ID A0A2Y9JSK6_ENHLU Unreviewed; 1103 AA.
AC A0A2Y9JSK6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-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=LOC111148486 {ECO:0000313|RefSeq:XP_022360775.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022360775.1};
RN [1] {ECO:0000313|RefSeq:XP_022360775.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022360775.1};
RG RefSeq;
RL Submitted (NOV-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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
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 RefSeq; XP_022360775.1; XM_022505067.1.
DR AlphaFoldDB; A0A2Y9JSK6; -.
DR STRING; 391180.A0A2Y9JSK6; -.
DR KEGG; elk:111148486; -.
DR OrthoDB; 876955at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; PTHR23257:SF717; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 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, ECO:0000313|RefSeq:XP_022360775.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000556};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
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 51..115
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 143..411
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 12..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..489
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..41
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..968
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-1"
FT BINDING 149..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2"
FT BINDING 170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1103 AA; 121740 MW; 301D01DD62AE8F36 CRC64;
MEPSRALLGC LASAAAAAPP GEDGAGAGAE EEEEEEEEAA AAAPGELGSD APLPYWTAVF
EYEAAGEDEL TLRLGDVVEV LSKDSQVSGD EGWWTGQLNQ RVGIFPSNYV TPRSAFSSRC
QHGGEDPSCY PPIQLLEIDF AELTLEEIIG IGGFGKVYRA FWIGDEVAVK AARHDPDEDI
SQTIENVRQE AKLFAMLKHP NIIALRGVCL KEPNLCLVME FARGGPLNRV LSGKRIPPDI
LVNWAVQIAR GMNYLHDEAI VPIIHRDLKS SNILILQKVE NGDLSNKILK ITDFGLAREW
HRTTKMSAAG TYAWMAPEVI RASMFSKGSD VWSYGVLLWE LLTGEVPFRG IDGLAVAYGV
AMNKLALPIP STCPEPFAKL MEDCWNPDPH SRPSFTNILD QLTTIEESGF FEMPKDSFHC
LQDDWKHEIQ EMFDQLRAKE KELRTWEEEL TRAALQQKTQ EELLRRREQE LAEREIDILE
RELNIIIHQL CQEKPRVKKR KGKFRKSRLK LKDGNRISLP SDFQHKFTVQ ASPTMDKRKS
LVSSRSSPPA SPTVIPRLRA IQLTPGESSK TWGRNSVILR EEGEEEEKRA PKKKGRTWGP
STLGQKELAS GDEGSPQRRE KANGLSTPSE SPHFHLGLKS LVDGYKQWSS SAPNLGKGPR
SSPALPGFTS LMEMEDEDSE GPRSGEGRLQ HPPNQSYLCI PFPRGEDGEG PSSDAVHEEP
TPVNSATSTP QLTPTNSLKR GGGHHRRCEV ALLGCGAVLA ATGLGFDLLE AGKYQLLPPE
EPEPPAREEK KRREGLFQRA SRPRRSTSPP SRKLFKKEEP MLLLGDPSAS LTLLSLSSIS
ECNSTRSLLR SDSDEIVVYE MPVSPAEAPP LSPCTRNPLV NVRVERFKRD PNQSLTPTHV
TLTAPAQPSG HRRTPSDGAL KPAALLASRS PSSNGLSPSP GAGMLKTPSP SRDPGEFPRL
PDPNVVFPPT PRRWNTQQDS TLERPKTLEF LPRPRPSANR QRLDPWWFVS PSHARSASPA
NSSSTETPSN LDSCFASSSS TVEERPGLPA LLPFQAGPLP PAERTLLDLD AEGQSQDSTV
PLCRAELNTH RPAPYEIQQE FWS
//
