ID PRTN3_HUMAN Reviewed; 256 AA. AC P24158; P15637; P18078; Q4VB08; Q4VB09; Q6LBM7; Q6LBN2; Q9UD25; Q9UQD8; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 3. DT 27-MAR-2024, entry version 233. DE RecName: Full=Myeloblastin; DE EC=3.4.21.76 {ECO:0000269|PubMed:2033050, ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:23202369, ECO:0000269|PubMed:28240246, ECO:0000269|PubMed:3198760, ECO:0000269|PubMed:7897245}; DE AltName: Full=AGP7; DE AltName: Full=C-ANCA antigen; DE AltName: Full=Leukocyte proteinase 3; DE Short=PR-3; DE Short=PR3; DE AltName: Full=Neutrophil proteinase 4; DE Short=NP-4; DE AltName: Full=P29; DE AltName: Full=Wegener autoantigen; DE Flags: Precursor; GN Name=PRTN3; Synonyms=MBN; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-119; THR-135 AND SER-136. RX PubMed=1681549; DOI=10.1073/pnas.88.20.9253; RA Labbaye C., Musette P., Cayre Y.E.; RT "Wegener autoantigen and myeloblastin are encoded by a single mRNA."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9253-9256(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-119. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-119. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 AND 22-256. RX PubMed=1518849; DOI=10.1073/pnas.89.17.8215; RA Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P., Jenne D.E.; RT "Three human elastase-like genes coordinately expressed in the RT myelomonocyte lineage are organized as a single genetic locus on 19pter."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-254, AND VARIANTS THR-135 AND RP SER-136. RX PubMed=1400430; DOI=10.1016/s0021-9258(19)36816-4; RA Sturrock A.B., Franklin K.F., Rao G., Marshall B.C., Rebentisch M.B., RA Lemons R.S., Hoidal J.R.; RT "Structure, chromosomal assignment, and expression of the gene for RT proteinase-3. The Wegener's granulomatosis autoantigen."; RL J. Biol. Chem. 267:21193-21199(1992). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200, AND VARIANT ILE-119. RX PubMed=9924693; DOI=10.1097/00002371-199901000-00001; RA Clave E., Molldrem J., Hensel N., Raptis A., Barrett A.J.; RT "Donor-recipient polymorphism of the proteinase 3 gene: a potential target RT for T-cell alloresponses to myeloid leukemia."; RL J. Immunother. 22:1-6(1999). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-42. RX PubMed=2001463; RA Musette P., Labbaye C., Dorner M.H., Cayre Y.E., Casanova J.-L., RA Kourilsky P.; RT "Wegener's autoantigen and leukemia."; RL Blood 77:1398-1399(1991). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-256, AND PROTEIN SEQUENCE OF 28-71; 156-181 RP AND 196-219. RX PubMed=2258701; DOI=10.1084/jem.172.6.1709; RA Campanelli D., Melchior M., Fu Y., Nakata M., Shuman H., Nathan C., RA Gabay J.E.; RT "Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and RT autoantigen from human neutrophils."; RL J. Exp. Med. 172:1709-1715(1990). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-256, AND VARIANTS ILE-119; THR-135 AND RP SER-136. RX PubMed=2598267; DOI=10.1016/0092-8674(89)90752-6; RA Bories D., Raynal M.-C., Solomon D.H., Darzynkiewicz Z., Cayre Y.E.; RT "Down-regulation of a serine protease, myeloblastin, causes growth arrest RT and differentiation of promyelocytic leukemia cells."; RL Cell 59:959-968(1989). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-256, PROTEIN SEQUENCE OF 28-48, VARIANTS RP ILE-119; THR-135 AND SER-136, AND IDENTITY OF WEGENER'S AUTOANTIGEN WITH RP PR-3. RX PubMed=2377228; DOI=10.1038/346520a0; RA Jenne D.E., Tschopp J., Luedemann J., Utecht B., Gross W.L.; RT "Wegener's autoantigen decoded."; RL Nature 346:520-520(1990). RN [12] RP PROTEIN SEQUENCE OF 28-67 AND 228-244, FUNCTION, CATALYTIC ACTIVITY, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=2033050; DOI=10.1016/s0021-9258(18)92854-1; RA Rao N.V., Wehner N.G., Marshall B.C., Gray W.R., Gray B.H., Hoidal J.R.; RT "Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. RT Structural and functional properties."; RL J. Biol. Chem. 266:9540-9548(1991). RN [13] RP PROTEIN SEQUENCE OF 28-47 AND 196-219. RX PubMed=2404977; DOI=10.1016/s0021-9258(19)39936-3; RA Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.; RT "Characterization of two azurphil granule proteases with active-site RT homology to neutrophil elastase."; RL J. Biol. Chem. 265:2038-2041(1990). RN [14] RP PROTEIN SEQUENCE OF 28-52. RX PubMed=2121162; DOI=10.1515/bchm3.1990.371.2.549; RA Ohlsson K., Linder C., Rosengren M.; RT "Monoclonal antibodies specific for neutrophil proteinase 4. Production and RT use for isolation of the enzyme."; RL Biol. Chem. Hoppe-Seyler 371:549-555(1990). RN [15] RP PROTEIN SEQUENCE OF 28-48. RX PubMed=2285532; DOI=10.1111/j.1600-0463.1990.tb05713.x; RA Goldschmeding R., Dolman K.M., van den Ende M.E., RA van der Meer-Gerritsen C.H., Sonnenberg A., von dem Borne A.E.; RT "The relation of 29 kD C-ANCA antigen to proteinase 3."; RL APMIS Suppl. 19:26-27(1990). RN [16] RP PROTEIN SEQUENCE OF 28-47. RX PubMed=2679910; RA Niles J.L., McCluskey R.T., Ahmad M.F., Arnaout M.A.; RT "Wegener's granulomatosis autoantigen is a novel neutrophil serine RT proteinase."; RL Blood 74:1888-1893(1989). RN [17] RP PROTEIN SEQUENCE OF 28-47. RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610; RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., RA Seeger M., Nathan C.F.; RT "Antibiotic proteins of human polymorphonuclear leukocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989). RN [18] RP PROTEIN SEQUENCE OF 28-47, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Neutrophil; RX PubMed=7897245; DOI=10.1016/0022-1759(94)00295-8; RA Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.; RT "Use of proteinase 3 purified by reverse phase HPLC to detect RT autoantibodies in systemic vasculitis."; RL J. Immunol. Methods 180:25-33(1995). RN [19] RP PROTEIN SEQUENCE OF 28-43. RX PubMed=1688612; DOI=10.1084/jem.171.1.357; RA Ludemann J., Utecht B., Gross W.L.; RT "Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis recognize RT an elastinolytic enzyme."; RL J. Exp. Med. 171:357-362(1990). RN [20] RP PROTEIN SEQUENCE OF 110-121, AND VARIANT ILE-119. RC TISSUE=Serum; RX PubMed=7539799; DOI=10.1074/jbc.270.23.14107; RA Duke-Cohan J.S., Morimoto C., Rocker J.A., Schlossman S.F.; RT "A novel form of dipeptidylpeptidase IV found in human serum. Isolation, RT characterization, and comparison with T lymphocyte membrane RT dipeptidylpeptidase IV (CD26)."; RL J. Biol. Chem. 270:14107-14114(1995). RN [21] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=3198760; DOI=10.1172/jci113816; RA Kao R.C., Wehner N.G., Skubitz K.M., Gray B.H., Hoidal J.R.; RT "Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that RT produces emphysema in hamsters."; RL J. Clin. Invest. 82:1963-1973(1988). RN [22] RP IDENTITY OF WEGENER'S AUTOANTIGEN WITH PROTEINASE 3. RX PubMed=2242436; RA Gupta S.K., Niles J.L., McCluskey R.T., Arnaout M.A.; RT "Identity of Wegener's autoantigen (p29) with proteinase 3 and RT myeloblastin."; RL Blood 76:2162-2162(1990). RN [23] RP INTERACTION WITH CD177, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17244676; DOI=10.1182/blood-2006-10-055327; RA von Vietinghoff S., Tunnemann G., Eulenberg C., Wellner M., RA Cristina Cardoso M., Luft F.C., Kettritz R.; RT "NB1 mediates surface expression of the ANCA antigen proteinase 3 on human RT neutrophils."; RL Blood 109:4487-4493(2007). RN [24] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP INDUCTION. RX PubMed=18462208; DOI=10.1111/j.1365-2249.2008.03663.x; RA von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.; RT "Neutrophil surface presentation of the anti-neutrophil cytoplasmic RT antibody-antigen proteinase 3 depends on N-terminal processing."; RL Clin. Exp. Immunol. 152:508-516(2008). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [26] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=21193407; DOI=10.1074/jbc.m110.171256; RA Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A., Luft F., RA Kettritz R.; RT "Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-ANCA RT neutrophil activation."; RL J. Biol. Chem. 286:7070-7081(2011). RN [27] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=22266279; DOI=10.4049/jimmunol.1102540; RA Kuckleburg C.J., Tilkens S.B., Santoso S., Newman P.J.; RT "Proteinase 3 contributes to transendothelial migration of NB1-positive RT neutrophils."; RL J. Immunol. 188:2419-2426(2012). RN [28] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23202369; DOI=10.1161/atvbaha.112.300474; RA Kuckleburg C.J., Newman P.J.; RT "Neutrophil proteinase 3 acts on protease-activated receptor-2 to enhance RT vascular endothelial cell barrier function."; RL Arterioscler. Thromb. Vasc. Biol. 33:275-284(2013). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [30] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=28240246; DOI=10.1038/srep43328; RA Jerke U., Marino S.F., Daumke O., Kettritz R.; RT "Characterization of the CD177 interaction with the ANCA antigen proteinase RT 3."; RL Sci. Rep. 7:43328-43328(2017). RN [31] RP INTERACTION WITH SERPINB1. RX PubMed=30692621; DOI=10.1038/s41590-018-0303-z; RA Choi Y.J., Kim S., Choi Y., Nielsen T.B., Yan J., Lu A., Ruan J., Lee H.R., RA Wu H., Spellberg B., Jung J.U.; RT "SERPINB1-mediated checkpoint of inflammatory caspase activation."; RL Nat. Immunol. 20:276-287(2019). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), GLYCOSYLATION AT ASN-174, AND RP DISULFIDE BONDS. RX PubMed=8757293; DOI=10.1006/jmbi.1996.0458; RA Fujinaga M., Charnaia M.M., Halenbeck R., Koths K., James M.N.G.; RT "The crystal structure of PR3, a neutrophil serine proteinase antigen of RT Wegener's granulomatosis antibodies."; RL J. Mol. Biol. 261:267-278(1996). CC -!- FUNCTION: Serine protease that degrades elastin, fibronectin, laminin, CC vitronectin, and collagen types I, III, and IV (in vitro) CC (PubMed:3198760, PubMed:2033050, PubMed:28240246). By cleaving and CC activating receptor F2RL1/PAR-2, enhances endothelial cell barrier CC function and thus vascular integrity during neutrophil transendothelial CC migration (PubMed:23202369). May play a role in neutrophil CC transendothelial migration, probably when associated with CD177 CC (PubMed:22266279). {ECO:0000269|PubMed:2033050, CC ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:23202369, CC ECO:0000269|PubMed:28240246, ECO:0000269|PubMed:3198760}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins, including elastin, by preferential CC cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.; EC=3.4.21.76; CC Evidence={ECO:0000269|PubMed:2033050, ECO:0000269|PubMed:22266279, CC ECO:0000269|PubMed:23202369, ECO:0000269|PubMed:28240246, CC ECO:0000269|PubMed:3198760, ECO:0000269|PubMed:7897245}; CC -!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF) CC and diisopropyl fluorophosphate (DFP). {ECO:0000269|PubMed:3198760}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.4. {ECO:0000269|PubMed:3198760}; CC -!- SUBUNIT: May form dimers (PubMed:28240246). Interacts with CD177; the CC interaction tethers PRTN3 to the cell surface; the interaction is CC direct (PubMed:17244676, PubMed:28240246). Interacts with SERPINB1 CC (PubMed:30692621). {ECO:0000269|PubMed:17244676, CC ECO:0000269|PubMed:28240246, ECO:0000269|PubMed:30692621}. CC -!- INTERACTION: CC P24158; P24001-4: IL32; NbExp=3; IntAct=EBI-465028, EBI-15570379; CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:18462208, CC ECO:0000269|PubMed:2033050, ECO:0000269|PubMed:3198760, CC ECO:0000269|PubMed:7897245, ECO:0000305|PubMed:17244676}. Secreted CC {ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:28240246}. Cell CC membrane {ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:18462208, CC ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:28240246}; Peripheral CC membrane protein {ECO:0000269|PubMed:17244676, CC ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:22266279, CC ECO:0000269|PubMed:28240246}; Extracellular side CC {ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:18462208, CC ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:28240246}. Membrane CC raft {ECO:0000269|PubMed:21193407}; Peripheral membrane protein CC {ECO:0000269|PubMed:21193407}; Extracellular side CC {ECO:0000269|PubMed:21193407}. Note=Localizes predominantly to CC azurophil granules (primary secretory granules) in neutrophils CC (PubMed:2033050, PubMed:3198760, PubMed:7897245, PubMed:18462208). CC Secreted upon neutrophil stimulation by TNF-alpha, lipopolysaccharide CC (LPS), fMLP and CXCL8/IL8 or during neutrophil transmigration CC (PubMed:22266279, PubMed:28240246). Following secretion tethered to the CC cell membrane by CD177 (PubMed:18462208, PubMed:22266279). CC {ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:2033050, CC ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:28240246, CC ECO:0000269|PubMed:3198760, ECO:0000269|PubMed:7897245}. CC -!- TISSUE SPECIFICITY: Expressed in polymorphonuclear leukocytes (at CC protein level) (PubMed:2033050, PubMed:7897245, PubMed:3198760). CC Expressed in neutrophils (at protein level) (PubMed:28240246, CC PubMed:18462208, PubMed:21193407, PubMed:22266279, PubMed:17244676). CC Expressed in differentiating neutrophils (PubMed:18462208). CC {ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:18462208, CC ECO:0000269|PubMed:2033050, ECO:0000269|PubMed:21193407, CC ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:28240246, CC ECO:0000269|PubMed:3198760, ECO:0000269|PubMed:7897245}. CC -!- INDUCTION: Induced during CSF3/G-CSF-mediated neutrophil CC differentiation. {ECO:0000269|PubMed:18462208}. CC -!- DISEASE: Note=Is the major autoantigen in anti-neutrophil cytoplasmic CC autoantibody (ANCA)-associated vasculitis (Wegener's granulomatosis) CC (PubMed:2377228, PubMed:2679910). This complex, systemic disease is CC characterized by granulomatous inflammation with necrotizing lesions in CC the respiratory tract, glomerulonephritis, vasculitis, and anti- CC neutrophil cytoplasmatic autoantibodies detected in patient sera CC (PubMed:2377228, PubMed:2679910). PRTN3 causes emphysema when CC administered by tracheal insufflation to hamsters (PubMed:3198760). CC {ECO:0000269|PubMed:3198760, ECO:0000303|PubMed:2377228, CC ECO:0000303|PubMed:2679910}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA36342.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA39598.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Proteinase 3 entry; CC URL="https://en.wikipedia.org/wiki/Proteinase_3"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M75154; AAA59558.1; -; mRNA. DR EMBL; AC004799; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471139; EAW69591.1; -; Genomic_DNA. DR EMBL; BC096183; AAH96183.1; -; mRNA. DR EMBL; BC096184; AAH96184.1; -; mRNA. DR EMBL; BC096185; AAH96185.1; -; mRNA. DR EMBL; BC096186; AAH96186.1; -; mRNA. DR EMBL; M96628; AAB59364.1; -; Genomic_DNA. DR EMBL; AH005293; AAB59493.1; -; Genomic_DNA. DR EMBL; M97911; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AH007523; AAD21524.1; -; Genomic_DNA. DR EMBL; X56606; CAA39943.1; -; mRNA. DR EMBL; X55668; CAA39203.1; -; mRNA. DR EMBL; M29142; AAA36342.1; ALT_FRAME; mRNA. DR EMBL; X56132; CAA39597.1; -; mRNA. DR EMBL; X56132; CAA39598.1; ALT_INIT; mRNA. DR CCDS; CCDS32860.1; -. DR PIR; A45080; PRHU3. DR RefSeq; NP_002768.3; NM_002777.3. DR PDB; 1FUJ; X-ray; 2.20 A; A/B/C/D=28-248. DR PDBsum; 1FUJ; -. DR AlphaFoldDB; P24158; -. DR SMR; P24158; -. DR BioGRID; 111638; 107. DR DIP; DIP-31107N; -. DR IntAct; P24158; 7. DR MINT; P24158; -. DR STRING; 9606.ENSP00000234347; -. DR BindingDB; P24158; -. DR ChEMBL; CHEMBL3900; -. DR DrugBank; DB05161; Elafin. DR DrugCentral; P24158; -. DR GuidetoPHARMACOLOGY; 2401; -. DR MEROPS; S01.134; -. DR GlyConnect; 1529; 2 N-Linked glycans (1 site). DR GlyCosmos; P24158; 2 sites, 1 glycan. DR GlyGen; P24158; 3 sites, 1 N-linked glycan (1 site). DR iPTMnet; P24158; -. DR BioMuta; PRTN3; -. DR DMDM; 6174926; -. DR CPTAC; non-CPTAC-1142; -. DR EPD; P24158; -. DR jPOST; P24158; -. DR MassIVE; P24158; -. DR PaxDb; 9606-ENSP00000234347; -. DR PeptideAtlas; P24158; -. DR PRIDE; P24158; -. DR ProteomicsDB; 54192; -. DR ABCD; P24158; 4 sequenced antibodies. DR Antibodypedia; 1069; 608 antibodies from 39 providers. DR DNASU; 5657; -. DR Ensembl; ENST00000234347.10; ENSP00000234347.3; ENSG00000196415.10. DR Ensembl; ENST00000612112.4; ENSP00000478977.1; ENSG00000277804.4. DR GeneID; 5657; -. DR KEGG; hsa:5657; -. DR MANE-Select; ENST00000234347.10; ENSP00000234347.3; NM_002777.4; NP_002768.3. DR UCSC; uc002lqa.2; human. DR AGR; HGNC:9495; -. DR CTD; 5657; -. DR DisGeNET; 5657; -. DR GeneCards; PRTN3; -. DR HGNC; HGNC:9495; PRTN3. DR HPA; ENSG00000196415; Tissue enriched (bone). DR MalaCards; PRTN3; -. DR MIM; 177020; gene. DR neXtProt; NX_P24158; -. DR OpenTargets; ENSG00000196415; -. DR Orphanet; 900; Granulomatosis with polyangiitis. DR PharmGKB; PA33842; -. DR VEuPathDB; HostDB:ENSG00000196415; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT01030000234528; -. DR HOGENOM; CLU_006842_1_0_1; -. DR InParanoid; P24158; -. DR OMA; FENNYDP; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; P24158; -. DR TreeFam; TF335284; -. DR BRENDA; 3.4.21.76; 2681. DR PathwayCommons; P24158; -. DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation. DR Reactome; R-HSA-449836; Other interleukin signaling. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6803157; Antimicrobial peptides. DR SABIO-RK; P24158; -. DR SignaLink; P24158; -. DR SIGNOR; P24158; -. DR BioGRID-ORCS; 5657; 11 hits in 1147 CRISPR screens. DR EvolutionaryTrace; P24158; -. DR GeneWiki; Proteinase_3; -. DR GenomeRNAi; 5657; -. DR Pharos; P24158; Tchem. DR PRO; PR:P24158; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P24158; Protein. DR Bgee; ENSG00000196415; Expressed in bone marrow and 73 other cell types or tissues. DR ExpressionAtlas; P24158; baseline and differential. DR GO; GO:0035578; C:azurophil granule lumen; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB. DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome. DR GO; GO:0045217; P:cell-cell junction maintenance; IMP:UniProtKB. DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW. DR GO; GO:0097029; P:mature conventional dendritic cell differentiation; IDA:UniProtKB. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:UniProtKB. DR GO; GO:0050765; P:negative regulation of phagocytosis; IDA:UniProtKB. DR GO; GO:0072672; P:neutrophil extravasation; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB. DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24257; CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER; 1. DR PANTHER; PTHR24257:SF15; MYELOBLASTIN; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; P24158; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Collagen degradation; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; KW Membrane; Protease; Reference proteome; Secreted; Serine protease; Signal; KW Zymogen. FT SIGNAL 1..25 FT PROPEP 26..27 FT /id="PRO_0000027707" FT CHAIN 28..248 FT /note="Myeloblastin" FT /evidence="ECO:0000305|PubMed:1688612, FT ECO:0000305|PubMed:2033050, ECO:0000305|PubMed:2258701, FT ECO:0000305|PubMed:7897245" FT /id="PRO_0000027708" FT PROPEP 249..256 FT /id="PRO_0000027709" FT DOMAIN 28..248 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 71 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 118 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 203 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT CARBOHYD 129 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 174 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8757293, FT ECO:0007744|PDB:1FUJ" FT DISULFID 56..72 FT /evidence="ECO:0000269|PubMed:8757293, FT ECO:0007744|PDB:1FUJ" FT DISULFID 152..209 FT /evidence="ECO:0000269|PubMed:8757293, FT ECO:0007744|PDB:1FUJ" FT DISULFID 182..188 FT /evidence="ECO:0000269|PubMed:8757293, FT ECO:0007744|PDB:1FUJ" FT DISULFID 199..224 FT /evidence="ECO:0000269|PubMed:8757293, FT ECO:0007744|PDB:1FUJ" FT VARIANT 119 FT /note="V -> I (in dbSNP:rs351111)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:1681549, ECO:0000269|PubMed:2377228, FT ECO:0000269|PubMed:2598267, ECO:0000269|PubMed:7539799, FT ECO:0000269|PubMed:9924693, ECO:0000269|Ref.3" FT /id="VAR_011691" FT VARIANT 135 FT /note="A -> T (in dbSNP:rs1042281)" FT /evidence="ECO:0000269|PubMed:1400430, FT ECO:0000269|PubMed:1681549, ECO:0000269|PubMed:2377228, FT ECO:0000269|PubMed:2598267" FT /id="VAR_011713" FT VARIANT 136 FT /note="T -> S (in dbSNP:rs1042282)" FT /evidence="ECO:0000269|PubMed:1400430, FT ECO:0000269|PubMed:1681549, ECO:0000269|PubMed:2377228, FT ECO:0000269|PubMed:2598267" FT /id="VAR_011714" FT CONFLICT 2 FT /note="A -> R (in Ref. 9; CAA39203)" FT /evidence="ECO:0000305" FT CONFLICT 38 FT /note="S -> I (in Ref. 19; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 40 FT /note="P -> PI (in Ref. 19; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 46 FT /note="Q -> E (in Ref. 13; AA sequence and 17; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 48 FT /note="R -> A (in Ref. 14; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 64 FT /note="S -> D (in Ref. 12; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 70 FT /note="A -> P (in Ref. 1; AAA59558)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="Missing (in Ref. 9; CAA39203)" FT /evidence="ECO:0000305" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 56..62 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:1FUJ" FT HELIX 70..73 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:1FUJ" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 81..86 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 98..107 FT /evidence="ECO:0007829|PDB:1FUJ" FT TURN 112..115 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 151..160 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 186..190 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 192..195 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 206..209 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 212..219 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 221..223 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:1FUJ" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:1FUJ" FT HELIX 236..239 FT /evidence="ECO:0007829|PDB:1FUJ" FT HELIX 240..247 FT /evidence="ECO:0007829|PDB:1FUJ" SQ SEQUENCE 256 AA; 27807 MW; CBECA36D8C4B2A40 CRC64; MAHRPPSPAL ASVLLALLLS GAARAAEIVG GHEAQPHSRP YMASLQMRGN PGSHFCGGTL IHPSFVLTAA HCLRDIPQRL VNVVLGAHNV RTQEPTQQHF SVAQVFLNNY DAENKLNDVL LIQLSSPANL SASVATVQLP QQDQPVPHGT QCLAMGWGRV GAHDPPAQVL QELNVTVVTF FCRPHNICTF VPRRKAGICF GDSGGPLICD GIIQGIDSFV IWGCATRLFP DFFTRVALYV DWIRSTLRRV EAKGRP //