PKN3_MOUSE
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 03-AUG-2022, entry version 160.
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; Q8K045; -.
DR PRIDE; Q8K045; -.
DR ProteomicsDB; 288230; -.
DR Antibodypedia; 31249; 192 antibodies from 28 providers.
DR DNASU; 263803; -.
DR Ensembl; ENSMUST00000045246; ENSMUSP00000041025; ENSMUSG00000026785.
DR GeneID; 263803; -.
DR KEGG; mmu:263803; -.
DR UCSC; uc008jbb.1; mouse.
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; NMNVAAW; -.
DR OrthoDB; 520651at2759; -.
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 76 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 138 other tissues.
DR ExpressionAtlas; Q8K045; baseline and differential.
DR Genevisible; Q8K045; MM.
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:0004698; F:calcium-dependent protein kinase C 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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd11622; HR1_PKN_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 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; SSF46585; SSF46585; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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
