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Neutrophil elastase (EC 3.4.21.37) (Elastase-2) (Leukocyte elastase)

 ELNE_MOUSE              Reviewed;         265 AA.
Q3UP87; A6H698; Q61515;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
12-SEP-2018, entry version 107.
RecName: Full=Neutrophil elastase;
EC=3.4.21.37;
AltName: Full=Elastase-2;
AltName: Full=Leukocyte elastase;
Flags: Precursor;
Name=Elane; Synonyms=Ela2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=8035830; DOI=10.1128/MCB.14.8.5558;
Nuchprayoon I., Meyers S., Scott L.M., Suzow J., Hiebert S.,
Friedman A.D.;
"PEBP2/CBF, the murine homolog of the human myeloid AML1 and PEBP2
beta/CBF beta proto-oncoproteins, regulates the murine myeloperoxidase
and neutrophil elastase genes in immature myeloid cells.";
Mol. Cell. Biol. 14:5558-5568(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Medullasin modifies the functions of natural killer
cells, monocytes and granulocytes. Inhibits C5a-dependent
neutrophil enzyme release and chemotaxis (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins, including elastin.
Preferential cleavage: Val-|-Xaa > Ala-|-Xaa.
-!- SUBUNIT: Interacts with NOTCH2NL. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; U04962; AAB60670.1; -; Genomic_DNA.
EMBL; U06076; AAB60670.1; JOINED; Genomic_DNA.
EMBL; AK143710; BAE25510.1; -; mRNA.
EMBL; BC145800; AAI45801.1; -; mRNA.
CCDS; CCDS23994.1; -.
PIR; I48679; I48679.
RefSeq; NP_056594.2; NM_015779.2.
UniGene; Mm.262194; -.
ProteinModelPortal; Q3UP87; -.
SMR; Q3UP87; -.
BioGrid; 206058; 1.
STRING; 10090.ENSMUSP00000038925; -.
BindingDB; Q3UP87; -.
ChEMBL; CHEMBL5156; -.
MEROPS; S01.131; -.
PhosphoSitePlus; Q3UP87; -.
MaxQB; Q3UP87; -.
PaxDb; Q3UP87; -.
PRIDE; Q3UP87; -.
Ensembl; ENSMUST00000046091; ENSMUSP00000038925; ENSMUSG00000020125.
GeneID; 50701; -.
KEGG; mmu:50701; -.
UCSC; uc007gai.1; mouse.
CTD; 1991; -.
MGI; MGI:2679229; Elane.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00910000144219; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q3UP87; -.
KO; K01327; -.
OMA; NWINSII; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q3UP87; -.
TreeFam; TF335284; -.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6803157; Antimicrobial peptides.
Reactome; R-MMU-977606; Regulation of Complement cascade.
ChiTaRS; Cela2a; mouse.
PRO; PR:Q3UP87; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000020125; Expressed in 45 organ(s), highest expression level in bone marrow.
CleanEx; MM_ELA2; -.
Genevisible; Q3UP87; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0030141; C:secretory granule; ISO:MGI.
GO; GO:0017053; C:transcriptional repressor complex; ISO:MGI.
GO; GO:0019955; F:cytokine binding; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
GO; GO:0008201; F:heparin binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IDA:MGI.
GO; GO:0002812; P:biosynthetic process of antibacterial peptides active against Gram-negative bacteria; ISO:MGI.
GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
GO; GO:0050832; P:defense response to fungus; IMP:MGI.
GO; GO:0050900; P:leukocyte migration; IMP:MGI.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISO:MGI.
GO; GO:0045079; P:negative regulation of chemokine biosynthetic process; ISO:MGI.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IMP:MGI.
GO; GO:0045415; P:negative regulation of interleukin-8 biosynthetic process; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0070947; P:neutrophil mediated killing of fungus; IMP:MGI.
GO; GO:0070945; P:neutrophil mediated killing of gram-negative bacterium; ISO:MGI.
GO; GO:0006909; P:phagocytosis; IMP:MGI.
GO; GO:0050778; P:positive regulation of immune response; IMP:MGI.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; ISO:MGI.
GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISO:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
GO; GO:0009411; P:response to UV; ISO:MGI.
GO; GO:0001878; P:response to yeast; IMP:MGI.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Protease;
Reference proteome; Serine protease; Signal.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 265 Neutrophil elastase.
/FTId=PRO_0000228686.
DOMAIN 29 247 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 69 69 Charge relay system. {ECO:0000250}.
ACT_SITE 116 116 Charge relay system. {ECO:0000250}.
ACT_SITE 202 202 Charge relay system. {ECO:0000250}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 70 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 150 208 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 180 187 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 198 223 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 26 26 A -> P (in Ref. 1; AAB60670).
{ECO:0000305}.
CONFLICT 68 68 A -> V (in Ref. 1; AAB60670).
{ECO:0000305}.
CONFLICT 102 102 R -> G (in Ref. 1; AAB60670).
{ECO:0000305}.
CONFLICT 181 181 R -> P (in Ref. 1; AAB60670).
{ECO:0000305}.
CONFLICT 236 236 A -> G (in Ref. 1; AAB60670).
{ECO:0000305}.
CONFLICT 239 239 A -> V (in Ref. 1; AAB60670).
{ECO:0000305}.
CONFLICT 248 248 S -> R (in Ref. 1; AAB60670).
{ECO:0000305}.
CONFLICT 261 261 E -> R (in Ref. 1; AAB60670).
{ECO:0000305}.
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


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