MOM4_CAEEL
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 03-AUG-2022, entry version 171.
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, ECO:0000312|WormBase:F52F12.3};
GN 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=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=2.7.11.25;
CC Evidence={ECO:0000269|PubMed:10391246, ECO:0000269|PubMed:11323434};
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=2.7.11.25; Evidence={ECO:0000269|PubMed:10391246,
CC 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_060219.7.
DR AlphaFoldDB; Q9XTC6; -.
DR SMR; Q9XTC6; -.
DR BioGRID; 38265; 10.
DR DIP; DIP-26637N; -.
DR IntAct; Q9XTC6; 1.
DR STRING; 6239.F52F12.3; -.
DR EPD; Q9XTC6; -.
DR PaxDb; Q9XTC6; -.
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 CTD; 172842; -.
DR WormBase; F52F12.3; CE24994; WBGene00003396; mom-4.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00940000170225; -.
DR HOGENOM; CLU_509264_0_0_1; -.
DR InParanoid; Q9XTC6; -.
DR OMA; REAKVMW; -.
DR OrthoDB; 635654at2759; -.
DR PhylomeDB; Q9XTC6; -.
DR SignaLink; Q9XTC6; -.
DR PRO; PR:Q9XTC6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003396; Expressed in germ line (C elegans) and 4 other 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:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion 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; IEA:RHEA.
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:0018107; P:peptidyl-threonine phosphorylation; IDA:WormBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017421; MAPKKK7.
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; PTHR46716; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 338..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..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
