MOK_MOUSE
ID MOK_MOUSE Reviewed; 420 AA.
AC Q9WVS4; Q8CFU4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=MAPK/MAK/MRK overlapping kinase;
DE EC=2.7.11.22 {ECO:0000269|PubMed:10421840};
DE AltName: Full=MOK protein kinase;
DE AltName: Full=Serine/threonine kinase 30;
GN Name=Mok; Synonyms=Rage, Stk30;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
RP THR-159 AND TYR-161.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10421840; DOI=10.1046/j.1365-2443.1999.00261.x;
RA Miyata Y., Akashi M., Nishida E.;
RT "Molecular cloning and characterization of a novel member of the MAP kinase
RT superfamily.";
RL Genes Cells 4:299-309(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25243405; DOI=10.1371/journal.pone.0108470;
RA Broekhuis J.R., Verhey K.J., Jansen G.;
RT "Regulation of cilium length and intraflagellar transport by the RCK-
RT kinases ICK and MOK in renal epithelial cells.";
RL PLoS ONE 9:E108470-E108470(2014).
CC -!- FUNCTION: Able to phosphorylate several exogenous substrates and to
CC undergo autophosphorylation (PubMed:10421840). Negatively regulates
CC cilium length in a cAMP and mTORC1 signaling-dependent manner
CC (PubMed:25243405). {ECO:0000269|PubMed:10421840,
CC ECO:0000269|PubMed:25243405}.
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=2.7.11.22;
CC Evidence={ECO:0000269|PubMed:10421840};
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=2.7.11.22; Evidence={ECO:0000269|PubMed:10421840};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10421840};
CC -!- ACTIVITY REGULATION: Phosphorylation appears to increase the enzymatic
CC activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10421840}. Cell
CC projection, cilium {ECO:0000269|PubMed:25243405}. Nucleus
CC {ECO:0000269|PubMed:25243405}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WVS4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVS4-2; Sequence=VSP_009147, VSP_009148, VSP_009149,
CC VSP_009150;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, and less in kidney,
CC brain and lung.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; AB022695; BAA81689.1; -; mRNA.
DR EMBL; BC037614; AAH37614.1; -; mRNA.
DR CCDS; CCDS49176.1; -. [Q9WVS4-1]
DR RefSeq; NP_036103.1; NM_011973.2. [Q9WVS4-1]
DR AlphaFoldDB; Q9WVS4; -.
DR SMR; Q9WVS4; -.
DR IntAct; Q9WVS4; 1.
DR STRING; 10090.ENSMUSP00000068904; -.
DR iPTMnet; Q9WVS4; -.
DR PhosphoSitePlus; Q9WVS4; -.
DR PaxDb; Q9WVS4; -.
DR PRIDE; Q9WVS4; -.
DR ProteomicsDB; 252589; -. [Q9WVS4-1]
DR ProteomicsDB; 252590; -. [Q9WVS4-2]
DR Antibodypedia; 27789; 436 antibodies from 33 providers.
DR DNASU; 26448; -.
DR Ensembl; ENSMUST00000070565; ENSMUSP00000068904; ENSMUSG00000056458. [Q9WVS4-1]
DR GeneID; 26448; -.
DR KEGG; mmu:26448; -.
DR UCSC; uc007pbv.1; mouse. [Q9WVS4-1]
DR UCSC; uc007pbx.1; mouse. [Q9WVS4-2]
DR CTD; 5891; -.
DR MGI; MGI:1336881; Mok.
DR VEuPathDB; HostDB:ENSMUSG00000056458; -.
DR eggNOG; KOG0661; Eukaryota.
DR GeneTree; ENSGT00940000159582; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q9WVS4; -.
DR OMA; WQISKEG; -.
DR OrthoDB; 76933at2759; -.
DR PhylomeDB; Q9WVS4; -.
DR TreeFam; TF328769; -.
DR BioGRID-ORCS; 26448; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Mok; mouse.
DR PRO; PR:Q9WVS4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9WVS4; protein.
DR Bgee; ENSMUSG00000056458; Expressed in superior surface of tongue and 107 other tissues.
DR ExpressionAtlas; Q9WVS4; baseline and differential.
DR Genevisible; Q9WVS4; MM.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..420
FT /note="MAPK/MAK/MRK overlapping kinase"
FT /id="PRO_0000086342"
FT DOMAIN 4..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 311..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..92
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009147"
FT VAR_SEQ 93..95
FT /note="IRG -> MKR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009148"
FT VAR_SEQ 232..289
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009149"
FT VAR_SEQ 328..420
FT /note="KQSLRHEEGHARRQGPTSLMELPKLRLSGMTKLSSCSSPALRSVLGTGANGK
FT VPVLRPLKCAAVNKKTDTQKDIKPHLKHYHLPTINRKGGEY -> V (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009150"
FT MUTAGEN 159
FT /note="T->A: Loss of activity; when associated with F-161."
FT /evidence="ECO:0000269|PubMed:10421840"
FT MUTAGEN 161
FT /note="Y->F: Loss of activity; when associated with A-159."
FT /evidence="ECO:0000269|PubMed:10421840"
SQ SEQUENCE 420 AA; 48065 MW; 1C637E1ECB33C998 CRC64;
MKNYKAIGKI GEGTFSEVMK MQSLRDGNYY ACKQMKQHFE SIEQVNSLRE IQALRRLNPH
PNILALHEVV FDRKSGSLAL ICELMDMNIY ELIRGRRHPL SEKKIMLYMY QLCKSLDHMH
RNGIFHRDVK PENILVKQDV LKLGDFGSCR SVYSKQPYTE YISTRWYRAP ECLLTDGFYT
YKMDLWSAGC VFYEIASLQP LFPGVNELDQ ISKIHDVIGT PCQKTLTKFK QSRAMSFDFP
FKKGSGIPLL TANLSPQCLS LLHAMVAYDP DERIAAHQAL QHPYFQVQRA AETQTLAKHR
RAFCPKFSMV PESSSHNWSF SQEGRKQKQS LRHEEGHARR QGPTSLMELP KLRLSGMTKL
SSCSSPALRS VLGTGANGKV PVLRPLKCAA VNKKTDTQKD IKPHLKHYHL PTINRKGGEY
