ELNE_MOUSE
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 03-AUG-2022, entry version 130.
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: Medullasin modifies the functions of natural killer cells,
CC monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme
CC release and chemotaxis (By similarity). Capable of killing E.coli;
CC probably digests outer membrane protein A (ompA) in E.coli
CC (PubMed:10947984). {ECO:0000250, 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 -!- SUBUNIT: Interacts with NOTCH2NL. {ECO:0000250}.
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}.
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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 GlyGen; Q3UP87; 2 sites.
DR PhosphoSitePlus; Q3UP87; -.
DR MaxQB; Q3UP87; -.
DR PaxDb; Q3UP87; -.
DR PRIDE; Q3UP87; -.
DR ProteomicsDB; 277786; -.
DR Antibodypedia; 4209; 711 antibodies from 42 providers.
DR DNASU; 50701; -.
DR Ensembl; ENSMUST00000046091; ENSMUSP00000038925; ENSMUSG00000020125.
DR GeneID; 50701; -.
DR KEGG; mmu:50701; -.
DR UCSC; uc007gai.1; mouse.
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; 1314811at2759; -.
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 71 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 tissues.
DR Genevisible; Q3UP87; MM.
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; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
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"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
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
