FUSED_DROME
ID FUSED_DROME Reviewed; 805 AA.
AC P23647; Q26346; Q26347; Q27412; Q9VWR7;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Serine/threonine-protein kinase fused;
DE EC=2.7.11.1;
GN Name=fu; ORFNames=CG6551;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Embryo, Ovary, and Pupae;
RX PubMed=8155575; DOI=10.1016/0925-4773(93)90017-r;
RA Thermond P., Busson D., Guillemet E., Limbourg-Bouchon B., Preat T.,
RA Terracol R., Tricoire H., Lamour-Isnard C.;
RT "Molecular organisation and expression pattern of the segment polarity gene
RT fused of Drosophila melanogaster.";
RL Mech. Dev. 44:65-80(1993).
RN [2]
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.
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 [GENOMIC DNA] OF 1-155, AND MUTAGENESIS.
RX PubMed=8307322; DOI=10.1093/genetics/135.4.1047;
RA Preat T., Therond P., Limbourg-Bouchon B., Pham A., Tricoire H., Busson D.,
RA Lamour-Isnard C.;
RT "Segmental polarity in Drosophila melanogaster: genetic dissection of fused
RT in a Suppressor of fused background reveals interaction with costal-2.";
RL Genetics 135:1047-1062(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273, AND FUNCTION.
RX PubMed=2168522; DOI=10.1038/347087a0;
RA Preat T., Therond P., Lamour-Isnard C., Limbourg-Bouchon B., Tricoire H.,
RA Erk I., Mariol M.-C., Busson D.;
RT "A putative serine/threonine protein kinase encoded by the segment-polarity
RT fused gene of Drosophila.";
RL Nature 347:87-89(1990).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422 AND SER-429, AND
RP 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: Probable serine/threonine-protein kinase; maternally required
CC for correct patterning in the posterior part of each embryonic
CC metamere. May be involved in control of cell division during
CC metamorphosis and ovarian development. May interact with costal-2.
CC {ECO:0000269|PubMed:2168522}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- INTERACTION:
CC P23647; P19538: ci; NbExp=8; IntAct=EBI-165536, EBI-94976;
CC P23647; O16844: cos; NbExp=6; IntAct=EBI-165536, EBI-102069;
CC P23647; Q9V853: Smurf; NbExp=5; IntAct=EBI-165536, EBI-133520;
CC P23647; Q95SI0: tkv; NbExp=4; IntAct=EBI-165536, EBI-3401975;
CC -!- TISSUE SPECIFICITY: Expressed in all imaginal disks, higher level in
CC wing disk. {ECO:0000269|PubMed:8155575}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically, low
CC expression is present in males, larvae and pupae.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X80468; CAA56640.1; -; Genomic_DNA.
DR EMBL; L34782; AAA28552.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48871.1; -; Genomic_DNA.
DR EMBL; S69165; AAB29840.1; -; Genomic_DNA.
DR EMBL; S69166; AAB29841.1; -; Genomic_DNA.
DR EMBL; X55759; CAA39285.1; -; Genomic_DNA.
DR PIR; S11380; S11380.
DR RefSeq; NP_477499.1; NM_058151.5.
DR PDB; 6LPH; X-ray; 1.91 A; B=363-387.
DR PDBsum; 6LPH; -.
DR AlphaFoldDB; P23647; -.
DR SMR; P23647; -.
DR BioGRID; 59167; 49.
DR ComplexPortal; CPX-1897; Fused-Smurf ubiquitin ligase complex.
DR DIP; DIP-492N; -.
DR IntAct; P23647; 9.
DR STRING; 7227.FBpp0074373; -.
DR iPTMnet; P23647; -.
DR PaxDb; P23647; -.
DR EnsemblMetazoa; FBtr0074602; FBpp0074373; FBgn0001079.
DR GeneID; 32855; -.
DR KEGG; dme:Dmel_CG6551; -.
DR CTD; 32855; -.
DR FlyBase; FBgn0001079; fu.
DR VEuPathDB; VectorBase:FBgn0001079; -.
DR eggNOG; KOG0597; Eukaryota.
DR HOGENOM; CLU_021728_0_0_1; -.
DR InParanoid; P23647; -.
DR PhylomeDB; P23647; -.
DR BRENDA; 2.7.11.1; 1994.
DR Reactome; R-DME-209159; Assembly of the CI containing complexes.
DR Reactome; R-DME-209190; Phosphorylation of CI.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-209338; Assembly of the 'signalling complexes'.
DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR Reactome; R-DME-216119; Activation of CI.
DR Reactome; R-DME-216217; Activation of SMO.
DR SignaLink; P23647; -.
DR BioGRID-ORCS; 32855; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32855; -.
DR PRO; PR:P23647; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0001079; Expressed in cleaving embryo and 22 other tissues.
DR ExpressionAtlas; P23647; baseline and differential.
DR Genevisible; P23647; DM.
DR GO; GO:0005929; C:cilium; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:FlyBase.
DR GO; GO:0035301; C:Hedgehog signaling complex; IPI:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0005119; F:smoothened binding; IDA:FlyBase.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0042073; P:intraciliary transport; IMP:FlyBase.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IGI:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0007228; P:positive regulation of hh target transcription factor activity; IBA:GO_Central.
DR GO; GO:0046824; P:positive regulation of nucleocytoplasmic transport; IMP:FlyBase.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:FlyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0007224; P:smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0035222; P:wing disc pattern formation; IMP:FlyBase.
DR InterPro; IPR045193; Fused-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22983; PTHR22983; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Developmental protein; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Segmentation polarity protein; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..805
FT /note="Serine/threonine-protein kinase fused"
FT /id="PRO_0000085954"
FT DOMAIN 4..254
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 269..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 139..141
FT /note="Missing: In FU-62."
FT /evidence="ECO:0000269|PubMed:8307322"
FT MUTAGEN 147
FT /note="A->T: In FU-H63."
FT /evidence="ECO:0000269|PubMed:8307322"
FT CONFLICT 9
FT /note="L -> M (in Ref. 2; AAF48871)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="F -> L (in Ref. 1; CAA56640/AAA28552)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="K -> KVSGAGQVIKQQVHTTSSHHIHVLQ (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..175
FT /note="EQ -> DE (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="S -> C (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="E -> D (in Ref. 1; CAA56640/AAA28552)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="G -> V (in Ref. 1; CAA56640/AAA28552)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="G -> S (in Ref. 1; CAA56640/AAA28552)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="R -> G (in Ref. 1; CAA56640/AAA28552)"
FT /evidence="ECO:0000305"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:6LPH"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:6LPH"
SQ SEQUENCE 805 AA; 90347 MW; A7804E2749B79D0C CRC64;
MNRYAVSSLV GQGSFGCVYK ATRKDDSKVV AIKVISKRGR ATKELKNLRR ECDIQARLKH
PHVIEMIESF ESKTDLFVVT EFALMDLHRY LSYNGAMGEE PARRVTGHLV SALYYLHSNR
ILHRDLKPQN VLLDKNMHAK LCDFGLARNM TLGTHVLTSI KGTPLYMAPE LLAEQPYDHH
ADMWSLGCIA YESMAGQPPF CASSILHLVK MIKHEDVKWP STLTSECRSF LQGLLEKDPG
LRISWTQLLC HPFVEGRIFI AETQAEAAKE SPFTNPEAKV KSSKQSDPEV GDLDEALAAL
DFGESRQENL TTSRDSINAI APSDVEHLET DVEDNMQRVV VPFADLSYRD LSGVRAMPMV
HQPVINSHTC FVSGNSNMIL NHMNDNFDFQ ASLRGGGVAA KPIVAPTVRQ SRSKDLEKRK
LSQNLDNFSV RLGHSVDHEA QRKATEIATQ EKHNQENKPP AEAISYANSQ PPQQQPQQLK
HSMHSTNEEK LSSDNTPPCL LPGWDSCDES QSPPIENDEW LAFLNRSVQE LLDGELDSLK
QHNLVSIIVA PLRNSKAIPR VLKSVAQLLS LPFVLVDPVL IVDLELIRNV YVDVKLVPNL
MYACKLLLSH KQLSDSAASA PLTTGSLSRT LRSIPELTVE ELETACSLYE LVCHLVHLQQ
QFLTQFCDAV AILAASDLFL NFLTHDFRQS DSDAASVRLA GCMLALMGCV LRELPENAEL
VERIVFNPRL NFVSLLQSRH HLLRQRSCQL LRLLARFSLR GVQRIWNGEL RFALQQLSEH
HSYPALRGEA AQTLDEISHF TFFVT
