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Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9)

 PCSK9_PONPY             Reviewed;         690 AA.
A8T658;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 1.
28-FEB-2018, entry version 53.
RecName: Full=Proprotein convertase subtilisin/kexin type 9;
EC=3.4.21.-;
AltName: Full=Proprotein convertase 9;
Short=PC9;
AltName: Full=Subtilisin/kexin-like protease PC9;
Flags: Precursor;
Name=PCSK9;
Pongo pygmaeus (Bornean orangutan).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9600;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=17971861; DOI=10.1371/journal.pone.0001098;
Ding K., McDonough S.J., Kullo I.J.;
"Evidence for positive selection in the C-terminal domain of the
cholesterol metabolism gene PCSK9 based on phylogenetic analysis in 14
primate species.";
PLoS ONE 2:E1098-E1098(2007).
-!- 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};
-!- ENZYME 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}.
-!- 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}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; EF692500; ABV59220.1; -; mRNA.
ProteinModelPortal; A8T658; -.
SMR; A8T658; -.
HOVERGEN; HBG053530; -.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0034185; F:apolipoprotein binding; ISS:UniProtKB.
GO; GO:0030169; F:low-density lipoprotein particle binding; ISS:UniProtKB.
GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0034189; F:very-low-density lipoprotein particle binding; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0032802; P:low-density lipoprotein particle receptor catabolic process; ISS:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
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; IPR010259; S8pro/Inhibitor_I9.
InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
Pfam; PF05922; Inhibitor_I9; 1.
Pfam; PF00082; Peptidase_S8; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 1.
2: Evidence at transcript level;
Apoptosis; Autocatalytic cleavage; Calcium; Cholesterol metabolism;
Cytoplasm; Disulfide bond; Endoplasmic reticulum; Endosome;
Glycoprotein; Golgi apparatus; Hydrolase; Lipid metabolism; Lysosome;
Phosphoprotein; Protease; Secreted; Serine protease; Signal;
Steroid metabolism; Sterol metabolism; Sulfation; Zymogen.
SIGNAL 1 28 {ECO:0000250}.
PROPEP 29 150 {ECO:0000250}.
/FTId=PRO_0000318292.
CHAIN 151 690 Proprotein convertase subtilisin/kexin
type 9.
/FTId=PRO_0000318293.
DOMAIN 180 421 Peptidase S8.
REGION 448 690 C-terminal domain. {ECO:0000250}.
ACT_SITE 184 184 Charge relay system. {ECO:0000250}.
ACT_SITE 224 224 Charge relay system. {ECO:0000250}.
ACT_SITE 384 384 Charge relay system. {ECO:0000250}.
SITE 150 151 Cleavage; by autolysis. {ECO:0000250}.
SITE 216 217 Cleavage; by furin and PCSK5.
{ECO:0000250}.
MOD_RES 36 36 Sulfotyrosine. {ECO:0000250}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NBP7}.
MOD_RES 686 686 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NBP7}.
CARBOHYD 531 531 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 221 253 {ECO:0000255}.
DISULFID 321 356 {ECO:0000255}.
DISULFID 455 525 {ECO:0000255}.
DISULFID 475 524 {ECO:0000255}.
DISULFID 484 507 {ECO:0000255}.
DISULFID 532 599 {ECO:0000255}.
DISULFID 550 598 {ECO:0000255}.
DISULFID 560 586 {ECO:0000255}.
DISULFID 606 677 {ECO:0000255}.
DISULFID 624 676 {ECO:0000255}.
DISULFID 633 652 {ECO:0000255}.
SEQUENCE 690 AA; 74267 MW; 6A751CDB74E618E9 CRC64;
MGTVSSRRSW WPLPLLLLLL LGPAGARAQE DEDGDYEELV LALRSEEDGL AEAPEHGATA
TFHRCAKDPW RLPGTYVVVL KEETHRSQSE RTARRLQAQA ARRGYLTKIL HVFHDLLPGF
LVKMSGDLLE LALKLPHVDY IEEDSSVFAQ SIPWNLERIT PPRYRADEYQ PPDGGSLVEV
YLLDTSIQSD HREIEGRVMV TDFENVPEED GTRFHRQASK CDSHGTHLAG VVSGRDAGVA
KGASMRSLRV LNCQGKGTVS GTLIGLEFIR KSQLVQPVGP LVVLMPLAGG YSRVLNAACQ
RLARAGVVLV TAAGNFRDDA CLYSPASAPE VITVGATNAQ DQPVTLGTLG TNFGRCVDLF
APGEDIIGAS SDCSTCFVSQ SGTSQAAAHV AGIAAMMLSV EPELTLAELR QRLIHFSAKD
VINEVWFPED QRVLTPNLVA ALPPSTHGAG WQLFCRTVWS AHSGPTRMAT AIARCAPDEE
LLSCSSFSRS GKRRGERMEA QGGKLVCRAH NAFGGEGVCA IARCCLLPQA NCSVHTAPPA
GSGMGTRVLC HQQVHVLTGC SSHWEVEDLG THKPPVLRPR GQPNQCVGHR EASIHASCCR
APGLECKVKE HGIPAPQEQV TVACEEGWTL TGCSALPGTS HVLGAYAVDN TCVVRSRDIS
TTGSTSEEAM AAVAICCRRR HLAQASQELQ


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