ID   F2Z4A5_MOUSE            Unreviewed;       128 AA.
AC   F2Z4A5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   Flags: Fragment;
GN   Name=Pdpk1 {ECO:0000313|Ensembl:ENSMUSP00000121771.2,
GN   ECO:0000313|MGI:MGI:1338068};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000121771.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000121771.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121771.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000121771.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121771.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   AlphaFoldDB; F2Z4A5; -.
DR   SMR; F2Z4A5; -.
DR   MaxQB; F2Z4A5; -.
DR   PeptideAtlas; F2Z4A5; -.
DR   ProteomicsDB; 303865; -.
DR   Antibodypedia; 3794; 1207 antibodies from 47 providers.
DR   Ensembl; ENSMUST00000144533.8; ENSMUSP00000121771.2; ENSMUSG00000024122.17.
DR   AGR; MGI:1338068; -.
DR   MGI; MGI:1338068; Pdpk1.
DR   VEuPathDB; HostDB:ENSMUSG00000024122; -.
DR   GeneTree; ENSGT00940000155267; -.
DR   HOGENOM; CLU_1964591_0_0_1; -.
DR   OMA; GYPSIRA; -.
DR   ChiTaRS; Pdpk1; mouse.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000024122; Expressed in rostral migratory stream and 271 other cell types or tissues.
DR   ExpressionAtlas; F2Z4A5; baseline and differential.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR24356:SF163; 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1-RELATED; 1.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Proteomics identification {ECO:0007829|EPD:F2Z4A5,
KW   ECO:0007829|MaxQB:F2Z4A5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          58..128
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         128
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000121771.2"
SQ   SEQUENCE   128 AA;  14485 MW;  C221A25BEBDEF0AA CRC64;
     MVRSQTEPGS SPGIPSGVSR QGSTMDGTTA EARPSTNPLQ QHPAQLPPQP RKKRPEDFKF
     GKILGEGSFS TVVLARELAT SREYAIKILE KRHIIKENKV PYVTRERDVM SRLDHPFFVK
     LYFTFQDD
//