GenomeNet

Database: UniProt
Entry: A0A2I3RQ30_PANTR
LinkDB: A0A2I3RQ30_PANTR
Original site: A0A2I3RQ30_PANTR 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system