel_CG10108.
NMPDRfig|7227.3.peg.5234.
UCSCCG10108-RA. d. melanogaster.

Organism-specific databases

CTD36606.
FlyBaseFBgn0013725. phyl.

Phylogenomic databases

eggNOGinNOG11831.
GeneTreeEMGT00050000015112.
InParanoidQ27934.
OMAINIYEPR.
OrthoDBEOG459ZZ0.
PhylomeDBQ27934.

Gene expression databases

ArrayExpressQ27934.
BgeeQ27934.
GermOnlineCG10108. Drosophila melanogaster.

Family and domain databases

InterProIPR012934. Znf_AD.
[Graphical view]
PfamPF07776. zf-AD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio799468.

Entry information

Entry namePHYL_DROME
AccessionPrimary (citable) accession number: Q27934
Secondary accession number(s): C0PV22, Q9V721
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: January 25, 2012
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase