LOCUS DSOR1_DROME 396 aa linear INV 27-NOV-2024
DEFINITION RecName: Full=Dual specificity mitogen-activated protein kinase
kinase dSOR1; Short=Downstream of RAF; Short=MAPKK.
ACCESSION Q24324
VERSION Q24324.2
DBSOURCE UniProtKB: locus DSOR1_DROME, accession Q24324;
class: standard.
extra accessions:Q8ISE0,Q9W360
created: Nov 1, 1997.
sequence updated: Aug 16, 2005.
annotation updated: Nov 27, 2024.
xrefs: D13782.1, BAA02925.1, AY135075.1, AAN17587.1, AY135076.1,
AAN17588.1, AY135077.1, AAN17589.1, AY135078.1, AAN17590.1,
AY135079.1, AAN17591.1, AY135080.1, AAN17592.1, AY135081.1,
AAN17593.1, AY135082.1, AAN17594.1, AY135083.1, AAN17595.1,
AY135084.1, AAN17596.1, AY135085.1, AAN17597.1, AY135086.1,
AAN17598.1, AY135087.1, AAN17599.1, AY135088.1, AAN17600.1,
AY135089.1, AAN17601.1, AY135090.1, AAN17602.1, AY135091.1,
AAN17603.1, AY135092.1, AAN17604.1, AY135093.1, AAN17605.1,
AE014298.5, AAF46475.1, AY058692.1, AAL13921.1, A45176,
NP_001285044.1, NP_511098.1, 8BW9_C
xrefs (non-sequence databases): PDBsum:8BW9, AlphaFoldDB:Q24324,
EMDB:EMD-16281, SMR:Q24324, BioGRID:58322, DIP:DIP-29770N,
IntAct:Q24324, MINT:Q24324, STRING:7227.FBpp0071248,
iPTMnet:Q24324, PaxDb:7227-FBpp0071248, EnsemblMetazoa:FBtr0071313,
EnsemblMetazoa:FBpp0071248, EnsemblMetazoa:FBgn0010269,
GeneID:31872, KEGG:dme:Dmel_CG15793, AGR:FB:FBgn0010269, CTD:31872,
FlyBase:FBgn0010269, VEuPathDB:VectorBase:FBgn0010269,
eggNOG:KOG0581, GeneTree:ENSGT00940000153487, InParanoid:Q24324,
OMA:ENKYHDL, OrthoDB:2900742at2759, PhylomeDB:Q24324,
BRENDA:2.4.1.222, BRENDA:2.7.12.2, Reactome:R-DME-110056,
Reactome:R-DME-112411, Reactome:R-DME-170968,
Reactome:R-DME-209190, Reactome:R-DME-209214,
Reactome:R-DME-432553, Reactome:R-DME-445144,
Reactome:R-DME-5673000, Reactome:R-DME-5674135,
Reactome:R-DME-5674499, SignaLink:Q24324, BioGRID-ORCS:31872,
GenomeRNAi:31872, PRO:PR:Q24324, Proteomes:UP000000803,
Bgee:FBgn0010269, ExpressionAtlas:Q24324, GO:0000793, GO:0005829,
GO:0005524, GO:0019900, GO:0004708, GO:0106310, GO:0004674,
GO:0004713, GO:0007298, GO:0071481, GO:0051607, GO:0008340,
GO:0009953, GO:0007173, GO:0070371, GO:0008543, GO:0042386,
GO:0008286, GO:0000165, GO:0033314, GO:0007095, GO:0042461,
GO:0006468, GO:0007465, GO:0045500, GO:0007430, GO:0007362,
GO:0008293, GO:0048010, CDD:cd06615, FunFam:1.10.510.10:FF:000115,
FunFam:3.30.200.20:FF:000100, Gene3D:1.10.510.10,
InterPro:IPR011009, InterPro:IPR050915, InterPro:IPR000719,
InterPro:IPR017441, InterPro:IPR008271, PANTHER:PTHR47448,
PANTHER:PTHR47448:SF1, Pfam:PF00069, SMART:SM00220,
SUPFAM:SSF56112, PROSITE:PS00107, PROSITE:PS50011, PROSITE:PS00108
KEYWORDS 3D-structure; ATP-binding; Developmental protein; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tyrosine-protein
kinase.
SOURCE Drosophila melanogaster (fruit fly)
ORGANISM Drosophila melanogaster
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Endopterygota; Diptera; Brachycera;
Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
REFERENCE 1 (residues 1 to 396)
AUTHORS Tsuda,L., Inoue,Y.H., Yoo,M.A., Mizuno,M., Hata,M., Lim,Y.M.,
Adachi-Yamada,T., Ryo,H., Masamune,Y. and Nishida,Y.
TITLE A protein kinase similar to MAP kinase activator acts downstream of
the raf kinase in Drosophila
JOURNAL Cell 72 (3), 407-414 (1993)
PUBMED 8381718
REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL
STAGE.
REFERENCE 2 (residues 1 to 396)
AUTHORS Riley,R.M., Jin,W. and Gibson,G.
TITLE Contrasting selection pressures on components of the Ras-mediated
signal transduction pathway in Drosophila
JOURNAL Mol Ecol 12 (5), 1315-1323 (2003)
PUBMED 12694293
REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA].;
STRAIN=5-17-88#b1, 5-17-88a#4, 5-17-88a#6, 5-17-88b#1, 5-17-88b#5,
7-21-88#b2, 7-21-88b#1, 7-21-88b#2, 7-21-88b#4, AA1, AA16, AA18,
AA20, AA3, CA2, M2, PYR2, Reids2, and wild5b
REFERENCE 3 (residues 1 to 396)
AUTHORS 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., Zhang,Q., Chen,L.X.,
Brandon,R.C., Rogers,Y.H., Blazej,R.G., Champe,M., Pfeiffer,B.D.,
Wan,K.H., Doyle,C., Baxter,E.G., Helt,G., Nelson,C.R., Gabor,G.L.,
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., 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.,
Kravitz,S., Kulp,D., Lai,Z., Lasko,P., Lei,Y., Levitsky,A.A.,
Li,J., 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., Scheeler,F., Shen,H., Shue,B.C., Siden-Kiamos,I.,
Simpson,M., Skupski,M.P., Smith,T., 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., WoodageT,
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., Zhu,X., Smith,H.O.,
Gibbs,R.A., Myers,E.W., Rubin,G.M. and Venter,J.C.
TITLE The genome sequence of Drosophila melanogaster
JOURNAL Science 287 (5461), 2185-2195 (2000)
PUBMED 10731132
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
STRAIN=Berkeley
REFERENCE 4 (residues 1 to 396)
AUTHORS 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., Whitfied,E.J., Bayraktaroglu,L.,
Berman,B.P., Bettencourt,B.R., Celniker,S.E., de Grey,A.D.,
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. and Lewis,S.E.
TITLE Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review
JOURNAL Genome Biol 3 (12), RESEARCH0083 (2002)
PUBMED 12537572
REMARK GENOME REANNOTATION.;
STRAIN=Berkeley
REFERENCE 5 (residues 1 to 396)
AUTHORS Stapleton,M., Carlson,J., Brokstein,P., Yu,C., Champe,M.,
George,R., Guarin,H., Kronmiller,B., Pacleb,J., Park,S., Wan,K.,
Rubin,G.M. and Celniker,S.E.
TITLE A Drosophila full-length cDNA resource
JOURNAL Genome Biol 3 (12), RESEARCH0080 (2002)
PUBMED 12537569
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
STRAIN=Berkeley; TISSUE=Embryo
REFERENCE 6 (residues 1 to 396)
AUTHORS Lavoie,H., Sahmi,M., Maisonneuve,P., Marullo,S.A., Thevakumaran,N.,
Jin,T., Kurinov,I., Sicheri,F. and Therrien,M.
TITLE MEK drives BRAF activation through allosteric control of KSR
proteins
JOURNAL Nature 554 (7693), 549-553 (2018)
PUBMED 29433126
REMARK INTERACTION WITH KSR AND RAF, AND PHOSPHORYLATION AT SER-237 AND
SER-241.
COMMENT On or before Jan 24, 2006 this sequence version replaced
gi:75016286, gi:75027901, gi:2499636.
[FUNCTION] Required downstream of Raf in the sevenless (sev), torso
(tor), and Drosophila EGF receptor homolog (DER) signal
transduction pathways. Involved in both positive regulation (at the
posterior terminus) and negative regulation (at the anterior
domain) of tll, as in other terminal class gene products, maybe via
the ERK-A kinase. {ECO:0000269|PubMed:8381718}.
[CATALYTIC ACTIVITY] Reaction=L-seryl-[protein] + ATP =
O-phospho-L-seryl-[protein] + ADP + H(+); Xref=Rhea:RHEA:17989,
Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
ChEBI:CHEBI:456216; EC=2.7.12.2.
[CATALYTIC ACTIVITY] Reaction=L-threonyl-[protein] + ATP =
O-phospho-L-threonyl-[protein] + ADP + H(+); Xref=Rhea:RHEA:46608,
Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
ChEBI:CHEBI:456216; EC=2.7.12.2.
[CATALYTIC ACTIVITY] Reaction=L-tyrosyl-[protein] + ATP =
O-phospho-L-tyrosyl-[protein] + ADP + H(+); Xref=Rhea:RHEA:10596,
Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620,
ChEBI:CHEBI:456216; EC=2.7.12.2.
[SUBUNIT] Interacts with Raf and ksr; Dsor1 binding to ksr probably
promotes ksr and Raf dimerization and ksr-mediated Raf
transactivation. {ECO:0000269|PubMed:29433126}.
[INTERACTION] Q24324; P11346: Raf; NbExp=4; IntAct=EBI-671282,
EBI-664624.
[DEVELOPMENTAL STAGE] Expressed both maternally and zygotically.
{ECO:0000269|PubMed:8381718}.
[PTM] Phosphorylation on Ser/Thr by MAP kinase kinase kinases
regulates positively the kinase activity. {ECO:0000250}.
[SIMILARITY] Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
[SEQUENCE CAUTION] Sequence=BAA02925.1; Type=Erroneous gene model
prediction; Evidence={ECO:0000305}.
FEATURES Location/Qualifiers
source 1..396
/organism="Drosophila melanogaster"
/db_xref="taxon:7227"
gene 1..396
/gene="Dsor1"
/locus_tag="CG15793"
Protein 1..396
/product="Dual specificity mitogen-activated protein
kinase kinase dSOR1"
/EC_number="2.7.12.2"
/note="Downstream of RAF; MAPKK"
/UniProtKB_evidence="Evidence at protein level"
Region 1..396
/region_name="Mature chain"
/note="Dual specificity mitogen-activated protein kinase
kinase dSOR1. /id=PRO_0000085928."
Region 25..44
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Region 29..43
/region_name="Compositionally biased region"
/note="Polar residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 84..86
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 85..382
/region_name="PKc_MEK"
/note="Catalytic domain of the dual-specificity Protein
Kinase, Mitogen-Activated Protein (MAP)/Extracellular
signal-Regulated Kinase (ERK) Kinase; cd06615"
/db_xref="CDD:132946"
Region 87..364
/region_name="Domain"
/note="Protein kinase.
/evidence=ECO:0000255|PROSITE-ProRule:PRU00159."
Site order(93..97,101,114,116,146,162..165,168..169,172,209,
211..214,216,226..227,230,242..245,247,274,283)
/site_type="active"
/db_xref="CDD:132946"
Site order(93..97,99,101,114,116,146,162..165,168..169,
171..172,211,213..214,216,227)
/site_type="other"
/note="ATP binding site [chemical binding]"
/db_xref="CDD:132946"
Region 95..99
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Site order(96..97,209,211..213,230,242..245,247,274,283)
/site_type="other"
/note="polypeptide substrate binding site [polypeptide
binding]"
/db_xref="CDD:132946"
Site order(97,116,134,137,146,160,162,227..231,234,238)
/site_type="other"
/note="noncompetitive inhibitor binding site [chemical
binding]"
/db_xref="CDD:132946"
Site order(100,120..121,156,249,253..256,314,317..318,321..322)
/site_type="other"
/note="homodimer interface [polypeptide binding]"
/db_xref="CDD:132946"
Region 116..119
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 124..131
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 135..138
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 148..154
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 157..163
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 170..177
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 182..203
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Site 209
/site_type="active"
/note="Proton acceptor.
/evidence=ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027."
Region 219..221
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Site 226..247
/site_type="other"
/note="activation loop (A-loop)"
/db_xref="CDD:132946"
Region 232..236
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Site 237
/site_type="phosphorylation"
/note="Phosphoserine; by RAF.
/evidence=ECO:0000269|PubMed:29433126."
Site 241
/site_type="phosphorylation"
/note="Phosphoserine; by RAF.
/evidence=ECO:0000269|PubMed:29433126."
Region 251..256
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 262..277
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 313..322
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 335..344
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 349..351
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 355..358
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 362..369
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 374..381
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:8BW9."
Region 394
/region_name="Variant"
/note="S -> L (in strain: Reids2)."
ORIGIN
1 msknklnlvl ppvnteatva aatvaptppf ktpsgtdths llgkpktsid altetlegld
61 mgdterkrik mflsqkekig elsdedlekl gelgsgnggv vmkvrhthth limarklihl
121 evkpaikkqi lrelkvlhec nfphivgfyg afysdgeisi cmeymdggsl dlilkragri
181 pesilgritl avlkglsylr dnhaiihrdv kpsnilvnss geikicdfgv sgqlidsman
241 sfvgtrsyms perlqgthys vqsdiwslgl slvemaigmy pipppntatl esifadnaee
301 sgqptdepra maifelldyi vnepppkleh kifstefkdf vdiclkkqpd eradlktlls
361 hpwirkaele evdisgwvck tmdlppstpk rntspn
//