Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 PCSK9_SAIBB             Reviewed;         691 AA.
A8T695;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 1.
31-JAN-2018, entry version 46.
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;
Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Platyrrhini; Cebidae; Saimiriinae; Saimiri.
NCBI_TaxID=39432;
[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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; EF692507; ABV59227.1; -; mRNA.
RefSeq; NP_001266928.1; NM_001279999.1.
ProteinModelPortal; A8T695; -.
SMR; A8T695; -.
GeneID; 101049523; -.
CTD; 255738; -.
HOVERGEN; HBG053530; -.
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; IEA:Ensembl.
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: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; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
GO; GO:0030547; F:receptor inhibitor activity; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0042157; P:lipoprotein metabolic process; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
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:0030182; P:neuron differentiation; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
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; IPR009020; Peptidase/Inhibitor_I9.
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.
SUPFAM; SSF54897; SSF54897; 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 29 {ECO:0000250}.
PROPEP 30 151 {ECO:0000250}.
/FTId=PRO_0000318296.
CHAIN 152 691 Proprotein convertase subtilisin/kexin
type 9.
/FTId=PRO_0000318297.
DOMAIN 181 423 Peptidase S8.
REGION 449 691 C-terminal domain. {ECO:0000250}.
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. {ECO:0000250}.
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:0000255}.
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}.
SEQUENCE 691 AA; 73866 MW; 129CA9413B0A8952 CRC64;
MGTVSSRRLW WPLPLLLLLL LLGPAGARAQ EDDDGDYEEL VLALRSEEDG LADALQHGAT
ATFHRCAKEP WRLPGTYVVV LKEETHRSQP ERTARRLQAQ AARRGYLIKL LHVFHDLLPG
FLVKMSRDLL ELALKLPHVD YIEEDSSVFA QSIPWNLERI TPARYRADEY QPPNGGSLVE
VYLLDTSIQS GHREIEGRVM VTDFGSVPEE DGTRFHRQAS KCDSHGTHLA GVVSGRDAGV
AKGASLRSLR VLNCQGKGTV SSTLIGLEFI RKSQLVQPVG PLVVLLPLAG GYSRVLNAAC
QRLARAGVVL VAAAGNFRDD ACLYSPASAP EVITVGATNA QDQPVTLGTL GTNFGRCVDL
FAPGEDIIGA SSDCSTCFVS RSGTSQAAAH VAGIAAVMLS AEPELTLAEL RQRLIHFSAK
DVINEAWFPE DQRVLTPNLV AALPPSTHGA GWQLFCRTVW SAHSGPTRMA TAMARCAPDE
ELLSCSSFSS SGKRRGERIE AQGGRRVCLA HNAFGGKGVY AIARCCLLPQ ANCSIHTAPP
AGASMGTRAH CHQQGHVLTG CSAHWEVEEL GTHKPPVLRP GGQPSQCMGH SGASTHATCC
HAPGLECKVK EHGLPAPQEQ VTVACEEGWT LTGCSALPGT SHILGAYAVD DTCVVRSQDV
STTGSTSEEA VAAVAICCRS RHLAQASQEL Q


Related products :

Catalog number Product name Quantity
EIAAB30205 Mouse,Mus musculus,PC5,PC6,Pcsk5,Proprotein convertase 5,Proprotein convertase 6,Proprotein convertase subtilisin_kexin type 5,SPC6,Subtilisin_kexin-like protease PC5,Subtilisin-like proprotein conver
EIAAB30209 Mouse,Mus musculus,PC7,Pc7,Pcsk7,Prohormone convertase 7,Proprotein convertase 7,Proprotein convertase subtilisin_kexin type 7,SPC7,Subtilisin_kexin-like protease PC7,Subtilisin-like proprotein conver
E02P0136 Rat Proprotein Convertase Subtilisin Kexin Type 9 ELISA 96T/kit
C250 Proprotein Convertase Subtilisin Kexin Type 9 PCSK9 500
E1690d Rat ELISA Kit FOR Proprotein convertase subtilisin per kexin type 4 96T
EGP040 Proprotein Convertase Subtilisin per Kexin Type 9 Elisa Kit 96T
C249 Proprotein Convertase Subtilisin Kexin Type 9 Pcsk9 500
EH251 Proprotein convertase subtilisin per kexin type 9 Elisa Kit 96T
C250 Proprotein Convertase Subtilisin Kexin Type 9 PCSK9 lmg
CA83 PCSK-9, Proprotein Convertase Subtilisin Kexin Type 9 500
CA83 PCSK-9, Proprotein Convertase Subtilisin Kexin Type 9 lmg
C249 Proprotein Convertase Subtilisin Kexin Type 9 Pcsk9 lmg
EM153 Proprotein convertase subtilisin per kexin type 9 Elisa Kit 96T
ER134 Proprotein convertase subtilisin per kexin type 9 Elisa Kit 96T
C248 Human Proprotein Convertase Subtilisin Kexin Type 9 PCSK9 l0
E01P0136 Human Proprotein Convertase Subtilisin Kexin Type 9 ELISA 96T/kit
G1944 Proprotein convertase subtilisin kexin type 7 (PCSK7), Rat, ELISA Kit 96T
C250 Human Proprotein Convertase Subtilisin Kexin Type 9 Pcsk9 l0
E12411634 Rat Proprotein Convertase Subtilisin per Kexin Type 1 (PCSK1) ELISA Kit 1
E03P0136 Mouse Proprotein Convertase Subtilisin Kexin Type 9 ELISA 96T/kit
E08P0136 Canine Proprotein Convertase Subtilisin Kexin Type 9 ELISA 96T/kit
E07P0136 Porcine Proprotein Convertase Subtilisin Kexin Type 9 ELISA 96T/kit
E14P0136 Sheep Proprotein Convertase Subtilisin Kexin Type 9 ELISA 96T/kit
CG88 Human PCSK-9, Proprotein Convertase Subtilisin Kexin Type 9 50
UB-E10519 Rat Proprotein Convertase Subtilisin per Kexin Type 1(PCSK1)ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur