M4K3_RAT
ID M4K3_RAT Reviewed; 873 AA.
AC Q924I2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=Germinal center kinase-related protein kinase;
DE Short=GLK;
DE AltName: Full=MAPK/ERK kinase kinase kinase 3;
DE Short=MEK kinase kinase 3;
DE Short=MEKKK 3;
GN Name=Map4k3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAK53214.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-75.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-873, AND INTERACTION WITH SH3GL2.
RX PubMed=11384986; DOI=10.1074/jbc.m103198200;
RA Ramjaun A.R., Angers A., Legendre-Guillemin V., Tong X.-K., McPherson P.S.;
RT "Endophilin regulates JNK activation through its interaction with the
RT germinal center kinase-like kinase.";
RL J. Biol. Chem. 276:28913-28919(2001).
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the JUN N-terminal pathway (By similarity).
CC {ECO:0000250}.
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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q8IVH8};
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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q8IVH8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IVH8};
CC -!- SUBUNIT: Interacts with SH3GL2. Interaction appears to regulate MAP4K3-
CC mediated JNK activation. {ECO:0000269|PubMed:11384986}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AI112857; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF312224; AAK53214.1; -; mRNA.
DR RefSeq; NP_596898.1; NM_133407.1.
DR AlphaFoldDB; Q924I2; -.
DR SMR; Q924I2; -.
DR BioGRID; 251030; 1.
DR MINT; Q924I2; -.
DR STRING; 10116.ENSRNOP00000010366; -.
DR iPTMnet; Q924I2; -.
DR PhosphoSitePlus; Q924I2; -.
DR PaxDb; Q924I2; -.
DR PRIDE; Q924I2; -.
DR Ensembl; ENSRNOT00000010366; ENSRNOP00000010366; ENSRNOG00000007172.
DR GeneID; 170920; -.
DR KEGG; rno:170920; -.
DR UCSC; RGD:621280; rat.
DR CTD; 8491; -.
DR RGD; 621280; Map4k3.
DR eggNOG; KOG0576; Eukaryota.
DR InParanoid; Q924I2; -.
DR OrthoDB; 996262at2759; -.
DR BRENDA; 2.7.11.25; 5301.
DR PRO; PR:Q924I2; -.
DR Proteomes; UP000002494; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0008349; F:MAP kinase kinase kinase 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; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..873
FT /note="Mitogen-activated protein kinase kinase kinase
FT kinase 3"
FT /id="PRO_0000086279"
FT DOMAIN 16..273
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 535..846
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 389..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVH8"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JP0"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVH8"
SQ SEQUENCE 873 AA; 98679 MW; 2EF27843498FA81D CRC64;
MNPGFDLSRR NPQEDFELIQ RIGSGTYGDV YKARNVNTGE LAAIKVIKLE PGEDFAVVQQ
EIIMMKDCKH ANIVAYFGSY LRRDKLWICM EFCGGGSLQD IYHVTGPLSE LQIAYVSRET
LQGLYYLHSK GKMHRDIKGA NILLTDNGHV KLADFGVSAQ ITATIAKRKS FIGTPYWMAP
EVAAVERKGG YNQLCDLWAV GITAIELAEL QPPMFDLHPM RALFLMTKSN FQPPKLKDKL
KWSNSFHHFV KMALTKNPKK RPTAEKLLQH PFVTQPLTRS LAIELLDKVN NPDHSTYHDF
DDDDPEPLVA VPHRIPSTSR NVREEKTRSE INFGQVKFDP PLRKETEPHH ELDLQLEYGQ
GHQSNYFLGG NKSLLKSVEE ELHQRGHVAH LEDDEGDDDD SKHSTLKAKV PPPLPPKPKS
ISIPQDTHSS EDSNQGTIKR CPSSGSPAKP SHVPPRPPPP RLPPQKPAVL GNGVSSFQLN
GERDGSVHQQ QSEQRGTNLS RKEKKDVPKP ISNGLPPTPK VHMGACFSKV FNGCPLKIHC
ATSWINPDTR DQYLIFGAEE GIYTLNLNEL HETSMEQLFP RRCTWLYVMN NCLLSVSGKA
SQLYSHNLPG LFDYARQMQK LPVAIPAHKL PDRILPRKFA VSAKIPETKW CQKCCVVRNP
YTGHKYLCGA LQTSIVLLEW VEPMQKFMLI KHIEFPMPCP LRMFEMLVVP EQEYPLVCVG
VSRGRDFNQV VRFETVNPNS TSSWFTESDT PQTNVTHVTQ LERDTILVCL DCCIKIVNLQ
GRLKSSRKLS SELTFDFQIE SIVCLQDSVL AFWKHGMQGR SFRSNEVTQE ISDNTRIFRL
LGSDRVVVLE SRPTDNPTAN SNLYILAGHE NSY
