ID A0A4D6K823_DROME Unreviewed; 439 AA. AC A0A4D6K823; DT 03-JUL-2019, integrated into UniProtKB/TrEMBL. DT 03-JUL-2019, sequence version 1. DT 31-JUL-2019, entry version 2. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127}; DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127}; GN Name=nmo {ECO:0000313|EMBL:QCD26219.1}; GN Synonyms=adk {ECO:0000313|EMBL:QCD26219.1}, adk1 GN {ECO:0000313|EMBL:QCD26219.1}, anon-EST:Gibbs3 GN {ECO:0000313|EMBL:QCD26219.1}, anon-EST:Liang-2.43 GN {ECO:0000313|EMBL:QCD26219.1}, anon-WO0118547.332 GN {ECO:0000313|EMBL:QCD26219.1}, anon-WO0140519.256 GN {ECO:0000313|EMBL:QCD26219.1}, anon-WO0172774.138 GN {ECO:0000313|EMBL:QCD26219.1}, CG7892 {ECO:0000313|EMBL:QCD26219.1}, GN clone 2.43 {ECO:0000313|EMBL:QCD26219.1}, Dmel\CG7892 GN {ECO:0000313|EMBL:QCD26219.1}, NEMO {ECO:0000313|EMBL:QCD26219.1}, GN Nemo {ECO:0000313|EMBL:QCD26219.1}, NLK {ECO:0000313|EMBL:QCD26219.1}, GN Nlk {ECO:0000313|EMBL:QCD26219.1}, Nmo {ECO:0000313|EMBL:QCD26219.1}, GN ORE-6 {ECO:0000313|EMBL:QCD26219.1}; GN ORFNames=Dmel_CG7892 {ECO:0000313|EMBL:QCD26219.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:QCD26219.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:QCD26219.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., RA Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:QCD26219.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:QCD26219.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:QCD26219.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002). RN [5] {ECO:0000313|EMBL:QCD26219.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:QCD26219.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:QCD26219.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:QCD26219.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). 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, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.24; Evidence={ECO:0000256|SAAS:SAAS01125144}; 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=2.7.11.24; Evidence={ECO:0000256|RuleBase:RU361165, CC ECO:0000256|SAAS:SAAS01125154}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361165}; CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine CC phosphorylation. {ECO:0000256|RuleBase:RU361165}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. MAP kinase subfamily. CC {ECO:0000256|RuleBase:RU361165}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014296; QCD26219.1; -; Genomic_DNA. DR Proteomes; UP000000803; Chromosome 3L. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003527; MAP_kinase_CS. 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; PS01351; MAPK; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574094}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574086}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574135}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574114}; KW Transferase {ECO:0000256|RuleBase:RU361165, KW ECO:0000256|SAAS:SAAS00574095, ECO:0000313|EMBL:QCD26219.1}. FT DOMAIN 40 329 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT REGION 419 439 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. SQ SEQUENCE 439 AA; 49161 MW; DA51A52AEEA59C70 CRC64; MSVSMSLVQG GAAGGAPQGA SAILAAAAPY YQPPAVPQDV QPDRPIGYGA FGVVWAVTDP RDGRRVALKK LPNVFQSLVS SKRVFRELKM LCFFKHENVL SALDILQPPH LDFFQEIYVI TELLQSDLHK IIVSPQHLSA DHIKVFLYQI LRGLKYLHSA RILHRDIKPG NLLVNSNCVL KICDFGLARV EEPDQAKHMT QEVVTQYYRA PEILMGARHY SSAVDVWSVG CIFGELLGRR ILFQAQNPVQ QLELITELLG TPTMEDMRHA CEGARTHMLR RAPKPPSFSV LYTLSSHATH EAVHLLCQML VFDPDKRISV TDALAHPYLD EGRLRYHSCM CKCCFTTSAG MRQYTADFEP SAGQPFDDLW ERKLTSVQQV KEEMHKFIAE QLQTGRVPLC INPQSAAFKS FASSTVAHPS ELPPSPHQWE XRQNEAIAA //