PYGO_DROME
ID PYGO_DROME Reviewed; 815 AA.
AC Q9V9W8;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein pygopus;
DE AltName: Full=Protein gammy legs;
GN Name=pygo; Synonyms=gam; ORFNames=CG11518;
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].
RX PubMed=11955446; DOI=10.1016/s0092-8674(02)00679-7;
RA Kramps T., Peter O., Brunner E., Nellen D., Froesch B., Chatterjee S.,
RA Murone M., Zuellig S., Basler K.;
RT "Wnt/wingless signaling requires BCL9/legless-mediated recruitment of
RT pygopus to the nuclear beta-catenin-TCF complex.";
RL Cell 109:47-60(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Head;
RX PubMed=12015286; DOI=10.1242/dev.129.11.2565;
RA Parker D.S., Jemison J., Cadigan K.M.;
RT "Pygopus, a nuclear PHD-finger protein required for wingless signaling in
RT Drosophila.";
RL Development 129:2565-2576(2002).
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=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).
CC -!- FUNCTION: Involved in signal transduction through the Wnt pathway.
CC -!- SUBUNIT: Binds to BCL9 via the PHD-type zinc finger motif, and thereby
CC becomes part of the nuclear ARM/PAN complex.
CC -!- INTERACTION:
CC Q9V9W8; Q961D9: lgs; NbExp=4; IntAct=EBI-152653, EBI-85519;
CC Q9V9W8; Q7KTX8: skd; NbExp=2; IntAct=EBI-152653, EBI-110730;
CC Q9V9W8; P47825: Taf4; NbExp=2; IntAct=EBI-152653, EBI-277958;
CC Q9V9W8; O00512: BCL9; Xeno; NbExp=3; IntAct=EBI-152653, EBI-533127;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous throughout embryogenesis and larval
CC development.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development.
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DR EMBL; AF457206; AAL91369.1; -; mRNA.
DR EMBL; AY075095; AAL79357.1; -; mRNA.
DR EMBL; AE014297; AAF57161.1; -; Genomic_DNA.
DR EMBL; AY058500; AAL13729.1; -; mRNA.
DR RefSeq; NP_651872.1; NM_143615.4.
DR PDB; 3ZPV; X-ray; 2.68 A; 1/3/5/7/9/A/C/E/G/I/K/M/O/Q/S/U/W/Y=747-804.
DR PDBsum; 3ZPV; -.
DR AlphaFoldDB; Q9V9W8; -.
DR SMR; Q9V9W8; -.
DR BioGRID; 68561; 13.
DR DIP; DIP-29989N; -.
DR IntAct; Q9V9W8; 5.
DR STRING; 7227.FBpp0085167; -.
DR PaxDb; Q9V9W8; -.
DR EnsemblMetazoa; FBtr0085806; FBpp0085167; FBgn0043900.
DR GeneID; 43718; -.
DR KEGG; dme:Dmel_CG11518; -.
DR CTD; 43718; -.
DR FlyBase; FBgn0043900; pygo.
DR VEuPathDB; VectorBase:FBgn0043900; -.
DR eggNOG; ENOG502QSRS; Eukaryota.
DR GeneTree; ENSGT00530000063948; -.
DR HOGENOM; CLU_377342_0_0_1; -.
DR InParanoid; Q9V9W8; -.
DR OMA; GGGKMYP; -.
DR OrthoDB; 1468158at2759; -.
DR PhylomeDB; Q9V9W8; -.
DR Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-DME-209407; Transport of ARM to the nucleus.
DR Reactome; R-DME-209421; Transcription activation by ARM.
DR SignaLink; Q9V9W8; -.
DR BioGRID-ORCS; 43718; 0 hits in 3 CRISPR screens.
DR ChiTaRS; pygo; fly.
DR GenomeRNAi; 43718; -.
DR PRO; PR:Q9V9W8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0043900; Expressed in cleaving embryo and 20 other tissues.
DR Genevisible; Q9V9W8; DM.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:FlyBase.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:FlyBase.
DR GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0060232; P:delamination; IMP:FlyBase.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:FlyBase.
DR GO; GO:0035214; P:eye-antennal disc development; IMP:FlyBase.
DR GO; GO:0048526; P:imaginal disc-derived wing expansion; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IPI:UniProtKB.
DR GO; GO:0007367; P:segment polarity determination; IMP:UniProtKB.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Segmentation polarity protein; Wnt signaling pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..815
FT /note="Protein pygopus"
FT /id="PRO_0000097124"
FT ZN_FING 747..805
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..45
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 15..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 393
FT /note="S -> P (in Ref. 1; AAL91369)"
FT /evidence="ECO:0000305"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:3ZPV"
FT STRAND 763..765
FT /evidence="ECO:0007829|PDB:3ZPV"
FT TURN 767..770
FT /evidence="ECO:0007829|PDB:3ZPV"
FT STRAND 773..775
FT /evidence="ECO:0007829|PDB:3ZPV"
FT HELIX 776..779
FT /evidence="ECO:0007829|PDB:3ZPV"
FT HELIX 783..791
FT /evidence="ECO:0007829|PDB:3ZPV"
FT STRAND 795..798
FT /evidence="ECO:0007829|PDB:3ZPV"
FT HELIX 800..803
FT /evidence="ECO:0007829|PDB:3ZPV"
SQ SEQUENCE 815 AA; 80493 MW; 369FD5A5D34BC136 CRC64;
MTHNLGMAPY RLPGPAGGLC PPDFKPPPPT DIISAPSNPK KRRKTSSAAN SAAAVAAAAA
AAAAANSMQQ QQAPPTPQDL LPPPPMGGFG DTIIASNPFD DSPQVSAMSS SAAAAMAAMN
QMGGGPGGGH FGGGGPGGHP HWEDRMGMGG GPPPPPHMHP HMHPHHPGGP MGHPHGPHPH
MGGPPPMRGM SPMHPHQMGP GPGVGLPPHM NHGRPGGPGG PGGPVPMGSP MGGIAGMGGM
SPMGGMGGPS ISPHHMGMGG LSPMGGGPNG PNPRAMQGSP MGGPGQNSPM NSLPMGSPMG
NPIGSPLGPP SGPGPGNPGN TGGPQQQQQQ PPQPPMNNGQ MGPPPLHSPL GNGPTGHGSH
MPGGPIPGPG PGPGGLVGPG GISPAHGNNP GGSGNNMLGG NPGGGNSNNN GSNTSNASNN
NQNPHLSPAA GRLGVPTSMQ SNGPSVSSVA SSSVPSPATP TLTPTSTATS MSTSVPTSSP
APPAMSPHHS LNSAGPSPGM PNSGPSPLQS PAGPNGPNNN NSNNNNGPMM GQMIPNAVPM
QHQQHMGGGP PGHGPGPMPG MGMNQMLPPQ QPSHLGPPHP NMMNHPHHPH HHPGGPPPHM
MGGPGMHGGP AGMPPHMGGG PNPHMMGGPH GNAGPHMGHG HMGGVPGPGP GPGGMNGPPH
PHMSPHHGHP HHHHNPMGGP GPNMFGGGGG GPMGPGGPMG NMGPMGGGPM GGPMGVGPKP
MTMGGGKMYP PGQPMVFNPQ NPNAPPIYPC GMCHKEVNDN DEAVFCESGC NFFFHRTCVG
LTEAAFQMLN KEVFAEWCCD KCVSSKHIPM VKFKC
