MAK1_CAEEL
ID MAK1_CAEEL Reviewed; 521 AA.
AC Q21360; Q65ZB6; Q65ZB7; Q7JM88; Q8I117;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=MAP kinase-activated protein kinase mak-1 {ECO:0000303|PubMed:25851606};
DE Short=MAPK-activated protein kinase mak-1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:25851606};
GN Name=mak-1 {ECO:0000303|PubMed:25851606, ECO:0000312|WormBase:K08F8.1a};
GN ORFNames=K08F8.1 {ECO:0000312|WormBase:K08F8.1a};
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, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH UNC-22,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND DISRUPTION
RP PHENOTYPE.
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 may play a role in body
CC wall muscle contraction. May phosphorylate unc-22/twitchin.
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:0000269|PubMed:25851606};
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:0000269|PubMed:25851606};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25851606};
CC -!- SUBUNIT: May interact (via protein kinase domain) with unc-22 (via
CC protein kinase and CRD domains). {ECO:0000269|PubMed:25851606}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:25851606}. Cytoplasm, myofibril, sarcomere, A band
CC {ECO:0000269|PubMed:25851606}. Note=Localizes between and around dense
CC bodies. Colocalizes with myosin heavy chain unc-54 at the outer edge of
CC A-bands. {ECO:0000269|PubMed:25851606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=a {ECO:0000312|WormBase:K08F8.1a};
CC IsoId=Q21360-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:K08F8.1b};
CC IsoId=Q21360-2; Sequence=VSP_058727, VSP_058730;
CC Name=c {ECO:0000312|WormBase:K08F8.1c};
CC IsoId=Q21360-3; Sequence=VSP_058725;
CC Name=d {ECO:0000312|WormBase:K08F8.1d};
CC IsoId=Q21360-4; Sequence=VSP_058726, VSP_058728, VSP_058729;
CC Name=e {ECO:0000312|WormBase:K08F8.1e};
CC IsoId=Q21360-5; Sequence=VSP_058725, VSP_058728, VSP_058729;
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles (at protein level).
CC Expressed in intestine. {ECO:0000269|PubMed:25851606}.
CC -!- PTM: Autophosphorylated in vitro. {ECO:0000269|PubMed:25851606}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction in motility. Partially resistant
CC to nicotine-induced paralysis; resistance is further increased in a
CC mak-2 gk1110 mutant background. Normal localization of several
CC components of the sarcomere including unc-52, unc-112, unc-95, atn-
CC 1,unc-89 and myo-3. {ECO:0000269|PubMed:25851606}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BX284602; CAA91283.1; -; Genomic_DNA.
DR EMBL; BX284602; CAD59153.1; -; Genomic_DNA.
DR EMBL; BX284602; CAE48503.1; -; Genomic_DNA.
DR EMBL; BX284602; CAH19101.1; -; Genomic_DNA.
DR EMBL; BX284602; CAH19102.1; -; Genomic_DNA.
DR PIR; T23489; T23489.
DR RefSeq; NP_001022238.1; NM_001027067.3. [Q21360-3]
DR RefSeq; NP_001022239.1; NM_001027068.3.
DR RefSeq; NP_001022240.1; NM_001027069.3.
DR RefSeq; NP_495860.1; NM_063459.4. [Q21360-1]
DR RefSeq; NP_871925.1; NM_182125.5.
DR AlphaFoldDB; Q21360; -.
DR SMR; Q21360; -.
DR IntAct; Q21360; 1.
DR MINT; Q21360; -.
DR STRING; 6239.K08F8.1a.2; -.
DR PaxDb; Q21360; -.
DR PeptideAtlas; Q21360; -.
DR EnsemblMetazoa; K08F8.1a.1; K08F8.1a.1; WBGene00010681. [Q21360-1]
DR EnsemblMetazoa; K08F8.1b.1; K08F8.1b.1; WBGene00010681. [Q21360-2]
DR EnsemblMetazoa; K08F8.1c.1; K08F8.1c.1; WBGene00010681. [Q21360-3]
DR EnsemblMetazoa; K08F8.1d.1; K08F8.1d.1; WBGene00010681.
DR EnsemblMetazoa; K08F8.1e.1; K08F8.1e.1; WBGene00010681. [Q21360-5]
DR GeneID; 174398; -.
DR KEGG; cel:CELE_K08F8.1; -.
DR UCSC; K08F8.1b.2; c. elegans.
DR CTD; 174398; -.
DR WormBase; K08F8.1a; CE03467; WBGene00010681; mak-1. [Q21360-1]
DR WormBase; K08F8.1b; CE32906; WBGene00010681; mak-1. [Q21360-2]
DR WormBase; K08F8.1c; CE35895; WBGene00010681; mak-1. [Q21360-3]
DR WormBase; K08F8.1d; CE52142; WBGene00010681; mak-1. [Q21360-4]
DR WormBase; K08F8.1e; CE37258; WBGene00010681; mak-1. [Q21360-5]
DR eggNOG; KOG0604; Eukaryota.
DR InParanoid; Q21360; -.
DR OMA; NVKCLLM; -.
DR OrthoDB; 843707at2759; -.
DR PhylomeDB; Q21360; -.
DR Reactome; R-CEL-171007; p38MAPK events.
DR Reactome; R-CEL-199920; CREB phosphorylation.
DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-CEL-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-CEL-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-CEL-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:Q21360; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010681; Expressed in larva and 4 other tissues.
DR GO; GO:0031672; C:A band; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0051019; F:mitogen-activated protein kinase binding; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IMP:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:UniProtKB.
DR GO; GO:0035095; P:behavioral response to nicotine; 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; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
DR Gene3D; 4.10.1170.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027442; MAPKAPK_C.
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; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..521
FT /note="MAP kinase-activated protein kinase mak-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438707"
FT DOMAIN 144..405
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 150..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..158
FT /note="Missing (in isoform c and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058725"
FT VAR_SEQ 1..74
FT /note="MMFEYEEDEDPMEQQKHEEFKHHSTDHSGSPQENPFRFSYDTGKRAASMFVT
FT PSSEDLIAYGTKHLLDSPTAVQ -> MKKMKIPWNNKNMKNSNIIQRITL (in
FT isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_058726"
FT VAR_SEQ 336
FT /note="L -> F (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058727"
FT VAR_SEQ 337..521
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058730"
FT VAR_SEQ 378..396
FT /note="TKDDIRCLLRTNPSDRLTI -> SKRLETTEFHDFSTLRIWS (in
FT isoform d and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058728"
FT VAR_SEQ 397..521
FT /note="Missing (in isoform d and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058729"
SQ SEQUENCE 521 AA; 58528 MW; F07131B7DC11DD63 CRC64;
MMFEYEEDED PMEQQKHEEF KHHSTDHSGS PQENPFRFSY DTGKRAASMF VTPSSEDLIA
YGTKHLLDSP TAVQRSLVLN ATTSLNIDCD LSSDDDLSPT TQRKICFCAS QNPAETQEQG
LRPAKSTLAI SFPCHQHQIT EDYTISAEII GIGESGKVMA CYQKVTGEKF ALKVLRDSQK
ARREVELHWL TNAHENVVSI LDIYENTFDN VKCLLMVVEF LEGGDLLSQF ESQGSIPYTE
KKVGEIIRQI GNAVMYLHDM NIAHRDIKLE NILCSGTGDN CVYKLGDYGF AKRPERNVLM
ESPCCTPFYA PPEVLGRERY DKSCDMWSLG VAMYILLCGY PPFYSMKGVA LSPGMRSRIA
NAYYAFPHEE WDCVSKDTKD DIRCLLRTNP SDRLTIHELM ATPLVTGEPI VPGKHITTAI
AIPGADESEC GGGVFDDGFI VEEEETPDTV AEILPVPKSV RFLRDGVKAP RLHSIQEEVG
RAMEIMRMGT DQVYIKNPTA SCNNLFERRR AVHLSIPRVY C
