KPEL_DROME
ID KPEL_DROME Reviewed; 501 AA.
AC Q05652; B8A3X2; Q8T005; Q9VB57;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Serine/threonine-protein kinase pelle;
DE EC=2.7.11.1 {ECO:0000269|PubMed:8440018};
GN Name=pll; ORFNames=CG5974;
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, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF LYS-240; ASP-346 AND ALA-350.
RC TISSUE=Embryo;
RX PubMed=8440018; DOI=10.1016/0092-8674(93)90071-w;
RA Shelton C.A., Wasserman S.A.;
RT "Pelle encodes a protein kinase required to establish dorsoventral polarity
RT in the Drosophila embryo.";
RL Cell 72:515-525(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 [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).
RN [5]
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 (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND INTERACTION WITH TUB.
RX PubMed=7527496; DOI=10.1038/372563a0;
RA Grosshans J., Bergmann A., Haffter P., Nuesslein-Volhard C.;
RT "Activation of the kinase Pelle by Tube in the dorsoventral signal
RT transduction pathway of Drosophila embryo.";
RL Nature 372:563-566(1994).
RN [7]
RP FUNCTION, INTERACTION WITH TUB, AND SUBCELLULAR LOCATION.
RX PubMed=7635064; DOI=10.1242/dev.121.7.2209;
RA Galindo R.L., Edwards D.N., Gillespie S.K.H., Wasserman S.A.;
RT "Interaction of the pelle kinase with the membrane-associated protein tube
RT is required for transduction of the dorsoventral signal in Drosophila
RT embryos.";
RL Development 121:2209-2218(1995).
RN [8]
RP FUNCTION, AND INTERACTION WITH PLI AND TUB.
RX PubMed=10330490; DOI=10.1016/s0925-4773(98)00236-6;
RA Grosshans J., Schnorrer F., Nuesslein-Volhard C.;
RT "Oligomerisation of Tube and Pelle leads to nuclear localisation of
RT dorsal.";
RL Mech. Dev. 81:127-138(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 26-129 IN COMPLEX WITH TUB.
RX PubMed=10589682; DOI=10.1016/s0092-8674(00)81542-1;
RA Xiao T., Towb P., Wasserman S.A., Sprang S.R.;
RT "Three-dimensional structure of a complex between the death domains of
RT Pelle and Tube.";
RL Cell 99:545-555(1999).
CC -!- FUNCTION: Plays an essential role in the Tl receptor signaling pathway
CC that establishes embryonic dorsoventral polarity; the signal directs
CC import of dl into ventral and ventrolateral nuclei, thereby
CC establishing dorsoventral polarity. Tub recruits pll to the plasma
CC membrane and protein-protein interaction activates pll.
CC {ECO:0000269|PubMed:10330490, ECO:0000269|PubMed:7527496,
CC ECO:0000269|PubMed:7635064, ECO:0000269|PubMed:8440018}.
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 Evidence={ECO:0000269|PubMed:8440018};
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; Evidence={ECO:0000269|PubMed:8440018};
CC -!- SUBUNIT: Interacts (via Death domain) with tub (via Death domain).
CC Interacts with Pellino (Pli). {ECO:0000269|PubMed:10330490,
CC ECO:0000269|PubMed:10589682, ECO:0000269|PubMed:7527496,
CC ECO:0000269|PubMed:7635064}.
CC -!- INTERACTION:
CC Q05652; P22812: tub; NbExp=9; IntAct=EBI-115059, EBI-93181;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7635064}.
CC Cytoplasm {ECO:0000269|PubMed:7635064}. Note=Associates with the plasma
CC membrane during interphase syncytial blastoderm embryos, more
CC specifically at the membrane invaginations around the nuclei.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically with low
CC levels of expression throughout the life cycle.
CC {ECO:0000269|PubMed:8440018}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. Pelle subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39802.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; L08476; AAA28750.1; -; mRNA.
DR EMBL; AE014297; AAF56686.1; -; Genomic_DNA.
DR EMBL; AY069657; AAL39802.1; ALT_TERM; mRNA.
DR EMBL; BT056264; ACL68711.1; -; mRNA.
DR PIR; A45775; A45775.
DR RefSeq; NP_001263008.1; NM_001276079.1.
DR RefSeq; NP_476971.1; NM_057623.4.
DR PDB; 1D2Z; X-ray; 2.00 A; A/C=26-129.
DR PDB; 1IK7; X-ray; 2.30 A; A/B=26-129.
DR PDB; 1YGO; NMR; -; A=26-131.
DR PDBsum; 1D2Z; -.
DR PDBsum; 1IK7; -.
DR PDBsum; 1YGO; -.
DR AlphaFoldDB; Q05652; -.
DR SMR; Q05652; -.
DR BioGRID; 68170; 14.
DR DIP; DIP-27622N; -.
DR IntAct; Q05652; 4.
DR MINT; Q05652; -.
DR STRING; 7227.FBpp0084549; -.
DR PaxDb; Q05652; -.
DR PRIDE; Q05652; -.
DR DNASU; 43283; -.
DR EnsemblMetazoa; FBtr0085179; FBpp0084549; FBgn0010441.
DR EnsemblMetazoa; FBtr0334732; FBpp0306780; FBgn0010441.
DR GeneID; 43283; -.
DR KEGG; dme:Dmel_CG5974; -.
DR UCSC; CG5974-RA; d. melanogaster.
DR CTD; 43283; -.
DR FlyBase; FBgn0010441; pll.
DR VEuPathDB; VectorBase:FBgn0010441; -.
DR eggNOG; KOG1187; Eukaryota.
DR GeneTree; ENSGT00940000169271; -.
DR HOGENOM; CLU_000288_21_15_1; -.
DR InParanoid; Q05652; -.
DR OMA; YLNTIRH; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q05652; -.
DR Reactome; R-DME-214842; DL and DIF homodimers bind to TUB and phosphorylated PLL in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214844; DL and DIF homodimers complexed with CACT are all phosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214862; Activated PLL kinase is autophosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214869; Phosphorylated CACT, DL and DIF homodimers dissociate from the TL receptor 'signalling complex'.
DR Reactome; R-DME-214874; PLL kinase binds to TUB in the TL receptor 'signalling complex'.
DR SignaLink; Q05652; -.
DR BioGRID-ORCS; 43283; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q05652; -.
DR GenomeRNAi; 43283; -.
DR PRO; PR:Q05652; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010441; Expressed in embryonic/larval hemocyte (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q05652; baseline and differential.
DR Genevisible; Q05652; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
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:0061760; P:antifungal innate immune response; IMP:FlyBase.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0048262; P:determination of dorsal/ventral asymmetry; IMP:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0035172; P:hemocyte proliferation; TAS:FlyBase.
DR GO; GO:0045087; P:innate immune response; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0002804; P:positive regulation of antifungal peptide production; IDA:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IGI:FlyBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0008063; P:Toll signaling pathway; IMP:FlyBase.
DR GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; IMP:FlyBase.
DR CDD; cd08307; Death_Pelle; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037924; Pelle_death.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 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; Cell membrane; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..501
FT /note="Serine/threonine-protein kinase pelle"
FT /id="PRO_0000086161"
FT DOMAIN 55..121
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT DOMAIN 213..499
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 219..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 348..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 240
FT /note="K->R: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:8440018"
FT MUTAGEN 346
FT /note="D->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:8440018"
FT MUTAGEN 350
FT /note="A->E: Reduced activity."
FT /evidence="ECO:0000269|PubMed:8440018"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:1D2Z"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:1D2Z"
SQ SEQUENCE 501 AA; 56160 MW; 4B29E2B40ACB81A8 CRC64;
MSGVQTAEAE AQAQNQANGN RTRSRSHLDN TMAIRLLPLP VRAQLCAHLD ALDVWQQLAT
AVKLYPDQVE QISSQKQRGR SASNEFLNIW GGQYNHTVQT LFALFKKLKL HNAMRLIKDY
VSEDLHKYIP RSVPTISELR AAPDSSAKVN NGPPFPSSSG VSNSNNNRTS TTATEEIPSL
ESLGNIHIST VQRAAESLLE IDYAELENAT DGWSPDNRLG QGGFGDVYRG KWKQLDVAIK
VMNYRSPNID QKMVELQQSY NELKYLNSIR HDNILALYGY SIKGGKPCLV YQLMKGGSLE
ARLRAHKAQN PLPALTWQQR FSISLGTARG IYFLHTARGT PLIHGDIKPA NILLDQCLQP
KIGDFGLVRE GPKSLDAVVE VNKVFGTKIY LPPEFRNFRQ LSTGVDVYSF GIVLLEVFTG
RQVTDRVPEN ETKKNLLDYV KQQWRQNRME LLEKHLAAPM GKELDMCMCA IEAGLHCTAL
DPQDRPSMNA VLKRFEPFVT D
