PKN1_BOVIN
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 03-AUG-2022, entry version 109.
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; A1A4I4; -.
DR PRIDE; A1A4I4; -.
DR Ensembl; ENSBTAT00000070272; ENSBTAP00000074304; ENSBTAG00000017037.
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; 520651at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000017037; Expressed in mesenteric lymph node and 106 other 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
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 kinase activity (H3-T11 specific); 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: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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11630; HR1_PKN1_2; 1.
DR CDD; cd11622; HR1_PKN_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 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; 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
