ID H2L9D7_ORYLA Unreviewed; 850 AA.
AC H2L9D7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 1 {ECO:0000256|PIRNR:PIRNR038172};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038172};
GN Name=LOC101166485 {ECO:0000313|Ensembl:ENSORLP00000002478.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000002478.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000002478.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000002478.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000002478.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000002478.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the JUN N-terminal pathway.
CC {ECO:0000256|PIRNR:PIRNR038172}.
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=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR038172};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000256|ARBA:ARBA00008874,
CC ECO:0000256|PIRNR:PIRNR038172}.
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DR RefSeq; XP_011480565.1; XM_011482263.1.
DR AlphaFoldDB; H2L9D7; -.
DR STRING; 8090.ENSORLP00000002478; -.
DR Ensembl; ENSORLT00000002479.2; ENSORLP00000002478.2; ENSORLG00000001987.2.
DR GeneID; 101166485; -.
DR KEGG; ola:101166485; -.
DR eggNOG; KOG0576; Eukaryota.
DR GeneTree; ENSGT00940000160308; -.
DR HOGENOM; CLU_006347_1_0_1; -.
DR InParanoid; H2L9D7; -.
DR OrthoDB; 152877at2759; -.
DR TreeFam; TF105121; -.
DR Proteomes; UP000001038; Chromosome 13.
DR Bgee; ENSORLG00000001987; Expressed in pharyngeal gill and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06613; STKc_MAP4K3_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF15; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 1; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038172};
KW Kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038172};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Transferase {ECO:0000256|PIRNR:PIRNR038172}.
FT DOMAIN 20..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 513..820
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 327..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 850 AA; 96079 MW; FD8A79DAB0E34AFF CRC64;
MDFHHRAALD ISTKNPQDDF EILLRVGGGT YGEVYKARNK QNGDLAAIKV IKMEPEDDFS
IIQQEIVIVK SCKHPNIVAY YGSYIQSNKL WICMEFCGGG SLQDIYHVTG PLSELQIAYI
CREMLQGLDY LHAQKKIHRD IKGANILLND QGEVKLADFG ISAQITATLA RRMSFIGTPY
WMAPEVAAVE IKGGYNELCD IWSVGITAIE LAELQPPLFD VHPLRVLFLM SKSGYQPPKL
KDKSRWSSTF YNFVKAMLVR NPKKRPSASK LLSHMFLTQQ GLSQEVTLKL LETYRNPEKL
KACVHTDDDD MEVAPLATLK RIQSINKHNR AERTNSDMSF EQIYTQRPVK TDSPTVTLRA
SPGSTGSSNS LVRDQGSDSD DDYDDVDIPT IQTSCHTMPA NEIPPPLPPK PKVRTSSEES
VASEEDRSRK PSSLHTPTPL SRTSSGTHVR PTSHTRASRH SVRLTDNPAD DVPPELPPKG
IRRRQLPPKD SECVSPVTKK PPVFLRKVFH GCPLKINWST TWENPTSKEQ HLILGAEEGI
YTLNLNGPEA TMELLYPGKC TWVYTINNVL MSVSGKSSQL HSHSLKELHE QARKDQRLVP
ISTHRLLPRK CVVTFKIPDT KGCKTCSVVE NMHRNCVFLC CALESSVLLL QWYEPMHKFM
LIKHFDFPLP NPLRVFEMVV APQQEYPLVC IGVSQGPDPS RPVCVDYINL NSSSSWFTNT
GMEKPSPEVV QVQQLDKNSL LVLMEKSVLC VGLNGEVKNL HHLPQQTTFF HEIESIVFFE
DTLLTVWRHG WQRRGKGFTE VLEELTDPRK IYRMVKSHRT VVMETHPVED QSGLSNLYVL
EIAEKYVLLP
//
