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Mitogen-activated protein kinase mpk-1 (EC 2.7.11.24) (MAP kinase sur-1)

 MPK1_CAEEL              Reviewed;         444 AA.
P39745; Q9U3F3;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
25-NOV-2002, sequence version 2.
10-OCT-2018, entry version 169.
RecName: Full=Mitogen-activated protein kinase mpk-1;
EC=2.7.11.24 {ECO:0000269|PubMed:20624915};
AltName: Full=MAP kinase sur-1;
Name=mpk-1; Synonyms=sur-1; ORFNames=F43C1.2;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND MUTAGENESIS OF ALA-106.
STRAIN=Bristol N2;
PubMed=8299935; DOI=10.1101/gad.8.2.147;
Wu Y., Han M.;
"Suppression of activated Let-60 ras protein defines a role of
Caenorhabditis elegans Sur-1 MAP kinase in vulval differentiation.";
Genes Dev. 8:147-159(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
STRAIN=Bristol N2;
PubMed=8299936; DOI=10.1101/gad.8.2.160;
Lackner M.R., Kornfeld K., Miller L.M., Horvitz H.R., Kim S.K.;
"A MAP kinase homolog, mpk-1, is involved in ras-mediated induction of
vulval cell fates in Caenorhabditis elegans.";
Genes Dev. 8:160-173(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4]
FUNCTION.
STRAIN=Bristol N2;
PubMed=11689700; DOI=10.1128/MCB.21.23.8104-8116.2001;
Schutzman J.L., Borland C.Z., Newman J.C., Robinson M.K., Kokel M.,
Stern M.J.;
"The Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-
like multisubstrate adaptor protein in fibroblast growth factor signal
transduction.";
Mol. Cell. Biol. 21:8104-8116(2001).
[5]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ALA-106.
PubMed=15268855; DOI=10.1016/j.cub.2004.07.022;
Nicholas H.R., Hodgkin J.;
"The ERK MAP kinase cascade mediates tail swelling and a protective
response to rectal infection in C. elegans.";
Curr. Biol. 14:1256-1261(2004).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16319922; DOI=10.1038/sj.emboj.7600901;
Lee M.H., Hook B., Lamont L.B., Wickens M., Kimble J.;
"LIP-1 phosphatase controls the extent of germline proliferation in
Caenorhabditis elegans.";
EMBO J. 25:88-96(2006).
[7]
FUNCTION, INTERACTION WITH GCK-1, DEVELOPMENTAL STAGE, PHOSPHORYLATION
AT THR-256 AND TYR-258, AND DISRUPTION PHENOTYPE.
PubMed=19826475; DOI=10.1371/journal.pone.0007450;
Schouest K.R., Kurasawa Y., Furuta T., Hisamoto N., Matsumoto K.,
Schumacher J.M.;
"The germinal center kinase GCK-1 is a negative regulator of MAP
kinase activation and apoptosis in the C. elegans germline.";
PLoS ONE 4:E7450-E7450(2009).
[8]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, TISSUE
SPECIFICITY, PHOSPHORYLATION AT THR-256 AND TYR-258, AND DISRUPTION
PHENOTYPE.
PubMed=20624915; DOI=10.1074/jbc.M110.146274;
Okuyama T., Inoue H., Ookuma S., Satoh T., Kano K., Honjoh S.,
Hisamoto N., Matsumoto K., Nishida E.;
"The ERK-MAPK pathway regulates longevity through SKN-1 and insulin-
like signaling in Caenorhabditis elegans.";
J. Biol. Chem. 285:30274-30281(2010).
[9]
FUNCTION.
PubMed=21160027; DOI=10.1152/ajpcell.00343.2010;
Falin R.A., Miyazaki H., Strange K.;
"C. elegans STK39/SPAK ortholog-mediated inhibition of ClC anion
channel activity is regulated by WNK-independent ERK kinase
signaling.";
Am. J. Physiol. 300:C624-635(2011).
[10]
FUNCTION, ACTIVITY REGULATION, DEVELOPMENTAL STAGE, DISRUPTION
PHENOTYPE, PHOSPHORYLATION AT THR-256 AND TYR-258, AND MUTAGENESIS OF
VAL-216.
PubMed=21901106; DOI=10.1371/journal.pgen.1002238;
Rutkowski R., Dickinson R., Stewart G., Craig A., Schimpl M.,
Keyse S.M., Gartner A.;
"Regulation of Caenorhabditis elegans p53/CEP-1-dependent germ cell
apoptosis by Ras/MAPK signaling.";
PLoS Genet. 7:E1002238-E1002238(2011).
[11]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT
THR-256 AND TYR-258, AND DISRUPTION PHENOTYPE.
PubMed=22820175; DOI=10.1016/j.bbamcr.2012.07.006;
Cha D.S., Datla U.S., Hollis S.E., Kimble J., Lee M.H.;
"The Ras-ERK MAPK regulatory network controls dedifferentiation in
Caenorhabditis elegans germline.";
Biochim. Biophys. Acta 1823:1847-1855(2012).
[12]
FUNCTION, MUTAGENESIS OF ALA-106, AND DISRUPTION PHENOTYPE.
PubMed=27525822; DOI=10.1371/journal.ppat.1005826;
Gravato-Nobre M.J., Vaz F., Filipe S., Chalmers R., Hodgkin J.;
"The invertebrate lysozyme effector ILYS-3 is systemically activated
in response to danger signals and confers antimicrobial protection in
C. elegans.";
PLoS Pathog. 12:E1005826-E1005826(2016).
-!- FUNCTION: Function in let-60 Ras signaling pathway; acts
downstream of lin-45 raf kinase, but before the lin-1 gene product
in controlling vulval cell differentiation (PubMed:8299935,
PubMed:8299936). Plays a negative role in proximal germline
proliferation in the mitotic zone (PubMed:16319922). Required for
progression of developing oocytes through the pachytene stage
(PubMed:16319922, PubMed:19826475, PubMed:21901106). In oocytes,
inhibits the activity of the chloride channel clh-3, likely by
activating gck-3 (PubMed:21160027). Plays a role in response to
M.nematophilum-mediated bacterial infection by promoting tail
swelling and preventing constipation (PubMed:15268855). Involved
in fluid homeostasis (PubMed:11689700). In addition, involved in
the up-regulation of lysozyme ilys-3 expression in the intestine
in responses to M.nematophilum-mediated bacterial infection
(PubMed:27525822). By phosphorylating transcription factor skn-1
(isoform c) may play a role in increasing life span downstream of
lin-45, let-60 and mek-2 (PubMed:20624915). By up-regulating cep-1
and down-regulating gld-1 expression in the late pachytene stage,
plays a role in germline apoptosis in response to DNA damage
(PubMed:21901106). Regulates egl-1 expression in response to DNA
damage, probably upstream of cep-1 (PubMed:21901106).
{ECO:0000269|PubMed:11689700, ECO:0000269|PubMed:15268855,
ECO:0000269|PubMed:16319922, ECO:0000269|PubMed:19826475,
ECO:0000269|PubMed:20624915, ECO:0000269|PubMed:21160027,
ECO:0000269|PubMed:21901106, ECO:0000269|PubMed:27525822,
ECO:0000269|PubMed:8299935, ECO:0000269|PubMed:8299936}.
-!- FUNCTION: Isoform b: Suppresses germline tumor formation by
preventing the dedifferentiation of secondary spermatocytes
probably upstream of rskn-1. {ECO:0000269|PubMed:22820175}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20624915}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:20624915};
-!- ACTIVITY REGULATION: Activated by dual phosphorylation at Thr-256
and Tyr-258 (PubMed:20624915). May be inactivated by lip-1-
mediated dephosphorylation (PubMed:21901106).
{ECO:0000269|PubMed:20624915, ECO:0000269|PubMed:21901106}.
-!- SUBUNIT: Isoform a interacts with gck-1 (via N-terminus).
{ECO:0000269|PubMed:19826475}.
-!- INTERACTION:
O02289:gla-3; NbExp=3; IntAct=EBI-321013, EBI-317795;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=b;
IsoId=P39745-1; Sequence=Displayed;
Name=a;
IsoId=P39745-2; Sequence=VSP_004848;
-!- TISSUE SPECIFICITY: Expressed in cells lining the rectum
(PubMed:15268855, PubMed:20624915). Isoform a is expressed in
nervous system, body wall muscles and posterior intestine
(PubMed:20624915). Isoform b expression may be restricted to
germline (PubMed:22820175). {ECO:0000269|PubMed:15268855,
ECO:0000269|PubMed:20624915, ECO:0000269|PubMed:22820175}.
-!- DEVELOPMENTAL STAGE: The phosphorylated form is present in early
to mid pachytene, is absent in late pachytene and
diplotene/diakinesis stages and is again present in oocytes when
they reach the spermatheca (PubMed:19826475, PubMed:21901106,
PubMed:22820175). The phosphorylated form is also present in sperm
(PubMed:22820175). {ECO:0000269|PubMed:19826475,
ECO:0000269|PubMed:21901106, ECO:0000269|PubMed:22820175}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Isoform a is phosphorylated at the pachytene stage during
oogenesis and is negatively regulated by gck-1. Isoform b is
phosphorylated in proximal oocytes. {ECO:0000269|PubMed:19826475}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an increase
in the number of germline cells in the mitotic zone, a lack of
transition zone and a defect in pachytene progression resulting in
a proximal gonad devoid of nuclei (PubMed:19826475,
PubMed:16319922). Causes sterility (PubMed:19826475). RNAi-
mediated knockdown in adults decreases lifespan (PubMed:20624915).
RNAi-mediated knockdown of isoform b in lip-1 and puf-8 double
mutant causes a decrease in number of germline tumors
(PubMed:22820175). RNAi-mediated knockdown causes a reduction in
intestinal ilys-3 expression in response to M.nematophilum-
mediated bacterial infection (PubMed:27525822).
{ECO:0000269|PubMed:16319922, ECO:0000269|PubMed:19826475,
ECO:0000269|PubMed:20624915, ECO:0000269|PubMed:22820175,
ECO:0000269|PubMed:27525822}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
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EMBL; U03879; AAA18956.1; -; mRNA.
EMBL; U27124; AAA73482.1; -; mRNA.
EMBL; Z46937; CAA87057.1; -; Genomic_DNA.
EMBL; Z46937; CAB60996.1; -; Genomic_DNA.
PIR; A36977; A36977.
PIR; A36978; A36978.
RefSeq; NP_001022583.1; NM_001027412.3.
RefSeq; NP_001022584.1; NM_001027413.2. [P39745-1]
UniGene; Cel.34032; -.
ProteinModelPortal; P39745; -.
SMR; P39745; -.
BioGrid; 40782; 67.
DIP; DIP-26227N; -.
IntAct; P39745; 52.
MINT; P39745; -.
STRING; 6239.F43C1.2b; -.
iPTMnet; P39745; -.
EPD; P39745; -.
PaxDb; P39745; -.
PeptideAtlas; P39745; -.
EnsemblMetazoa; F43C1.2a; F43C1.2a; WBGene00003401. [P39745-2]
EnsemblMetazoa; F43C1.2b; F43C1.2b; WBGene00003401. [P39745-1]
GeneID; 175545; -.
KEGG; cel:CELE_F43C1.2; -.
UCSC; F43C1.2a.1; c. elegans. [P39745-1]
CTD; 175545; -.
WormBase; F43C1.2a; CE01583; WBGene00003401; mpk-1. [P39745-2]
WormBase; F43C1.2b; CE24971; WBGene00003401; mpk-1. [P39745-1]
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00910000144035; -.
HOGENOM; HOG000233024; -.
InParanoid; P39745; -.
KO; K04371; -.
OMA; MEKCLTF; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; P39745; -.
BRENDA; 2.7.11.24; 1045.
Reactome; R-CEL-110056; MAPK3 (ERK1) activation.
Reactome; R-CEL-112409; RAF-independent MAPK1/3 activation.
Reactome; R-CEL-112411; MAPK1 (ERK2) activation.
Reactome; R-CEL-198753; ERK/MAPK targets.
Reactome; R-CEL-202670; ERKs are inactivated.
Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-CEL-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-CEL-375165; NCAM signaling for neurite out-growth.
Reactome; R-CEL-437239; Recycling pathway of L1.
Reactome; R-CEL-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-CEL-444257; RSK activation.
Reactome; R-CEL-445144; Signal transduction by L1.
Reactome; R-CEL-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-CEL-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-CEL-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-CEL-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-CEL-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
Reactome; R-CEL-5674135; MAP2K and MAPK activation.
Reactome; R-CEL-5674499; Negative feedback regulation of MAPK pathway.
Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
Reactome; R-CEL-6798695; Neutrophil degranulation.
Reactome; R-CEL-74749; Signal attenuation.
Reactome; R-CEL-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
SignaLink; P39745; -.
PRO; PR:P39745; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00003401; Expressed in 6 organ(s), highest expression level in germ line (C elegans).
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004707; F:MAP kinase activity; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0001556; P:oocyte maturation; IMP:WormBase.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IMP:WormBase.
GO; GO:0007265; P:Ras protein signal transduction; IGI:WormBase.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0040025; P:vulval development; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008349; MAPK_ERK1/2.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01770; ERK1ERK2MAPK.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell cycle; Complete proteome;
Differentiation; Kinase; Magnesium; Meiosis; Metal-binding;
Nucleotide-binding; Oogenesis; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 444 Mitogen-activated protein kinase mpk-1.
/FTId=PRO_0000186306.
DOMAIN 96 384 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 102 110 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 256 258 TXY.
ACT_SITE 220 220 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 125 125 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 256 256 Phosphothreonine.
{ECO:0000269|PubMed:19826475,
ECO:0000269|PubMed:20624915,
ECO:0000269|PubMed:21901106,
ECO:0000269|PubMed:22820175}.
MOD_RES 258 258 Phosphotyrosine.
{ECO:0000269|PubMed:19826475,
ECO:0000269|PubMed:20624915,
ECO:0000269|PubMed:21901106,
ECO:0000269|PubMed:22820175}.
VAR_SEQ 1 68 Missing (in isoform a).
{ECO:0000303|PubMed:8299936}.
/FTId=VSP_004848.
MUTAGEN 106 106 A->V: In ku1; loss of function and ATP-
binding. Lack of tail swelling, severe
constipation and loss of ilys-3
expression up-regulation following
M.nematophilium infection.
{ECO:0000269|PubMed:15268855,
ECO:0000269|PubMed:27525822,
ECO:0000269|PubMed:8299935}.
MUTAGEN 216 216 V->G: In ga111; at the restrictive
temperature of 25 degrees Celsius, causes
an increase in gld-1 expression and a
loss of cep-1 expression in late
pachytene germ cells. Loss of egl-1 mRNA
expression in response to gamma
irradiation. 70 percent of mutants have
germ cells arrested at the pachytene
stage. Partial phosphorylation at Thr-256
and Tyr-258.
{ECO:0000269|PubMed:21901106}.
CONFLICT 9 10 LC -> FF (in Ref. 2; AAA18956).
{ECO:0000305}.
SEQUENCE 444 AA; 50663 MW; 11BA27D17641980D CRC64;
MPTWIPNNLC AQPTTRNAKP PSNGHPQATQ QQSAPGSLAY RNSSNIPNGA TNHVRQQKWQ
YTRSGHRKMA DGEAVISTVN NVEEVHGQLF EVAPRYVNLS YIGEGAYGMV ASALDTITRD
RVAIKKISPF EHQTFCQRTL REIKILNRFK HENIINIQEI IRSETVDSLK DIYIVQCLME
TDLYKLLKTQ KLSNDHVCYF LYQILRGLKY IHSANVLHRD LKPSNLLLNT TCDLKICDFG
LARVTDPQTD HTGFLTEYVA TRWYRAPEIM LNSKGYTKSI DVWSVGCILA EMLSNRPLFP
GKHYLDQLNL ILAVVGSPSN ADLQCIINDK ARSYLISLPH KPKQPWARLY PGADPRALDL
LDKMLTFNPH NRIDIEQALA HPYLEQYYDP GDEPVCEEPF TLEMEFDDLP KEKLKELIWE
EAEAHHRRME AEAAARNNGG QNPV


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E1206m ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
E1206r ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
U1206m CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
U1206r CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T


 

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