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Q80W65

- PCSK9_MOUSE

UniProt

Q80W65 - PCSK9_MOUSE

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Protein

Proprotein convertase subtilisin/kexin type 9

Gene

Pcsk9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Cofactori

Calcium.Curated

Enzyme regulationi

Its proteolytic activity is autoinhibited by the non-covalent binding of the propeptide to the catalytic domain. Inhibited by EGTA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei155 – 1562Cleavage; by autolysisBy similarity
Active sitei189 – 1891Charge relay systemBy similarity
Sitei221 – 2222Cleavage; by furin and PCSK5By similarity
Active sitei229 – 2291Charge relay systemBy similarity
Active sitei389 – 3891Charge relay systemBy similarity

GO - Molecular functioni

  1. apolipoprotein binding Source: UniProtKB
  2. low-density lipoprotein particle binding Source: UniProtKB
  3. low-density lipoprotein particle receptor binding Source: HGNC
  4. poly(A) RNA binding Source: Ensembl
  5. protein self-association Source: UniProtKB
  6. serine-type endopeptidase activity Source: HGNC
  7. sodium channel inhibitor activity Source: Ensembl
  8. very-low-density lipoprotein particle binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular response to insulin stimulus Source: HGNC
  3. cellular response to starvation Source: HGNC
  4. cholesterol homeostasis Source: HGNC
  5. cholesterol metabolic process Source: MGI
  6. kidney development Source: HGNC
  7. lipoprotein metabolic process Source: MGI
  8. liver development Source: HGNC
  9. low-density lipoprotein particle receptor catabolic process Source: UniProtKB
  10. low-density lipoprotein receptor particle metabolic process Source: MGI
  11. lysosomal transport Source: Ensembl
  12. negative regulation of low-density lipoprotein particle clearance Source: Ensembl
  13. negative regulation of receptor recycling Source: Ensembl
  14. neurogenesis Source: HGNC
  15. neuron differentiation Source: HGNC
  16. phospholipid metabolic process Source: MGI
  17. positive regulation of neuron apoptotic process Source: HGNC
  18. positive regulation of receptor internalization Source: Ensembl
  19. protein autoprocessing Source: HGNC
  20. proteolysis Source: RefGenome
  21. regulation of low-density lipoprotein particle receptor catabolic process Source: MGI
  22. regulation of neuron apoptotic process Source: UniProtKB
  23. regulation of receptor activity Source: Ensembl
  24. triglyceride metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Apoptosis, Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_206713. NGF processing.

Protein family/group databases

MEROPSiS08.039.

Names & Taxonomyi

Protein namesi
Recommended name:
Proprotein convertase subtilisin/kexin type 9 (EC:3.4.21.-)
Alternative name(s):
Neural apoptosis-regulated convertase 1
Short name:
NARC-1
Proprotein convertase 9
Short name:
PC9
Subtilisin/kexin-like protease PC9
Gene namesi
Name:Pcsk9
Synonyms:Narc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:2140260. Pcsk9.

Subcellular locationi

Cytoplasm By similarity. Secreted. Endosome By similarity. Lysosome By similarity. Cell surface By similarity. Endoplasmic reticulum By similarity. Golgi apparatus By similarity
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.By similarity

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. early endosome Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB
  5. endoplasmic reticulum lumen Source: Reactome
  6. ER to Golgi transport vesicle Source: MGI
  7. extracellular region Source: MGI
  8. extracellular space Source: HGNC
  9. Golgi apparatus Source: UniProtKB
  10. late endosome Source: UniProtKB
  11. lysosome Source: UniProtKB
  12. perinuclear region of cytoplasm Source: Ensembl
  13. rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence AnalysisAdd
BLAST
Propeptidei35 – 155121PRO_0000027122Add
BLAST
Chaini156 – 694539Proprotein convertase subtilisin/kexin type 9PRO_0000027123Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411SulfotyrosineBy similarity
Modified residuei50 – 501Phosphoserine1 Publication
Disulfide bondi226 ↔ 258Sequence Analysis
Disulfide bondi326 ↔ 361Sequence Analysis
Disulfide bondi460 ↔ 530Sequence Analysis
Disulfide bondi480 ↔ 529Sequence Analysis
Disulfide bondi489 ↔ 512Sequence Analysis
Glycosylationi536 – 5361N-linked (GlcNAc...)By similarity
Disulfide bondi537 ↔ 604Sequence Analysis
Disulfide bondi555 ↔ 603Sequence Analysis
Disulfide bondi565 ↔ 591Sequence Analysis
Disulfide bondi611 ↔ 682Sequence Analysis
Disulfide bondi629 ↔ 681Sequence Analysis
Disulfide bondi638 ↔ 657Sequence Analysis
Modified residuei691 – 6911PhosphoserineBy similarity

Post-translational modificationi

Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation.By similarity
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.By similarity
Phosphorylation protects the propeptide against proteolysis.By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

MaxQBiQ80W65.
PaxDbiQ80W65.
PRIDEiQ80W65.

PTM databases

PhosphoSiteiQ80W65.

Expressioni

Tissue specificityi

Hepatocytes, kidney mesenchymal cells, intestinal ileum, colon epithelia and embryonic brain telencephalon neurons.

Developmental stagei

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.

Inductioni

Down-regulated following a high-cholesterol diet.1 Publication

Gene expression databases

BgeeiQ80W65.
CleanExiMM_PCSK9.
GenevestigatoriQ80W65.

Interactioni

Subunit structurei

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 By similarity.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055757.

Structurei

3D structure databases

ProteinModelPortaliQ80W65.
SMRiQ80W65. Positions 64-685.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini185 – 423239Peptidase S8Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni453 – 694242C-terminal domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi499 – 5013Cell attachment siteSequence Analysis

Domaini

The C-terminal domain (CRD) is essential for the LDLR-binding and degrading activities.By similarity
The catalytic domain is responsible for mediating its self-association.By similarity

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1404.
GeneTreeiENSGT00490000043472.
HOGENOMiHOG000049267.
HOVERGENiHBG053530.
InParanoidiQ80W65.
KOiK13050.
OMAiHVLTGCS.
OrthoDBiEOG79PJNT.
PhylomeDBiQ80W65.
TreeFamiTF106271.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR010259. Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q80W65-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGTHCSAWLR WPLLPLLPPL LLLLLLLCPT GAGAQDEDGD YEELMLALPS
60 70 80 90 100
QEDGLADEAA HVATATFRRC SKEAWRLPGT YIVVLMEETQ RLQIEQTAHR
110 120 130 140 150
LQTRAARRGY VIKVLHIFYD LFPGFLVKMS SDLLGLALKL PHVEYIEEDS
160 170 180 190 200
FVFAQSIPWN LERIIPAWHQ TEEDRSPDGS SQVEVYLLDT SIQGAHREIE
210 220 230 240 250
GRVTITDFNS VPEEDGTRFH RQASKCDSHG THLAGVVSGR DAGVAKGTSL
260 270 280 290 300
HSLRVLNCQG KGTVSGTLIG LEFIRKSQLI QPSGPLVVLL PLAGGYSRIL
310 320 330 340 350
NAACRHLART GVVLVAAAGN FRDDACLYSP ASAPEVITVG ATNAQDQPVT
360 370 380 390 400
LGTLGTNFGR CVDLFAPGKD IIGASSDCST CFMSQSGTSQ AAAHVAGIVA
410 420 430 440 450
RMLSREPTLT LAELRQRLIH FSTKDVINMA WFPEDQQVLT PNLVATLPPS
460 470 480 490 500
THETGGQLLC RTVWSAHSGP TRTATATARC APEEELLSCS SFSRSGRRRG
510 520 530 540 550
DWIEAIGGQQ VCKALNAFGG EGVYAVARCC LVPRANCSIH NTPAARAGLE
560 570 580 590 600
THVHCHQKDH VLTGCSFHWE VEDLSVRRQP ALRSRRQPGQ CVGHQAASVY
610 620 630 640 650
ASCCHAPGLE CKIKEHGISG PSEQVTVACE AGWTLTGCNV LPGASLTLGA
660 670 680 690
YSVDNLCVAR VHDTARADRT SGEATVAAAI CCRSRPSAKA SWVQ
Length:694
Mass (Da):74,823
Last modified:November 7, 2003 - v2
Checksum:i977BD4BD1FAF98C0
GO

Sequence cautioni

The sequence AAP31672.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAE28934.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAC60362.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 193Missing in CAC60362. 1 PublicationCurated
Sequence conflicti34 – 341A → T in CAC60362. 1 PublicationCurated
Sequence conflicti189 – 1891D → G in CAC60362. 1 PublicationCurated
Sequence conflicti196 – 1961H → Y in CAC60362. 1 PublicationCurated
Sequence conflicti200 – 2001E → A in CAC60362. 1 PublicationCurated
Sequence conflicti305 – 3051R → Q in CAC60362. 1 PublicationCurated
Sequence conflicti534 – 5341R → H in CAC60362. 1 PublicationCurated
Sequence conflicti626 – 6261T → A in CAC60362. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AX207688 Unassigned DNA. Translation: CAC60362.1. Different initiation.
AY273821 mRNA. Translation: AAP31672.1. Different initiation.
AK149520 mRNA. Translation: BAE28934.1. Different initiation.
AL954352 Genomic DNA. Translation: CAM15751.1.
BC038085 mRNA. Translation: AAH38085.1.
CCDSiCCDS18418.1.
RefSeqiNP_705793.1. NM_153565.2.
UniGeneiMm.133268.

Genome annotation databases

EnsembliENSMUST00000049507; ENSMUSP00000055757; ENSMUSG00000044254.
GeneIDi100102.
KEGGimmu:100102.
UCSCiuc008tyi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AX207688 Unassigned DNA. Translation: CAC60362.1 . Different initiation.
AY273821 mRNA. Translation: AAP31672.1 . Different initiation.
AK149520 mRNA. Translation: BAE28934.1 . Different initiation.
AL954352 Genomic DNA. Translation: CAM15751.1 .
BC038085 mRNA. Translation: AAH38085.1 .
CCDSi CCDS18418.1.
RefSeqi NP_705793.1. NM_153565.2.
UniGenei Mm.133268.

3D structure databases

ProteinModelPortali Q80W65.
SMRi Q80W65. Positions 64-685.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000055757.

Protein family/group databases

MEROPSi S08.039.

PTM databases

PhosphoSitei Q80W65.

Proteomic databases

MaxQBi Q80W65.
PaxDbi Q80W65.
PRIDEi Q80W65.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049507 ; ENSMUSP00000055757 ; ENSMUSG00000044254 .
GeneIDi 100102.
KEGGi mmu:100102.
UCSCi uc008tyi.2. mouse.

Organism-specific databases

CTDi 255738.
MGIi MGI:2140260. Pcsk9.

Phylogenomic databases

eggNOGi COG1404.
GeneTreei ENSGT00490000043472.
HOGENOMi HOG000049267.
HOVERGENi HBG053530.
InParanoidi Q80W65.
KOi K13050.
OMAi HVLTGCS.
OrthoDBi EOG79PJNT.
PhylomeDBi Q80W65.
TreeFami TF106271.

Enzyme and pathway databases

Reactomei REACT_206713. NGF processing.

Miscellaneous databases

NextBioi 354261.
PROi Q80W65.
SOURCEi Search...

Gene expression databases

Bgeei Q80W65.
CleanExi MM_PCSK9.
Genevestigatori Q80W65.

Family and domain databases

Gene3Di 3.40.50.200. 1 hit.
InterProi IPR010259. Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view ]
PANTHERi PTHR10795. PTHR10795. 1 hit.
Pfami PF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view ]
PRINTSi PR00723. SUBTILISIN.
SUPFAMi SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Narc-1, novel subtilase-like homologs."
    Chiang L.W.
    Patent number WO0157081, 09-AUG-2001
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Novel putative SREBP and LXR target genes identified by microarray analysis in liver of cholesterol-fed mice."
    Maxwell K.N., Soccio R.E., Duncan E.M., Sehayek E., Breslow J.L.
    J. Lipid Res. 44:2109-2119(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: C57BL/6.
    Tissue: Liver.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Eye.
  6. "The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): liver regeneration and neuronal differentiation."
    Seidah N.G., Benjannet S., Wickham L., Marcinkiewicz J., Jasmin S.B., Stifani S., Basak A., Prat A., Chretien M.
    Proc. Natl. Acad. Sci. U.S.A. 100:928-933(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROPEPTIDE CLEAVAGE SITE, CHARACTERIZATION.
  7. Cited for: AUTOCATALYTIC CLEAVAGE SITE.
  8. "PCSK9 is phosphorylated by a Golgi casein kinase-like kinase ex vivo and circulates as a phosphoprotein in humans."
    Dewpura T., Raymond A., Hamelin J., Seidah N.G., Mbikay M., Chretien M., Mayne J.
    FEBS J. 275:3480-3493(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Proprotein convertase subtilisin/kexin type 9 interacts with apolipoprotein B and prevents its intracellular degradation, irrespective of the low-density lipoprotein receptor."
    Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B.
    Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "PCSK9 regulates neuronal apoptosis by adjusting ApoER2 levels and signaling."
    Kysenius K., Muggalla P., Maetlik K., Arumaee U., Huttunen H.J.
    Cell. Mol. Life Sci. 69:1903-1916(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPCSK9_MOUSE
AccessioniPrimary (citable) accession number: Q80W65
Secondary accession number(s): B1AZI4
, Q3UEH7, Q8BXW9, Q8CFT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: October 29, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3