ID B4LQZ8_DROVI Unreviewed; 375 AA. AC B4LQZ8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 16-JAN-2019, entry version 89. 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=Dvir\GJ17518 {ECO:0000313|EMBL:EDW64537.1}; GN ORFNames=Dvir_GJ17518 {ECO:0000313|EMBL:EDW64537.1}, GJ17518 GN {ECO:0000313|FlyBase:FBgn0204688}; OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW64537.1, ECO:0000313|Proteomes:UP000008792}; RN [1] {ECO:0000313|EMBL:EDW64537.1, ECO:0000313|Proteomes:UP000008792} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW64537.1}, and Tucson RC 15010-1051.87 {ECO:0000313|Proteomes:UP000008792}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). RN [2] {ECO:0000313|EMBL:EDW64537.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW64537.1}; RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542; RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.; RT "Assembly reconciliation."; RL Bioinformatics 24:42-45(2008). RN [3] {ECO:0000313|EMBL:EDW64537.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW64537.1}; RG FlyBase; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:KRF81685.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:KRF81685.1}; RG FlyBase; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. 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; CH940649; EDW64537.1; -; Genomic_DNA. DR EMBL; CH940649; KRF81685.1; -; Genomic_DNA. DR EMBL; CH940649; KRF81686.1; -; Genomic_DNA. DR RefSeq; XP_002052382.1; XM_002052346.2. DR RefSeq; XP_015028433.1; XM_015172947.1. DR RefSeq; XP_015028434.1; XM_015172948.1. DR SMR; B4LQZ8; -. DR STRING; 7244.FBpp0231935; -. DR EnsemblMetazoa; FBtr0233443; FBpp0231935; FBgn0204688. DR EnsemblMetazoa; FBtr0440757; FBpp0397328; FBgn0204688. DR EnsemblMetazoa; FBtr0442342; FBpp0398820; FBgn0204688. DR GeneID; 6629054; -. DR KEGG; dvi:Dvir_GJ17518; -. DR FlyBase; FBgn0204688; Dvir\GJ17518. DR eggNOG; KOG0660; Eukaryota. DR eggNOG; ENOG410XNY0; LUCA. DR InParanoid; B4LQZ8; -. DR KO; K04371; -. DR OMA; DIYIVQC; -. DR OrthoDB; 741207at2759; -. DR Proteomes; UP000008792; Unassembled WGS sequence. DR Bgee; FBgn0204688; Expressed in 1 organ(s), highest expression level in adult organism. DR GO; GO:0030054; C:cell junction; IEA:EnsemblMetazoa. DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa. DR GO; GO:0031594; C:neuromuscular junction; IEA:EnsemblMetazoa. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0019901; F:protein kinase binding; IEA:EnsemblMetazoa. DR GO; GO:0008134; F:transcription factor binding; IEA:EnsemblMetazoa. DR GO; GO:0034334; P:adherens junction maintenance; IEA:EnsemblMetazoa. DR GO; GO:0048149; P:behavioral response to ethanol; IEA:EnsemblMetazoa. DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IEA:EnsemblMetazoa. DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:EnsemblMetazoa. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:EnsemblMetazoa. DR GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblMetazoa. DR GO; GO:0051607; P:defense response to virus; IEA:EnsemblMetazoa. DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa. DR GO; GO:0046843; P:dorsal appendage formation; IEP:FlyBase. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:EnsemblMetazoa. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:EnsemblMetazoa. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:EnsemblMetazoa. DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IEA:EnsemblMetazoa. DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:EnsemblMetazoa. DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IEA:EnsemblMetazoa. DR GO; GO:0035170; P:lymph gland crystal cell differentiation; IEA:EnsemblMetazoa. DR GO; GO:0035169; P:lymph gland plasmatocyte differentiation; IEA:EnsemblMetazoa. DR GO; GO:0000278; P:mitotic cell cycle; IEA:EnsemblMetazoa. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:EnsemblMetazoa. DR GO; GO:0016242; P:negative regulation of macroautophagy; IEA:EnsemblMetazoa. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:EnsemblMetazoa. DR GO; GO:0045793; P:positive regulation of cell size; IEA:EnsemblMetazoa. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:EnsemblMetazoa. DR GO; GO:0046534; P:positive regulation of photoreceptor cell differentiation; IEA:EnsemblMetazoa. DR GO; GO:0090303; P:positive regulation of wound healing; IEA:EnsemblMetazoa. DR GO; GO:2000826; P:regulation of heart morphogenesis; IEA:EnsemblMetazoa. DR GO; GO:2001023; P:regulation of response to drug; IEA:EnsemblMetazoa. DR GO; GO:0045500; P:sevenless signaling pathway; IEA:EnsemblMetazoa. DR GO; GO:0007430; P:terminal branching, open tracheal system; IEA:EnsemblMetazoa. DR GO; GO:0007362; P:terminal region determination; IEA:EnsemblMetazoa. DR GO; GO:0008293; P:torso signaling pathway; IEA:EnsemblMetazoa. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR008349; MAPK_ERK1/2. 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 PRINTS; PR01770; ERK1ERK2MAPK. 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:UP000008792}; 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:UP000008792}; 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:EDW64537.1}. FT DOMAIN 37 325 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. SQ SEQUENCE 375 AA; 42993 MW; E2B753B3ADABB61D CRC64; MAEGNTGTSA EGAAALAAPH PNAEVIRGQI FEVGPRYRKL TYIGEGAYGM VVSADDTLTN QRVAIKKISP FEHQTYCQRT LREITILTRF KHENIIDIRD ILRVDSIEQM RDVYIVQCLM ETDLYKLLKT QRLSNDHICY FLYQILRGLK YIHSANVLHR DLKPSNLLLN KTCDLKICDF GLARIADPEH DHTGFLTEYV ATRWYRAPEI MLNSKGYTKS IDIWSVGCIL AEMLSNRPIF PGKHYLDQLN HILGVLGSPS QEDLECIINE KARNYLESLP FKPNVPWSRL FPNADALALD LLGKMLTFNP HKRIPVEEAL AHPYLEQYYD PGDEPVAEVP FRINMENDDI SRDALKSLIF EETLKFKERQ PEQAL //