STK40_RAT
ID STK40_RAT Reviewed; 435 AA.
AC Q7TNL4; Q498V1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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; Synonyms=Lyk4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Placenta;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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DR EMBL; AY336055; AAQ01589.1; -; mRNA.
DR EMBL; BC100062; AAI00063.1; -; mRNA.
DR RefSeq; NP_898879.2; NM_183056.2.
DR RefSeq; XP_006238943.1; XM_006238881.3.
DR AlphaFoldDB; Q7TNL4; -.
DR SMR; Q7TNL4; -.
DR STRING; 10116.ENSRNOP00000032827; -.
DR PhosphoSitePlus; Q7TNL4; -.
DR PaxDb; Q7TNL4; -.
DR GeneID; 360230; -.
DR KEGG; rno:360230; -.
DR UCSC; RGD:727884; rat.
DR CTD; 83931; -.
DR RGD; 727884; Stk40.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; Q7TNL4; -.
DR OrthoDB; 1362510at2759; -.
DR PhylomeDB; Q7TNL4; -.
DR PRO; PR:Q7TNL4; -.
DR Proteomes; UP000002494; Unplaced.
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:0005977; P:glycogen metabolic process; ISO:RGD.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0060425; P:lung morphogenesis; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0003016; P:respiratory system process; ISO:RGD.
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..435
FT /note="Serine/threonine-protein kinase 40"
FT /id="PRO_0000252264"
FT DOMAIN 35..332
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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 397
FT /note="A -> T (in Ref. 2; AAI00063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 48960 MW; 8D2AA03152CE5211 CRC64;
MKRRASDRGA GETSAKAQAL GTGIAGNNAK RAGPFILGPR LGNSPVPSIV QCLARKDGTD
DFYQLKILTL EERGEQGIES QEERQGKMLL HTEYSLLSLL HTQDGVVHHH GLFQDRTCEA
VEDTESGRMV KKMKKRICLV LDCLCAHDFS DKTADLINLQ HYVIKEKRLS ERETVVIFYD
VVRVVEALHQ KNIVHRDLKL GNMVLNKRTH RITITNFCLG KHLVSEGDLL KDQRGSPAYI
SPDVLSGRPY RGKPSDMWAL GVVLFTMLYG QFPFYDSIPQ ELFRKIKAAE YTIPEDGRVS
ENTVCLIRKL LVLDPQQRLA AADVLEALSA IIASWQSLSS LSGPLQVVPD IDDQMSSSDS
SQEAKVTEEC SQYEFENYMR QQLLLAEEKS SIHEARAWVP KRQFGSMPPV RRLGHDAQPM
TSLDTAILAQ RYLRK
