MK14C_DROME
ID MK14C_DROME Reviewed; 356 AA.
AC P83100; A8E6X5;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Putative mitogen-activated protein kinase 14C;
DE Short=MAP kinase 14C;
DE Short=MAPK 14C;
DE EC=2.7.11.24;
DE AltName: Full=MAP kinase p38c;
GN Name=p38c; ORFNames=CG33338;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Booth B., Frise E., Kapadia B., Park S.,
RA Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Kinase involved in a signal transduction pathway.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PTM: The phosphorylation on Thr-177 activates the enzyme (By
CC similarity). A conserved Tyr, which must also be phosphorylated to
CC activate the enzyme in closely related sequences, is replaced by His-
CC 179 in this sequence. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; AE014297; AAS65203.1; -; Genomic_DNA.
DR EMBL; BT030917; ABV82299.1; -; mRNA.
DR EMBL; BT030937; ABV82319.1; -; mRNA.
DR EMBL; BT030954; ABV82336.1; -; mRNA.
DR EMBL; BT032708; ACD81722.1; -; mRNA.
DR RefSeq; NP_996277.1; NM_206554.2.
DR AlphaFoldDB; P83100; -.
DR SMR; P83100; -.
DR BioGRID; 77547; 27.
DR IntAct; P83100; 3.
DR STRING; 7227.FBpp0083967; -.
DR PaxDb; P83100; -.
DR PRIDE; P83100; -.
DR DNASU; 2768679; -.
DR EnsemblMetazoa; FBtr0084582; FBpp0083967; FBgn0267339.
DR GeneID; 2768679; -.
DR KEGG; dme:Dmel_CG33338; -.
DR UCSC; CG33338-RA; d. melanogaster.
DR CTD; 2768679; -.
DR FlyBase; FBgn0267339; p38c.
DR VEuPathDB; VectorBase:FBgn0267339; -.
DR eggNOG; KOG0660; Eukaryota.
DR GeneTree; ENSGT00940000170951; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P83100; -.
DR OMA; KCWKELV; -.
DR OrthoDB; 683132at2759; -.
DR PhylomeDB; P83100; -.
DR Reactome; R-DME-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-DME-171007; p38MAPK events.
DR Reactome; R-DME-198753; ERK/MAPK targets.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-376172; DSCAM interactions.
DR Reactome; R-DME-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-DME-432142; Platelet sensitization by LDL.
DR Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DME-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-DME-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-DME-525793; Myogenesis.
DR Reactome; R-DME-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR BioGRID-ORCS; 2768679; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 2768679; -.
DR PRO; PR:P83100; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0267339; Expressed in midgut and 14 other tissues.
DR Genevisible; P83100; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP 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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0038066; P:p38MAPK cascade; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0048082; P:regulation of adult chitin-containing cuticle pigmentation; IGI:FlyBase.
DR GO; GO:0010883; P:regulation of lipid storage; IMP:FlyBase.
DR GO; GO:1902882; P:regulation of response to oxidative stress; IMP:FlyBase.
DR GO; GO:0009617; P:response to bacterium; IMP:FlyBase.
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 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..356
FT /note="Putative mitogen-activated protein kinase 14C"
FT /id="PRO_0000186302"
FT DOMAIN 20..305
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 41969 MW; F90340860375BAF9 CRC64;
MPEFVRVAIN ESLWEFPDIY EFVRFLGGGS FGQVAKVRLR GTENYFAMKR LMRPFEREED
AKGTYREIRL LKHMNHRNVI SLLNVFHPPA HNMMEFQQVY LVTHLMDADL HRYSRSKRMS
DQEIRIILYQ ILRGLKYIHS AGVVHRDLKP CNIAVNGNSE VRILDFGLSR MCADKMTDHV
GTMWYLAPEI IFLRGQYTKA IDVWSVGCIL AELITDRVLF RGENYVSQIR CLINIMGTPT
REFITGISME RSRNYLEGYP LRQRCDFHHL FMGYDVQAID LMEKMLEMVP EKRITAAEAM
LHPYLRDLIE PHHHAEDTAP VYDQNFENMV LPVKCWKELV SHEIRNFRPD QLDLHF
