# Furin

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> Source: https://en.wikipedia.org/wiki/Furin
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Enzyme found in humans

FURIN Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4OMC, 4OMD, 4RYD, 4Z2A Identifiers Aliases FURIN, FUR, PACE, PCSK3, SPC1, furin, paired basic amino acid cleaving enzyme External IDs OMIM: 136950; MGI: 97513; HomoloGene: 1930; GeneCards: FURIN; OMA:FURIN - orthologs Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q26.1 Start 90,868,588 bp[1] End 90,883,458 bp[1] Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7 D2|7 45.65 cM Start 80,038,333 bp[2] End 80,055,184 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver body of pancreas right lung right lobe of thyroid gland left lobe of thyroid gland apex of heart skin of leg upper lobe of left lung salivary gland anterior pituitary Top expressed in epithelium of stomach Ileal epithelium parotid gland granulocyte lip right kidney lactiferous gland corneal stroma extensor digitorum longus muscle secondary oocyte More reference expression data BioGPS More reference expression data Gene ontology Molecular function nerve growth factor binding peptide binding metal ion binding protease binding peptidase activity protein binding serine-type endopeptidase inhibitor activity serine-type peptidase activity hydrolase activity endopeptidase activity serine-type endopeptidase activity Cellular component integral component of membrane Golgi apparatus membrane plasma membrane cell surface trans-Golgi network endoplasmic reticulum Golgi lumen membrane raft trans-Golgi network transport vesicle extracellular exosome extracellular space Golgi membrane extracellular region endosome endosome membrane integral component of Golgi membrane Biological process negative regulation of low-density lipoprotein particle receptor catabolic process negative regulation of transforming growth factor beta1 production viral life cycle secretion by cell peptide biosynthetic process protein processing positive regulation of membrane protein ectodomain proteolysis extracellular matrix disassembly extracellular matrix organization viral protein processing proteolysis signal peptide processing peptide hormone processing regulation of signal transduction regulation of protein catabolic process collagen catabolic process negative regulation of nerve growth factor production nerve growth factor processing nerve growth factor production cell population proliferation transforming growth factor beta receptor signaling pathway regulation of endopeptidase activity negative regulation of endopeptidase activity cornification zymogen activation regulation of lipoprotein lipase activity dibasic protein processing zymogen inhibition positive regulation of transforming growth factor beta1 activation Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 5045 18550 Ensembl ENSG00000140564 ENSMUSG00000030530 UniProt P09958 P23188 RefSeq (mRNA) NM_002569 NM_001289823 NM_001289824 NM_001081454 NM_011046 RefSeq (protein) NP_001276752 NP_001276753 NP_002560 NP_001369548 NP_001369549 NP_001369550 NP_001369551 NP_001276752.1 NP_001276753.1 NP_002560.1 NP_001074923 NP_035176 Location (UCSC) Chr 15: 90.87 – 90.88 Mb Chr 7: 80.04 – 80.06 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Furin** is a [protease](/source/Protease), a proteolytic [enzyme](/source/Enzyme) activated by [substrate presentation](/source/Substrate_presentation) that in humans and other animals is encoded by the *FURIN* [gene](/source/Gene). Some proteins are inactive when they are first synthesized, and must have sections removed in order to become active. Furin cleaves these sections and activates the proteins.[5][6][7][8] It was named furin because it was in the upstream region of an [oncogene](/source/Oncogene) known as [FES](/source/Feline_sarcoma_oncogene). The gene was known as FUR (FES Upstream Region) and therefore the protein was named furin. Furin is also known as **PACE** (Paired basic Amino acid Cleaving Enzyme). A member of [family S8](/source/Serine_protease#Classification), furin is a [subtilisin](/source/Subtilisin)-like peptidase.

## Function

The [protein](/source/Protein) encoded by this gene is an [enzyme](/source/Enzyme) that belongs to the [subtilisin](/source/Subtilisin)-like [proprotein convertase](/source/Proprotein_convertase) family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine [endoprotease](/source/Endopeptidase) that can efficiently cleave precursor proteins at their paired basic amino acid processing sites. Some of its substrates are: pro[parathyroid hormone](/source/Parathyroid_hormone), [transforming growth factor beta 1](/source/TGFB1) precursor, pro[albumin](/source/Albumin), pro-[beta-secretase](/source/Beta-secretase_1), [membrane type-1 matrix metalloproteinase](/source/MMP1), beta subunit of pro-[nerve growth factor](/source/Nerve_growth_factor) and [von Willebrand factor](/source/Von_Willebrand_factor). A furin-like pro-protein convertase has been implicated in the processing of RGMc (also called [hemojuvelin](/source/Hemojuvelin)), a gene involved in a severe iron-overload disorder called juvenile hemochromatosis. Both the Ganz and Rotwein groups demonstrated that furin-like [proprotein convertases](/source/Proprotein_convertase) (PPC) are responsible for conversion of 50 kDa HJV to a 40 kDa protein with a truncated COOH-terminus, at a conserved polybasic RNRR site. This suggests a potential mechanism to generate the soluble forms of HJV/hemojuvelin (s-hemojuvelin) found in the blood of rodents and humans.[9][10]

The furin substrates and the locations of furin cleavage sites in protein sequences can be predicted by two bioinformatics methods: ProP[11] and PiTou.[12]

## Clinical significance

Furin is one of the proteases responsible for the proteolytic cleavage of HIV envelope polyprotein precursor [gp160](/source/Gp160) to [gp120](/source/Gp120) and [gp41](/source/Gp41) prior to viral assembly.[13] This protease is also thought to play a role in tumor progression.[7] The use of alternate polyadenylation sites has been found for the FURIN gene.[*[citation needed](https://en.wikipedia.org/wiki/Wikipedia:Citation_needed)*]

Furin is enriched in the [Golgi apparatus](/source/Golgi_apparatus), where it functions to cleave other proteins into their mature/active forms.[14] Furin cleaves proteins just downstream of a basic amino acid target sequence (canonically, Arg-X-(Arg/Lys) -Arg'). In addition to processing cellular precursor proteins, furin is also used by a number of pathogens. For example, the envelope proteins of viruses such as [HIV](/source/HIV), [influenza](/source/Orthomyxoviridae), [dengue fever](/source/Dengue_fever), several filoviruses including [ebola](/source/Ebola) and [marburg virus](/source/Marburg_virus), and the spike protein of [SARS-CoV-2](/source/SARS-CoV-2),[15][16][17] must be cleaved by furin or furin-like proteases to become fully functional. When SARS-CoV-2 virus is being synthesized in an infected cell, furin or furin-like proteases cleave the [spike protein](/source/Coronavirus_spike_protein) into two portions (S1 and S2), which remain associated.[18]

[Anthrax toxin](/source/Anthrax_toxin), *[Pseudomonas](/source/Pseudomonas)* exotoxin, and [papillomaviruses](/source/Papillomavirus) must be processed by furin during their initial entry into host cells. Inhibitors of furin are under consideration as therapeutic agents for treating [anthrax](/source/Anthrax) infection.[19]

Furin is regulated by cholesterol and [substrate presentation](/source/Substrate_presentation). When cholesterol is high, furin traffics to [GM1](/source/GM1) [lipid rafts](/source/Lipid_raft). When cholesterol is low, furin traffics to the disordered region.[20] This is speculated to contribute to cholesterol and age dependent priming of SARS-CoV.

Expression of furin in T-cells is required for maintenance of [peripheral immune tolerance](/source/Peripheral_tolerance).[21]

## Interactions

Furin has been shown to [interact](/source/Protein-protein_interaction) with [PACS1](/source/PACS1).[22]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000140564](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000140564) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000030530](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000030530) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=5045). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=18550). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid2251280_5-0)** Wise RJ, Barr PJ, Wong PA, Kiefer MC, Brake AJ, Kaufman RJ (December 1990). ["Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC55168). *Proceedings of the National Academy of Sciences of the United States of America*. **87** (23): 9378–82. [Bibcode](/source/Bibcode_(identifier)):[1990PNAS...87.9378W](https://ui.adsabs.harvard.edu/abs/1990PNAS...87.9378W). [doi](/source/Doi_(identifier)):[10.1073/pnas.87.23.9378](https://doi.org/10.1073%2Fpnas.87.23.9378). [PMC](/source/PMC_(identifier)) [55168](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC55168). [PMID](/source/PMID_(identifier)) [2251280](https://pubmed.ncbi.nlm.nih.gov/2251280).

1. **[^](#cite_ref-pmid1741956_6-0)** Kiefer MC, Tucker JE, Joh R, Landsberg KE, Saltman D, Barr PJ (December 1991). "Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15". *DNA and Cell Biology*. **10** (10): 757–69. [doi](/source/Doi_(identifier)):[10.1089/dna.1991.10.757](https://doi.org/10.1089%2Fdna.1991.10.757). [PMID](/source/PMID_(identifier)) [1741956](https://pubmed.ncbi.nlm.nih.gov/1741956).

1. ^ [***a***](#cite_ref-entrez_5045_7-0) [***b***](#cite_ref-entrez_5045_7-1) ["Entrez Gene: FURIN furin (paired basic amino acid cleaving enzyme)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=5045).

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1. **[^](#cite_ref-pmid17869549_9-0)** Lin L, Nemeth E, Goodnough JB, Thapa DR, Gabayan V, Ganz T (2008). ["Soluble hemojuvelin is released by proprotein convertase-mediated cleavage at a conserved polybasic RNRR site"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2211380). *Blood Cells, Molecules & Diseases*. **40** (1): 122–31. [doi](/source/Doi_(identifier)):[10.1016/j.bcmd.2007.06.023](https://doi.org/10.1016%2Fj.bcmd.2007.06.023). [PMC](/source/PMC_(identifier)) [2211380](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2211380). [PMID](/source/PMID_(identifier)) [17869549](https://pubmed.ncbi.nlm.nih.gov/17869549).

1. **[^](#cite_ref-pmid18384687_10-0)** Kuninger D, Kuns-Hashimoto R, Nili M, Rotwein P (April 2008). ["Pro-protein convertases control the maturation and processing of the iron-regulatory protein, RGMc/hemojuvelin"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2323002). *BMC Biochemistry*. **9** 9. [doi](/source/Doi_(identifier)):[10.1186/1471-2091-9-9](https://doi.org/10.1186%2F1471-2091-9-9). [PMC](/source/PMC_(identifier)) [2323002](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2323002). [PMID](/source/PMID_(identifier)) [18384687](https://pubmed.ncbi.nlm.nih.gov/18384687).

1. **[^](#cite_ref-pmid14985543_11-0)** Duckert P, Brunak S, Blom N (January 2004). ["Prediction of proprotein convertase cleavage sites"](https://doi.org/10.1093%2Fprotein%2Fgzh013). *Protein Engineering, Design & Selection*. **17** (1): 107–12. [doi](/source/Doi_(identifier)):[10.1093/protein/gzh013](https://doi.org/10.1093%2Fprotein%2Fgzh013). [PMID](/source/PMID_(identifier)) [14985543](https://pubmed.ncbi.nlm.nih.gov/14985543).

1. **[^](#cite_ref-pmid22355773_12-0)** Tian S, Huajun W, Wu J (February 2012). ["Computational prediction of furin cleavage sites by a hybrid method and understanding mechanism underlying diseases"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3281273). *Scientific Reports*. **2** 261. [Bibcode](/source/Bibcode_(identifier)):[2012NatSR...2..261T](https://ui.adsabs.harvard.edu/abs/2012NatSR...2..261T). [doi](/source/Doi_(identifier)):[10.1038/srep00261](https://doi.org/10.1038%2Fsrep00261). [PMC](/source/PMC_(identifier)) [3281273](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3281273). [PMID](/source/PMID_(identifier)) [22355773](https://pubmed.ncbi.nlm.nih.gov/22355773).

1. **[^](#cite_ref-pmid1360148_13-0)** Hallenberger S, Bosch V, Angliker H, Shaw E, Klenk HD, Garten W (November 1992). "Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160". *Nature*. **360** (6402): 358–61. [Bibcode](/source/Bibcode_(identifier)):[1992Natur.360..358H](https://ui.adsabs.harvard.edu/abs/1992Natur.360..358H). [doi](/source/Doi_(identifier)):[10.1038/360358a0](https://doi.org/10.1038%2F360358a0). [PMID](/source/PMID_(identifier)) [1360148](https://pubmed.ncbi.nlm.nih.gov/1360148). [S2CID](/source/S2CID_(identifier)) [4306605](https://api.semanticscholar.org/CorpusID:4306605).

1. **[^](#cite_ref-pmid12360192_14-0)** Thomas G (October 2002). ["Furin at the cutting edge: from protein traffic to embryogenesis and disease"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1964754). *Nature Reviews. Molecular Cell Biology*. **3** (10): 753–66. [doi](/source/Doi_(identifier)):[10.1038/nrm934](https://doi.org/10.1038%2Fnrm934). [PMC](/source/PMC_(identifier)) [1964754](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1964754). [PMID](/source/PMID_(identifier)) [12360192](https://pubmed.ncbi.nlm.nih.gov/12360192).

1. **[^](#cite_ref-pmid32057769_15-0)** Coutard B, Valle C, de Lamballerie X, Canard B, Seidah NG, Decroly E (April 2020). ["The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114094). *Antiviral Research*. **176** 104742. [doi](/source/Doi_(identifier)):[10.1016/j.antiviral.2020.104742](https://doi.org/10.1016%2Fj.antiviral.2020.104742). [PMC](/source/PMC_(identifier)) [7114094](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114094). [PMID](/source/PMID_(identifier)) [32057769](https://pubmed.ncbi.nlm.nih.gov/32057769).

1. **[^](#cite_ref-16)** Hoffmann M, Kleine-Weber H, Pöhlmann S (May 2020). ["A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7194065). *Molecular Cell*. **78** (4): 779–784.e5. [doi](/source/Doi_(identifier)):[10.1016/j.molcel.2020.04.022](https://doi.org/10.1016%2Fj.molcel.2020.04.022). [PMC](/source/PMC_(identifier)) [7194065](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7194065). [PMID](/source/PMID_(identifier)) [32362314](https://pubmed.ncbi.nlm.nih.gov/32362314).

1. **[^](#cite_ref-17)** ["The origin of COVID-19: Evidence piles up, but the jury's still out"](https://thebulletin.org/2021/10/the-origin-of-covid-19-evidence-piles-up-but-the-jurys-still-out/amp/?__twitter_impression=true). 11 October 2021. The furin cleavage site on the SARS-CoV-2 virus allows its spikes to be cut and "primed" as it moves out of one cell and into another. The site is thought to make the virus more transmissible.

1. **[^](#cite_ref-pmid34611326_18-0)** Jackson CB, Farzan M, Chen B, Choe H (2022). ["Mechanisms of SARS-CoV-2 entry into cells"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8491763). *[Nature Reviews Molecular Cell Biology](/source/Nature_Reviews_Molecular_Cell_Biology)*. **23** (1): 3–20. [doi](/source/Doi_(identifier)):[10.1038/s41580-021-00418-x](https://doi.org/10.1038%2Fs41580-021-00418-x). [PMC](/source/PMC_(identifier)) [8491763](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8491763). [PMID](/source/PMID_(identifier)) [34611326](https://pubmed.ncbi.nlm.nih.gov/34611326).

1. **[^](#cite_ref-pmid17537721_19-0)** Shiryaev SA, Remacle AG, Ratnikov BI, Nelson NA, Savinov AY, Wei G, et al. (July 2007). ["Targeting host cell furin proprotein convertases as a therapeutic strategy against bacterial toxins and viral pathogens"](https://doi.org/10.1074%2Fjbc.M703847200). *The Journal of Biological Chemistry*. **282** (29): 20847–53. [doi](/source/Doi_(identifier)):[10.1074/jbc.M703847200](https://doi.org/10.1074%2Fjbc.M703847200). [PMID](/source/PMID_(identifier)) [17537721](https://pubmed.ncbi.nlm.nih.gov/17537721).

1. **[^](#cite_ref-20)** Wang H, Yuan Z, Pavel MA, Jablonski SM, Jablonski J, Hobson R, et al. (2023). ["The role of high cholesterol in SARS-CoV-2 infectivity"](https://doi.org/10.1016%2Fj.jbc.2023.104763). *Journal of Biological Chemistry*. **299** (6) 104763. [bioRxiv](/source/BioRxiv_(identifier)) [10.1101/2020.05.09.086249](https://doi.org/10.1101%2F2020.05.09.086249). [doi](/source/Doi_(identifier)):[10.1016/j.jbc.2023.104763](https://doi.org/10.1016%2Fj.jbc.2023.104763).

1. **[^](#cite_ref-pmid18701887_21-0)** Pesu M, Watford WT, Wei L, Xu L, Fuss I, Strober W, et al. (September 2008). ["T-cell-expressed proprotein convertase furin is essential for maintenance of peripheral immune tolerance"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2758057). *Nature*. **455** (7210): 246–50. [Bibcode](/source/Bibcode_(identifier)):[2008Natur.455..246P](https://ui.adsabs.harvard.edu/abs/2008Natur.455..246P). [doi](/source/Doi_(identifier)):[10.1038/nature07210](https://doi.org/10.1038%2Fnature07210). [PMC](/source/PMC_(identifier)) [2758057](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2758057). [PMID](/source/PMID_(identifier)) [18701887](https://pubmed.ncbi.nlm.nih.gov/18701887).

1. **[^](#cite_ref-pmid9695949_22-0)** Wan L, Molloy SS, Thomas L, Liu G, Xiang Y, Rybak SL, Thomas G (July 1998). ["PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization"](https://doi.org/10.1016%2FS0092-8674%2800%2981420-8). *Cell*. **94** (2): 205–16. [doi](/source/Doi_(identifier)):[10.1016/S0092-8674(00)81420-8](https://doi.org/10.1016%2FS0092-8674%2800%2981420-8). [PMID](/source/PMID_(identifier)) [9695949](https://pubmed.ncbi.nlm.nih.gov/9695949). [S2CID](/source/S2CID_(identifier)) [15027198](https://api.semanticscholar.org/CorpusID:15027198).

## Further reading

- Nakayama K (November 1997). ["Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1218878). *The Biochemical Journal*. 327 ( Pt 3) (3): 625–35. [doi](/source/Doi_(identifier)):[10.1042/bj3270625](https://doi.org/10.1042%2Fbj3270625). [PMC](/source/PMC_(identifier)) [1218878](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1218878). [PMID](/source/PMID_(identifier)) [9599222](https://pubmed.ncbi.nlm.nih.gov/9599222).

- Bassi DE, Mahloogi H, Klein-Szanto AJ (June 2000). "The proprotein convertases furin and PACE4 play a significant role in tumor progression". *Molecular Carcinogenesis*. **28** (2): 63–9. [doi](/source/Doi_(identifier)):[10.1002/1098-2744(200006)28:2<63::AID-MC1>3.0.CO;2-C](https://doi.org/10.1002%2F1098-2744%28200006%2928%3A2%3C63%3A%3AAID-MC1%3E3.0.CO%3B2-C). [PMID](/source/PMID_(identifier)) [10900462](https://pubmed.ncbi.nlm.nih.gov/10900462). [S2CID](/source/S2CID_(identifier)) [22849623](https://api.semanticscholar.org/CorpusID:22849623).

- Hallenberger S, Bosch V, Angliker H, Shaw E, Klenk HD, Garten W (November 1992). "Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160". *Nature*. **360** (6402): 358–61. [Bibcode](/source/Bibcode_(identifier)):[1992Natur.360..358H](https://ui.adsabs.harvard.edu/abs/1992Natur.360..358H). [doi](/source/Doi_(identifier)):[10.1038/360358a0](https://doi.org/10.1038%2F360358a0). [PMID](/source/PMID_(identifier)) [1360148](https://pubmed.ncbi.nlm.nih.gov/1360148). [S2CID](/source/S2CID_(identifier)) [4306605](https://api.semanticscholar.org/CorpusID:4306605).

- Rehemtulla A, Kaufman RJ (May 1992). ["Preferred sequence requirements for cleavage of pro-von Willebrand factor by propeptide-processing enzymes"](https://doi.org/10.1182%2Fblood.V79.9.2349.2349). *Blood*. **79** (9): 2349–55. [doi](/source/Doi_(identifier)):[10.1182/blood.V79.9.2349.2349](https://doi.org/10.1182%2Fblood.V79.9.2349.2349). [PMID](/source/PMID_(identifier)) [1571548](https://pubmed.ncbi.nlm.nih.gov/1571548).

- Leduc R, Molloy SS, Thorne BA, Thomas G (July 1992). ["Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage"](https://doi.org/10.1016%2FS0021-9258%2819%2949712-3). *The Journal of Biological Chemistry*. **267** (20): 14304–8. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(19)49712-3](https://doi.org/10.1016%2FS0021-9258%2819%2949712-3). [PMID](/source/PMID_(identifier)) [1629222](https://pubmed.ncbi.nlm.nih.gov/1629222).

- Barr PJ, Mason OB, Landsberg KE, Wong PA, Kiefer MC, Brake AJ (June 1991). "cDNA and gene structure for a human subtilisin-like protease with cleavage specificity for paired basic amino acid residues". *DNA and Cell Biology*. **10** (5): 319–28. [doi](/source/Doi_(identifier)):[10.1089/dna.1991.10.319](https://doi.org/10.1089%2Fdna.1991.10.319). [PMID](/source/PMID_(identifier)) [1713771](https://pubmed.ncbi.nlm.nih.gov/1713771).

- Herz J, Kowal RC, Goldstein JL, Brown MS (June 1990). ["Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC551881). *The EMBO Journal*. **9** (6): 1769–76. [doi](/source/Doi_(identifier)):[10.1002/j.1460-2075.1990.tb08301.x](https://doi.org/10.1002%2Fj.1460-2075.1990.tb08301.x). [PMC](/source/PMC_(identifier)) [551881](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC551881). [PMID](/source/PMID_(identifier)) [2112085](https://pubmed.ncbi.nlm.nih.gov/2112085).

- van den Ouweland AM, van Duijnhoven HL, Keizer GD, Dorssers LC, Van de Ven WJ (February 1990). ["Structural homology between the human fur gene product and the subtilisin-like protease encoded by yeast KEX2"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC333486). *Nucleic Acids Research*. **18** (3): 664. [doi](/source/Doi_(identifier)):[10.1093/nar/18.3.664](https://doi.org/10.1093%2Fnar%2F18.3.664). [PMC](/source/PMC_(identifier)) [333486](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC333486). [PMID](/source/PMID_(identifier)) [2408021](https://pubmed.ncbi.nlm.nih.gov/2408021).

- Van den Ouweland AM, Van Groningen JJ, Roebroek AJ, Onnekink C, Van de Ven WJ (September 1989). ["Nucleotide sequence analysis of the human fur gene"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC318436). *Nucleic Acids Research*. **17** (17): 7101–2. [doi](/source/Doi_(identifier)):[10.1093/nar/17.17.7101](https://doi.org/10.1093%2Fnar%2F17.17.7101). [PMC](/source/PMC_(identifier)) [318436](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC318436). [PMID](/source/PMID_(identifier)) [2674906](https://pubmed.ncbi.nlm.nih.gov/2674906).

- Roebroek AJ, Schalken JA, Leunissen JA, Onnekink C, Bloemers HP, Van de Ven WJ (September 1986). ["Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1167100). *The EMBO Journal*. **5** (9): 2197–202. [doi](/source/Doi_(identifier)):[10.1002/j.1460-2075.1986.tb04484.x](https://doi.org/10.1002%2Fj.1460-2075.1986.tb04484.x). [PMC](/source/PMC_(identifier)) [1167100](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1167100). [PMID](/source/PMID_(identifier)) [3023061](https://pubmed.ncbi.nlm.nih.gov/3023061).

- Molloy SS, Thomas L, VanSlyke JK, Stenberg PE, Thomas G (January 1994). ["Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394775). *The EMBO Journal*. **13** (1): 18–33. [doi](/source/Doi_(identifier)):[10.1002/j.1460-2075.1994.tb06231.x](https://doi.org/10.1002%2Fj.1460-2075.1994.tb06231.x). [PMC](/source/PMC_(identifier)) [394775](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394775). [PMID](/source/PMID_(identifier)) [7508380](https://pubmed.ncbi.nlm.nih.gov/7508380).

- Brakch N, Dettin M, Scarinci C, Seidah NG, Di Bello C (August 1995). "Structural investigation and kinetic characterization of potential cleavage sites of HIV GP160 by human furin and PC1". *Biochemical and Biophysical Research Communications*. **213** (1): 356–61. [Bibcode](/source/Bibcode_(identifier)):[1995BBRC..213..356B](https://ui.adsabs.harvard.edu/abs/1995BBRC..213..356B). [doi](/source/Doi_(identifier)):[10.1006/bbrc.1995.2137](https://doi.org/10.1006%2Fbbrc.1995.2137). [PMID](/source/PMID_(identifier)) [7639757](https://pubmed.ncbi.nlm.nih.gov/7639757).

- Takahashi S, Kasai K, Hatsuzawa K, Kitamura N, Misumi Y, Ikehara Y, et al. (September 1993). "A mutation of furin causes the lack of precursor-processing activity in human colon carcinoma LoVo cells". *Biochemical and Biophysical Research Communications*. **195** (2): 1019–26. [Bibcode](/source/Bibcode_(identifier)):[1993BBRC..195.1019T](https://ui.adsabs.harvard.edu/abs/1993BBRC..195.1019T). [doi](/source/Doi_(identifier)):[10.1006/bbrc.1993.2146](https://doi.org/10.1006%2Fbbrc.1993.2146). [PMID](/source/PMID_(identifier)) [7690548](https://pubmed.ncbi.nlm.nih.gov/7690548).

- Hendy GN, Bennett HP, Gibbs BF, Lazure C, Day R, Seidah NG (April 1995). ["Proparathyroid hormone is preferentially cleaved to parathyroid hormone by the prohormone convertase furin. A mass spectrometric study"](https://doi.org/10.1074%2Fjbc.270.16.9517). *The Journal of Biological Chemistry*. **270** (16): 9517–25. [doi](/source/Doi_(identifier)):[10.1074/jbc.270.16.9517](https://doi.org/10.1074%2Fjbc.270.16.9517). [PMID](/source/PMID_(identifier)) [7721880](https://pubmed.ncbi.nlm.nih.gov/7721880).

- Dubois CM, Laprise MH, Blanchette F, Gentry LE, Leduc R (May 1995). ["Processing of transforming growth factor beta 1 precursor by human furin convertase"](https://doi.org/10.1074%2Fjbc.270.18.10618). *The Journal of Biological Chemistry*. **270** (18): 10618–24. [doi](/source/Doi_(identifier)):[10.1074/jbc.270.18.10618](https://doi.org/10.1074%2Fjbc.270.18.10618). [PMID](/source/PMID_(identifier)) [7737999](https://pubmed.ncbi.nlm.nih.gov/7737999).

- Gu M, Rappaport J, Leppla SH (May 1995). "Furin is important but not essential for the proteolytic maturation of gp160 of HIV-1". *FEBS Letters*. **365** (1): 95–7. [Bibcode](/source/Bibcode_(identifier)):[1995FEBSL.365...95G](https://ui.adsabs.harvard.edu/abs/1995FEBSL.365...95G). [doi](/source/Doi_(identifier)):[10.1016/0014-5793(95)00447-H](https://doi.org/10.1016%2F0014-5793%2895%2900447-H). [PMID](/source/PMID_(identifier)) [7774724](https://pubmed.ncbi.nlm.nih.gov/7774724). [S2CID](/source/S2CID_(identifier)) [21231590](https://api.semanticscholar.org/CorpusID:21231590).

- Schäfer W, Stroh A, Berghöfer S, Seiler J, Vey M, Kruse ML, et al. (June 1995). ["Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC398356). *The EMBO Journal*. **14** (11): 2424–35. [doi](/source/Doi_(identifier)):[10.1002/j.1460-2075.1995.tb07240.x](https://doi.org/10.1002%2Fj.1460-2075.1995.tb07240.x). [PMC](/source/PMC_(identifier)) [398356](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC398356). [PMID](/source/PMID_(identifier)) [7781597](https://pubmed.ncbi.nlm.nih.gov/7781597).

- Mbikay M, Seidah NG, Chrétien M, Simpson EM (March 1995). "Chromosomal assignment of the genes for proprotein convertases PC4, PC5, and PACE 4 in mouse and human". *Genomics*. **26** (1): 123–9. [doi](/source/Doi_(identifier)):[10.1016/0888-7543(95)80090-9](https://doi.org/10.1016%2F0888-7543%2895%2980090-9). [PMID](/source/PMID_(identifier)) [7782070](https://pubmed.ncbi.nlm.nih.gov/7782070).

## External links

- Overview of all the structural information available in the [PDB](/source/Protein_Data_Bank) for [UniProt](/source/UniProt): *[P09958](https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P09958)* (Human Furin) at the [PDBe-KB](/source/PDBe-KB).

- Overview of all the structural information available in the [PDB](/source/Protein_Data_Bank) for [UniProt](/source/UniProt): *[P23188](https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P23188)* (Mouse Furin) at the [PDBe-KB](/source/PDBe-KB).

v t e PDB gallery 1p8j: CRYSTAL STRUCTURE OF THE PROPROTEIN CONVERTASE FURIN

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21) Digestive enzymes Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic Coagulation factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue-type plasminogen activator Urinary plasminogen activator Complement system Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase Other immune system Chymase Granzyme Tryptase Proteinase 3/Myeloblastin Venombin Ancrod Batroxobin Other Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics Types EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

[Portal](https://en.wikipedia.org/wiki/Wikipedia:Contents/Portals):
- [Biology](https://en.wikipedia.org/wiki/Portal:Biology)

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Adapted from the Wikipedia article [Furin](https://en.wikipedia.org/wiki/Furin) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Furin?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.