ID A0A2K6CGU1_MACNE Unreviewed; 792 AA.
AC A0A2K6CGU1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 1 {ECO:0000256|PIRNR:PIRNR038172};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038172};
GN Name=MAP4K1 {ECO:0000313|Ensembl:ENSMNEP00000022882.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000022882.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000022882.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the JUN N-terminal pathway.
CC {ECO:0000256|PIRNR:PIRNR038172}.
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:0000256|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR038172};
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:0000256|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000256|ARBA:ARBA00008874,
CC ECO:0000256|PIRNR:PIRNR038172}.
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DR AlphaFoldDB; A0A2K6CGU1; -.
DR Ensembl; ENSMNET00000047142.1; ENSMNEP00000022882.1; ENSMNEG00000035006.1.
DR GeneTree; ENSGT00940000160308; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000035006; Expressed in lymph node and 6 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR48012:SF15; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 1; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 2.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038172};
KW Kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038172};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Transferase {ECO:0000256|PIRNR:PIRNR038172}.
FT DOMAIN 13..245
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 466..771
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 267..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 792 AA; 87084 MW; D35C0B031AC32241 CRC64;
LAKSRGRYPR DHYDLLQRLG GGTYGEVFKA RDKATGDLVA LKMVKMEPDD DVSTLQKEIL
ILKTCRHANI VAYHGSYLWL QKLWICMEFC GAGSLQDIYQ VTGSLSELQI SYVCREVLQG
LAYLHSQKKI HRDIKGANIL INDAGEVRLA DFGISAQIGA TLARRLSFIG TPYCPGVSQA
IELAELQPPG LVRLLFLMTK SGYQPPRMKE KGKWSAAFHN FIKVTLTKSP KKRPSATKML
SHQLVSQPGL NRGLILDLLD KLKNPGKGPS IGDIEDEEPE LPPAIPRRIR STHRSSSLGI
PDADCCRRHM EFRKLRGMET RPPANTACLQ PPRDLRSSSP REQQSESSDD DYDDVDIPTP
AEDTPPPLPP KPKFRSPSDE GPGGMGDDGR LSPGVLVRCA SGPPPHNPRP GPPPSTSSPH
LTAHSEPSLW NPPSRELDKP PLLPPKKEKM KRKGCALLVK LFNGCPLRIH STAAWTHPST
KDQHLLLGAE EGIFILNRND QEATLEMLFP SRTTWVYSIN NVLMSLSGKT PHLYSHSILG
LLERKETRAG NPIAHISPHR LLARKNMVST KIQDTKGCRA CCVAEGASSG GPFLCGALET
SVVLLQWYQP MNKFLLVRQV LFPLPTPLSV FALLTGPGSE LPAVCIGVSP GRPGKSVLFH
TVRFGALSCW LGEMSTEHKG PVQVTQVEED MVMVLMDGSL KLVTPEGSPV RGLRTPEIPM
TEAVEAVAMV GGQLQAFWKH GVQVWALGSD QLLQELRDPT LTFRLLGSPR PVVVETRPVD
DPTAPSNLYI QE
//
