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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_MOUSE             Reviewed;         694 AA.
Q80W65; B1AZI4; Q3UEH7; Q8BXW9; Q8CFT6;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
07-NOV-2003, sequence version 2.
31-JAN-2018, entry version 139.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE.
Chiang L.W.;
"Narc-1, novel subtilase-like homologs.";
Patent number WO0157081, 09-AUG-2001.
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=12897189; DOI=10.1194/jlr.M300203-JLR200;
Maxwell K.N., Soccio R.E., Duncan E.M., Sehayek E., Breslow J.L.;
"Novel putative SREBP and LXR target genes identified by microarray
analysis in liver of cholesterol-fed mice.";
J. Lipid Res. 44:2109-2119(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
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).
[6]
IDENTIFICATION OF PROPEPTIDE CLEAVAGE SITE, AND 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).
[7]
AUTOCATALYTIC CLEAVAGE SITE.
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).
[8]
PHOSPHORYLATION AT SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18498363; DOI=10.1111/j.1742-4658.2008.06495.x;
Dewpura T., Raymond A., Hamelin J., Seidah N.G., Mbikay M.,
Chretien M., Mayne J.;
"PCSK9 is phosphorylated by a Golgi casein kinase-like kinase ex vivo
and circulates as a phosphoprotein in humans.";
FEBS J. 275:3480-3493(2008).
[9]
FUNCTION.
PubMed=22580899; DOI=10.1161/ATVBAHA.112.250043;
Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B.;
"Proprotein convertase subtilisin/kexin type 9 interacts with
apolipoprotein B and prevents its intracellular degradation,
irrespective of the low-density lipoprotein receptor.";
Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012).
[10]
FUNCTION.
PubMed=22481440; DOI=10.1007/s00018-012-0977-6;
Kysenius K., Muggalla P., Maetlik K., Arumaee U., Huttunen H.J.;
"PCSK9 regulates neuronal apoptosis by adjusting ApoER2 levels and
signaling.";
Cell. Mol. Life Sci. 69:1903-1916(2012).
-!- 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.
{ECO:0000269|PubMed:22481440, ECO:0000269|PubMed:22580899}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
-!- ENZYME REGULATION: Its proteolytic activity is autoinhibited by
the non-covalent binding of the propeptide to the catalytic
domain. Inhibited by EGTA.
-!- 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. 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 co-localizes 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: Hepatocytes, kidney mesenchymal cells,
intestinal ileum, colon epithelia and embryonic brain
telencephalon neurons.
-!- DEVELOPMENTAL STAGE: In the embryo, expressed in the liver at day
E9, in the skin and transiently in the telencephalon at day E12,
and in the kidney, small intestine and cerebellum at E15.
-!- INDUCTION: Down-regulated following a high-cholesterol diet.
{ECO:0000269|PubMed:12897189}.
-!- 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=AAP31672.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAE28934.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAC60362.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AX207688; CAC60362.1; ALT_INIT; Unassigned_DNA.
EMBL; AY273821; AAP31672.1; ALT_INIT; mRNA.
EMBL; AK149520; BAE28934.1; ALT_INIT; mRNA.
EMBL; AL954352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC038085; AAH38085.1; -; mRNA.
CCDS; CCDS18418.1; -.
RefSeq; NP_705793.1; NM_153565.2.
UniGene; Mm.133268; -.
ProteinModelPortal; Q80W65; -.
SMR; Q80W65; -.
IntAct; Q80W65; 1.
STRING; 10090.ENSMUSP00000055757; -.
MEROPS; S08.039; -.
iPTMnet; Q80W65; -.
PhosphoSitePlus; Q80W65; -.
MaxQB; Q80W65; -.
PaxDb; Q80W65; -.
PeptideAtlas; Q80W65; -.
PRIDE; Q80W65; -.
Ensembl; ENSMUST00000049507; ENSMUSP00000055757; ENSMUSG00000044254.
GeneID; 100102; -.
KEGG; mmu:100102; -.
UCSC; uc008tyi.2; mouse.
CTD; 255738; -.
MGI; MGI:2140260; Pcsk9.
eggNOG; KOG1153; Eukaryota.
eggNOG; COG1404; LUCA.
GeneTree; ENSGT00490000043472; -.
HOGENOM; HOG000049267; -.
HOVERGEN; HBG053530; -.
InParanoid; Q80W65; -.
KO; K13050; -.
OMA; HVLTGCS; -.
OrthoDB; EOG091G067E; -.
PhylomeDB; Q80W65; -.
TreeFam; TF106271; -.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
Reactome; R-MMU-8964038; LDL clearance.
PRO; PR:Q80W65; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000044254; -.
CleanEx; MM_PCSK9; -.
Genevisible; Q80W65; MM.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:HGNC.
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; ISS:BHF-UCL.
GO; GO:1990666; C:PCSK9-LDLR complex; ISS:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
GO; GO:0034185; F:apolipoprotein binding; IDA:UniProtKB.
GO; GO:0034190; F:apolipoprotein receptor binding; ISO:MGI.
GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:UniProtKB.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:HGNC.
GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
GO; GO:0030547; F:receptor inhibitor activity; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:HGNC.
GO; GO:0019871; F:sodium channel inhibitor activity; ISO:MGI.
GO; GO:0034189; F:very-low-density lipoprotein particle binding; IDA:UniProtKB.
GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; ISO:MGI.
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; ISS:HGNC.
GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
GO; GO:0001822; P:kidney development; IEP:HGNC.
GO; GO:0042157; P:lipoprotein metabolic process; IDA:MGI.
GO; GO:0001889; P:liver development; IEP:HGNC.
GO; GO:0032802; P:low-density lipoprotein particle receptor catabolic process; ISS:UniProtKB.
GO; GO:0032799; P:low-density lipoprotein receptor particle metabolic process; IDA:MGI.
GO; GO:0007041; P:lysosomal transport; ISO:MGI.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; ISO:MGI.
GO; GO:1905596; P:negative regulation of low-density lipoprotein particle receptor binding; ISO:MGI.
GO; GO:1905598; P:negative regulation of low-density lipoprotein receptor activity; ISO:MGI.
GO; GO:0001920; P:negative regulation of receptor recycling; ISO:MGI.
GO; GO:1905601; P:negative regulation of receptor-mediated endocytosis involved in cholesterol transport; ISO:MGI.
GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; ISO:MGI.
GO; GO:0022008; P:neurogenesis; IEP:HGNC.
GO; GO:0030182; P:neuron differentiation; IDA:HGNC.
GO; GO:0006644; P:phospholipid metabolic process; IDA:MGI.
GO; GO:0032805; P:positive regulation of low-density lipoprotein particle receptor catabolic process; ISO:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:HGNC.
GO; GO:0002092; P:positive regulation of receptor internalization; ISO:MGI.
GO; GO:0016540; P:protein autoprocessing; ISS:HGNC.
GO; GO:0032803; P:regulation of low-density lipoprotein particle receptor catabolic process; IMP:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:0010469; P:regulation of receptor activity; ISO:MGI.
GO; GO:0006641; P:triglyceride metabolic process; IDA:MGI.
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; IPR037045; S8pro/Inhibitor_I9_sf.
Pfam; PF00082; Peptidase_S8; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 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 34 {ECO:0000255}.
PROPEP 35 155
/FTId=PRO_0000027122.
CHAIN 156 694 Proprotein convertase subtilisin/kexin
type 9.
/FTId=PRO_0000027123.
DOMAIN 185 423 Peptidase S8.
REGION 453 694 C-terminal domain. {ECO:0000250}.
MOTIF 499 501 Cell attachment site. {ECO:0000255}.
ACT_SITE 189 189 Charge relay system. {ECO:0000250}.
ACT_SITE 229 229 Charge relay system. {ECO:0000250}.
ACT_SITE 389 389 Charge relay system. {ECO:0000250}.
SITE 155 156 Cleavage; by autolysis. {ECO:0000250}.
SITE 221 222 Cleavage; by furin and PCSK5.
{ECO:0000250}.
MOD_RES 41 41 Sulfotyrosine. {ECO:0000250}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000269|PubMed:18498363}.
MOD_RES 691 691 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NBP7}.
CARBOHYD 536 536 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 226 258 {ECO:0000255}.
DISULFID 326 361 {ECO:0000255}.
DISULFID 460 530 {ECO:0000255}.
DISULFID 480 529 {ECO:0000255}.
DISULFID 489 512 {ECO:0000255}.
DISULFID 537 604 {ECO:0000255}.
DISULFID 555 603 {ECO:0000255}.
DISULFID 565 591 {ECO:0000255}.
DISULFID 611 682 {ECO:0000255}.
DISULFID 629 681 {ECO:0000255}.
DISULFID 638 657 {ECO:0000255}.
CONFLICT 17 19 Missing (in Ref. 1; CAC60362).
{ECO:0000305}.
CONFLICT 34 34 A -> T (in Ref. 1; CAC60362).
{ECO:0000305}.
CONFLICT 189 189 D -> G (in Ref. 1; CAC60362).
{ECO:0000305}.
CONFLICT 196 196 H -> Y (in Ref. 1; CAC60362).
{ECO:0000305}.
CONFLICT 200 200 E -> A (in Ref. 1; CAC60362).
{ECO:0000305}.
CONFLICT 305 305 R -> Q (in Ref. 1; CAC60362).
{ECO:0000305}.
CONFLICT 534 534 R -> H (in Ref. 1; CAC60362).
{ECO:0000305}.
CONFLICT 626 626 T -> A (in Ref. 1; CAC60362).
{ECO:0000305}.
SEQUENCE 694 AA; 74823 MW; 977BD4BD1FAF98C0 CRC64;
MGTHCSAWLR WPLLPLLPPL LLLLLLLCPT GAGAQDEDGD YEELMLALPS QEDGLADEAA
HVATATFRRC SKEAWRLPGT YIVVLMEETQ RLQIEQTAHR LQTRAARRGY VIKVLHIFYD
LFPGFLVKMS SDLLGLALKL PHVEYIEEDS FVFAQSIPWN LERIIPAWHQ TEEDRSPDGS
SQVEVYLLDT SIQGAHREIE GRVTITDFNS VPEEDGTRFH RQASKCDSHG THLAGVVSGR
DAGVAKGTSL HSLRVLNCQG KGTVSGTLIG LEFIRKSQLI QPSGPLVVLL PLAGGYSRIL
NAACRHLART GVVLVAAAGN FRDDACLYSP ASAPEVITVG ATNAQDQPVT LGTLGTNFGR
CVDLFAPGKD IIGASSDCST CFMSQSGTSQ AAAHVAGIVA RMLSREPTLT LAELRQRLIH
FSTKDVINMA WFPEDQQVLT PNLVATLPPS THETGGQLLC RTVWSAHSGP TRTATATARC
APEEELLSCS SFSRSGRRRG DWIEAIGGQQ VCKALNAFGG EGVYAVARCC LVPRANCSIH
NTPAARAGLE THVHCHQKDH VLTGCSFHWE VEDLSVRRQP ALRSRRQPGQ CVGHQAASVY
ASCCHAPGLE CKIKEHGISG PSEQVTVACE AGWTLTGCNV LPGASLTLGA YSVDNLCVAR
VHDTARADRT SGEATVAAAI CCRSRPSAKA SWVQ


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EIAAB30213 Mouse,Mus musculus,Narc1,NARC-1,Neural apoptosis-regulated convertase 1,PC9,Pcsk9,Proprotein convertase 9,Proprotein convertase subtilisin_kexin type 9,Subtilisin_kexin-like protease PC9
EIAAB30214 Homo sapiens,Human,NARC1,NARC-1,Neural apoptosis-regulated convertase 1,PC9,PCSK9,Proprotein convertase 9,Proprotein convertase subtilisin_kexin type 9,PSEC0052,Subtilisin_kexin-like protease PC9
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
C249 Proprotein Convertase Subtilisin Kexin Type 9 Pcsk9 lmg
ER134 Proprotein convertase subtilisin per kexin type 9 Elisa Kit 96T
C250 Proprotein Convertase Subtilisin Kexin Type 9 PCSK9 lmg
EGP040 Proprotein Convertase Subtilisin per Kexin Type 9 Elisa Kit 96T
CA83 PCSK-9, Proprotein Convertase Subtilisin Kexin Type 9 lmg
E02P0136 Rat Proprotein Convertase Subtilisin Kexin Type 9 ELISA 96T/kit
E1690d Rat ELISA Kit FOR Proprotein convertase subtilisin per kexin type 4 96T
EH251 Proprotein convertase subtilisin per kexin type 9 Elisa Kit 96T
C250 Proprotein Convertase Subtilisin Kexin Type 9 PCSK9 500
C249 Proprotein Convertase Subtilisin Kexin Type 9 Pcsk9 500
CA83 PCSK-9, Proprotein Convertase Subtilisin Kexin Type 9 500
EM153 Proprotein convertase subtilisin per kexin type 9 Elisa Kit 96T
EIAAB30210 Homo sapiens,hPC8,Human,LPC,Lymphoma proprotein convertase,PC7,PC7,PC8,PC8,PCSK7,Prohormone convertase 7,Proprotein convertase 7,Proprotein convertase 8,Proprotein convertase subtilisin_kexin type 7,S
UB-E10519 Rat Proprotein Convertase Subtilisin per Kexin Type 1(PCSK1)ELISA kit 96T
G1941 Proprotein convertase subtilisin kexin type 6 (PCSK6), Rat, ELISA Kit 96T
E11P0136 Bovine Proprotein Convertase Subtilisin Kexin Type 9 ELISA 96T/kit
G1944 Proprotein convertase subtilisin kexin type 7 (PCSK7), Rat, ELISA Kit 96T
E08P0136 Canine Proprotein Convertase Subtilisin Kexin Type 9 ELISA 96T/kit


 

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