ID A0A3P9A396_ESOLU Unreviewed; 1026 AA.
AC A0A3P9A396;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=MAP3K21 {ECO:0000313|Ensembl:ENSELUP00000035221.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000035221.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000035221.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000035221.1}
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 RefSeq; XP_010887033.1; XM_010888731.3.
DR AlphaFoldDB; A0A3P9A396; -.
DR STRING; 8010.ENSELUP00000035221; -.
DR Ensembl; ENSELUT00000022690.2; ENSELUP00000035221.1; ENSELUG00000014068.2.
DR GeneID; 105021218; -.
DR KEGG; els:105021218; -.
DR GeneTree; ENSGT00940000159629; -.
DR OrthoDB; 876955at2759; -.
DR Proteomes; UP000265140; LG05.
DR Bgee; ENSELUG00000014068; Expressed in testis 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; cd14061; STKc_MLK; 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:SF750; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 21; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000556};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
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 38..102
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 129..391
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 408..442
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 508..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-1"
FT BINDING 135..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1026 AA; 113680 MW; E17CE3167E3E084C CRC64;
MDVSKAGFPN GEGRPKDTGE HAWTDSPTAR AWAHSAHLSR SLWTAVFAYE GTGEDELSLR
RGDVVEVLSK DAAISGDEGW WTGKINHRVG IFPANYVTYQ PAIYRLPAGN TVGVRERPST
PVQIHFGELV LEEIIGVGGF GKVYRGTWKD QEVAVKAARH DPDADITATS DGVKQEAKLF
SMLQHPNIIK LEGVCLEEPN LCLVMEYARG GTLNRALTGR RIPPHILVNW AVQIARGMHY
LHEEAIVPII HRDLKSSNIL LHEKIENDDI GRKTLKITDF GLAREWHNTT KMSAAGTYSW
MAPEVIKSSL FSKGSDVWSY GVLLWELLTG EVPYRGIDGL AVAYGVAVNK LTLPIPSTCP
EPFAKLMEEC WEQDPHIRPS FASILEQLTA IEEAVMATMP QDSFHSMQED WRVEIQEMFD
ELRTKEKELR SREEELTRAA LQQKSHEELL KRREQQLAER EINVLERELN ILIFQLNKDK
PNVKKRKGKF KRSRLKLKDG NRISLPSDFQ HKITVQASPS MEKRRSLNSS SSSPPSSPTL
IPRLRAIQLT LDESNRTWGR STIYKEEFDD VKKGIKKKGR TWGPSSVQTK ERGTCAERVR
PLSDGSNPWS TSLVKSVPLA ALFAEQQAGA DKDETSSPDC SDNTKPKQLK FPNQVYIDLP
LWKDEQQQLG GGEGAAMGCS GESLEDPTTT STSSASTTPQ HTPTNSLKRA STRRRTDAVL
YGCASMLASV ALGFDLRDAL KAPPADDPEL TPGAEKERKK KEGLFQRAAR FRRSTSPPGG
RSSRKEEAAQ VWAAAPPGPV NLTAMSAISE CNSTRCLLQA DQDGPQPSPV KEEAPIGLSD
ARLQPGSSSC SHSPKGPDNR NPAKAEPRPL SQTAPERTPR QTMSSRLRTK KSAFIQNTNG
SHNTSLGQSP TTTFQKKKSD RENTPEKAAC GETISTRPRP LSLRSKPHSW GLLRGRNKSY
SLGHYSGEKS ARNLNIVLSS TEVKVGCSLL DMDTEGQKRD CTVPLCRIQS GPSRPSVFQL
EKKFLS
//