Reviewed, UniProtKB/Swiss-Prot O42781 (MAPK2_PNECA)

Names and origin

Protein names

Recommended name:
    Mitogen-activated protein kinase 2
    EC=2.7.11.24
Alternative name(s):
    PCM

Gene names

Name:	MKP2
Synonyms:	MAPK

Organism

Pneumocystis carinii

Taxonomic identifier

4754 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Pneumocystidomycetes › Pneumocystidaceae › Pneumocystis

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Serine-threonine protein kinase which may be involved in pheromone signaling. Functionally complements the MAPK pheromone signaling pathway in S.cerevisiae. Ref.1 Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1
Cofactor	Divalent cations including magnesium and manganese. Calcium, copper and nickel have little effect on kinase activity while cobalt abolishes kinase activity. Ref.3
Enzyme regulation	Activated by tyrosine and threonine phosphorylation By similarity. Inhibited by the MEK inhibitor U0126 but not by the p38 inhibitor SB203580. Ref.3 UniProtKB P16892
Subcellular location	Nucleus By similarity. UniProtKB P27638
Developmental stage	Activity is significantly higher in trophic forms than in cysts. Ref.3
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Dually phosphorylated on Thr-176 and Tyr-178, which activates the enzyme By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5. Ref.3 Temperature dependence: Optimum temperature is 30-35 degrees Celsius. Ref.3

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cell cycle arrest in response to pheromone Ref.1 Non-traceable author statement. Source: UniProtKB protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro signal transduction Ref.3 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 351	351	Mitogen-activated protein kinase 2		PRO_0000247744
Regions
	Domain	16 – 304	289	Protein kinase
	Nucleotide binding	22 – 30	9	ATP By similarity
	Motif	176 – 178	3	TXY
Sites
	Active site	140	1	Proton acceptor By similarity
	Binding site	45	1	ATP By similarity
Amino acid modifications
	Modified residue	176	1	Phosphothreonine By similarity UniProtKB P16892
	Modified residue	178	1	Phosphotyrosine By similarity UniProtKB P16892

Sequences

	Sequence		Length	Mass (Da)
	O42781-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 53766B1A95F050AB	FASTA	351	40,574
	10 20 30 40 50 60 MTASSRNVRF NVSDDYEILD VIGEGAYGIV CSAIHKPSGQ KVAIKKISPF DHSMFCLRTL 70 80 90 100 110 120 REMKLLRYFN HENIISILDI QQPQDFESFS EVYLIQELME TDMHRVIRTQ DLSDDHCQYF 130 140 150 160 170 180 IYQILRALKA MHSADILHRD LKPSNLLLNA NCDLKVCDFG LARSAVSTED SSSFMTEYVA 190 200 210 220 230 240 TRWYRAPEIM LTFKEYTKAI DIWSVGCILA EMLSGRPLFP GKDYHHQLML ILDVLGTPTM 250 260 270 280 290 300 EDYYGIKSRR AREYIRSLPF KKRVSFASIF PRANPLALDL LEKLLAFNPA KRVTAEEALQ 310 320 330 340 350 HNYLEPYHDP DDEPTAPPIS PSFFDFDRIK DSLTKNDLKI LIYKEIMSMN N

References

[1]	"Characterization of a mitogen-activated protein kinase from Pneumocystis carinii." Thomas C.F. Jr., Kottom T.J., Leof E.B., Limper A.H. Am. J. Physiol. 275:L193-L199(1998) [PubMed: 9688951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
[2]	Smulian A.G. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complementation and characterization of the Pneumocystis carinii MAPK, PCM." Vohra P.K., Puri V., Thomas C.F. Jr. FEBS Lett. 551:139-146(2003) [PubMed: 12965219] [Abstract] Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF043941 mRNA. Translation: AAC98088.1. AF077548 Genomic DNA. Translation: AAC27327.1.
3D structure databases
HSSP	HSSP built from PDB template 1KV1 based on UniProtKB Q16539.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.11.24. 3409.
Family and domain databases
InterPro	IPR003527. MAP_kinase_CS. IPR008352. MAPK_p38. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR01773. P38MAPKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MAPK2_PNECA

Accession

Primary (citable) accession number: O42781

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	June 1, 1998
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)