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Database: UniProt
Entry: G7PHV3_MACFA
LinkDB: G7PHV3_MACFA
Original site: G7PHV3_MACFA 
ID   G7PHV3_MACFA            Unreviewed;       890 AA.
AC   G7PHV3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 12 {ECO:0000256|PIRNR:PIRNR038165};
DE            EC=2.7.11.25 {ECO:0000256|PIRNR:PIRNR038165};
GN   ORFNames=EGM_03300 {ECO:0000313|EMBL:EHH66328.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1] {ECO:0000313|EMBL:EHH66328.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CE-4 {ECO:0000313|EMBL:EHH66328.1};
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA   Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA   Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA   Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA   Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA   Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal models,
RT   the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
CC   -!- FUNCTION: May be an activator of the JNK/SAPK pathway.
CC       {ECO:0000256|PIRNR:PIRNR038165}.
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:0000256|ARBA:ARBA00000478};
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:0000256|ARBA:ARBA00000106};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038165};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000256|PIRNR:PIRNR038165}.
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DR   EMBL; CM001286; EHH66328.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7PHV3; -.
DR   eggNOG; KOG4721; Eukaryota.
DR   Proteomes; UP000009130; Chromosome 11.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007254; P:JNK cascade; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14059; STKc_MAP3K12_13; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017419; MAP3K12_MAP3K13.
DR   InterPro; IPR027257; MAPKKK12.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR23257:SF707; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 12; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF500741; MAPKKK12; 1.
DR   PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR038165, ECO:0000256|PIRSR:PIRSR038165-
KW   51}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|PIRNR:PIRNR038165, ECO:0000313|EMBL:EHH66328.1};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR038165};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR038165,
KW   ECO:0000256|PIRSR:PIRSR038165-51};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038165};
KW   Transferase {ECO:0000256|PIRNR:PIRNR038165}.
FT   DOMAIN          158..399
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          50..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          452..500
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        761..808
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..846
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038165-50"
FT   BINDING         164..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
FT   BINDING         185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
SQ   SEQUENCE   890 AA;  96142 MW;  6A23D5BC9D4726FE CRC64;
     MACLHETRTP SSSFGGFVST LSEASMRKLD PDTSDCTPEK DLTPTQCVLR DVVPLGGQGG
     GGPSPSPGGE PPPEPFANSV LQLHEQDAGG PGGAAGSPES RASRVRADEV RLQCQSGSGF
     LEGLFGCLRP VWTMIGKAYS TEHKQQQEDL WEVPFEEILD LQWVGSGAQG AVFLGRFHGE
     EVAVKKVRDL KETDIKHLRK LKHPNIITFK GVCTQAPCYC ILMEFCAQGQ LYEVLRAGRP
     VTPSLLVDWS MGIAGGMNYL HLHKIIHRDL KSPNMLITYD DVVKISDFGT SKELSDKSTK
     MSFAGTVAWM APEVIRNEPV SEKVDIWSFG VVLWELLTGE IPYKDVDSSA IIWGVGSNSL
     HLPVPSSCPD GFKILLRQCW NSKPRNRPSF RQILLHLDIA SADVLSTPQE TYFKSQAEWR
     EEVKLHFEKI KSEGTCLHRL EEELVMRRRE ELRHALDIRE HYERKLERAN NLYMELNALM
     LQLELKEREL LRREQALERR CPGLLKTHPS RGLLHGNTME KLIKKRNVPQ KLSPHSKRPD
     ILKTESLLPK LDAALSGVGL PGCPKGPPSP GRSRRGKTRH RKASAKGSCG DLPGLRTAVP
     PNEPGGPGSL GGGPSAWEAC PPALRGLHHD LLLRKMSSSS PDLLSAALGS RGRGATSGAG
     DPGSPPPARG DTPPSEGSAP GSTSPDSPGG AKGEPPPPVG PGEGVGLLGT GREGTSGRGG
     SRAGSQHLTP AALLYRAAVT RSQKRGISSE EEEGEVDSEV ELTSSQRWPQ SLNMRQSLST
     FSSENPSDGE EGTASEPSPS GTPEVGSTNT DERPDERSDD MCSQGSEIPL DPPPSEVIPS
     PEPSSLPIPH QELLRGKQGP PNSEDSDCDS TELDNSSSVD ALRPPASLPP
//
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