MPKC_ASPFC
ID MPKC_ASPFC Reviewed; 378 AA.
AC B0Y462;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Mitogen-activated protein kinase mpkC {ECO:0000303|PubMed:26878695};
DE Short=MAPK mpkC {ECO:0000303|PubMed:26878695};
DE EC=2.7.11.24 {ECO:0000305|PubMed:26878695};
GN Name=mpkC {ECO:0000303|PubMed:26878695}; ORFNames=AFUB_056640;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=26878695; DOI=10.1111/mmi.13354;
RA Bruder Nascimento A.C., Dos Reis T.F., de Castro P.A., Hori J.I., Bom V.L.,
RA de Assis L.J., Ramalho L.N., Rocha M.C., Malavazi I., Brown N.A.,
RA Valiante V., Brakhage A.A., Hagiwara D., Goldman G.H.;
RT "Mitogen activated protein kinases SakA(HOG1) and MpkC collaborate for
RT Aspergillus fumigatus virulence.";
RL Mol. Microbiol. 100:841-859(2016).
CC -!- FUNCTION: Mitogen-activated protein kinase (MAPK), part of the high-
CC osmolarity glycerol (HOG) pathway (PubMed:26878695). With sakA, plays a
CC role in the osmotic and oxidative stress responses (PubMed:26878695).
CC Involved in paradoxical growth, the cell wall integrity (CWI) pathway
CC and biofilm formation (PubMed:26878695). SakA and mpkC collaborate
CC during virulence and mpkC could act by modulating sakA activity upon
CC exposure to several types of stresses and during cell wall biosynthesis
CC (PubMed:26878695). {ECO:0000269|PubMed:26878695}.
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:0000305|PubMed:26878695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:26878695};
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:0000305|PubMed:26878695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:26878695};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|RuleBase:RU361165};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. {ECO:0000255|RuleBase:RU361165}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26878695}.
CC Note=Translocates to the nucleus upon osmotic stress and cell wall
CC damage. {ECO:0000269|PubMed:26878695}.
CC -!- DISRUPTION PHENOTYPE: Increases the sensitivity to osmotic and
CC oxidative stresses as well as to cell wall damaging agents when sakA is
CC also deleted (PubMed:26878695). Affects virulence when sakA is also
CC deleted (PubMed:26878695). The double sakA/mpkC deletion also abolishes
CC mpkA phosphorylation (PubMed:26878695). {ECO:0000269|PubMed:26878695}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; DS499597; EDP51653.1; -; Genomic_DNA.
DR EnsemblFungi; EDP51653; EDP51653; AFUB_056640.
DR VEuPathDB; FungiDB:AFUB_056640; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR PhylomeDB; B0Y462; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Kinase; Magnesium; Nucleotide-binding; Nucleus;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..378
FT /note="Mitogen-activated protein kinase mpkC"
FT /id="PRO_0000454883"
FT DOMAIN 20..300
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10027"
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"
SQ SEQUENCE 378 AA; 43040 MW; 88AC6DD782E44C7F CRC64;
MAEFVRAEVL GTKFEYTTRY VNPQPIGMGS FGLVCSAFDQ ITQQPVALKK IMKPFDSSSL
AKRTYREIRL LKYLRHENLI CMRDIFISPL EDIYIATELL GTDLGRLLSI KPLDSKFSQY
FIYQILRGLK YIHSANVIHR DLKPTNILIN ENCDLKICDF GLARLQEPQM TGYVATRYYR
APEIMLTWQR YGVQVDVWSA GCILAEMLRG KPLFPGKDHV HQFHLITNIL GNPPDAVIEK
ITSKNTVNFV KSLPSREPRD LSTVVPKDTD FDAIDLLKKM LVIDPDTRIS AQDALRHPYL
APYHDPTDEP VASGPFDWSF DSADFPKETS KIMIYSEVLD YLNVDNPADP APFDPSTPFD
PSALEREFSE FLSDSGQT
