ID A0A3B4V0A4_SERDU Unreviewed; 1041 AA.
AC A0A3B4V0A4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=MAP3K11 {ECO:0000313|Ensembl:ENSSDUP00000024208.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000024208.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000024208.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B4V0A4; -.
DR STRING; 41447.ENSSDUP00000024208; -.
DR Ensembl; ENSSDUT00000024663.1; ENSSDUP00000024208.1; ENSSDUG00000017588.1.
DR GeneTree; ENSGT00940000161064; -.
DR OMA; IKNTHRA; -.
DR OrthoDB; 876955at2759; -.
DR Proteomes; UP000261420; Unplaced.
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; cd14147; STKc_MLK3; 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; PTHR23257:SF757; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PIRSF; PIRSF000556; MAPKKK9_11; 2.
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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000556};
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 27..91
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 123..385
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 513..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 402..438
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 592..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-1"
FT BINDING 129..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1041 AA; 115037 MW; 62552967B6E55C54 CRC64;
MEPLKNIFSR GPLSNWKNLD QSQKGNFTNP VWTALFDYEA SCKDELTLRK GDLVEVLSLD
SEISGDEGWW AGKVNNKVGI FPSNYGSFKP SGYGKLPGSS VVGELGPAVV GEFEPDVLDF
RELSLEEVIG VGGFGKVYRG TWRGGLVAVK AARQDPDEDI SVTAQNVRQE ARLFAMLTHP
NIIALKGVCL QEPNLCLIME YASGGPLSRA LAGRRIPPHV LVNWAVQIAK GMLYLHSEAI
VPVIHRDLKS NNILLAQPIE NECMEGLTLK ITDFGLAREW HKTTKMSTAG TYAWMAPEVI
KSSTFSKGSD VWSYGVLLWE LLTGEAPYKG IDGLAVAYGV AVNKLTLPIP STCPEPFAQL
MSECWDQDPH RRPNFGSILA QLMALEQQVK EEMPQDSFHS LQEDWKLEIQ DMFDELRAKE
KELRCREEEL KRAALEQKSH EEFLRQREQQ LAQWEQDVFE RELSLLILHL NQNQEKPNVK
KRKGTFKKHK LKCKNGEKIS MPQDFIHKIT VQASPGLEKR RNSPDLGSGS SPSFGPRFRA
IQLSPSDNSR TFGLSAVWPL EAPSLKQANG DLRLGPHWRP QSPKSPKSPK VLRLSPQESS
LSMRAKLLES DSNENGESKD DFEEYRPSTP TPPPAQNGSS VKDSMRLPLP HGDSGSEEGG
SSPAGSPRPE RGSLSGMFKS THRALLGGGS LLASVGLGRC LDIPPRVPPR TNPPSLEDRT
TFELEISSPK PLISEPPVVD DLITFSTSEP LPRPLLDLAL QYQELKPLPL TPPPPNPRER
SGQRTPHSPQ TPRTPVQQDK PSPGEWMPCS HSTNGELGCE AWEHRADRRR RSSQGLHTTQ
LVLDLPLCQD TQESDDKPAV PYALHPNPAL WSPKTRRLEV SVIPRPRPSP IRPRIDPWSF
ISAGGGNSGG GRSPNRSDSN HLSYQPSPTN PFTNCDPFPS PDCDPFALKA DPSSGSDTAS
PFDPFLAPFP TSRSAPCSTN GSPTLPSFRI APLNPADSPL IDLGWAACSK PLDSTKERAH
PRRTLGLKPF KSPTQLRDDR F
//
