STK16_RAT
ID STK16_RAT Reviewed; 305 AA.
AC P57760;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine/threonine-protein kinase 16;
DE EC=2.7.11.1;
DE AltName: Full=Myristoylated and palmitoylated serine/threonine-protein kinase;
DE Short=MPSK;
DE AltName: Full=Protein kinase PKL12;
DE AltName: Full=TGF-beta-stimulated factor 1;
DE Short=TSF-1;
DE AltName: Full=Tyrosine-protein kinase STK16;
DE EC=2.7.10.2;
GN Name=Stk16; Synonyms=Mpsk1, Tsf1;
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], POSSIBLE FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=10947953; DOI=10.1042/bj3500395;
RA Ohta S., Takeuchi M., Deguchi M., Tsuji T., Gahara Y., Nagata K.;
RT "A novel transcriptional factor with Ser/Thr kinase activity involved in
RT the transforming growth factor (TGF)-beta signalling pathway.";
RL Biochem. J. 350:395-404(2000).
CC -!- FUNCTION: Membrane-associated protein kinase that phosphorylates on
CC serine and threonine residues. In vitro substrates include DRG1, ENO1
CC and EIF4EBP1. Also autophosphorylates (By similarity). May be involved
CC in secretory vesicle trafficking or intracellular signaling. May have a
CC role in regulating stromal-epithelial interactions that occur during
CC ductal morphogenesis in the mammary gland. May be involved in TGF-beta
CC signaling. Able to autophosphorylate on Tyr residue; it is however
CC unclear whether it has tyrosine-protein kinase toward other proteins.
CC {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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- SUBUNIT: Monomer. Interacts with DRG1 (via its N-terminal); the
CC interaction phosphorylates DRG1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi
CC and Golgi-derived vesicles. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, liver, brain, spleen, lung,
CC skeletal muscle, kidney and testis. {ECO:0000269|PubMed:10947953}.
CC -!- INDUCTION: By TGF-beta. {ECO:0000269|PubMed:10947953}.
CC -!- PTM: Mainly autophosphorylated on serine/threonine residues. Also
CC autophosphorylated on Tyr-198 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D86220; BAB16310.1; -; mRNA.
DR RefSeq; NP_775165.1; NM_173142.1.
DR AlphaFoldDB; P57760; -.
DR SMR; P57760; -.
DR STRING; 10116.ENSRNOP00000026194; -.
DR iPTMnet; P57760; -.
DR PhosphoSitePlus; P57760; -.
DR PaxDb; P57760; -.
DR PRIDE; P57760; -.
DR Ensembl; ENSRNOT00000026194; ENSRNOP00000026194; ENSRNOG00000019294.
DR GeneID; 286927; -.
DR KEGG; rno:286927; -.
DR UCSC; RGD:629474; rat.
DR CTD; 8576; -.
DR RGD; 629474; Stk16.
DR eggNOG; KOG2345; Eukaryota.
DR GeneTree; ENSGT00550000075037; -.
DR HOGENOM; CLU_000288_109_2_1; -.
DR InParanoid; P57760; -.
DR OMA; MHQYKVK; -.
DR OrthoDB; 831026at2759; -.
DR PhylomeDB; P57760; -.
DR TreeFam; TF350433; -.
DR BRENDA; 2.7.11.1; 5301.
DR PRO; PR:P57760; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000019294; Expressed in stomach and 19 other tissues.
DR Genevisible; P57760; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IDA:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75716"
FT CHAIN 2..305
FT /note="Serine/threonine-protein kinase 16"
FT /id="PRO_0000086703"
FT DOMAIN 20..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 166..202
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 197
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75716"
FT MOD_RES 198
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75716"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 8
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 305 AA; 34409 MW; 16E255E4732221CB CRC64;
MGHALCVCSR GTVIIDNKRY LFVQKLGEGG FSYVDLVEGL HDGHFYALKR ILCHEQQDQE
EAQREADMHR LFQHPNILRL MAYSLKERGA KHEAWLLLPF FKRGTLWNEI ERLKDQGNFL
TEDQILPLLL GICRGLEAIH AKGYAHRDLK PTNILLGDEG QPVLMDLGSM NQACIQVEGS
RQALALQDWA AQRCTISYRA PELFSVQSHC VIDERTDVWS LGCVLYAMMF GEGPYDMVFQ
KGDSVALAVQ NDLSIPQSPR HSSALRQLLA SMMTVDPQQR PHIPVLLSQL EALQPPAPGQ
HTTQI
