ID H3DGB6_TETNG Unreviewed; 891 AA.
AC H3DGB6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR038165};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR038165};
GN Name=MAP3K13 {ECO:0000313|Ensembl:ENSTNIP00000019560.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000019560.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000019560.1}
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 -!- 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:PIRNR038165}.
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DR AlphaFoldDB; H3DGB6; -.
DR STRING; 99883.ENSTNIP00000019560; -.
DR Ensembl; ENSTNIT00000019790.1; ENSTNIP00000019560.1; ENSTNIG00000016461.1.
DR GeneTree; ENSGT00940000158216; -.
DR HOGENOM; CLU_009311_2_1_1; -.
DR InParanoid; H3DGB6; -.
DR OMA; CAEDRGY; -.
DR TreeFam; TF105119; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44329:SF14; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 13; 1.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF038165; MAPKKK12_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 Nucleotide-binding {ECO:0000256|PIRNR:PIRNR038165,
KW ECO:0000256|PIRSR:PIRSR038165-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038165};
KW Transferase {ECO:0000256|PIRNR:PIRNR038165}.
FT DOMAIN 107..348
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 401..435
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 701..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038165-50"
FT BINDING 113..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
SQ SEQUENCE 891 AA; 98789 MW; E89E3F02168AD62B CRC64;
SPLNTALSVD STRSEGQHFE NSVLQLQDQD QDEAGSPASC EHGGCGSHHH QPEDIKLHFH
RAGPGSGGFL EGLFGCLRPV LNIIGKTYST EYKLQQQDMW EVPFEEISEL QWLGSGAQGA
VFLGKFRSEE VAIKKVREQK ETEIKHLRKL KHPNIISFKA VCTQAPCYCI IMEYCAQGQL
YEVLRAGRKV TPRMLVDWAS GIASGMNYLH LHKIIHRDLK SPNVLVTHND TVKISDFGTS
KELSDKSTKM SFAGTVAWMA PEVIRNEPVS EKVDIWSFGV VLWELLTGEI PYKDVDSSAI
IWGVGSNSLH LPVPSTCPDG FKILMKQTWQ AKPRNRPSFR QILLHLDIAS ADVLGAPQET
YFKCQSEWRE EVKKHFEKIK SEGTCIHRLD EELIRRRRDE LRHALDIREH YERKLERANN
LYMELSAIML QLEVREKELM KREQAVEKKY PGTYKRHLVR PIVRSNAVEK LIKKKGSLSH
KPGMPSAKRP DLLRSDGIGS DPLPSPSPLS ASPKVSTPPG KARYRSKPRH RRANSKGSHS
EFAGVLKPVS GPPEGPQAPK EQQLLHHHPH PPTPGPFLPL KGREEAVVNC ANNLRYFGPA
AALRSPQTDH LQGRVSSSGP DLICTAVDAD TRQRTSSTGA GSDPAPGCGS LCPCSQAHPF
PGCLKCQETS PAFEDAAPPY CSQLQTEDRA LPPGSPHSHP ASEREAAERR GGEEEGARPQ
TQPLPTPTPR TLRALRKGGD ESSEEEEGEV DSEVEFPRRQ RPHRCMSSFQ SCSTFSSENL
SVSDGEEGNT SDHSHSGPLE RLSASQEEHL DELLSHTPDI PIDISTQSDG LSDKECAVRR
VKTQISLGKL CSDEHSYENP LQFGDSDCDS SEAECSDATI RNNKVGAPSS W
//