ID A0A2I3RQ30_PANTR Unreviewed; 1082 AA.
AC A0A2I3RQ30;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR000556};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR000556};
GN Name=MAP3K9 {ECO:0000313|Ensembl:ENSPTRP00000066811.1,
GN ECO:0000313|VGNC:VGNC:57254};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000066811.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000066811.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000066811.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 ECO:0000256|PIRNR:PIRNR000556};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- ACTIVITY REGULATION: Homodimerization via the leucine zipper domains is
CC required for autophosphorylation. {ECO:0000256|PIRNR:PIRNR000556}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000556}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529, ECO:0000256|PIRNR:PIRNR000556}.
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DR EMBL; AACZ04008443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3RQ30; -.
DR Ensembl; ENSPTRT00000111134.1; ENSPTRP00000066811.1; ENSPTRG00000006499.7.
DR VGNC; VGNC:57254; MAP3K9.
DR GeneTree; ENSGT00940000158243; -.
DR Proteomes; UP000002277; Chromosome 14.
DR Bgee; ENSPTRG00000006499; Expressed in cerebellum and 14 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12059; SH3_MLK1-3; 1.
DR CDD; cd14145; STKc_MLK1; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR035779; MLK1-3_SH3.
DR InterPro; IPR016231; MLK1-4.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR44329:SF35; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 9; 1.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF000556; MAPKKK9_11; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000556};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|PIRNR:PIRNR000556};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000556};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000556};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|PIRNR:PIRNR000556}.
FT DOMAIN 53..117
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 145..413
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 12..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..491
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..41
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..947
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-1"
FT BINDING 151..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1082 AA; 119410 MW; 2E59BE5B6D21E80B CRC64;
MEPSRALLGC LASAAAAAPP GEDGAGAGAE EEEEEEEEAA AAAAGPGELG CDAPLPYWTA
VFEYEAAGED ELTLRLGDVV EVLSKDSQVS GDEGWWTGQL NQRVGIFPSN YVTPRSAFSS
RCQPGGEDPS CYPPIQLLEI DFAELTLEEI IGIGGFGKVY RAFWIGDEVA VKAARHDPDE
DISQTIENVR QEAKLFAMLK HPNIIALRGV CLKEPNLCLV MEFARGGPLN RVLSGKRIPP
DILVNWAVQI ARGMNYLHDE AIVPIIHRDL KSSNILILQK VENGDLSNKI LKITDFGLAR
EWHRTTKMSA AGTYAWMAPE VIRASMFSKG SDVWSYGVLL WELLTGEVPF RGIDGLAVAY
GVAMNKLALP IPSTCPEPFA KLMEDCWNPD PHSRPSFTNI LDQLTTIEES GFFEMPKDSF
HCLQDDWKHE IQEMFDQLRA KEKELRTWEE ELTRAALQQK NQEELLRRRE QELAEREIDI
LERELNIIIH QLCQEKPRVK KRKGKFRKSR LKLKDGNRIS LPSDFQHKFT VQASPTMDKR
KSLINSRSSP PASPTIIPRL RAIQLTPGES SKTWGRSSVV PKDEGEEEEK RAPKKKGRTW
GPGTLGQKEL ASGDEGLKSL VDGYKQWSSS APNLVKGPRS SLALPGFTSL MEMEDEDSEG
PGSGESRLQH SPSQSYLCIP FPRGEDGDGP SSDGIHDEPT PVNSATSTPQ LTPTNSLKRG
GAHHRRCEVA LLGCGAVLAA TGLGFDLLEA GKCQLLPLEE PEPPAREEKK RREGLFQRSS
RPRRSTSPPS RKLFKKEEPM LLLGDPSASL TLLSLSSISE CNSTRSLLRS DSDEIVVYEM
PVSPVEAPPL SPCTHNPLVN VRVERFKRDP NQSLTPTHVT LTAPSQPSSH RRTPSDGALK
PETLLASRSP SSNGLSPSPG AGMLKTPSPS RDPGEFPRLP DPNVVFPPTP RRWNTQQDST
LERPKTLEFL PRPRPSANRQ RLDPWWFVSP SHARSTSPAN SSSTETPSNL DSCFASSSST
VEERPGLPAL LPFQAGPLPP TERTLLDLDA EGQSQDSTVP LCRVELNTHR PAPYEIQQEF
WS
//