ID B8A6G9_DANRE Unreviewed; 878 AA.
AC B8A6G9; A0A8M3AZ98;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
GN Name=map4k5 {ECO:0000313|Ensembl:ENSDARP00000034684,
GN ECO:0000313|RefSeq:XP_009305737.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-6497};
GN Synonyms=fl74c10 {ECO:0000313|RefSeq:XP_009305737.1}, wu:fl74c10
GN {ECO:0000313|RefSeq:XP_009305737.1}, zgc:55719
GN {ECO:0000313|RefSeq:XP_009305737.1}, zgc:55985
GN {ECO:0000313|RefSeq:XP_009305737.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000034684};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000034684, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000034684};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000034684}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000034684};
RG Ensembl;
RL Submitted (AUG-2013) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_009305737.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_009305737.1};
RG RefSeq;
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 EMBL; BX936452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009305737.1; XM_009307462.3.
DR STRING; 7955.ENSDARP00000034684; -.
DR PaxDb; 7955-ENSDARP00000034684; -.
DR PeptideAtlas; B8A6G9; -.
DR Ensembl; ENSDART00000029824; ENSDARP00000034684; ENSDARG00000039125.
DR Ensembl; ENSDART00000029824.8; ENSDARP00000034684.6; ENSDARG00000039125.7.
DR GeneID; 334565; -.
DR AGR; ZFIN:ZDB-GENE-030131-6497; -.
DR CTD; 11183; -.
DR ZFIN; ZDB-GENE-030131-6497; map4k5.
DR eggNOG; KOG0576; Eukaryota.
DR OMA; XQYIIFG; -.
DR OrthoDB; 152877at2759; -.
DR PhylomeDB; B8A6G9; -.
DR TreeFam; TF105121; -.
DR Proteomes; UP000000437; Chromosome 13.
DR Bgee; ENSDARG00000039125; Expressed in early embryo and 27 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06646; STKc_MAP4K5; 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:SF19; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 5; 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 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038172};
KW Kinase {ECO:0000256|PIRNR:PIRNR038172, ECO:0000313|RefSeq:XP_009305737.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038172};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B8A6G9};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
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 539..851
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 320..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..478
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 878 AA; 98404 MW; CB3FF072E6C61DB0 CRC64;
MDPLARSGGE IQRRNPQHDF ELIQRVGSGT YGDVYKARKI STGELAAVKI IKLEPGDDFS
IIQQEIFMVK ECTHHNIVAY FGSYLCREKL WICMEYCGGG SLQDIYHVTG PLSELQIAYV
CRETLQGLGY LHSKGKMHRD IKGANILLTD NGDVKLADFG VAAKITATMA KRKSFIGTPY
WMAPEVAAVE KNGGYNHLCD IWAVGITSIE LAELQPPMFD LHPMRALFLM SKSNFQPPKL
KDKTKWSTAF HNFVKLSLTK NPKRRPTAEK MLSHLFVGQT GLTRRLALEL LDKMNNPDNH
QSHFSQGDED DFEPLAERHT IRSTHSRSAR AERTQSQINF DKLQFEPPLR KETEASAEMD
VTKDNDFPSP WSPFTDGPIT SRGHLAPLED AFEDVDLSTL GKGVPPPLPP KPSQARSSSV
SDEFGLADGC QTVRRFPGSD NGPMPVARRQ STPERGSNAE HTHSDYLSVS VSSPGLLSHT
TDHEEDSDGS VNGDVSKSPP GRPQRKERKD FPKPAINGLP PTPKVLMGAC FSKVFDGCPL
KINCATSWIH PETKDQYLIF GTEDGIYTLN LNELHEATME QLFPRRCTWL YIINNNLMSL
SGKTFQLYSH NLIGLFEQLR KPGLATQFHT HRFPDKILPR RFALTTKIPD TKGCHKCCIV
RNPYTGHKYL CGALQSGIVL LQWYEPMQRF MLIKHFDFPV PSPLRVFEML VVPEQEYPLV
CVAVSQGSEP GQVVRFQTIN LNSCSSWFTE VGSGGNQVDA IHVTQLERDT VLVCLDKNVK
IVNLQGKLKS NKKLASELSF DFCVDSVVCL QDSVLAFWKH GMQGKNFKSN EVTQEISDPS
RVFRLLGSDR VVVLESRPTD NPTAYSNLYI LAGHENSY
//
