MAPK2_PNECA
ID MAPK2_PNECA Reviewed; 351 AA.
AC O42781;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Mitogen-activated protein kinase 2;
DE EC=2.7.11.24;
DE AltName: Full=PCM;
GN Name=MKP2 {ECO:0000312|EMBL:AAC98088.1};
GN Synonyms=MAPK {ECO:0000312|EMBL:AAC27327.1};
OS Pneumocystis carinii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX NCBI_TaxID=4754;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC98088.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9688951; DOI=10.1152/ajplung.1998.275.1.l193;
RA Thomas C.F. Jr., Kottom T.J., Leof E.B., Limper A.H.;
RT "Characterization of a mitogen-activated protein kinase from Pneumocystis
RT carinii.";
RL Am. J. Physiol. 275:L193-L199(1998).
RN [2] {ECO:0000312|EMBL:AAC27327.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smulian A.G.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
RX PubMed=12965219; DOI=10.1016/s0014-5793(03)00914-1;
RA Vohra P.K., Puri V., Thomas C.F. Jr.;
RT "Complementation and characterization of the Pneumocystis carinii MAPK,
RT PCM.";
RL FEBS Lett. 551:139-146(2003).
CC -!- FUNCTION: Serine-threonine protein kinase which may be involved in
CC pheromone signaling. Functionally complements the MAPK pheromone
CC signaling pathway in S.cerevisiae. {ECO:0000269|PubMed:12965219,
CC ECO:0000269|PubMed:9688951}.
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:9688951};
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:9688951};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12965219};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12965219};
CC Note=Divalent cations including magnesium and manganese.
CC {ECO:0000269|PubMed:12965219};
CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine
CC phosphorylation (By similarity). Inhibited by the MEK inhibitor U0126
CC but not by the p38 inhibitor SB203580. Cobalt abolishes kinase
CC activity, while calcium, copper and nickel have little effect on kinase
CC activity. {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:12965219};
CC Temperature dependence:
CC Optimum temperature is 30-35 degrees Celsius.
CC {ECO:0000269|PubMed:12965219};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27638}.
CC -!- DEVELOPMENTAL STAGE: Activity is significantly higher in trophic forms
CC than in cysts. {ECO:0000269|PubMed:12965219}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-176 and Tyr-178, which activates the
CC enzyme. {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; AF043941; AAC98088.1; -; mRNA.
DR EMBL; AF077548; AAC27327.1; -; Genomic_DNA.
DR AlphaFoldDB; O42781; -.
DR SMR; O42781; -.
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; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000751; P:mitotic cell cycle G1 arrest in response to pheromone; NAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0019236; P:response to pheromone; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008352; MAPK_p38-like.
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; PR01773; P38MAPKINASE.
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; Nucleus; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..351
FT /note="Mitogen-activated protein kinase 2"
FT /id="PRO_0000247744"
FT DOMAIN 16..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 176..178
FT /note="TXY"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16892"
FT MOD_RES 178
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16892"
SQ SEQUENCE 351 AA; 40574 MW; 53766B1A95F050AB CRC64;
MTASSRNVRF NVSDDYEILD VIGEGAYGIV CSAIHKPSGQ KVAIKKISPF DHSMFCLRTL
REMKLLRYFN HENIISILDI QQPQDFESFS EVYLIQELME TDMHRVIRTQ DLSDDHCQYF
IYQILRALKA MHSADILHRD LKPSNLLLNA NCDLKVCDFG LARSAVSTED SSSFMTEYVA
TRWYRAPEIM LTFKEYTKAI DIWSVGCILA EMLSGRPLFP GKDYHHQLML ILDVLGTPTM
EDYYGIKSRR AREYIRSLPF KKRVSFASIF PRANPLALDL LEKLLAFNPA KRVTAEEALQ
HNYLEPYHDP DDEPTAPPIS PSFFDFDRIK DSLTKNDLKI LIYKEIMSMN N
