ID   PKN1_BOVIN              Reviewed;         944 AA.
AC   A1A4I4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Serine/threonine-protein kinase N1;
DE            EC=2.7.11.13 {ECO:0000250|UniProtKB:Q16512};
DE   AltName: Full=Protein kinase C-like 1;
DE   AltName: Full=Protein kinase C-like PKN;
DE   AltName: Full=Protein kinase PKN-alpha;
DE   AltName: Full=Protein-kinase C-related kinase 1;
DE   AltName: Full=Serine-threonine protein kinase N;
GN   Name=PKN1; Synonyms=PKN, PRK1, PRKCL1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal brain;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PKC-related serine/threonine-protein kinase involved in
CC       various processes such as regulation of the intermediate filaments of
CC       the actin cytoskeleton, cell migration, tumor cell invasion and
CC       transcription regulation. Part of a signaling cascade that begins with
CC       the activation of the adrenergic receptor ADRA1B and leads to the
CC       activation of MAPK14. Regulates the cytoskeletal network by
CC       phosphorylating proteins such as VIM and neurofilament proteins NEFH,
CC       NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates
CC       'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to
CC       bind to microtubules, resulting in disruption of tubulin assembly. Acts
CC       as a key coactivator of androgen receptor (ANDR)-dependent
CC       transcription, by being recruited to ANDR target genes and specifically
CC       mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a
CC       specific tag for epigenetic transcriptional activation that promotes
CC       demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C.
CC       Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import
CC       in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-
CC       163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in
CC       vitro. {ECO:0000250|UniProtKB:Q16512}.
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         Evidence={ECO:0000250|UniProtKB:Q16512};
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; Evidence={ECO:0000250|UniProtKB:Q16512};
CC   -!- ACTIVITY REGULATION: Kinase activity is activated upon binding to Rho
CC       proteins (RHOA, RHOB and RAC1). Activated by lipids, particularly
CC       cardiolipin and to a lesser extent by other acidic phospholipids.
CC       Activated by caspase-3 (CASP3) cleavage during apoptosis. Two specific
CC       sites, Thr-776 (activation loop of the kinase domain) and Ser-918 (turn
CC       motif), need to be phosphorylated for its full activation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ZFAND6 (By similarity). Interacts with ANDR.
CC       Interacts with PRKCB. Interacts (via REM 1 and REM 2 repeats) with
CC       RAC1. Interacts (via REM 1 repeat) with RHOA. Interacts with RHOB.
CC       Interacts (via C-terminus) with PDPK1. Interacts with CCNT2; enhances
CC       MYOD1-dependent transcription. Component of a signaling complex
CC       containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this
CC       complex, AKAP13 interacts directly with PKN1, which in turn recruits
CC       MAPK14, MAP2K3 and ZAK (By similarity). {ECO:0000250|UniProtKB:P70268,
CC       ECO:0000250|UniProtKB:Q16512}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16512}. Nucleus
CC       {ECO:0000250|UniProtKB:Q16512}. Endosome
CC       {ECO:0000250|UniProtKB:Q16512}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q63433}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q63433}. Cleavage furrow
CC       {ECO:0000250|UniProtKB:Q16512}. Midbody {ECO:0000250|UniProtKB:Q16512}.
CC       Note=Associates with chromatin in a ligand-dependent manner.
CC       Localization to endosomes is mediated via its interaction with RHOB.
CC       Association to the cell membrane is dependent on Ser-377
CC       phosphorylation. Accumulates during telophase at the cleavage furrow
CC       and finally concentrates around the midbody in cytokinesis.
CC       {ECO:0000250|UniProtKB:Q16512, ECO:0000250|UniProtKB:Q63433}.
CC   -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC       {ECO:0000250}.
CC   -!- PTM: Autophosphorylated; preferably on serine. Phosphorylated during
CC       mitosis. {ECO:0000250|UniProtKB:Q16512}.
CC   -!- PTM: Activated by limited proteolysis with trypsin. {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; BC126539; AAI26540.1; -; mRNA.
DR   RefSeq; NP_001073715.1; NM_001080246.1.
DR   AlphaFoldDB; A1A4I4; -.
DR   SMR; A1A4I4; -.
DR   STRING; 9913.ENSBTAP00000022652; -.
DR   PaxDb; 9913-ENSBTAP00000022652; -.
DR   Ensembl; ENSBTAT00000070272.1; ENSBTAP00000074304.1; ENSBTAG00000017037.6.
DR   GeneID; 509080; -.
DR   KEGG; bta:509080; -.
DR   CTD; 5585; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017037; -.
DR   VGNC; VGNC:32945; PKN1.
DR   eggNOG; KOG0694; Eukaryota.
DR   GeneTree; ENSGT00940000154990; -.
DR   HOGENOM; CLU_000288_132_1_1; -.
DR   InParanoid; A1A4I4; -.
DR   OrthoDB; 5400441at2759; -.
DR   Reactome; R-BTA-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-BTA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   Reactome; R-BTA-8980692; RHOA GTPase cycle.
DR   Reactome; R-BTA-9013106; RHOC GTPase cycle.
DR   Reactome; R-BTA-9013149; RAC1 GTPase cycle.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000017037; Expressed in mesenteric lymph node and 106 other cell types or tissues.
DR   ExpressionAtlas; A1A4I4; baseline and differential.
DR   GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
DR   GO; GO:0035402; F:histone H3T11 kinase activity; ISS:UniProtKB.
DR   GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR   GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR   GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR   GO; GO:0006972; P:hyperosmotic response; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR   GO; GO:0002634; P:regulation of germinal center formation; IEA:Ensembl.
DR   GO; GO:0002637; P:regulation of immunoglobulin production; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0003014; P:renal system process; IEA:Ensembl.
DR   GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR   CDD; cd08687; C2_PKN-like; 1.
DR   CDD; cd11630; HR1_PKN1_2; 1.
DR   CDD; cd11636; HR1_PKN1_3; 1.
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; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037784; C2_PKN.
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; IPR037317; PKN1_HR1_2.
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; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356:SF246; SERINE_THREONINE-PROTEIN KINASE N1; 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; PS50004; C2; 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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cell membrane; Chromatin regulator; Coiled coil;
KW   Cytoplasm; Endosome; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   CHAIN           2..944
FT                   /note="Serine/threonine-protein kinase N1"
FT                   /id="PRO_0000394261"
FT   DOMAIN          25..100
FT                   /note="REM-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          113..194
FT                   /note="REM-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          200..281
FT                   /note="REM-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          308..471
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          617..876
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          877..944
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          528..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        742
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         623..631
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   SITE            109..110
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000250"
FT   SITE            455..456
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000250"
FT   SITE            559..560
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         375
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63433"
FT   MOD_RES         449
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         534
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         563
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         610
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         776
FT                   /note="Phosphothreonine; by PDPK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         780
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         916
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
FT   MOD_RES         918
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16512"
SQ   SEQUENCE   944 AA;  104133 MW;  11B6833ED4F8D57E CRC64;
     MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL KLKEGAENLR
     RATTDLGRNL GPVELVLRGS SRRLALLHQQ LQELHAHVVL PDPAVGVHDA PQSPGTGDSA
     CSATNLSRVA GLEKQLAIEL KVKQGAENMI QTYSNGSTKD RKLLLTAQQM LQDSKTKIDI
     IRMQLHRALQ ACQLESQAAP DEAQGSPDLG AVELRIEELR HHFRVEHAVA EGAKNVLRLL
     SAAKAPDRKA VSEAQEKLTE SNQKLGLLRE ALERRLGELP ADHPKGRLLR EELAAASSAA
     FSARLAGPFP ATHYSTLSKP APLTGTLEVR VVGCRDLPET IPWNPSPSVG GPGTPDSRTP
     FLSRPARGLY SRTGSLSGRS SLKAEAENTN EVSTVLKLDN TVVGQTSWKP CGPNAWDQSF
     TLELERAREL ELAVFWRDQR GLCALKFLKL EDFLDNERHE VQLDMEPQGC LVAEVTFRNP
     VIERIPRLRR QKKIFSKQQG KAFQRARQMN IDVATWVRLL RRLIPNATAT GTFSPGASPG
     PEARSTGDIS VEKLNLGTET DSSPQKSPLG PPSSPSSLSS PIQATTTTPE LPSETQETPG
     PTLCSPLRKS PLTLEDFKFL AVLGRGHFGK VLLSEFRPSG ELFAIKALKK GDIVARDEVE
     SLMCEKRILA AVTNAGHPFL VNLFGCFQTP EHVCFVMEYS AGGDLMLHIH SDVFSEPRAV
     FYSACVVLGL QFLHEHKIVY RDLKLDNLLL DTEGYVKIAD FGLCKEGMGY GDRTSTFCGT
     PEFLAPEVLT DTSYTRAVDW WGLGVLLYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL
     SAEAIGIMRR LLRRNPERRL GSSERDAEDV KKQPFFRTLG WDALLARRLP PPFVPTLAGR
     TDVSNFDEEF TGEAPTLSPP RDARPLTATE QAAFRDFDFV AGSC
//