Proteinase 3

PRTN3

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1FUJ

Identifiers

Aliases

PRTN3, ACPA, AGP7, C-ANCA, CANCA, MBN, MBT, NP-4, NP4, P29, PR-3, PR3, proteinase 3

External IDs

OMIM: 177020 MGI: 893580 HomoloGene: 120934 GeneCards: PRTN3

Gene ontology
Molecular function	• enzyme binding • peptidase activity • serine-type peptidase activity • serine-type endopeptidase activity • hydrolase activity
Cellular component	• extracellular matrix • extracellular fluid • plasma membrane • extracellular exosome • cytosol
Biological process	• collagen catabolic process • blood coagulation • negative regulation of phagocytosis • mature conventional dendritic cell differentiation • positive regulation of cell proliferation • proteolysis
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


5657


19152

Ensembl


n/a


ENSMUSG00000057729

UniProt


P24158


Q61096

RefSeq (mRNA)


NM_002777


NM_011178

RefSeq (protein)


NP_002768.3


NP_035308.2

Location (UCSC)

Chr 19: 0.84 – 0.85 Mb

Chr 10: 79.87 – 79.88 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Proteinase 3 also known as PRTN3 is an enzyme that in humans is encoded by the PRTN3 gene.^[3]

Function

PRTN3 is a serine protease enzyme expressed mainly in neutrophil granulocytes. Its exact role in the function of the neutrophil is unknown, but, in human neutrophils, proteinase 3 contributes to the proteolytic generation of antimicrobial peptides. It is also the epitope of anti-neutrophil cytoplasmic antibodies (ANCAs) of the c-ANCA (cytoplasmic subtype) class, a type of antibody frequently found in the disease granulomatosis with polyangiitis (formerly known as "Wegener's granulomatosis").^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Campanelli D, Melchior M, Fu Y, Nakata M, Shuman H, Nathan C, Gabay JE (December 1990). "Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and autoantigen from human neutrophils". J. Exp. Med. 172 (6): 1709–15. doi:10.1084/jem.172.6.1709. PMC 2188764. PMID 2258701.
↑ van der Geld YM, Limburg PC, Kallenberg CG (February 2001). "Proteinase 3, Wegener's autoantigen: from gene to antigen". J. Leukoc. Biol. 69 (2): 177–90. PMID 11272267.

Watorek E, Boratyńska M, Klinger M (2004). "Wegener's granulomatosis--autoimmunity to neutrophil proteinase 3". Arch. Immunol. Ther. Exp. (Warsz.). 51 (3): 157–67. PMID 12894870.
van der Helm-van Mil AH, Huizinga TW, de Vries RR, Toes RE (2007). "Emerging patterns of risk factor make-up enable subclassification of rheumatoid arthritis". Arthritis Rheum. 56 (6): 1728–35. doi:10.1002/art.22716. PMID 17534941.
Sturrock AB, Franklin KF, Rao G, et al. (1992). "Structure, chromosomal assignment, and expression of the gene for proteinase-3. The Wegener's granulomatosis autoantigen". J. Biol. Chem. 267 (29): 21193–9. PMID 1400430.
Zimmer M, Medcalf RL, Fink TM, et al. (1992). "Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter". Proc. Natl. Acad. Sci. U.S.A. 89 (17): 8215–9. doi:10.1073/pnas.89.17.8215. PMC 49888. PMID 1518849.
Labbaye C, Musette P, Cayre YE (1991). "Wegener autoantigen and myeloblastin are encoded by a single mRNA". Proc. Natl. Acad. Sci. U.S.A. 88 (20): 9253–6. doi:10.1073/pnas.88.20.9253. PMC 52692. PMID 1681549.
Lüdemann J, Utecht B, Gross WL (1990). "Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis recognize an elastinolytic enzyme". J. Exp. Med. 171 (1): 357–62. doi:10.1084/jem.171.1.357. PMC 2187669. PMID 1688612.
Musette P, Labbaye C, Dorner MH, et al. (1991). "Wegener's autoantigen and leukemia". Blood. 77 (6): 1398–9. PMID 2001463.
Rao NV, Wehner NG, Marshall BC, et al. (1991). "Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties". J. Biol. Chem. 266 (15): 9540–8. PMID 2033050.
Ohlsson K, Linder C, Rosengren M (1990). "Monoclonal antibodies specific for neutrophil proteinase 4. Production and use for isolation of the enzyme". Biol. Chem. Hoppe-Seyler. 371 (7): 549–55. doi:10.1515/bchm3.1990.371.2.549. PMID 2121162.
Gupta SK, Niles JL, McCluskey RT, Arnaout MA (1990). "Identity of Wegener's autoantigen (p29) with proteinase 3 and myeloblastin". Blood. 76 (10): 2162. PMID 2242436.
Campanelli D, Melchior M, Fu Y, et al. (1991). "Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and autoantigen from human neutrophils". J. Exp. Med. 172 (6): 1709–15. doi:10.1084/jem.172.6.1709. PMC 2188764. PMID 2258701.
Goldschmeding R, Dolman KM, van den Ende ME, et al. (1991). "The relation of 29 kD C-ANCA antigen to proteinase 3". APMIS Suppl. 19: 26–7. PMID 2285532.
Jenne DE, Tschopp J, Lüdemann J, et al. (1990). "Wegener's autoantigen decoded". Nature. 346 (6284): 520. doi:10.1038/346520a0. PMID 2377228.
Wilde CG, Snable JL, Griffith JE, Scott RW (1990). "Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase". J. Biol. Chem. 265 (4): 2038–41. PMID 2404977.
Gabay JE, Scott RW, Campanelli D, et al. (1989). "Antibiotic proteins of human polymorphonuclear leukocytes". Proc. Natl. Acad. Sci. U.S.A. 86 (14): 5610–4. doi:10.1073/pnas.86.14.5610. PMC 297672. PMID 2501794.
Bories D, Raynal MC, Solomon DH, et al. (1990). "Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells". Cell. 59 (6): 959–68. doi:10.1016/0092-8674(89)90752-6. PMID 2598267.
Niles JL, McCluskey RT, Ahmad MF, Arnaout MA (1989). "Wegener's granulomatosis autoantigen is a novel neutrophil serine proteinase". Blood. 74 (6): 1888–93. PMID 2679910.
Pontremoli S, Melloni E, Michetti M, et al. (1986). "Cytolytic effects of neutrophils: role for a membrane-bound neutral proteinase". Proc. Natl. Acad. Sci. U.S.A. 83 (6): 1685–9. doi:10.1073/pnas.83.6.1685. PMC 323148. PMID 3513185.
Sugimori T, Cooley J, Hoidal JR, Remold-O'Donnell E (1995). "Inhibitory properties of recombinant human monocyte/neutrophil elastase inhibitor". Am. J. Respir. Cell Mol. Biol. 13 (3): 314–22. doi:10.1165/ajrcmb.13.3.7654387. PMID 7654387.
Muller-Bérat N, Minowada J, Tsuji-Takayama K, et al. (1994). "The phylogeny of proteinase 3/myeloblastin, the autoantigen in Wegener's granulomatosis, and myeloperoxidase as shown by immunohistochemical studies on human leukemic cell lines". Clin. Immunol. Immunopathol. 70 (1): 51–9. doi:10.1006/clin.1994.1010. PMID 8261669.

External links

Proteinase 3 at the US National Library of Medicine Medical Subject Headings (MeSH)

PDB gallery

1fuj: PR3 (MYELOBLASTIN)

Antimicrobial peptides: Granulocyte granule contents

Azurophilic granules (1°)

Myeloperoxidase
Defensins
neutral serine proteases (Proteinase 3)
Lysozyme
Bactericidal/permeability-increasing protein
Collagenase

Specific granules (2°)

Neutrophil	Alkaline phosphatase Lactoferrin Lysozyme NADPH oxidase Collagenase Cathelicidin

Eosinophil	Cathepsin Major basic protein Eosinophil cationic protein Eosinophil peroxidase Eosinophil-derived neurotoxin

Basophil	Heparin Histamine

see also platelet alpha-granule, dense granule

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 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 Streptokinase S1P Cathepsin A G

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

This article is issued from Wikipedia - version of the 5/24/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

Proteinase 3

Function

References

Further reading

External links