DSOR1_DROME
ID DSOR1_DROME Reviewed; 396 AA.
AC Q24324; Q8ISE0; Q9W360;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase dSOR1;
DE Short=Downstream of RAF;
DE Short=MAPKK;
DE EC=2.7.12.2;
GN Name=Dsor1; ORFNames=CG15793;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8381718; DOI=10.1016/0092-8674(93)90117-9;
RA Tsuda L., Inoue Y.H., Yoo M.-A., Mizuno M., Hata M., Lim Y.-M.,
RA Adachi-Yamada T., Ryo H., Masamune Y., Nishida Y.;
RT "A protein kinase similar to MAP kinase activator acts downstream of the
RT raf kinase in Drosophila.";
RL Cell 72:407-414(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=5-17-88#b1, 5-17-88a#4, 5-17-88a#6, 5-17-88b#1, 5-17-88b#5,
RC 7-21-88#b2, 7-21-88b#1, 7-21-88b#2, 7-21-88b#4, AA1, AA16, AA18, AA20, AA3,
RC CA2, M2, PYR2, Reids2, and wild5b;
RX PubMed=12694293; DOI=10.1046/j.1365-294x.2003.01741.x;
RA Riley R.M., Jin W., Gibson G.;
RT "Contrasting selection pressures on components of the Ras-mediated signal
RT transduction pathway in Drosophila.";
RL Mol. Ecol. 12:1315-1323(2003).
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).
RN [6]
RP INTERACTION WITH KSR AND RAF, AND PHOSPHORYLATION AT SER-237 AND SER-241.
RX PubMed=29433126; DOI=10.1038/nature25478;
RA Lavoie H., Sahmi M., Maisonneuve P., Marullo S.A., Thevakumaran N., Jin T.,
RA Kurinov I., Sicheri F., Therrien M.;
RT "MEK drives BRAF activation through allosteric control of KSR proteins.";
RL Nature 554:549-553(2018).
CC -!- FUNCTION: Required downstream of Raf in the sevenless (sev), torso
CC (tor), and Drosophila EGF receptor homolog (DER) signal transduction
CC pathways. Involved in both positive regulation (at the posterior
CC terminus) and negative regulation (at the anterior domain) of tll, as
CC in other terminal class gene products, maybe via the ERK-A kinase.
CC {ECO:0000269|PubMed:8381718}.
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=2.7.12.2;
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=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- SUBUNIT: Interacts with Raf and ksr; Dsor1 binding to ksr probably
CC promotes ksr and Raf dimerization and ksr-mediated Raf transactivation.
CC {ECO:0000269|PubMed:29433126}.
CC -!- INTERACTION:
CC Q24324; P11346: Raf; NbExp=4; IntAct=EBI-671282, EBI-664624;
CC Q24324; P40417: rl; NbExp=2; IntAct=EBI-671282, EBI-867790;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:8381718}.
CC -!- PTM: Phosphorylation on Ser/Thr by MAP kinase kinase kinases regulates
CC positively the kinase activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02925.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D13782; BAA02925.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY135075; AAN17587.1; -; Genomic_DNA.
DR EMBL; AY135076; AAN17588.1; -; Genomic_DNA.
DR EMBL; AY135077; AAN17589.1; -; Genomic_DNA.
DR EMBL; AY135078; AAN17590.1; -; Genomic_DNA.
DR EMBL; AY135079; AAN17591.1; -; Genomic_DNA.
DR EMBL; AY135080; AAN17592.1; -; Genomic_DNA.
DR EMBL; AY135081; AAN17593.1; -; Genomic_DNA.
DR EMBL; AY135082; AAN17594.1; -; Genomic_DNA.
DR EMBL; AY135083; AAN17595.1; -; Genomic_DNA.
DR EMBL; AY135084; AAN17596.1; -; Genomic_DNA.
DR EMBL; AY135085; AAN17597.1; -; Genomic_DNA.
DR EMBL; AY135086; AAN17598.1; -; Genomic_DNA.
DR EMBL; AY135087; AAN17599.1; -; Genomic_DNA.
DR EMBL; AY135088; AAN17600.1; -; Genomic_DNA.
DR EMBL; AY135089; AAN17601.1; -; Genomic_DNA.
DR EMBL; AY135090; AAN17602.1; -; Genomic_DNA.
DR EMBL; AY135091; AAN17603.1; -; Genomic_DNA.
DR EMBL; AY135092; AAN17604.1; -; Genomic_DNA.
DR EMBL; AY135093; AAN17605.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46475.1; -; Genomic_DNA.
DR EMBL; AY058692; AAL13921.1; -; mRNA.
DR PIR; A45176; A45176.
DR RefSeq; NP_001285044.1; NM_001298115.1.
DR RefSeq; NP_511098.1; NM_078543.4.
DR AlphaFoldDB; Q24324; -.
DR SMR; Q24324; -.
DR BioGRID; 58322; 108.
DR DIP; DIP-29770N; -.
DR IntAct; Q24324; 3.
DR MINT; Q24324; -.
DR STRING; 7227.FBpp0071248; -.
DR iPTMnet; Q24324; -.
DR PaxDb; Q24324; -.
DR PRIDE; Q24324; -.
DR EnsemblMetazoa; FBtr0071313; FBpp0071248; FBgn0010269.
DR GeneID; 31872; -.
DR KEGG; dme:Dmel_CG15793; -.
DR CTD; 31872; -.
DR FlyBase; FBgn0010269; Dsor1.
DR VEuPathDB; VectorBase:FBgn0010269; -.
DR eggNOG; KOG0581; Eukaryota.
DR GeneTree; ENSGT00940000153487; -.
DR InParanoid; Q24324; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q24324; -.
DR BRENDA; 2.4.1.222; 1994.
DR BRENDA; 2.7.12.2; 1994.
DR Reactome; R-DME-110056; MAPK3 (ERK1) activation.
DR Reactome; R-DME-112411; MAPK1 (ERK2) activation.
DR Reactome; R-DME-170968; Frs2-mediated activation.
DR Reactome; R-DME-209190; Phosphorylation of CI.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-445144; Signal transduction by L1.
DR Reactome; R-DME-5673000; RAF activation.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-5674499; Negative feedback regulation of MAPK pathway.
DR SignaLink; Q24324; -.
DR BioGRID-ORCS; 31872; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 31872; -.
DR PRO; PR:Q24324; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0010269; Expressed in mouthpart and 26 other tissues.
DR ExpressionAtlas; Q24324; baseline and differential.
DR Genevisible; Q24324; DM.
DR GO; GO:0000793; C:condensed chromosome; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007298; P:border follicle cell migration; IGI:FlyBase.
DR GO; GO:0071481; P:cellular response to X-ray; IMP:FlyBase.
DR GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:FlyBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0042386; P:hemocyte differentiation; IGI:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:FlyBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:0042461; P:photoreceptor cell development; IGI:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0007465; P:R7 cell fate commitment; IMP:FlyBase.
DR GO; GO:0045500; P:sevenless signaling pathway; IMP:FlyBase.
DR GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0007362; P:terminal region determination; IMP:FlyBase.
DR GO; GO:0008293; P:torso signaling pathway; IMP:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:FlyBase.
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 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 ATP-binding; Developmental protein; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..396
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase dSOR1"
FT /id="PRO_0000085928"
FT DOMAIN 87..364
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 209
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 93..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 237
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000269|PubMed:29433126"
FT MOD_RES 241
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000269|PubMed:29433126"
FT VARIANT 394
FT /note="S -> L (in strain: Reids2)"
SQ SEQUENCE 396 AA; 43870 MW; 9245CED1DA750C33 CRC64;
MSKNKLNLVL PPVNTEATVA AATVAPTPPF KTPSGTDTHS LLGKPKTSID ALTETLEGLD
MGDTERKRIK MFLSQKEKIG ELSDEDLEKL GELGSGNGGV VMKVRHTHTH LIMARKLIHL
EVKPAIKKQI LRELKVLHEC NFPHIVGFYG AFYSDGEISI CMEYMDGGSL DLILKRAGRI
PESILGRITL AVLKGLSYLR DNHAIIHRDV KPSNILVNSS GEIKICDFGV SGQLIDSMAN
SFVGTRSYMS PERLQGTHYS VQSDIWSLGL SLVEMAIGMY PIPPPNTATL ESIFADNAEE
SGQPTDEPRA MAIFELLDYI VNEPPPKLEH KIFSTEFKDF VDICLKKQPD ERADLKTLLS
HPWIRKAELE EVDISGWVCK TMDLPPSTPK RNTSPN
