ID   PKN3_MOUSE              Reviewed;         878 AA.
AC   Q8K045;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Serine/threonine-protein kinase N3;
DE            EC=2.7.11.13;
DE   AltName: Full=Protein kinase PKN-beta;
DE   AltName: Full=Protein-kinase C-related kinase 3;
GN   Name=Pkn3; Synonyms=Pknbeta;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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).
RN   [2]
RP   FUNCTION IN MALIGNANT CELL GROWTH.
RX   PubMed=15282551; DOI=10.1038/sj.emboj.7600345;
RA   Leenders F., Moepert K., Schmiedeknecht A., Santel A., Czauderna F.,
RA   Aleku M., Penschuck S., Dames S., Sternberger M., Roehl T., Wellmann A.,
RA   Arnold W., Giese K., Kaufmann J., Klippel A.;
RT   "PKN3 is required for malignant prostate cell growth downstream of
RT   activated PI 3-kinase.";
RL   EMBO J. 23:3303-3313(2004).
CC   -!- FUNCTION: Contributes to invasiveness in malignant prostate cancer.
CC       {ECO:0000269|PubMed:15282551}.
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=2.7.11.13;
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=2.7.11.13;
CC   -!- ACTIVITY REGULATION: Two specific sites, Thr-707 (activation loop of
CC       the kinase domain) and Thr-849 (turn motif), need to be phosphorylated
CC       for its full activation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear
CC       region {ECO:0000250}. Note=Nuclear and perinuclear Golgi region.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000305}.
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DR   EMBL; BC034126; AAH34126.1; -; mRNA.
DR   CCDS; CCDS15867.1; -.
DR   RefSeq; NP_722500.1; NM_153805.1.
DR   AlphaFoldDB; Q8K045; -.
DR   SMR; Q8K045; -.
DR   BioGRID; 234455; 4.
DR   STRING; 10090.ENSMUSP00000041025; -.
DR   iPTMnet; Q8K045; -.
DR   PhosphoSitePlus; Q8K045; -.
DR   MaxQB; Q8K045; -.
DR   PaxDb; 10090-ENSMUSP00000041025; -.
DR   ProteomicsDB; 288230; -.
DR   Antibodypedia; 31249; 217 antibodies from 29 providers.
DR   DNASU; 263803; -.
DR   Ensembl; ENSMUST00000045246.8; ENSMUSP00000041025.8; ENSMUSG00000026785.15.
DR   GeneID; 263803; -.
DR   KEGG; mmu:263803; -.
DR   UCSC; uc008jbb.1; mouse.
DR   AGR; MGI:2388285; -.
DR   CTD; 29941; -.
DR   MGI; MGI:2388285; Pkn3.
DR   VEuPathDB; HostDB:ENSMUSG00000026785; -.
DR   eggNOG; KOG0694; Eukaryota.
DR   GeneTree; ENSGT00940000161818; -.
DR   HOGENOM; CLU_000288_132_1_1; -.
DR   InParanoid; Q8K045; -.
DR   OMA; HDPNHTD; -.
DR   OrthoDB; 5400441at2759; -.
DR   PhylomeDB; Q8K045; -.
DR   TreeFam; TF102005; -.
DR   Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR   Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR   Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR   BioGRID-ORCS; 263803; 1 hit in 81 CRISPR screens.
DR   ChiTaRS; Pkn3; mouse.
DR   PRO; PR:Q8K045; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8K045; Protein.
DR   Bgee; ENSMUSG00000026785; Expressed in humerus cartilage element and 141 other cell types or tissues.
DR   ExpressionAtlas; Q8K045; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0010631; P:epithelial cell migration; ISO:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd11622; HR1_PKN_1; 1.
DR   CDD; cd05589; STKc_PKN; 1.
DR   Gene3D; 1.10.287.160; HR1 repeat; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036274; HR1_rpt_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR037313; PKN_HR1_1.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF242; PROTEIN KINASE C; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF02185; HR1; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00742; Hr1; 3.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF46585; HR1 repeat; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51860; REM_1; 3.
DR   Genevisible; Q8K045; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..878
FT                   /note="Serine/threonine-protein kinase N3"
FT                   /id="PRO_0000055726"
FT   DOMAIN          2..77
FT                   /note="REM-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          86..165
FT                   /note="REM-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          169..238
FT                   /note="REM-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          548..807
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          808..878
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          461..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        673
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         554..562
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5Z2"
FT   MOD_RES         707
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5Z2"
FT   MOD_RES         711
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5Z2"
FT   MOD_RES         849
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5Z2, ECO:0000305"
SQ   SEQUENCE   878 AA;  97881 MW;  F4DC174A6E89047D CRC64;
     MEHRKPGTGQ RAPKDEKEMV RRAIQKELKI KEGMENMRRV ATDRRHLGHV QQLLRASNRR
     LEQLHGELRE LHAQVLLPAS AEPVTSEPQP RAEQSRARLS EALHRQLQVE LKVKQGAENM
     IHTCASGTPK ERKLLAAAQQ MLKDSQLKVA LLRMKISSLE SSGSPEPGPD LLAEELQHRL
     RVEAAVAAGA KNVVKLLGGQ RMQDRKALAE AQAQLQESSQ KLDLLRLALE LLLERLPPTH
     SLRSRVTQEL WMAMLGNPQP LGTLVKPIAL TGTLQVRLLG CKDLLVAVPG RSPMAVLAGS
     PSESWLRTRS RQQRGGGELA SEVLAVLKVD NRVVGQTGWG LVAEKSWDQS FIISLDRARE
     LEIGVHWRDW RQLCGVAFLK LEDFLDNACH QLSLSLVPQG RLFAQVTFCE PVIERRPRLQ
     RQRCIFSKRR GRDFMRASQM NLSMAAWGRL VMSLLPPCSS PNTASPPKGR PSTAVCGTPS
     AASPSNFLPM KTLSKEDTKP PPKPPRLYLQ EPAPGTPCTK RPHMDPRPAV VPALAALSTR
     KPPRLQDFRC LAVLGRGHFG KVLLVQYKGT GKYYAIKALK KQEVLGRDEI DSLYCEKRIL
     ETVGRTGHPF LLSLLACLQT SSHACFVTEF LPGGDLMAQI HEDVFPEPQA CFYLACVVLG
     LQFLHEKRII YRDLKLDNLL LDAQGFLKIA DFGLCKEGIG FGDRTSTFCG TPEFLAPEVL
     TQEAYTRAVD WWGLGVLLYE MLVGECPFPG DTEEEVFECI VSADVPCPHF LSVQGLELIQ
     KLLQKSPEKR LGAGERDAEE IKVQPFFRTT NWQALLARTV QPPFVPTLCG PADLRYFEGE
     FTSLPPTLTP PVSQSSLTAR QQAAFRDFDF VSEQFLES
//