ID ELNE_MOUSE Reviewed; 265 AA. AC Q3UP87; A6H698; Q61515; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 138. DE RecName: Full=Neutrophil elastase; DE EC=3.4.21.37; DE AltName: Full=Elastase-2; DE AltName: Full=Leukocyte elastase; DE Flags: Precursor; GN Name=Elane; Synonyms=Ela2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BALB/cJ; RX PubMed=8035830; DOI=10.1128/mcb.14.8.5558-5568.1994; RA Nuchprayoon I., Meyers S., Scott L.M., Suzow J., Hiebert S., Friedman A.D.; RT "PEBP2/CBF, the murine homolog of the human myeloid AML1 and PEBP2 beta/CBF RT beta proto-oncoproteins, regulates the murine myeloperoxidase and RT neutrophil elastase genes in immature myeloid cells."; RL Mol. Cell. Biol. 14:5558-5568(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [4] RP FUNCTION IN DEFENSE AGAINST BACTERIA, AND DISRUPTION PHENOTYPE. RX PubMed=10947984; DOI=10.1126/science.289.5482.1185; RA Belaaouaj A., Kim K.S., Shapiro S.D.; RT "Degradation of outer membrane protein A in Escherichia coli killing by RT neutrophil elastase."; RL Science 289:1185-1188(2000). CC -!- FUNCTION: Serine protease that modifies the functions of natural killer CC cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil CC enzyme release and chemotaxis (By similarity). Capable of killing CC E.coli; probably digests outer membrane protein A (ompA) in E.coli CC (PubMed:10947984). {ECO:0000250|UniProtKB:P08246, CC ECO:0000269|PubMed:10947984}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins, including elastin. Preferential CC cleavage: Val-|-Xaa > Ala-|-Xaa.; EC=3.4.21.37; CC Evidence={ECO:0000250|UniProtKB:P08246}; CC -!- SUBUNIT: Interacts with NOTCH2NL. {ECO:0000250|UniProtKB:P08246}. CC -!- DISRUPTION PHENOTYPE: Mice with a homozygous knockout of this gene are CC more easily killed by wild-type E.coli, but the knockout has no visible CC killing effect on E.coli deleted for outer membrane protein A (ompA). CC {ECO:0000269|PubMed:10947984}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. 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; U04962; AAB60670.1; -; Genomic_DNA. DR EMBL; U06076; AAB60670.1; JOINED; Genomic_DNA. DR EMBL; AK143710; BAE25510.1; -; mRNA. DR EMBL; BC145800; AAI45801.1; -; mRNA. DR CCDS; CCDS23994.1; -. DR PIR; I48679; I48679. DR RefSeq; NP_056594.2; NM_015779.2. DR AlphaFoldDB; Q3UP87; -. DR SMR; Q3UP87; -. DR BioGRID; 206058; 1. DR STRING; 10090.ENSMUSP00000038925; -. DR BindingDB; Q3UP87; -. DR ChEMBL; CHEMBL5156; -. DR DrugCentral; Q3UP87; -. DR MEROPS; S01.131; -. DR GlyCosmos; Q3UP87; 2 sites, No reported glycans. DR GlyGen; Q3UP87; 2 sites. DR PhosphoSitePlus; Q3UP87; -. DR MaxQB; Q3UP87; -. DR PaxDb; 10090-ENSMUSP00000038925; -. DR ProteomicsDB; 277786; -. DR Antibodypedia; 4209; 803 antibodies from 42 providers. DR DNASU; 50701; -. DR Ensembl; ENSMUST00000046091.7; ENSMUSP00000038925.5; ENSMUSG00000020125.8. DR GeneID; 50701; -. DR KEGG; mmu:50701; -. DR UCSC; uc007gai.1; mouse. DR AGR; MGI:2679229; -. DR CTD; 1991; -. DR MGI; MGI:2679229; Elane. DR VEuPathDB; HostDB:ENSMUSG00000020125; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT01030000234528; -. DR HOGENOM; CLU_006842_1_0_1; -. DR InParanoid; Q3UP87; -. DR OMA; RRRVNVC; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; Q3UP87; -. DR TreeFam; TF335284; -. DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix. DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases. DR Reactome; R-MMU-5620971; Pyroptosis. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-6803157; Antimicrobial peptides. DR Reactome; R-MMU-977606; Regulation of Complement cascade. DR BioGRID-ORCS; 50701; 1 hit in 76 CRISPR screens. DR ChiTaRS; Cela2a; mouse. DR PRO; PR:Q3UP87; -. DR Proteomes; UP000000589; Chromosome 10. DR RNAct; Q3UP87; Protein. DR Bgee; ENSMUSG00000020125; Expressed in femorotibial joint and 36 other cell types or tissues. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0030141; C:secretory granule; ISO:MGI. DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI. DR GO; GO:0019955; F:cytokine binding; ISO:MGI. DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI. DR GO; GO:0008201; F:heparin binding; ISO:MGI. DR GO; GO:0008233; F:peptidase activity; ISO:MGI. DR GO; GO:0002020; F:protease binding; ISO:MGI. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI. DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI. DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IDA:MGI. DR GO; GO:0002812; P:biosynthetic process of antibacterial peptides active against Gram-negative bacteria; ISO:MGI. DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI. DR GO; GO:0050832; P:defense response to fungus; IMP:MGI. DR GO; GO:0050900; P:leukocyte migration; IMP:MGI. DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISO:MGI. DR GO; GO:0032682; P:negative regulation of chemokine production; ISO:MGI. DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0070947; P:neutrophil-mediated killing of fungus; IMP:MGI. DR GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; ISO:MGI. DR GO; GO:0006909; P:phagocytosis; IMP:MGI. DR GO; GO:0050778; P:positive regulation of immune response; IMP:MGI. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI. DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISO:MGI. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI. DR GO; GO:0006508; P:proteolysis; ISO:MGI. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI. DR GO; GO:0009411; P:response to UV; ISO:MGI. DR GO; GO:0001878; P:response to yeast; IMP:MGI. 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:SF16; NEUTROPHIL ELASTASE; 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; Q3UP87; MM. PE 1: Evidence at protein level; KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome; KW Serine protease; Signal. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..265 FT /note="Neutrophil elastase" FT /id="PRO_0000228686" FT DOMAIN 29..247 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 69 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P08246" FT ACT_SITE 116 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P08246" FT ACT_SITE 202 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P08246" FT CARBOHYD 123 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 172 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 54..70 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 150..208 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 180..187 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 198..223 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT CONFLICT 26 FT /note="A -> P (in Ref. 1; AAB60670)" FT /evidence="ECO:0000305" FT CONFLICT 68 FT /note="A -> V (in Ref. 1; AAB60670)" FT /evidence="ECO:0000305" FT CONFLICT 102 FT /note="R -> G (in Ref. 1; AAB60670)" FT /evidence="ECO:0000305" FT CONFLICT 181 FT /note="R -> P (in Ref. 1; AAB60670)" FT /evidence="ECO:0000305" FT CONFLICT 236 FT /note="A -> G (in Ref. 1; AAB60670)" FT /evidence="ECO:0000305" FT CONFLICT 239 FT /note="A -> V (in Ref. 1; AAB60670)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="S -> R (in Ref. 1; AAB60670)" FT /evidence="ECO:0000305" FT CONFLICT 261 FT /note="E -> R (in Ref. 1; AAB60670)" FT /evidence="ECO:0000305" SQ SEQUENCE 265 AA; 28648 MW; 666029A299275EB6 CRC64; MALGRLSSRT LAAMLLALFL GGPALASEIV GGRPARPHAW PFMASLQRRG GHFCGATLIA RNFVMSAAHC VNGLNFRSVQ VVLGAHDLRR QERTRQTFSV QRIFENGFDP SQLLNDIVII QLNGSATINA NVQVAQLPAQ GQGVGDRTPC LAMGWGRLGT NRPSPSVLQE LNVTVVTNMC RRRVNVCTLV PRRQAGICFG DSGGPLVCNN LVQGIDSFIR GGCGSGLYPD AFAPVAEFAD WINSIIRSHN DHLLTHPKDR EGRTN //