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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Neural apoptosis-regulated convertase 1) (NARC-1) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)

 PCSK9_RAT               Reviewed;         691 AA.
P59996; Q5I6U6;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
07-NOV-2003, sequence version 1.
12-SEP-2018, entry version 122.
RecName: Full=Proprotein convertase subtilisin/kexin type 9;
EC=3.4.21.-;
AltName: Full=Neural apoptosis-regulated convertase 1;
Short=NARC-1;
AltName: Full=Proprotein convertase 9;
Short=PC9;
AltName: Full=Subtilisin/kexin-like protease PC9;
Flags: Precursor;
Name=Pcsk9; Synonyms=Narc1;
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.
Chiang L.W.;
"Narc-1, novel subtilase-like homologs.";
Patent number WO0157081, 09-AUG-2001.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
Petkov P., Grozdanov P., Hadjiolova K., Karagyozov L., Dabeva M.;
"Rat proprotein convertase subtilisin/kexin type 9.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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]
CHARACTERIZATION.
PubMed=12552133; DOI=10.1073/pnas.0335507100;
Seidah N.G., Benjannet S., Wickham L., Marcinkiewicz J., Jasmin S.B.,
Stifani S., Basak A., Prat A., Chretien M.;
"The secretory proprotein convertase neural apoptosis-regulated
convertase 1 (NARC-1): liver regeneration and neuronal
differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 100:928-933(2003).
[5]
CHARACTERIZATION, AUTOCATALYTIC CLEAVAGE SITE, AND MUTAGENESIS OF
GLN-151; SER-152; HIS-225 AND SER-385.
PubMed=14622975; DOI=10.1016/j.abb.2003.09.011;
Naureckiene S., Ma L., Sreekumar K., Purandare U., Lo C.F., Huang Y.,
Chiang L.W., Grenier J.M., Ozenberger B.A., Jacobsen J.S.,
Kennedy J.D., DiStefano P.S., Wood A., Bingham B.;
"Functional characterization of Narc 1, a novel proteinase related to
proteinase K.";
Arch. Biochem. Biophys. 420:55-67(2003).
-!- FUNCTION: Crucial player in the regulation of plasma cholesterol
homeostasis. Binds to low-density lipid receptor family members:
low density lipoprotein receptor (LDLR), very low density
lipoprotein receptor (VLDLR), apolipoprotein E receptor
(LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and
promotes their degradation in intracellular acidic compartments.
Acts via a non-proteolytic mechanism to enhance the degradation of
the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway.
May prevent the recycling of LDLR from endosomes to the cell
surface or direct it to lysosomes for degradation. Can induce
ubiquitination of LDLR leading to its subsequent degradation.
Inhibits intracellular degradation of APOB via the
autophagosome/lysosome pathway in a LDLR-independent manner.
Involved in the disposal of non-acetylated intermediates of BACE1
in the early secretory pathway. Inhibits epithelial Na(+) channel
(ENaC)-mediated Na(+) absorption by reducing ENaC surface
expression primarily by increasing its proteasomal degradation.
Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels
and related anti-apoptotic signaling pathways (By similarity).
{ECO:0000250}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Its proteolytic activity is autoinhibited by
the non-covalent binding of the propeptide to the catalytic
domain. Inhibited by EGTA (By similarity). {ECO:0000250}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8-11.;
Temperature dependence:
Optimum temperature is 37 degrees Celsius.;
-!- SUBUNIT: Monomer. Can self-associate to form dimers and higher
multimers which may have increased LDLR degrading activity. The
precursor protein but not the mature protein may form multimers.
Interacts with APOB, VLDLR, LRP8/APOER2 and BACE1. The full-length
immature form (pro-PCSK9) interacts with SCNN1A, SCNN1B and
SCNN1G. The pro-PCSK9 form (via C-terminal domain) interacts with
LDLR. Interacts (via the C-terminal domain) with ANXA2 (via repeat
Annexin 1); the interaction inhibits the degradation of LDLR.
{ECO:0000250|UniProtKB:Q8NBP7}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted
{ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}.
Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is
required to transport it from the endoplasmic reticulum to the
Golgi apparatus and for the secretion of the mature protein.
Localizes to the endoplasmic reticulum in the absence of LDLR and
colocalizes to the cell surface and to the endosomes/lysosomes in
the presence of LDLR. The sorting to the cell surface and
endosomes is required in order to fully promote LDLR degradation
(By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in 12-day embryo. In the
adult, strongly expressed in liver, small intestine, jejunum, and
to a lesser extent in kidney, lung, spleen and thymus. Expression
in the liver is up-regulated following partial hepatectomy.
-!- DOMAIN: The C-terminal domain (CRD) is essential for the LDLR-
binding and degrading activities. {ECO:0000250}.
-!- DOMAIN: The catalytic domain is responsible for mediating its
self-association. {ECO:0000250}.
-!- PTM: Cleavage by furin and PCSK5 generates a truncated inactive
protein that is unable to induce LDLR degradation. {ECO:0000250}.
-!- PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum
to release the propeptide from the N-terminus and the cleavage of
the propeptide is strictly required for its maturation and
activation. The cleaved propeptide however remains associated with
the catalytic domain through non-covalent interactions, preventing
potential substrates from accessing its active site. As a result,
it is secreted from cells as a propeptide-containing,
enzymatically inactive protein (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylation protects the propeptide against proteolysis.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAC60363.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AX207690; CAC60363.1; ALT_INIT; Unassigned_DNA.
EMBL; AY847775; AAW31850.1; -; mRNA.
EMBL; BC133063; AAI33064.1; -; mRNA.
RefSeq; NP_954862.2; NM_199253.2.
UniGene; Rn.19195; -.
ProteinModelPortal; P59996; -.
SMR; P59996; -.
STRING; 10116.ENSRNOP00000008536; -.
MEROPS; S08.039; -.
iPTMnet; P59996; -.
PhosphoSitePlus; P59996; -.
PaxDb; P59996; -.
PRIDE; P59996; -.
Ensembl; ENSRNOT00000008535; ENSRNOP00000008536; ENSRNOG00000006280.
GeneID; 298296; -.
KEGG; rno:298296; -.
UCSC; RGD:728909; rat.
CTD; 255738; -.
RGD; 728909; Pcsk9.
eggNOG; KOG1153; Eukaryota.
eggNOG; COG1404; LUCA.
GeneTree; ENSGT00490000043472; -.
HOGENOM; HOG000049267; -.
HOVERGEN; HBG053530; -.
InParanoid; P59996; -.
KO; K13050; -.
OMA; HVLTGCS; -.
OrthoDB; EOG091G067E; -.
PhylomeDB; P59996; -.
TreeFam; TF106271; -.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-RNO-8866427; VLDLR internalisation and degradation.
Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
Reactome; R-RNO-8964038; LDL clearance.
PRO; PR:P59996; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000006280; Expressed in 5 organ(s), highest expression level in liver.
Genevisible; P59996; RN.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005770; C:late endosome; ISS:UniProtKB.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:1990667; C:PCSK9-AnxA2 complex; IEA:Ensembl.
GO; GO:1990666; C:PCSK9-LDLR complex; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0034185; F:apolipoprotein binding; ISS:UniProtKB.
GO; GO:0034190; F:apolipoprotein receptor binding; IEA:Ensembl.
GO; GO:0030169; F:low-density lipoprotein particle binding; ISS:UniProtKB.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISS:HGNC.
GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
GO; GO:0030547; F:receptor inhibitor activity; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:HGNC.
GO; GO:0019871; F:sodium channel inhibitor activity; IEA:Ensembl.
GO; GO:0034189; F:very-low-density lipoprotein particle binding; ISS:UniProtKB.
GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:HGNC.
GO; GO:0009267; P:cellular response to starvation; IDA:HGNC.
GO; GO:0042632; P:cholesterol homeostasis; IEP:RGD.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0001822; P:kidney development; IEP:HGNC.
GO; GO:0042157; P:lipoprotein metabolic process; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEP:HGNC.
GO; GO:0032802; P:low-density lipoprotein particle receptor catabolic process; ISS:UniProtKB.
GO; GO:0007041; P:lysosomal transport; IEA:Ensembl.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:1905596; P:negative regulation of low-density lipoprotein particle receptor binding; IEA:Ensembl.
GO; GO:1905598; P:negative regulation of low-density lipoprotein receptor activity; IEA:Ensembl.
GO; GO:0001920; P:negative regulation of receptor recycling; IEA:Ensembl.
GO; GO:1905601; P:negative regulation of receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl.
GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0022008; P:neurogenesis; IEP:HGNC.
GO; GO:0030182; P:neuron differentiation; ISS:HGNC.
GO; GO:0006644; P:phospholipid metabolic process; IEA:Ensembl.
GO; GO:0032805; P:positive regulation of low-density lipoprotein particle receptor catabolic process; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:HGNC.
GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
GO; GO:0016540; P:protein autoprocessing; IDA:RGD.
GO; GO:0016485; P:protein processing; IDA:RGD.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 1.
Gene3D; 3.30.70.80; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR034193; PCSK9_ProteinaseK-like.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
Pfam; PF00082; Peptidase_S8; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 1.
1: Evidence at protein level;
Apoptosis; Autocatalytic cleavage; Calcium; Cholesterol metabolism;
Complete proteome; Cytoplasm; Disulfide bond; Endoplasmic reticulum;
Endosome; Glycoprotein; Golgi apparatus; Hydrolase; Lipid metabolism;
Lysosome; Phosphoprotein; Protease; Reference proteome; Secreted;
Serine protease; Signal; Steroid metabolism; Sterol metabolism;
Sulfation; Zymogen.
SIGNAL 1 30 {ECO:0000255}.
PROPEP 31 151
/FTId=PRO_0000027124.
CHAIN 152 691 Proprotein convertase subtilisin/kexin
type 9.
/FTId=PRO_0000027125.
DOMAIN 181 422 Peptidase S8.
REGION 449 691 C-terminal domain. {ECO:0000250}.
MOTIF 495 497 Cell attachment site. {ECO:0000255}.
ACT_SITE 185 185 Charge relay system. {ECO:0000250}.
ACT_SITE 225 225 Charge relay system. {ECO:0000250}.
ACT_SITE 385 385 Charge relay system. {ECO:0000250}.
SITE 151 152 Cleavage; by autolysis.
SITE 217 218 Cleavage; by furin and PCSK5.
{ECO:0000250}.
MOD_RES 37 37 Sulfotyrosine. {ECO:0000250}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NBP7}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NBP7}.
CARBOHYD 532 532 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 222 254 {ECO:0000255}.
DISULFID 322 357 {ECO:0000255}.
DISULFID 456 526 {ECO:0000255}.
DISULFID 476 525 {ECO:0000255}.
DISULFID 485 508 {ECO:0000255}.
DISULFID 533 600 {ECO:0000255}.
DISULFID 551 599 {ECO:0000255}.
DISULFID 561 587 {ECO:0000255}.
DISULFID 607 678 {ECO:0000255}.
DISULFID 625 677 {ECO:0000255}.
DISULFID 634 653 {ECO:0000255}.
MUTAGEN 151 151 Q->E,N: No effect; when associated with
A-152. {ECO:0000269|PubMed:14622975}.
MUTAGEN 151 151 Q->I: Abolishes autocleavage; when
associated with V-152.
{ECO:0000269|PubMed:14622975}.
MUTAGEN 152 152 S->A: No effect; when associated with E-
151 or N-151.
{ECO:0000269|PubMed:14622975}.
MUTAGEN 152 152 S->V: Abolishes autocleavage; when
associated with I-151.
{ECO:0000269|PubMed:14622975}.
MUTAGEN 225 225 H->W: Abolishes autocleavage.
{ECO:0000269|PubMed:14622975}.
MUTAGEN 385 385 S->A: Abolishes autocleavage.
{ECO:0000269|PubMed:14622975}.
SEQUENCE 691 AA; 74709 MW; 8084A880CCAE5BA6 CRC64;
MGIRCSTWLR WPLSPQLLLL LLLCPTGSRA QDEDGDYEEL MLALPSQEDS LVDEASHVAT
ATFRRCSKEA WRLPGTYVVV LMEETQRLQV EQTAHRLQTW AARRGYVIKV LHVFYDLFPG
FLVKMSSDLL GLALKLPHVE YIEEDSLVFA QSIPWNLERI IPAWQQTEED SSPDGSSQVE
VYLLDTSIQS GHREIEGRVT ITDFNSVPEE DGTRFHRQAS KCDSHGTHLA GVVSGRDAGV
AKGTSLHSLR VLNCQGKGTV SGTLIGLEFI RKSQLIQPSG PLVVLLPLAG GYSRILNTAC
QRLARTGVVL VAAAGNFRDD ACLYSPASAP EVITVGATNA QDQPVTLGTL GTNFGRCVDL
FAPGKDIIGA SSDCSTCYMS QSGTSQAAAH VAGIVAMMLN RDPALTLAEL RQRLILFSTK
DVINMAWFPE DQRVLTPNRV ATLPPSTQET GGQLLCRTVW SAHSGPTRTA TATARCAPEE
ELLSCSSFSR SGRRRGDRIE AIGGQQVCKA LNAFGGEGVY AVARCCLLPR VNCSIHNTPA
ARAGPQTPVH CHQKDHVLTG CSFHWEVENL RAQQQPLLRS RHQPGQCVGH QEASVHASCC
HAPGLECKIK EHGIAGPAEQ VTVACEAGWT LTGCNVLPGA SLPLGAYSVD NVCVARIRDA
GRADRTSEEA TVAAAICCRS RPSAKASWVH Q


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