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Mitogen-activated protein kinase pmk-3 (EC 2.7.11.24) (Stress-activated protein kinase pmk-3) (p38 MAP kinase 3)

 PMK3_CAEEL              Reviewed;         474 AA.
O44514;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 2.
17-JUN-2020, entry version 159.
RecName: Full=Mitogen-activated protein kinase pmk-3;
EC=2.7.11.24;
AltName: Full=Stress-activated protein kinase pmk-3;
AltName: Full=p38 MAP kinase 3;
Name=pmk-3; ORFNames=F42G8.4;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
STRAIN=Bristol N2;
PubMed=11703092; DOI=10.1006/mcbr.2001.0300;
Berman K., McKay J., Avery L., Cobb M.;
"Isolation and characterization of pmk-(1-3): three p38 homologs in
Caenorhabditis elegans.";
Mol. Cell Biol. Res. Commun. 4:337-344(2001).
[2]
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).
[3]
FUNCTION, AND INTERACTION WITH MAK-2.
PubMed=19737525; DOI=10.1016/j.cell.2009.06.023;
Yan D., Wu Z., Chisholm A.D., Jin Y.;
"The DLK-1 kinase promotes mRNA stability and local translation in C.
elegans synapses and axon regeneration.";
Cell 138:1005-1018(2009).
[4]
FUNCTION, AND INTERACTION WITH VHP-1.
PubMed=21670305; DOI=10.1073/pnas.1104830108;
Nix P., Hisamoto N., Matsumoto K., Bastiani M.;
"Axon regeneration requires coordinate activation of p38 and JNK MAPK
pathways.";
Proc. Natl. Acad. Sci. U.S.A. 108:10738-10743(2011).
[5]
INTERACTION WITH UEV-3.
PubMed=20592265; DOI=10.1534/genetics.110.117341;
Trujillo G., Nakata K., Yan D., Maruyama I.N., Jin Y.;
"A ubiquitin E2 variant protein acts in axon termination and synaptogenesis
in Caenorhabditis elegans.";
Genetics 186:135-145(2010).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26657059; DOI=10.1371/journal.pgen.1005733;
van der Vaart A., Rademakers S., Jansen G.;
"DLK-1/p38 MAP Kinase signaling controls cilium length by regulating RAB-5
mediated endocytosis in Caenorhabditis elegans.";
PLoS Genet. 11:E1005733-E1005733(2015).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27123983; DOI=10.1371/journal.pgen.1006010;
D'Souza S.A., Rajendran L., Bagg R., Barbier L., van Pel D.M., Moshiri H.,
Roy P.J.;
"The MADD-3 LAMMER kinase interacts with a p38 MAP kinase pathway to
regulate the display of the EVA-1 guidance receptor in Caenorhabditis
elegans.";
PLoS Genet. 12:E1006010-E1006010(2016).
-!- FUNCTION: Responds to activation by environmental stress and pro-
inflammatory cytokines by phosphorylating downstream targets
(PubMed:11703092). Involved in axon regeneration after injury, probably
downstream of dlk-1 and mkk-4 and upstream of mak-2 (PubMed:21670305,
PubMed:19737525). May phosphorylate mak-2 (PubMed:19737525). Plays a
role in cilium length regulation, possibly by reducing rab-5 mediated
endocytosis (PubMed:26657059). Plays a role in the formation of muscle
connections, also called muscle arm extensions, between the body wall
and the motor axons in the dorsal and ventral cord (PubMed:27123983).
{ECO:0000269|PubMed:11703092, ECO:0000269|PubMed:19737525,
ECO:0000269|PubMed:21670305, ECO:0000269|PubMed:26657059,
ECO:0000269|PubMed:27123983}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
Evidence={ECO:0000269|PubMed:11703092};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.24; Evidence={ECO:0000269|PubMed:11703092};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11703092};
-!- ACTIVITY REGULATION: Activated by phosphorylation on threonine and
tyrosine. {ECO:0000250|UniProtKB:Q16539}.
-!- SUBUNIT: Interacts with mak-2 (PubMed:19737525). May interact with vhp-
1 (PubMed:21670305). May interact with uev-3 (PubMed:20592265).
{ECO:0000269|PubMed:19737525, ECO:0000269|PubMed:20592265,
ECO:0000269|PubMed:21670305}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11703092,
ECO:0000269|PubMed:26657059}. Cytoplasm {ECO:0000269|PubMed:26657059}.
Cell projection, axon {ECO:0000269|PubMed:26657059}. Cell projection,
dendrite {ECO:0000269|PubMed:26657059}. Cell projection, cilium
{ECO:0000269|PubMed:26657059}.
-!- TISSUE SPECIFICITY: Expressed throughout the intestine.
{ECO:0000269|PubMed:11703092}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-285 and Tyr-287, which activates the
enzyme. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Weak defect in the extension of body wall muscle
connections or arms towards the ventral nerve cord. Double knockout
with madd-3 suppresses the muscle arm extension defects, eva-1 and rab-
7 expression defects and restores the defect in the recruitment of
madd-4 to the muscle membrane in the madd-3 single knockout. Triple
knockout with madd-3 and unc-54 results in paralysis (as in the unc-54
single knockout), and suppresses the lethality phenotype in the double
madd-3 and unc-54 mutant. {ECO:0000269|PubMed:27123983}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
protein kinase family. MAP kinase subfamily. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; FO080126; CCD61404.1; -; Genomic_DNA.
PIR; T32642; T32642.
RefSeq; NP_501363.1; NM_068962.4.
SMR; O44514; -.
BioGRID; 42723; 1.
DIP; DIP-59691N; -.
IntAct; O44514; 1.
STRING; 6239.F42G8.4.1; -.
iPTMnet; O44514; -.
EPD; O44514; -.
PaxDb; O44514; -.
PeptideAtlas; O44514; -.
EnsemblMetazoa; F42G8.4a.1; F42G8.4a.1; WBGene00004057.
EnsemblMetazoa; F42G8.4a.2; F42G8.4a.2; WBGene00004057.
GeneID; 177610; -.
KEGG; cel:CELE_F42G8.4; -.
UCSC; F42G8.4.1; c. elegans.
CTD; 177610; -.
WormBase; F42G8.4a; CE29318; WBGene00004057; pmk-3.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
InParanoid; O44514; -.
KO; K04441; -.
OMA; RADHIFD; -.
OrthoDB; 741207at2759; -.
PhylomeDB; O44514; -.
Reactome; R-CEL-168638; NOD1/2 Signaling Pathway.
Reactome; R-CEL-171007; p38MAPK events.
Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-CEL-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-CEL-525793; Myogenesis.
SignaLink; O44514; -.
PRO; PR:O44514; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00004057; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
ExpressionAtlas; O44514; differential.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IMP:UniProtKB.
GO; GO:0031103; P:axon regeneration; IGI:UniProtKB.
GO; GO:0035095; P:behavioral response to nicotine; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0000165; P:MAPK cascade; IGI:WormBase.
GO; GO:0038066; P:p38MAPK cascade; IMP:WormBase.
GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IMP:UniProtKB.
GO; GO:1905868; P:regulation of 3'-UTR-mediated mRNA stabilization; IGI:UniProtKB.
GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IGI:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0050807; P:regulation of synapse organization; IGI:WormBase.
GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF00069; Pkinase; 1.
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.
1: Evidence at protein level;
ATP-binding; Cell projection; Cytoplasm; Kinase; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1..474
/note="Mitogen-activated protein kinase pmk-3"
/id="PRO_0000186305"
DOMAIN 114..419
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 124..132
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOTIF 285..287
/note="TXY"
ACT_SITE 252
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 150
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 285
/note="Phosphothreonine"
/evidence="ECO:0000250"
MOD_RES 287
/note="Phosphotyrosine"
/evidence="ECO:0000250"
SEQUENCE 474 AA; 54894 MW; E405C45FDCC6ABA9 CRC64;
MASVPSSSSL PVSHVRRHED VSTPSAPPTK RSNNQSQPPE SYEPNTWLQQ QREQEQQKKL
AAENIKKQSI EATGNNEMVG EEEEDILSKP CGPHKRRFQF VMIRNITFAI PEGYDVEPNS
IEYLGGGSFG NVIKTSAVCR DGLRRYVAIK KMREPFFDPH HARRIFRETK LLQLMRHDNI
ICALDIYTPD EENDFRDVYV VTEFAGRSLY QILKQQRDYG RRVLTDEHIK FIIYQIIRAL
KYIHSANIIH RDLKPGNLAL TDDSDLMILD FGLARSLEKK DTSLTQYVQT RWYRSPEVIY
WKIDSYTNLA DMWSLGCIAA ELLTGEPLFP GDEPNAQYQR ITQLCGSPDE ELLTKIENDN
SSAIKAVIQS YTTHKRRNFR DVFSAHNPSE DFIDLLEKLL VLDPEKRITV EEAIQHPYLA
EFSLPEDEPR ADHIFDLDDS QARTRFEWRD AVWKEIMNYK RLSSSPLIPG EADR


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Related Genes :
[pmk-3 F42G8.4] Mitogen-activated protein kinase pmk-3 (EC 2.7.11.24) (Stress-activated protein kinase pmk-3) (p38 MAP kinase 3)
[pmk-1 B0218.3] Mitogen-activated protein kinase pmk-1 (EC 2.7.11.24) (Stress-activated protein kinase pmk-1) (p38 MAP kinase 1)
[MAPK12 ERK6 SAPK3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[MAPK11 PRKM11 SAPK2 SAPK2B] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38b) (Stress-activated protein kinase 2b) (SAPK2b) (p38-2)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[MAPK13 PRKM13 SAPK4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk13] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk13 Serk4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Mapk14 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Mapk11 Prkm11] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38B)
[MAPK14 CSBP1 CSBP2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[mapk14a mapk14] Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (zp38a)
[mapk14b mapk14] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (zp38b)
[spm1 pmk1 SPBC119.08] Mitogen-activated protein kinase spm1 (MAP kinase spm1) (EC 2.7.11.24) (MAP kinase pmk1)
[p38b CG7393] Mitogen-activated protein kinase p38b (MAP kinase p38b) (MAPK p38b) (EC 2.7.11.24)
[mapk14b] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (cp38b)
[MAPK14 CSBP1] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a)
[mapk14a] Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (cp38a)
[MAPK3 ERK1 PRKM3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[MAPKAPK5 PRAK] MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAP-K5) (MAPKAPK-5) (MK-5) (MK5) (EC 2.7.11.1) (p38-regulated/activated protein kinase) (PRAK)
[MAP2K6 MEK6 MKK6 PRKMK6 SKK3] Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)
[MAPK10 JNK3 JNK3A PRKM10 SAPK1B] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase 1b) (SAPK1b) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)
[MAPK1 ERK2 PRKM1 PRKM2] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (SAPK gamma) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1) (p54 gamma)
[Mapk10 Jnk3 Prkm10 Serk2] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)
[HOG1 SSK3 YLR113W L2931 L9354.2] Mitogen-activated protein kinase HOG1 (MAP kinase HOG1) (EC 2.7.11.24) (High osmolarity glycerol response protein 1)

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