Reviewed, UniProtKB/Swiss-Prot Q63433 (PKN1_RAT)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase N1
    EC=2.7.11.13
Alternative name(s):
    Protein kinase C-like 1
    Protein-kinase C-related kinase 1
    Protein kinase C-like PKN
    Serine-threonine protein kinase N
    Protease-activated kinase 1
      Short name=PAK-1

Gene names

Name:	Pkn1
Synonyms:	Pkn, Prk1, Prkcl1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	946 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Can phosphorylate ribosomal protein S6. Mediates GTPase Rho dependent intracellular signaling.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids. 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.
Subunit structure	Interacts with RhoA, Rac1 and ZA20D3 By similarity.
Subcellular location	Cytoplasm.
Domain	The C1 domain does not bind the diacylglycerol (DAG).
Post-translational modification	Autophosphorylated; preferably on serine. Activated by limited proteolysis with trypsin.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 1 protein kinase domain. Contains 3 REM (Hr1) repeats.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from direct assay. Source: RGD signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase C activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 946	946	Serine/threonine-protein kinase N1		PRO_0000055721
Regions
	Repeat	34 – 110	77	REM 1
	Repeat	123 – 212	90	REM 2
	Repeat	213 – 294	82	REM 3
	Domain	328 – 464	137	C2
	Domain	619 – 878	260	Protein kinase
	Domain	879 – 946	68	AGC-kinase C-terminal
	Nucleotide binding	625 – 633	9	ATP By similarity
Sites
	Active site	744	1	Proton acceptor By similarity
	Binding site	648	1	ATP By similarity
Amino acid modifications
	Modified residue	356	1	Phosphothreonine By similarity
	Modified residue	379	1	Phosphoserine By similarity
	Modified residue	451	1	N6-acetyllysine By similarity
	Modified residue	536	1	Phosphoserine By similarity
	Modified residue	540	1	Phosphoserine By similarity
	Modified residue	562	1	Phosphoserine By similarity
	Modified residue	565	1	Phosphoserine By similarity
	Modified residue	778	1	Phosphothreonine Potential
	Modified residue	782	1	Phosphothreonine By similarity
	Modified residue	920	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63433-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: FE9D4EFF8E9EEA4B	FASTA	946	104,469
	10 20 30 40 50 60 MAGDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLKREIRKEL KLKEGAENLR 70 80 90 100 110 120 RATTDLGRSL APVELLLRGS ARRLDLLHQQ LQELHAHVVL PDPTAGSDAP QSLAEGSPVC 130 140 150 160 170 180 SSTNLSRVAG LEKQLAIELK VKQGAENMIQ TYSNGSTKDR KLLLTAQQML QDSKTKIDII 190 200 210 220 230 240 RMQLRRALQA LQAGQLESQA APDEAHGDPD LGAVELRIEE LRHHFRVEHA VAEGAKNVLR 250 260 270 280 290 300 LLSAAKAPDR KAVSEAQEKL TESNQKLGLL RESLERRLGE LPADHPKGRL LREELTAASS 310 320 330 340 350 360 AAFSAILPGP FPATHYSTLS KPAPLTGTLE VRVVGCKNLP ETIPWSPPPS VGASGTPDSR 370 380 390 400 410 420 TPFLSRPARG LYNRSGSLSG RSSLKGEAEN STEVSTVLKL DNTVVGQTAW KPCGPNAWDQ 430 440 450 460 470 480 SFTLELERAR ELELAVFWRD QRGLCALKFL KLEDFLDNER HEVQLDMEPQ GCLVAEVTFR 490 500 510 520 530 540 NPIIERIPRL QRQKKIFSKQ QGQTFQRARH MNIDVATWVR LLRRLIPNAV ATGSFSPNAS 550 560 570 580 590 600 PGSEIRSTGD ISMEKLNLGA DSDSSSQKSP AGLPSTSCSL SSPTHESTTS PELPSETQET 610 620 630 640 650 660 PGPGLCSPLR KSPLTLEDFK FLAVLGRGHF GKVLLSEFHS SGELFAIKAL KKGDIVARDE 670 680 690 700 710 720 VESLMCEKRI LATVTRAGHP FLVNLFGCFQ TPEHVCFVME YSAGGDLMLH IHSDVFSEPR 730 740 750 760 770 780 AGFYSACVVL GLQFLHEHKI VYRDLKLDNL LLDTEGYVKI ADFGLCKEGM GYGDRTSTFC 790 800 810 820 830 840 GTPEFLAPEV LTDTSYTRAV DWWGLGVFLY EMLVGESPFP GDDEEEVFDS IVNDEVRYPR 850 860 870 880 890 900 FLSAEAIGIM RRLLRRNPER RLGSTERDAE DVKKQPFFRT LDWDALLARR LPPPFVPTLS 910 920 930 940 GRTDVSNFDE EFTGEAPTLS PPRDARPLTA AEQAAFRDFD FVAGGY

References

[1]	"A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C." Mukai H., Ono Y. Biochem. Biophys. Res. Commun. 199:897-904(1994) [PubMed: 8135837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[2]	"A cardiolipin-activated protein kinase from rat liver structurally distinct from the protein kinases C." Morrice N.A., Gabrielli B., Kemp B.E., Wettenhall R.E. J. Biol. Chem. 269:20040-20046(1994) [PubMed: 8051089] [Abstract] Cited for: CHARACTERIZATION. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D26180 mRNA. Translation: BAA05168.1.
IPI	IPI00780192.
RefSeq	NP_058871.2.
UniGene	Rn.49880
3D structure databases
HSSP	HSSP built from PDB template 1GZK based on UniProtKB P31751.
SMR	Q63433. Positions 13-98, 122-202.
ModBase	Search...
Protein-protein interaction databases
STRING	Q63433.
PTM databases
PhosphoSite	Q63433.
Genome annotation databases
Ensembl	ENSRNOT00000005770; ENSRNOP00000005770; ENSRNOG00000004131; Rattus norvegicus. [Genome view] ENSRNOT00000060050; ENSRNOP00000056799; ENSRNOG00000004131; Rattus norvegicus. [Genome view]
GeneID	29355.
KEGG	rno:29355.
UCSC	BC061836. rat.
Organism-specific databases
CTD	29355.
RGD	69308. Pkn1.
Phylogenomic databases
HOVERGEN	Q63433.
Enzyme and pathway databases
BRENDA	2.7.11.13. 248.
Gene expression databases
ArrayExpress	Q63433.
Genevestigator	Q63433.
GermOnline	ENSRNOG00000004131. Rattus norvegicus.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000008. C2_Ca-dep. IPR000861. HR1-like_rho-bd. IPR011072. HR1_rho-bd. IPR017892. Pkinase_C. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Gene3D	G3DSA:1.10.287.160. HR1_rho-bd. 3 hits.
Pfam	PF02185. HR1. 3 hits. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00239. C2. 1 hit. SM00742. Hr1. 3 hits. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS50004. C2. False negative. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	608866.

Entry information

Entry name

PKN1_RAT

Accession

Primary (citable) accession number: Q63433

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)