ID   B3MPN7_DROAN            Unreviewed;       376 AA.
AC   B3MPN7;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Stress-activated protein kinase JNK {ECO:0000256|RuleBase:RU368052};
DE            EC=2.7.11.24 {ECO:0000256|RuleBase:RU368052};
GN   Name=Dana\GF14126 {ECO:0000313|EMBL:EDV32285.2};
GN   Synonyms=dana_GLEANR_14886 {ECO:0000313|EMBL:EDV32285.2};
GN   ORFNames=GF14126 {ECO:0000313|EMBL:EDV32285.2};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV32285.2, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV32285.2, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., 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., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., 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., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., 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., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., 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., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., 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., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., 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).
CC   -!- FUNCTION: Responds to activation by environmental stress and pro-
CC       inflammatory cytokines by phosphorylating a number of transcription
CC       factors, and thus regulates transcriptional activity.
CC       {ECO:0000256|RuleBase:RU368052}.
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=2.7.11.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00000494};
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|ARBA:ARBA00000088};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU368052};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368052}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase subfamily.
CC       {ECO:0000256|RuleBase:RU368052}.
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DR   EMBL; CH902620; EDV32285.2; -; Genomic_DNA.
DR   RefSeq; XP_001963064.2; XM_001963028.2.
DR   AlphaFoldDB; B3MPN7; -.
DR   SMR; B3MPN7; -.
DR   STRING; 7217.B3MPN7; -.
DR   EnsemblMetazoa; FBtr0118826; FBpp0117318; FBgn0091153.
DR   GeneID; 6496954; -.
DR   KEGG; dan:6496954; -.
DR   eggNOG; KOG0665; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; B3MPN7; -.
DR   OrthoDB; 158564at2759; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0030424; C:axon; IEA:EnsemblMetazoa.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004705; F:JUN kinase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019731; P:antibacterial humoral response; IEA:EnsemblMetazoa.
DR   GO; GO:0048675; P:axon extension; IEA:EnsemblMetazoa.
DR   GO; GO:0007411; P:axon guidance; 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:0046844; P:chorion micropyle formation; IEA:EnsemblMetazoa.
DR   GO; GO:0048674; P:collateral sprouting of injured axon; IEA:EnsemblMetazoa.
DR   GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IEA:EnsemblMetazoa.
DR   GO; GO:0046843; P:dorsal appendage formation; IEA:EnsemblMetazoa.
DR   GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IEA:EnsemblMetazoa.
DR   GO; GO:0048615; P:embryonic anterior midgut (ectodermal) morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0043652; P:engulfment of apoptotic cell; IEA:EnsemblMetazoa.
DR   GO; GO:0030707; P:follicle cell of egg chamber development; IEA:EnsemblMetazoa.
DR   GO; GO:0046529; P:imaginal disc fusion, thorax closure; IEA:EnsemblMetazoa.
DR   GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0007258; P:JUN phosphorylation; IEA:EnsemblMetazoa.
DR   GO; GO:0007616; P:long-term memory; IEA:EnsemblMetazoa.
DR   GO; GO:0035006; P:melanization defense response; IEA:EnsemblMetazoa.
DR   GO; GO:0016319; P:mushroom body development; IEA:EnsemblMetazoa.
DR   GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0010508; P:positive regulation of autophagy; IEA:EnsemblMetazoa.
DR   GO; GO:1903688; P:positive regulation of border follicle cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblMetazoa.
DR   GO; GO:1904801; P:positive regulation of neuron remodeling; IEA:EnsemblMetazoa.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblMetazoa.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEA:EnsemblMetazoa.
DR   CDD; cd07850; STKc_JNK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR008351; MAPK_JNK.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF605; STRESS-ACTIVATED PROTEIN KINASE JNK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01772; JNKMAPKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01351; MAPK; 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:RU368052};
KW   Kinase {ECO:0000256|RuleBase:RU368052};
KW   Magnesium {ECO:0000256|RuleBase:RU368052};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU368052};
KW   Phosphoprotein {ECO:0000256|RuleBase:RU368052};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU368052};
KW   Transferase {ECO:0000256|RuleBase:RU368052, ECO:0000313|EMBL:EDV32285.2}.
FT   DOMAIN          28..324
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   376 AA;  43455 MW;  FABEB7A95119DA90 CRC64;
     MTKHKMAAQH QHYTVEVGDT NFTIHSRYIN LRPIGSGAQG IVCAAYDTVT EQNVAIKKLS
     RPFQNVTHAK RAYREFKLMK LVNHKNIIGL LNAFTPQRNL EEFQDVYLVM ELMDANLCQV
     IQMDLDHDRM SYLLYQMLCG IKHLHSAGII HRDLKPSNIV VKADCTLKIL DFGLARTAGT
     TFMMTPYVVT RYYRAPEVIL GMGYTENVDI WSVGCIMGEM IRGGVLFPGT DHIDQWNKII
     EQLGTPSPSF MQRLQPTVRN YVENRPRYTG YSFDRLFPDG LFPSDNNQSS RRKASDARNL
     LSKMLVIDPE QRISVDEALK HEYINVWYDA EEVDAPAPEP YDHSVDEREH TVEQWKELIY
     EEVMDYEAHN TNNRTR
//