ID A0A2K5Y7V5_MANLE Unreviewed; 966 AA.
AC A0A2K5Y7V5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 13 {ECO:0000256|PIRNR:PIRNR038165};
DE EC=2.7.11.25 {ECO:0000256|PIRNR:PIRNR038165};
GN Name=MAP3K13 {ECO:0000313|Ensembl:ENSMLEP00000011651.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000011651.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000011651.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Activates the JUN N-terminal pathway through activation of
CC the MAP kinase kinase MAP2K7. {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 RefSeq; XP_011837262.1; XM_011981872.1.
DR RefSeq; XP_011837263.1; XM_011981873.1.
DR AlphaFoldDB; A0A2K5Y7V5; -.
DR STRING; 9568.ENSMLEP00000011651; -.
DR Ensembl; ENSMLET00000035076.1; ENSMLEP00000011651.1; ENSMLEG00000029983.1.
DR GeneID; 105541038; -.
DR KEGG; mleu:105541038; -.
DR CTD; 9175; -.
DR GeneTree; ENSGT00940000158216; -.
DR OrthoDB; 876955at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0106137; F:IkappaB kinase complex binding; IEA:Ensembl.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:1905492; P:positive regulation of branching morphogenesis of a nerve; IEA:Ensembl.
DR GO; GO:0014042; P:positive regulation of neuron maturation; IEA:Ensembl.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; IEA:Ensembl.
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; IPR027258; MAPKKK13.
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:SF945; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 13; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
DR PIRSF; PIRSF500742; 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};
KW Magnesium {ECO:0000256|PIRNR:PIRNR038165};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR038165};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR038165,
KW ECO:0000256|PIRSR:PIRSR038165-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038165};
KW Transferase {ECO:0000256|PIRNR:PIRNR038165}.
FT DOMAIN 168..409
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 462..496
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 96..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038165-50"
FT BINDING 174..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
SQ SEQUENCE 966 AA; 108379 MW; 8FBADD033B1349BB CRC64;
MANFQEHLSC SSSPHLPFSE SKTFNGLQDE LAAMGNHPSP KLLEDQQEKG MVRTELIESV
NSPITTTVLT SVSEDSRDQF ENSVLQLREH DESEMAVSQG NSNTMDGEST SGTEDIKIQF
SRSGSGSGGF LEGLFGCLRP VWNIIGKAYS TDYKLQQQDT WEVPFEEISE LQWLGSGAQG
AVFLGKFRAE EVAIKKVREQ NETDIKHLRK LKHPNIIAFK GVCTQAPCYC IIMEYCAHGQ
LYEVLRAGRK ITPRLLVDWS TGIASGMNYL HLHKIIHRDL KSPNVLVTHT DAVKISDFGT
SKELSDKSTK MSFAGTVAWM APEVIRNEPV SEKVDIWSFG VVLWELLTGE IPYKDVDSSA
IIWGVGSNSL HLPVPSTCPD GFKILMKQTW QSKPRNRPSF RQTLMHLDIA SADVLATPQE
TYFKSQAEWR EEVKKHFEKI KSEGTCIHRL DEELIRRRRE ELRHALDIRE HYERKLERAN
NLYMELSAIM LQLEMREKEL IKREQAVEKK YPGTYKRHPV RPIIHSNAME KLMKRKGVPH
KSGMQTKRPD LLRSEGIPST EVAPTASPLS VSPKMSTSSS KSRYRSKPRH RRGNSRGSHS
DFAAILKNQP AQENSPHPAY LHQAQSQYPS LHHHNSLQQQ YQQPPPAMSQ SHHPRLNMHG
QDIATCANNL RYFGPAAALR SPLSNHAQRQ LPGSSPDLIS TAMAADCWRS SEPDKGQAGP
WGCCQADPYD PCLQCRPEQY GSLDIPSAEA VGRSPDLSKS PAHNPLLENA QSSEKMEENE
FSGCRSESSL GTSHLVTPPA LPRKTRPLQK SGDDSSEEEE GEVDSEVEFP RRQRPHRCIS
SCQSYSTFSS ENFSVSDGEE GNTSDHSNSP DELADKLEDR LAEKLDDLLS QTPEIPIDIS
SHSDGLSDKE CAVRRVKTQM SLGKLCVEER GYENPMQFEE SDCDSSDGEC SDATVRTNKH
YSSATW
//
