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 16-JUN-2009, entry version 62. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; 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 RT project: 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., RA Wellmann A., 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 CC cancer. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Two specific sites, Thr-707 (activation loop of CC the kinase domain) and Thr-849 (turn motif), need to be CC phosphorylated for its full activation (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm, CC perinuclear region (By similarity). Note=Nuclear and perinuclear CC Golgi region (By similarity). CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG). CC -!- PTM: Autophosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. PKC subfamily. CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SIMILARITY: Contains 3 REM (Hr1) repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC034126; AAH34126.1; -; mRNA. DR IPI; IPI00169493; -. DR RefSeq; NP_722500.1; -. DR UniGene; Mm.233843; -. DR HSSP; P31751; 1GZK. DR PhosphoSite; Q8K045; -. DR PRIDE; Q8K045; -. DR Ensembl; ENSMUSG00000026785; Mus musculus. DR GeneID; 263803; -. DR KEGG; mmu:263803; -. DR MGI; MGI:2388285; Pkn3. DR HOGENOM; Q8K045; -. DR HOVERGEN; Q8K045; -. DR OMA; Q8K045; IFSKRRG. DR BRENDA; 2.7.11.13; 244. DR NextBio; 392137; -. DR Bgee; Q8K045; -. DR CleanEx; MM_PKN3; -. DR GermOnline; ENSMUSG00000026785; Mus musculus. 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:protein kinase C activity; IEA:EC. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR000861; HR1-like_rho-bd. DR InterPro; IPR011072; HR1_rho-bd. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR017442; Se/Thr_pkinase-rel. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Gene3D; G3DSA:1.10.287.160; HR1_rho-bd; 3. DR Pfam; PF02185; HR1; 3. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00742; Hr1; 3. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 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. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; KW Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 878 Serine/threonine-protein kinase N3. FT /FTId=PRO_0000055726. FT REPEAT 15 87 REM 1. FT REPEAT 98 169 REM 2. FT REPEAT 171 249 REM 3. FT DOMAIN 548 807 Protein kinase. FT DOMAIN 808 878 AGC-kinase C-terminal. FT NP_BIND 554 562 ATP (By similarity). FT COMPBIAS 456 543 Pro-rich. FT ACT_SITE 673 673 Proton acceptor (By similarity). FT BINDING 577 577 ATP (By similarity). FT MOD_RES 300 300 Phosphoserine (By similarity). FT MOD_RES 539 539 Phosphothreonine (By similarity). FT MOD_RES 707 707 Phosphothreonine (By similarity). FT MOD_RES 711 711 Phosphothreonine (By similarity). FT MOD_RES 849 849 Phosphothreonine (Probable). 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 //