Reviewed, UniProtKB/Swiss-Prot Q3UP87 (ELNE_MOUSE)

Names and origin

Protein names

Recommended name:
    Leukocyte elastase
    EC=3.4.21.37
Alternative name(s):
    Elastase-2
    Neutrophil elastase

Gene names

Name:

Ela2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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
Gene Ontology (GO)
Biological process	leukocyte migration Inferred from mutant phenotype. Source: MGI phagocytosis Inferred from mutant phenotype. Source: MGI proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
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	Leukocyte 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)
	Q3UP87-1 [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: 8035830] [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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Spleen.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U04962, U06076 Genomic DNA. Translation: AAB60670.1. AK143710 mRNA. Translation: BAE25510.1.
IPI	IPI00122302.
PIR	I48679.
RefSeq	NP_056594.2.
UniGene	Mm.262194
3D structure databases
HSSP	HSSP built from PDB template 1PPF based on UniProtKB P08246.
SMR	Q3UP87. Positions 29-247.
ModBase	Search...
Protein family/group databases
MEROPS	S01.131.
Genome annotation databases
Ensembl	ENSMUSG00000020125. Mus musculus. [Contig view]
GeneID	50701.
KEGG	mmu:50701.
NMPDR	fig|10090.3.peg.14002.
Organism-specific databases
MGI	MGI:2679229. Ela2.
Phylogenomic databases
HOGENOM	Q3UP87.
HOVERGEN	Q3UP87.
OMA	Q3UP87. WINSIIR.
Enzyme and pathway databases
BRENDA	3.4.21.37. 244.
Gene expression databases
ArrayExpress	Q3UP87.
Bgee	Q3UP87.
CleanEx	MM_ELA2.
GermOnline	ENSMUSG00000020125. Mus musculus.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	307549.
SOURCE	Search...

Entry information

Entry name

ELNE_MOUSE

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	October 11, 2005
Last modified:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)