MKNK1_XENLA
ID MKNK1_XENLA Reviewed; 418 AA.
AC Q9YGW0; Q66KH6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
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; Synonyms=mnk1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ono Y., Iwashita J., Sagata N.;
RT "cDNA cloning of Xenopus MNK1 and its biological activity in oocytes.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA75304.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023807; BAA75304.1; ALT_INIT; mRNA.
DR EMBL; BC080389; AAH80389.1; -; mRNA.
DR RefSeq; NP_001080920.1; NM_001087451.1.
DR RefSeq; XP_018114929.1; XM_018259440.1.
DR AlphaFoldDB; Q9YGW0; -.
DR SMR; Q9YGW0; -.
DR GeneID; 387327; -.
DR KEGG; xla:387327; -.
DR CTD; 387327; -.
DR Xenbase; XB-GENE-979975; mknk1.S.
DR OrthoDB; 608695at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 387327; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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..418
FT /note="MAP kinase-interacting serine/threonine-protein
FT kinase 1"
FT /id="PRO_0000226970"
FT DOMAIN 37..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
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 418 AA; 46916 MW; E3292089480A1D3C CRC64;
MVSSQPVPFD DGGKRRKKKR KTRAMESFTG KFADLYRLTD ELLGEGAYAK VQGCVSLQNG
KDYAVKIVEK KAGHSRSRVF REVETLYQCQ GNKNILELIE FCEDDARFYL VFEKLLGGSI
LSHIQKRKHF NEREASKVVK DIASALDFLH TKGIAHRDLK PENILCEFKD KVSPVKICDF
DLGSGVKLNS ACTTITTPEL TTPCGSAEYM APEVVEVFTE EATFYDKRCD LWSLGVILYI
MLSGYPPFVG NCGTDCGWDR GEVCRVCQNK LFESIQEGKY EFPEKDWSHI SISAKDLISK
LLVRDAKERL SAFQVLQHPW LQGDAPERGL PTPLVLQRNS STKDLTIFAA EAIAFNRQLS
QHDNDLNEED ESFIHAVCSM RLSPPSKSRL AKRRAQAHAR KGGSHPTHST VTASQGTP
