MNK_CAEEL
ID MNK_CAEEL Reviewed; 707 AA.
AC Q8I113; Q22005;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=MAP kinase-interacting serine/threonine-protein kinase mnk-1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9BUB5};
DE AltName: Full=MAP kinase integrating kinase-1 {ECO:0000303|PubMed:17277769};
GN Name=mnk-1 {ECO:0000312|WormBase:R166.5b};
GN ORFNames=R166.5 {ECO:0000312|WormBase:R166.5b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17277769; DOI=10.1038/nature05603;
RA Syntichaki P., Troulinaki K., Tavernarakis N.;
RT "eIF4E function in somatic cells modulates ageing in Caenorhabditis
RT elegans.";
RL Nature 445:922-926(2007).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19528325; DOI=10.1534/genetics.109.104885;
RA Dorfman M., Gomes J.E., O'Rourke S., Bowerman B.;
RT "Using RNA interference to identify specific modifiers of a temperature-
RT sensitive, embryonic-lethal mutation in the Caenorhabditis elegans
RT ubiquitin-like Nedd8 protein modification pathway E1-activating gene rfl-
RT 1.";
RL Genetics 182:1035-1049(2009).
RN [4] {ECO:0000305}
RP FUNCTION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=25851606; DOI=10.1091/mbc.e14-05-1009;
RA Matsunaga Y., Qadota H., Furukawa M., Choe H.H., Benian G.M.;
RT "Twitchin kinase interacts with MAPKAP kinase 2 in Caenorhabditis elegans
RT striated muscle.";
RL Mol. Biol. Cell 26:2096-2111(2015).
CC -!- FUNCTION: Serine/threonine-protein kinase which is required in the
CC germline to regulate positively lifespan (PubMed:17277769). May play a
CC role in body wall muscle contraction (PubMed:25851606). May be involved
CC in embryonic cytokinesis (PubMed:19528325).
CC {ECO:0000269|PubMed:17277769, ECO:0000269|PubMed:19528325,
CC ECO:0000269|PubMed:25851606}.
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:0000250|UniProtKB:Q9BUB5};
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:0000250|UniProtKB:Q9BUB5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BUB5};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19528325}. Cytoplasm
CC {ECO:0000269|PubMed:19528325}. Note=Predominantly localizes in the
CC nucleus in the 1- and 2-cell embryos. {ECO:0000269|PubMed:19528325}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:R166.5b};
CC IsoId=Q8I113-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:R166.5a};
CC IsoId=Q8I113-2; Sequence=VSP_058707;
CC -!- TISSUE SPECIFICITY: Expressed in pharynx, intestine, vulva and body
CC wall muscles. {ECO:0000269|PubMed:25851606}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a reduction in
CC lifespan but not in a glp-4 bn2 mutant background. In an ife-2 ok306
CC mutant background, partially reduces the lifespan increase
CC (PubMed:17277769). In a rfl-1 or198 mutant background, partially
CC rescues embryonic viability by restoring normal cytokinesis
CC (PubMed:19528325). {ECO:0000269|PubMed:17277769,
CC ECO:0000269|PubMed:19528325}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BX284602; CAA90665.2; -; Genomic_DNA.
DR EMBL; BX284602; CAD59152.2; -; Genomic_DNA.
DR PIR; T24230; T24230.
DR RefSeq; NP_496272.2; NM_063871.4. [Q8I113-2]
DR RefSeq; NP_871924.2; NM_182124.4. [Q8I113-1]
DR AlphaFoldDB; Q8I113; -.
DR SMR; Q8I113; -.
DR STRING; 6239.R166.5b; -.
DR EPD; Q8I113; -.
DR PaxDb; Q8I113; -.
DR EnsemblMetazoa; R166.5a.1; R166.5a.1; WBGene00011304. [Q8I113-2]
DR EnsemblMetazoa; R166.5b.1; R166.5b.1; WBGene00011304. [Q8I113-1]
DR EnsemblMetazoa; R166.5b.2; R166.5b.2; WBGene00011304. [Q8I113-1]
DR EnsemblMetazoa; R166.5b.3; R166.5b.3; WBGene00011304. [Q8I113-1]
DR GeneID; 174623; -.
DR KEGG; cel:CELE_R166.5; -.
DR UCSC; R166.5a; c. elegans.
DR CTD; 174623; -.
DR WormBase; R166.5a; CE40867; WBGene00011304; mnk-1. [Q8I113-2]
DR WormBase; R166.5b; CE40868; WBGene00011304; mnk-1. [Q8I113-1]
DR eggNOG; KOG0607; Eukaryota.
DR GeneTree; ENSGT00940000154587; -.
DR InParanoid; Q8I113; -.
DR OMA; FHRIQDG; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q8I113; -.
DR PRO; PR:Q8I113; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011304; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
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:0035095; P:behavioral response to nicotine; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0060625; P:regulation of protein deneddylation; IGI:WormBase.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..707
FT /note="MAP kinase-interacting serine/threonine-protein
FT kinase mnk-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438684"
FT DOMAIN 203..493
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 209..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 2..43
FT /note="FFLDNTDSMTSSSRGITMPNTISSHEDVGGYSPRKVGIQHDY -> TILHAG
FT YPQSPVVHFGRHHNVNINQLNLNHLGQVDNIPNN (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058707"
SQ SEQUENCE 707 AA; 78934 MW; 43ACF06B41AA807E CRC64;
MFFLDNTDSM TSSSRGITMP NTISSHEDVG GYSPRKVGIQ HDYSAVGGGG AAFHHLHTSA
ATPRHVATSE FYDDEEATSP RGGIEIGAGG GKMMANLRRH RQRERETYED EDVLSSSDES
SGRPIPRYVG RDTDHVFGEF EMDDEDVVMR REDGYGEDET DEDYFDEEEP VAELLPLGGG
TRRVPRTPGR KNSSKCGFFD YYKLTDEHLG SGAYGSVTTC KSIKSGVEYA VKIVDKQGET
HSRKRILREV NIFKTCKDHP NIVQLLDWFE DETNFYLVME KMRGGPLLQH ILQRKYFTEE
EARRVTKDIS LALKFMHDRG IAHRDVKPEN VLCTDPNHVS PVKLCDLDLA SQRPPQHERH
PLSQVASEPD LASPVGSAEF MAPEVVDAYV GDSLKYDKKC DTWSLGVILY IMLAGYAPFQ
GMCDDEDCGW SEGKPCEDCQ QDLFHRIQDG YYEFPEEEWG MISEEAKDLV SNLLKRDPVD
RFNADQILSH RWLQQSAAST ILQTPSNLIN RKDSARDVQQ MSEHFNLMNR LADTRLSARF
DNKMTMSECG SDLGTATIHG DGSFLSMGGE PFGTFPRKKS VGIAIEKSRS GEFTPPISRA
SPTTPPPSML NLSEDLTDSP VKRRSADDSG TFSLFSPASS NGDDSICSPP MVFVDMPSIQ
LFGTGALLTS VQMTPRHTTE DDASLKSFED EQENANPIHR IETQVNV
