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Serine/threonine-protein kinase N1 (EC 2 7 11 13) (Protease-activated kinase 1) (PAK-1) (Protein kinase C-like 1) (Protein kinase C-like PKN) (Protein-kinase C-related kinase 1) (Serine-threonine protein kinase N)

 PKN1_RAT                Reviewed;         946 AA.
Q63433; Q6P748; Q8VIJ2;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
23-MAY-2018, entry version 163.
RecName: Full=Serine/threonine-protein kinase N1;
EC=2.7.11.13 {ECO:0000269|PubMed:8051089};
AltName: Full=Protease-activated kinase 1;
Short=PAK-1;
AltName: Full=Protein kinase C-like 1;
AltName: Full=Protein kinase C-like PKN;
AltName: Full=Protein-kinase C-related kinase 1;
AltName: Full=Serine-threonine protein kinase N;
Name=Pkn1; Synonyms=Pkn, Prk1, Prkcl1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=8135837; DOI=10.1006/bbrc.1994.1313;
Mukai H., Ono Y.;
"A novel protein kinase with leucine zipper-like sequences: its
catalytic domain is highly homologous to that of protein kinase C.";
Biochem. Biophys. Res. Commun. 199:897-904(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=8943281; DOI=10.1074/jbc.271.50.32233;
Peng B., Morrice N.A., Groenen L.C., Wettenhall R.E.;
"Phosphorylation events associated with different states of activation
of a hepatic cardiolipin/protease-activated protein kinase. Structural
identity to the protein kinase N-type protein kinases.";
J. Biol. Chem. 271:32233-32240(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 633-648; 747-767; 776-822; 880-889 AND 938-946,
FUNCTION, AND CATALYTIC ACTIVITY.
TISSUE=Liver;
PubMed=8051089;
Morrice N.A., Gabrielli B., Kemp B.E., Wettenhall R.E.;
"A cardiolipin-activated protein kinase from rat liver structurally
distinct from the protein kinases C.";
J. Biol. Chem. 269:20040-20046(1994).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-377.
PubMed=15375078; DOI=10.1096/fj.04-1876fje;
Zhu Y., Stolz D.B., Guo F., Ross M.A., Watkins S.C., Tan B.J.,
Qi R.Z., Manser E., Li Q.T., Bay B.H., Teo T.S., Duan W.;
"Signaling via a novel integral plasma membrane pool of a
serine/threonine protein kinase PRK1 in mammalian cells.";
FASEB J. 18:1722-1724(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: PKC-related serine/threonine-protein kinase involved in
various processes such as regulation of the intermediate filaments
of the actin cytoskeleton, cell migration, tumor cell invasion and
transcription regulation (PubMed:8051089, PubMed:15375078). Part
of a signaling cascade that begins with the activation of the
adrenergic receptor ADRA1B and leads to the activation of MAPK14
(By similarity). Regulates the cytoskeletal network by
phosphorylating proteins such as VIM and neurofilament proteins
NEFH, NEFL and NEFM, leading to inhibit their polymerization.
Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau,
lowering its ability to bind to microtubules, resulting in
disruption of tubulin assembly. Acts as a key coactivator of
androgen receptor (ANDR)-dependent transcription, by being
recruited to ANDR target genes and specifically mediating
phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific
tag for epigenetic transcriptional activation that promotes
demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C.
Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their
import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-
159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to
phosphorylate RPS6 in vitro (By similarity).
{ECO:0000250|UniProtKB:Q16512, ECO:0000269|PubMed:15375078,
ECO:0000269|PubMed:8051089}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:8051089}.
-!- ENZYME REGULATION: Kinase activity is activated upon binding to
Rho proteins (RHOA, RHOB and RAC1). Activated by lipids,
particularly cardiolipin and to a lesser extent by other acidic
phospholipids. Activated by caspase-3 (CASP3) cleavage during
apoptosis. Two specific sites, Thr-778 (activation loop of the
kinase domain) and Ser-920 (turn motif), need to be phosphorylated
for its full activation (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with ZFAND6 (By similarity). Interacts with
ANDR. Interacts with PRKCB. Interacts (via REM 1 and REM 2
repeats) with RAC1. Interacts (via REM 1 repeat) with RHOA.
Interacts with RHOB. Interacts (via C-terminus) with PDPK1.
Interacts with CCNT2; enhances MYOD1-dependent transcription.
Component of a signaling complex containing at least AKAP13, PKN1,
MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts
directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK
(By similarity). {ECO:0000250|UniProtKB:P70268,
ECO:0000250|UniProtKB:Q16512}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15375078}.
Nucleus {ECO:0000250|UniProtKB:Q16512}. Endosome
{ECO:0000250|UniProtKB:Q16512}. Cell membrane
{ECO:0000269|PubMed:15375078}; Peripheral membrane protein
{ECO:0000269|PubMed:15375078}. Cleavage furrow
{ECO:0000250|UniProtKB:Q16512}. Midbody
{ECO:0000250|UniProtKB:Q16512}. Note=Associates with chromatin in
a ligand-dependent manner (By similarity). Localization to
endosomes is mediated via its interaction with RHOB. Accumulates
during telophase at the cleavage furrow and finally concentrates
around the midbody in cytokinesis (By similarity). Association to
the cell membrane is dependent on Ser-377 phosphorylation.
{ECO:0000250|UniProtKB:Q16512, ECO:0000269|PubMed:15375078}.
-!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
{ECO:0000250}.
-!- PTM: Autophosphorylated; preferably on serine. Phosphorylated
during mitosis. {ECO:0000250|UniProtKB:Q16512}.
-!- PTM: Activated by limited proteolysis with trypsin. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D26180; BAA05168.1; -; mRNA.
EMBL; L35634; AAL31374.1; -; mRNA.
EMBL; BC061836; AAH61836.1; -; mRNA.
PIR; JC2130; JC2130.
RefSeq; NP_058871.2; NM_017175.2.
UniGene; Rn.49880; -.
ProteinModelPortal; Q63433; -.
SMR; Q63433; -.
BioGrid; 248010; 1.
DIP; DIP-60097N; -.
IntAct; Q63433; 1.
STRING; 10116.ENSRNOP00000005770; -.
iPTMnet; Q63433; -.
PhosphoSitePlus; Q63433; -.
PaxDb; Q63433; -.
PRIDE; Q63433; -.
Ensembl; ENSRNOT00000005770; ENSRNOP00000005770; ENSRNOG00000004131.
GeneID; 29355; -.
KEGG; rno:29355; -.
CTD; 5585; -.
RGD; 69308; Pkn1.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233032; -.
HOVERGEN; HBG108317; -.
InParanoid; Q63433; -.
KO; K06071; -.
OMA; TMYAIKA; -.
OrthoDB; EOG091G00YT; -.
BRENDA; 2.7.11.13; 5301.
Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
Reactome; R-RNO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
PRO; PR:Q63433; -.
Proteomes; UP000002494; Chromosome 19.
Bgee; ENSRNOG00000004131; -.
Genevisible; Q63433; RN.
GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0030496; C:midbody; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0050681; F:androgen receptor binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0017049; F:GTP-Rho binding; ISS:UniProtKB.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
GO; GO:0035402; F:histone kinase activity (H3-T11 specific); ISS:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:RGD.
GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
GO; GO:0035407; P:histone H3-T11 phosphorylation; ISS:UniProtKB.
GO; GO:0006972; P:hyperosmotic response; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
GO; GO:0002634; P:regulation of germinal center formation; IEA:Ensembl.
GO; GO:0002637; P:regulation of immunoglobulin production; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0003014; P:renal system process; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd08687; C2_PKN-like; 1.
CDD; cd11630; HR1_PKN1_2; 1.
CDD; cd11622; HR1_PKN_1; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR037784; C2_PKN.
InterPro; IPR011072; HR1_rho-bd.
InterPro; IPR036274; HR1_rpt_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR037317; PKN1_HR1_2.
InterPro; IPR037313; PKN_HR1_1.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF02185; HR1; 3.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00742; Hr1; 3.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF46585; SSF46585; 3.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS51860; REM_1; 3.
1: Evidence at protein level;
Acetylation; ATP-binding; Cell membrane; Chromatin regulator;
Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing;
Endosome; Kinase; Membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q16512}.
CHAIN 2 946 Serine/threonine-protein kinase N1.
/FTId=PRO_0000055721.
DOMAIN 25 100 REM-1 1. {ECO:0000255|PROSITE-
ProRule:PRU01207}.
DOMAIN 114 193 REM-1 2. {ECO:0000255|PROSITE-
ProRule:PRU01207}.
DOMAIN 202 283 REM-1 3. {ECO:0000255|PROSITE-
ProRule:PRU01207}.
DOMAIN 328 464 C2.
DOMAIN 619 878 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 879 946 AGC-kinase C-terminal.
NP_BIND 625 633 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 744 744 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 648 648 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 108 109 Cleavage; by caspase-3. {ECO:0000250}.
SITE 457 458 Cleavage; by caspase-3. {ECO:0000250}.
SITE 561 562 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000269|PubMed:15375078}.
MOD_RES 451 451 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 536 536 Phosphoserine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 543 543 Phosphoserine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 565 565 Phosphoserine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 778 778 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 782 782 Phosphothreonine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 918 918 Phosphothreonine.
{ECO:0000250|UniProtKB:Q16512}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 298 298 A -> R (in Ref. 2; AAL31374).
{ECO:0000305}.
CONFLICT 510 510 Q -> H (in Ref. 1; BAA05168).
{ECO:0000305}.
CONFLICT 650 650 L -> V (in Ref. 2; AAL31374).
{ECO:0000305}.
CONFLICT 722 722 V -> G (in Ref. 1; BAA05168).
{ECO:0000305}.
CONFLICT 808 808 L -> F (in Ref. 1; BAA05168).
{ECO:0000305}.
SEQUENCE 946 AA; 104468 MW; 63DF250C8D2DA444 CRC64;
MAGDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLKREIRKEL KLKEGAENLR
RATTDLGRSL APVELLLRGS ARRLDLLHQQ LQELHAHVVL PDPTAGSDAP QSLAEGSPVC
SSTNLSRVAG LEKQLAIELK VKQGAENMIQ TYSNGSTKDR KLLLTAQQML QDSKTKIDII
RMQLRRALQA LQAGQLESQA APDEAHGDPD LGAVELRIEE LRHHFRVEHA VAEGAKNVLR
LLSAAKAPDR KAVSEAQEKL TESNQKLGLL RESLERRLGE LPADHPKGRL LREELTAASS
AAFSAILPGP FPATHYSTLS KPAPLTGTLE VRVVGCKNLP ETIPWSPPPS VGASGTPDSR
TPFLSRPARG LYNRSGSLSG RSSLKGEAEN STEVSTVLKL DNTVVGQTAW KPCGPNAWDQ
SFTLELERAR ELELAVFWRD QRGLCALKFL KLEDFLDNER HEVQLDMEPQ GCLVAEVTFR
NPIIERIPRL QRQKKIFSKQ QGQTFQRARQ MNIDVATWVR LLRRLIPNAV ATGSFSPNAS
PGSEIRSTGD ISMEKLNLGA DSDSSSQKSP AGLPSTSCSL SSPTHESTTS PELPSETQET
PGPGLCSPLR KSPLTLEDFK FLAVLGRGHF GKVLLSEFHS SGELFAIKAL KKGDIVARDE
VESLMCEKRI LATVTRAGHP FLVNLFGCFQ TPEHVCFVME YSAGGDLMLH IHSDVFSEPR
AVFYSACVVL GLQFLHEHKI VYRDLKLDNL LLDTEGYVKI ADFGLCKEGM GYGDRTSTFC
GTPEFLAPEV LTDTSYTRAV DWWGLGVLLY EMLVGESPFP GDDEEEVFDS IVNDEVRYPR
FLSAEAIGIM RRLLRRNPER RLGSTERDAE DVKKQPFFRT LDWDALLARR LPPPFVPTLS
GRTDVSNFDE EFTGEAPTLS PPRDARPLTA AEQAAFRDFD FVAGGY


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