Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3UP87 (ELNE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neutrophil elastase

EC=3.4.21.37
Alternative name(s):
Elastase-2
Leukocyte elastase
Gene names
Name:Elane
Synonyms:Ela2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute inflammatory response to antigenic stimulus

Inferred from direct assay PubMed 17878334. Source: MGI

defense response to bacterium

Inferred from electronic annotation. Source: Ensembl

defense response to fungus

Inferred from mutant phenotype PubMed 10714686PubMed 11907569. Source: MGI

leukocyte migration

Inferred from mutant phenotype PubMed 15034066. Source: MGI

negative regulation of chemokine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

response to UV

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 10714686. Source: MGI

response to yeast

Inferred from mutant phenotype PubMed 11907569. Source: MGI

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 17878334. Source: MGI

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: Ensembl

serine-type endopeptidase activity

Inferred from direct assay PubMed 17878334. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 265239Neutrophil elastase
PRO_0000228686

Regions

Domain29 – 247219Peptidase S1

Sites

Active site691Charge relay system By similarity
Active site1161Charge relay system By similarity
Active site2021Charge relay system By similarity

Amino acid modifications

Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 70 By similarity
Disulfide bond150 ↔ 208 By similarity
Disulfide bond180 ↔ 187 By similarity
Disulfide bond198 ↔ 223 By similarity

Experimental info

Sequence conflict261A → P in AAB60670. Ref.1
Sequence conflict681A → V in AAB60670. Ref.1
Sequence conflict1021R → G in AAB60670. Ref.1
Sequence conflict1811R → P in AAB60670. Ref.1
Sequence conflict2361A → G in AAB60670. Ref.1
Sequence conflict2391A → V in AAB60670. Ref.1
Sequence conflict2481S → R in AAB60670. Ref.1
Sequence conflict2611E → R in AAB60670. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3UP87 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 666029A299275EB6

FASTA26528,648
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
CCDSCCDS23994.1.
PIRI48679.
RefSeqNP_056594.2. NM_015779.2.
UniGeneMm.262194.

3D structure databases

ProteinModelPortalQ3UP87.
SMRQ3UP87. Positions 29-247.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206058. 1 interaction.

Chemistry

BindingDBQ3UP87.
ChEMBLCHEMBL5156.

Protein family/group databases

MEROPSS01.131.

Proteomic databases

PRIDEQ3UP87.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046091; ENSMUSP00000038925; ENSMUSG00000020125.
GeneID50701.
KEGGmmu:50701.
UCSCuc007gai.1. mouse.

Organism-specific databases

CTD1991.
MGIMGI:2679229. Elane.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00700000104045.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidA6H698.
KOK01327.
OMALRGGHFC.
OrthoDBEOG7MKW6Q.
PhylomeDBQ3UP87.
TreeFamTF335284.

Gene expression databases

BgeeQ3UP87.
CleanExMM_ELA2.
GenevestigatorQ3UP87.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307549.
PROQ3UP87.
SOURCESearch...

Entry information

Entry nameELNE_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot