ID   MOM4_CAEEL              Reviewed;         536 AA.
AC   Q9XTC6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   04-NOV-2026, entry version 189.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase mom-4;
DE            EC=2.7.11.25 {ECO:0000269|PubMed:10391246, ECO:0000269|PubMed:11323434};
GN   Name=mom-4 {ECO:0000312|EMBL:AAD39816.1,
GN   ECO:0000312|WormBase:F52F12.3}; ORFNames=F52F12.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAD37359.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:AAD37359.1};
RX   PubMed=10488343; DOI=10.1016/s1097-2765(00)80375-5;
RA   Shin T.H., Yasuda J., Rocheleau C.E., Lin R., Soto M., Bei Y., Davis R.J.,
RA   Mello C.C.;
RT   "MOM-4, a MAP kinase kinase kinase-related protein, activates WRM-1/LIT-1
RT   kinase to transduce anterior/posterior polarity signals in C. elegans.";
RL   Mol. Cell 4:275-280(1999).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAD39816.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP   INTERACTION WITH TAP-1.
RC   STRAIN=Bristol N2 {ECO:0000269|PubMed:10391246};
RX   PubMed=10391246; DOI=10.1038/21666;
RA   Meneghini M.D., Ishitani T., Carter J.C., Hisamoto N., Ninomiya-Tsuji J.,
RA   Thorpe C.J., Hamill D.R., Matsumoto K., Bowerman B.;
RT   "MAP kinase and Wnt pathways converge to downregulate an HMG-domain
RT   repressor in Caenorhabditis elegans.";
RL   Nature 399:793-797(1999).
RN   [3] {ECO:0000312|EMBL:CAB60998.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB60998.1};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9288749; DOI=10.1016/s0092-8674(00)80530-9;
RA   Thorpe C.J., Schlesinger A., Carter J.C., Bowerman B.;
RT   "Wnt signaling polarizes an early C. elegans blastomere to distinguish
RT   endoderm from mesoderm.";
RL   Cell 90:695-705(1997).
RN   [5] {ECO:0000305}
RP   CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH TAP-1, AND PHOSPHORYLATION.
RX   PubMed=11323434; DOI=10.1074/jbc.m102631200;
RA   Ono K., Ohtomo T., Sato S., Sugamata Y., Suzuki M., Hisamoto N.,
RA   Ninomiya-Tsuji J., Tsuchiya M., Matsumoto K.;
RT   "An evolutionarily conserved motif in the TAB1 C-terminal region is
RT   necessary for interaction with and activation of TAK1 MAPKKK.";
RL   J. Biol. Chem. 276:24396-24400(2001).
RN   [6] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=16077004; DOI=10.1101/gad.1323705;
RA   Nakamura K., Kim S., Ishidate T., Bei Y., Pang K., Shirayama M.,
RA   Trzepacz C., Brownell D.R., Mello C.C.;
RT   "Wnt signaling drives WRM-1/beta-catenin asymmetries in early C. elegans
RT   embryos.";
RL   Genes Dev. 19:1749-1754(2005).
CC   -!- FUNCTION: Part of the Wnt signaling pathway essential for the
CC       specification of the mesodermal cell fate in early embryos. Stimulates
CC       the wrm-1/lit-1-dependent phosphorylation of pop-1 and plays a role in
CC       the initial nuclear accumulation of wrm-1.
CC       {ECO:0000269|PubMed:10391246, ECO:0000269|PubMed:10488343,
CC       ECO:0000269|PubMed:16077004, ECO:0000269|PubMed:9288749}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=2.7.11.25;
CC         Evidence={ECO:0000269|PubMed:10391246, ECO:0000269|PubMed:11323434};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC         Evidence={ECO:0000269|PubMed:10391246, ECO:0000269|PubMed:11323434};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10391246, ECO:0000269|PubMed:11323434};
CC   -!- SUBUNIT: Interacts with, and is activated by, tap-1.
CC       {ECO:0000269|PubMed:10391246, ECO:0000269|PubMed:11323434}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the embryo.
CC       {ECO:0000269|PubMed:10488343}.
CC   -!- PTM: May be autophosphorylated. {ECO:0000269|PubMed:11323434}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal with severely defective
CC       embryonic morphogenesis with no endoderm and excess mesoderm.
CC       {ECO:0000269|PubMed:9288749}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000250|UniProtKB:O43318}.
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DR   EMBL; AF143242; AAD37359.1; -; mRNA.
DR   EMBL; AF145377; AAD39816.1; -; mRNA.
DR   EMBL; Z83228; CAB60998.1; -; Genomic_DNA.
DR   RefSeq; NP_492620.1; NM_060219.11.
DR   AlphaFoldDB; Q9XTC6; -.
DR   SMR; Q9XTC6; -.
DR   BioGRID; 38265; 13.
DR   DIP; DIP-26637N; -.
DR   FunCoup; Q9XTC6; 2182.
DR   IntAct; Q9XTC6; 1.
DR   STRING; 6239.F52F12.3.1; -.
DR   PaxDb; 6239-F52F12.3.1; -.
DR   PeptideAtlas; Q9XTC6; -.
DR   EnsemblMetazoa; F52F12.3.1; F52F12.3.1; WBGene00003396.
DR   GeneID; 172842; -.
DR   KEGG; cel:CELE_F52F12.3; -.
DR   UCSC; F52F12.3; c. elegans.
DR   AGR; WB:WBGene00003396; -.
DR   CTD; 172842; -.
DR   WormBase; F52F12.3; CE24994; WBGene00003396; mom-4.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_509264_0_0_1; -.
DR   InParanoid; Q9XTC6; -.
DR   OMA; AIYHEHG; -.
DR   OrthoDB; 10013149at2759; -.
DR   PhylomeDB; Q9XTC6; -.
DR   Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR   SignaLink; Q9XTC6; -.
DR   PRO; PR:Q9XTC6; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003396; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; HDA:WormBase.
DR   GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:WormBase.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; EXP:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR   GO; GO:0008356; P:asymmetric cell division; IMP:WormBase.
DR   GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
DR   GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:UniProtKB.
DR   GO; GO:0007492; P:endoderm development; IMP:WormBase.
DR   GO; GO:0001714; P:endodermal cell fate specification; IMP:WormBase.
DR   GO; GO:0000165; P:MAPK cascade; IDA:WormBase.
DR   GO; GO:0042694; P:muscle cell fate specification; IMP:WormBase.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR46716; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7; 1.
DR   PANTHER; PTHR46716:SF1; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Developmental protein; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT   CHAIN           1..536
FT                   /note="Mitogen-activated protein kinase kinase kinase mom-
FT                   4"
FT                   /id="PRO_0000351145"
FT   DOMAIN          51..305
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O43318,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         57..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43318,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43318,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   536 AA;  61543 MW;  686DD6C3A91F7EB9 CRC64;
     MDNSSQSKPS SSSSSHSPSP AAITPTQRTT RDSGLCSTID IPEIQAQCID NLNSHYLGKG
     TYGLVEKTRY RKTRQDDFRP AAIKYSSQLH MATLIREAKV MWDLRNHPNI IKIYGLYKSP
     RNGQGVVMEY MDCGSMADLL YDRTHINYTI DHVASWMFQL SSAVDFFHSN SQVHRDLKLQ
     NMLLSDRYRT MKLCDFGTFT SMHQSMTSNR GTPITMAPEV FRCEQYNMKS DIYSIGIIMW
     QIIARNHPYR RDLSVPGLLY NVATANLRPQ ELECNPILSE FYKKCWNDNA DIRPTSSECV
     EYFTLLKDEY PNGSVPLSDS STNGPAETPP PHAHRPTMLG TSSGSGIGSN NRTPTASKLL
     NPQQPGQGHR RNRSETFVVQ PDLPYPTVPG EAGASRIPKS QSEAKNFRDR AKSEQRQPHR
     DARPPPPFEH RRDSNDEEKH AVFMNICSNE ETRPIDPDTR DEKSLEIFHQ HCDNNKQYAD
     AWVIKKEVMR AKHELIAQWP QHDHTVELLE RKYYLEQEIA RYRDIQDDNY FSTERM
//