MAPK1_PNECA
ID MAPK1_PNECA Reviewed; 370 AA.
AC O94737;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Mitogen-activated protein kinase 1;
DE EC=2.7.11.24;
DE AltName: Full=MAP kinase Mkp1;
GN Name=MKP1 {ECO:0000312|EMBL:AAD16043.1};
OS Pneumocystis carinii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX NCBI_TaxID=4754;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD10000.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-52; THR-186 AND TYR-188.
RX PubMed=10564487; DOI=10.1046/j.1365-2958.1999.01606.x;
RA Fox D., Smulian A.G.;
RT "Mitogen-activated protein kinase Mkp1 of Pneumocystis carinii complements
RT the slt2Delta defect in the cell integrity pathway of Saccharomyces
RT cerevisiae.";
RL Mol. Microbiol. 34:451-462(1999).
RN [2] {ECO:0000305}
RP MUTAGENESIS OF LYS-52; THR-182; TYR-184; THR-186 AND TYR-188, AND
RP PHOSPHORYLATION AT THR-186 AND TYR-188.
RX PubMed=10889467; DOI=10.1016/s0898-6568(00)00076-0;
RA Fox D., Smulian A.G.;
RT "Mkp1 of Pneumocystis carinii associates with the yeast transcription
RT factor Rlm1 via a mechanism independent of the activation state.";
RL Cell. Signal. 12:381-390(2000).
CC -!- FUNCTION: Serine-threonine protein kinase which may be involved in
CC maintenance of cell integrity. Functionally complements SLT2 null
CC mutant in S.cerevisiae. {ECO:0000269|PubMed:10564487}.
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:0000269|PubMed:10564487};
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:0000269|PubMed:10564487};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. Activated by oxidative stress.
CC {ECO:0000269|PubMed:10564487}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-186 and Tyr-188, which activates the
CC enzyme.
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; AF077677; AAD10000.1; -; mRNA.
DR EMBL; AF084383; AAD16043.1; -; Genomic_DNA.
DR AlphaFoldDB; O94737; -.
DR SMR; O94737; -.
DR iPTMnet; O94737; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043008; F:ATP-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016043; P:cellular component organization; IMP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR GO; GO:0040010; P:positive regulation of growth rate; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..370
FT /note="Mitogen-activated protein kinase 1"
FT /id="PRO_0000247743"
FT DOMAIN 21..314
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 186..188
FT /note="TXY"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10889467"
FT MOD_RES 188
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10889467"
FT MUTAGEN 52
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:10564487,
FT ECO:0000269|PubMed:10889467"
FT MUTAGEN 182
FT /note="T->A: No change in activity; when associated with F-
FT 184."
FT /evidence="ECO:0000269|PubMed:10889467"
FT MUTAGEN 184
FT /note="Y->F: No change in activity; when associated with A-
FT 182."
FT /evidence="ECO:0000269|PubMed:10889467"
FT MUTAGEN 186
FT /note="T->A: Loss of kinase activity; when associated with
FT F-188."
FT /evidence="ECO:0000269|PubMed:10564487,
FT ECO:0000269|PubMed:10889467"
FT MUTAGEN 188
FT /note="Y->F: Loss of kinase activity; when associated with
FT A-186."
FT /evidence="ECO:0000269|PubMed:10564487,
FT ECO:0000269|PubMed:10889467"
SQ SEQUENCE 370 AA; 42396 MW; 7DE7E10B8A06536E CRC64;
MDSKHSVFNV MGQEFVLQKG YEVIKGLGKG SYGVVCSAKN IEVEDNNKVA IKKITNIFSK
KMLAKRALRE IMLLQHFRNH KNITTLYDMD IVDPSKFNEL YLYEELMQAN LNSIIRSDQP
LTDAHFQSFI YQILCGLKYI HSANVLHRDL KPSNLLINAD CKLKICDFGL SRGISVNQGQ
GTEYMTEYVT TRWYRAPEVM LSFQSYSKAI DLWSVGCILA ELLGRKPFFK GSNYVDQLNQ
IFCILGTPNE NIISKIKSAS AQSYIRSLPT LPKMPYSKIF PYANPDALDL LNCLLTFDPY
DRISCEEALE HPYLIIWHDP NKEPVCSEQF DFGFEAIDSI EEIRQMIINE VSRFKGLTGN
QKLYHSISNT
