MOM4_CAEBR
ID MOM4_CAEBR Reviewed; 545 AA.
AC A8WWX1;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase mom-4;
DE EC=2.7.11.25;
GN Name=mom-4 {ECO:0000250|UniProtKB:Q9XTC6}; ORFNames=CBG03852;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP24673.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP24673.1};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9XTC6}.
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:0000250|UniProtKB:O43318};
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:0000250|UniProtKB:O43318};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O43318};
CC -!- SUBUNIT: Interacts with, and is activated by, tap-1.
CC {ECO:0000250|UniProtKB:Q9XTC6}.
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; HE600906; CAP24673.1; -; Genomic_DNA.
DR RefSeq; XP_002639286.1; XM_002639240.1.
DR AlphaFoldDB; A8WWX1; -.
DR SMR; A8WWX1; -.
DR STRING; 6238.CBG03852; -.
DR EnsemblMetazoa; CBG03852.1; CBG03852.1; WBGene00026627.
DR GeneID; 8581279; -.
DR KEGG; cbr:CBG_03852; -.
DR CTD; 8581279; -.
DR WormBase; CBG03852; CBP06575; WBGene00026627; Cbr-mom-4.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_509264_0_0_1; -.
DR InParanoid; A8WWX1; -.
DR OMA; REAKVMW; -.
DR OrthoDB; 635654at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IEA:UniProtKB-EC.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; PF00069; Pkinase; 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 3: Inferred from homology;
KW ATP-binding; Developmental protein; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..545
FT /note="Mitogen-activated protein kinase kinase kinase mom-
FT 4"
FT /id="PRO_0000351144"
FT DOMAIN 53..308
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43318,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 59..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43318,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43318,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 545 AA; 61858 MW; AA27D2EE4637E5CF CRC64;
MDTSPHSKPS SSSASQSSHS PSPAPVTAPR KTRDSGLCMT QDIPEIPTHC IDNLNSHQLG
RGTYGIVEKT RYRRSRNHEY RPAAIKYSSP IHLATLIREA KVMWALRDHS NIIKIYGLYR
DARHGQGVVM EYMDCGSMSE LIYDRKSIDY TIDHVASWLY QMASAVNTFH RNDQVHRDLK
LQNMLLCDRY RTMKLCDFGT FTAMHQSMTS NRGTPITMAP EVFRCEEYNQ KSDIYSIGII
MWQMIARNHP YNRNLSVPGL LYNVATASLR PPELDCNPIL SDFYKQCWHD DPVSRPTAAE
CLQYFTALKT EYPNGNVPLA DANTNRPVET PPPRVHRPSG LGSASGSGLG TNGRTPTASN
HLNAPQAVNT HRRNRSETIQ MKPELPYPVM PGEVAASSSG AFRGPRSQSE AKNLRDAGRS
QSGQRHPHRN APPIPIDDRR DSNESNEKDA IFMELLRNDD TRPVDPDARD EASLDIFHQH
CSSNKEYADA LLLKKEVLRA KHELLSRWPQ HQRHVELLER QNYLEQEIAK LEYNSDDDFS
ITERL
