Q3UP87 (ELNE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neutrophil elastase
EC=3.4.21.37

Alternative name(s):
Elastase-2
Leukocyte elastase

Gene names

Name:	Elane
Synonyms:	Ela2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	265 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis By similarity.
Catalytic activity	Hydrolysis of proteins, including elastin. Preferential cleavage: Val-|-Xaa > Ala-|-Xaa.
Subunit structure	Interacts with NOTCH2NL By similarity.
Sequence similarities	Belongs to the peptidase S1 family. Elastase subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acute inflammatory response to antigenic stimulus Inferred from direct assay PubMed 17878334. Source: MGI leukocyte migration Inferred from mutant phenotype PubMed 15034066. Source: MGI negative regulation of chemokine biosynthetic process Inferred from electronic annotation. Source: Compara negative regulation of growth of symbiont in host Inferred from mutant phenotype PubMed 10714686. Source: MGI negative regulation of interleukin-8 biosynthetic process Inferred from electronic annotation. Source: Compara neutrophil mediated killing of fungus Inferred from mutant phenotype PubMed 11907569. Source: MGI phagocytosis Inferred from mutant phenotype PubMed 15034066. Source: MGI positive regulation of immune response Inferred from mutant phenotype PubMed 10714686. Source: MGI positive regulation of interleukin-8 biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to UV Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from mutant phenotype PubMed 10714686. Source: MGI response to yeast Inferred from mutant phenotype PubMed 11907569. Source: MGI
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay PubMed 17878334. Source: MGI secretory granule Inferred from electronic annotation. Source: Compara
Molecular_function	heparin binding Inferred from electronic annotation. Source: Compara serine-type endopeptidase activity Inferred from direct assay PubMed 17878334. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 265	239	Neutrophil elastase		PRO_0000228686
Regions
	Domain	29 – 247	219	Peptidase S1
Sites
	Active site	69	1	Charge relay system By similarity
	Active site	116	1	Charge relay system By similarity
	Active site	202	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	123	1	N-linked (GlcNAc...) Potential
	Glycosylation	172	1	N-linked (GlcNAc...) Potential
	Disulfide bond	54 ↔ 70		By similarity
	Disulfide bond	150 ↔ 208		By similarity
	Disulfide bond	180 ↔ 187		By similarity
	Disulfide bond	198 ↔ 223		By similarity
Experimental info
	Sequence conflict	26	1	A → P in AAB60670. Ref.1
	Sequence conflict	68	1	A → V in AAB60670. Ref.1
	Sequence conflict	102	1	R → G in AAB60670. Ref.1
	Sequence conflict	181	1	R → P in AAB60670. Ref.1
	Sequence conflict	236	1	A → G in AAB60670. Ref.1
	Sequence conflict	239	1	A → V in AAB60670. Ref.1
	Sequence conflict	248	1	S → R in AAB60670. Ref.1
	Sequence conflict	261	1	E → R in AAB60670. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q3UP87 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 666029A299275EB6	FASTA	265	28,648
	10 20 30 40 50 60 MALGRLSSRT LAAMLLALFL GGPALASEIV GGRPARPHAW PFMASLQRRG GHFCGATLIA 70 80 90 100 110 120 RNFVMSAAHC VNGLNFRSVQ VVLGAHDLRR QERTRQTFSV QRIFENGFDP SQLLNDIVII 130 140 150 160 170 180 QLNGSATINA NVQVAQLPAQ GQGVGDRTPC LAMGWGRLGT NRPSPSVLQE LNVTVVTNMC 190 200 210 220 230 240 RRRVNVCTLV PRRQAGICFG DSGGPLVCNN LVQGIDSFIR GGCGSGLYPD AFAPVAEFAD 250 260 WINSIIRSHN DHLLTHPKDR EGRTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Nuchprayoon I., Meyers S., Scott L.M., Suzow J., Hiebert S., Friedman A.D. Mol. Cell. Biol. 14:5558-5568(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c.
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Spleen.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U04962, U06076 Genomic DNA. Translation: AAB60670.1. AK143710 mRNA. Translation: BAE25510.1. BC145800 mRNA. Translation: AAI45801.1.
IPI	IPI00122302.
PIR	I48679.
RefSeq	NP_056594.2. NM_015779.2.
UniGene	Mm.262194.
3D structure databases
ProteinModelPortal	Q3UP87.
SMR	Q3UP87. Positions 29-247.
ModBase	Search...
Protein family/group databases
MEROPS	S01.131.
Proteomic databases
PRIDE	Q3UP87.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000046091; ENSMUSP00000038925; ENSMUSG00000020125.
GeneID	50701.
KEGG	mmu:50701.
UCSC	uc007gai.1. mouse.
Organism-specific databases
CTD	1991.
MGI	MGI:2679229. Elane.
Phylogenomic databases
eggNOG	COG5640.
GeneTree	ENSGT00700000104045.
HOGENOM	HOG000251820.
HOVERGEN	HBG013304.
InParanoid	A6H698.
KO	K01327.
OMA	LRGGHFC.
OrthoDB	EOG4XSKQQ.
Gene expression databases
Bgee	Q3UP87.
CleanEx	MM_ELA2.
Genevestigator	Q3UP87.
GermOnline	ENSMUSG00000020125. Mus musculus.
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q3UP87.
ChEMBL	CHEMBL5156.
NextBio	307549.
SOURCE	Search...

Entry information

Entry name

ELNE_MOUSE

Accession

Primary (citable) accession number: Q3UP87
Secondary accession number(s): A6H698, Q61515

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	October 11, 2005
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program