STK40_XENTR
ID STK40_XENTR Reviewed; 443 AA.
AC Q7T0B0; B1H340;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Serine/threonine-protein kinase 40;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase lyk4;
GN Name=stk40;
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 [MRNA].
RC TISSUE=Egg;
RA Shan Y.X., Yu L.;
RT "Cloning and characterization of human, mouse, rat, chick and frog lyk4
RT gene.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAI61237.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus {ECO:0000312|EMBL:AAI61237.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
CC -!- FUNCTION: May be a negative regulator of NF-kappa-B and p53-mediated
CC gene transcription. {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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from X.laevis. However,
CC sequence identity with X.tropicalis is much higher than with X.laevis,
CC suggesting that the sequence is from X.tropicalis. {ECO:0000305}.
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DR EMBL; AY336058; AAQ01592.1; -; mRNA.
DR EMBL; AAMC01091013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01091014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC161237; AAI61237.1; -; mRNA.
DR RefSeq; NP_001120455.1; NM_001126983.1.
DR RefSeq; XP_012811947.1; XM_012956493.2.
DR AlphaFoldDB; Q7T0B0; -.
DR SMR; Q7T0B0; -.
DR PRIDE; Q7T0B0; -.
DR Ensembl; ENSXETT00000011493; ENSXETP00000011493; ENSXETG00000005259.
DR GeneID; 100145549; -.
DR KEGG; xtr:100145549; -.
DR CTD; 83931; -.
DR Xenbase; XB-GENE-1007328; stk40.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_035107_0_0_1; -.
DR OMA; RMKRRIC; -.
DR OrthoDB; 1362510at2759; -.
DR TreeFam; TF329785; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000005259; Expressed in egg cell and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP 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 CDD; cd13974; STKc_SHIK; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR024236; Ser/Thr_kinase_40.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024104; Tribbles/Ser_Thr_kinase_40.
DR PANTHER; PTHR22961; PTHR22961; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..443
FT /note="Serine/threonine-protein kinase 40"
FT /id="PRO_0000252266"
FT DOMAIN 35..332
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 41..49
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"
FT CONFLICT 16
FT /note="R -> K (in Ref. 1; AAQ01592)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="E -> D (in Ref. 1; AAQ01592)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="R -> K (in Ref. 1; AAQ01592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 50140 MW; 606C8D1B179D133E CRC64;
MKRRASERDA GETSARSKAL CSSISGSNAK RAGPFILGPR LGNSPVPSIV QCLARKDGTD
DFYQLKILSL EERGDKAGET QEERQGKMLL HTEYSLLSLL HNQDGVVHHH GLFQDRTCEI
VEDLEANKLV RKMRKRICLV LDCLCAHDFS DKTADLINLQ HYVIKEKRLG ERETVVIFYD
VVRVVEALHK KNIVHRDLKL GNMVLNKRTH RITVTNFCLG KHLVSEDDLL KDQRGSPAYI
SPDVLSGRPY RGKPSDMWAL GVVLFTMLYG QFPFYDSIPQ ELFRKIKAAE YSIPEDGRVS
ESTVCLIRKL LVLDPQQRLT ASEVLESLGA IISSWQSMSS LSGPLQVVPD IDHLTSLENS
QEAKVTEESS QYEFENYMRQ QLLLAEEKNT IHEAKNFPQK RHFGNFPPIR RLGYDAQPVS
PLDAAILAQR YLPPPHMALS NSH
