MKNK1_XENTR
ID MKNK1_XENTR Reviewed; 417 AA.
AC Q66JF3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=MAP kinase-interacting serine/threonine-protein kinase 1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9BUB5};
DE AltName: Full=MAP kinase signal-integrating kinase 1;
DE Short=MAPK signal-integrating kinase 1;
DE Short=Mnk1;
GN Name=mknk1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in the response to environmental stress and
CC cytokines. Appears to regulate translation by phosphorylating EIF4E,
CC thus increasing the affinity of this protein for the 7-methylguanosine-
CC containing mRNA cap (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BC080937; AAH80937.1; -; mRNA.
DR RefSeq; NP_001008051.1; NM_001008050.1.
DR AlphaFoldDB; Q66JF3; -.
DR SMR; Q66JF3; -.
DR STRING; 8364.ENSXETP00000052774; -.
DR PaxDb; Q66JF3; -.
DR DNASU; 493413; -.
DR GeneID; 493413; -.
DR KEGG; xtr:493413; -.
DR CTD; 8569; -.
DR Xenbase; XB-GENE-979969; mknk1.
DR eggNOG; KOG0607; Eukaryota.
DR InParanoid; Q66JF3; -.
DR OrthoDB; 608695at2759; -.
DR Reactome; R-XTR-1295596; Spry regulation of FGF signaling.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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 ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Translation regulation.
FT CHAIN 1..417
FT /note="MAP kinase-interacting serine/threonine-protein
FT kinase 1"
FT /id="PRO_0000226971"
FT DOMAIN 37..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 43..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 417 AA; 46786 MW; CE904268EFBBEA54 CRC64;
MVSSQPVPID DGGKRRKKKR RTRAMESFTG KFADLYRLTD ELLGEGAYAK VQGCVSLQNG
KDYAVKIVEK KAGHSRSRVF REVETLYQCQ GNKNILELIE FCEDDARFYL VFEKLRGGSI
LSHIQKRKHF NEREASKVVK DIASALDFLH TKGIAHRDLK PENILCEFKD KVSPVKICDF
DLGSGVKLNS ACTPITTPEL TTPCGSAEYM APEVVEVFTE EATFYDKRCD LWSLGVILYI
MLSGYPPFVG NCGADCGWDR GEMCRVCQNK LFESIQEGKY EFPEKDWSHI SNSAKDLISK
LLVRDAKERL SAAQVLQHPW LQGDAPERGL PTPLVLQRNS STKDLTIFAA EAVALNRQLS
QHDSDLNEEH ESFIHTVCSM RLSPPSKSRL AKRRAQAHAR KGGSHLTHTT VTSQGAT
