Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neutrophil elastase

Gene

Elane

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity).By similarity

Catalytic activityi

Hydrolysis of proteins, including elastin. Preferential cleavage: Val-|-Xaa > Ala-|-Xaa.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei69Charge relay systemBy similarity1
Active sitei116Charge relay systemBy similarity1
Active sitei202Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

  • acute inflammatory response to antigenic stimulus Source: MGI
  • biosynthetic process of antibacterial peptides active against Gram-negative bacteria Source: MGI
  • defense response to bacterium Source: MGI
  • defense response to fungus Source: MGI
  • leukocyte migration Source: MGI
  • leukocyte migration involved in inflammatory response Source: MGI
  • negative regulation of chemokine biosynthetic process Source: MGI
  • negative regulation of growth of symbiont in host Source: MGI
  • negative regulation of interleukin-8 biosynthetic process Source: MGI
  • negative regulation of transcription by RNA polymerase II Source: MGI
  • neutrophil mediated killing of fungus Source: MGI
  • neutrophil mediated killing of gram-negative bacterium Source: MGI
  • phagocytosis Source: MGI
  • positive regulation of immune response Source: MGI
  • positive regulation of interleukin-8 biosynthetic process Source: MGI
  • positive regulation of leukocyte tethering or rolling Source: MGI
  • positive regulation of smooth muscle cell proliferation Source: MGI
  • proteolysis Source: MGI
  • response to lipopolysaccharide Source: MGI
  • response to UV Source: MGI
  • response to yeast Source: MGI

Keywordsi

Molecular functionHydrolase, Protease, Serine protease

Enzyme and pathway databases

ReactomeiR-MMU-1474228 Degradation of the extracellular matrix
R-MMU-1592389 Activation of Matrix Metalloproteinases
R-MMU-6798695 Neutrophil degranulation
R-MMU-6803157 Antimicrobial peptides
R-MMU-977606 Regulation of Complement cascade

Protein family/group databases

MEROPSiS01.131

Names & Taxonomyi

Protein namesi
Recommended name:
Neutrophil elastase (EC:3.4.21.37)
Alternative name(s):
Elastase-2
Leukocyte elastase
Gene namesi
Name:Elane
Synonyms:Ela2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2679229 Elane

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5156

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000022868627 – 265Neutrophil elastaseAdd BLAST239

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 70PROSITE-ProRule annotation
Glycosylationi123N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi150 ↔ 208PROSITE-ProRule annotation
Glycosylationi172N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi180 ↔ 187PROSITE-ProRule annotation
Disulfide bondi198 ↔ 223PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ3UP87
PaxDbiQ3UP87
PRIDEiQ3UP87

PTM databases

PhosphoSitePlusiQ3UP87

Expressioni

Gene expression databases

BgeeiENSMUSG00000020125
CleanExiMM_ELA2
GenevisibleiQ3UP87 MM

Interactioni

Subunit structurei

Interacts with NOTCH2NL.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi206058, 1 interactor
STRINGi10090.ENSMUSP00000038925

Chemistry databases

BindingDBiQ3UP87

Structurei

3D structure databases

ProteinModelPortaliQ3UP87
SMRiQ3UP87
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 247Peptidase S1PROSITE-ProRule annotationAdd BLAST219

Sequence similaritiesi

Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627 Eukaryota
COG5640 LUCA
GeneTreeiENSGT00910000144219
HOGENOMiHOG000251820
HOVERGENiHBG013304
InParanoidiQ3UP87
KOiK01327
OMAiNWINSII
OrthoDBiEOG091G0DF7
PhylomeDBiQ3UP87
TreeFamiTF335284

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
InterProiView protein in InterPro
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3UP87-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALGRLSSRT LAAMLLALFL GGPALASEIV GGRPARPHAW PFMASLQRRG
60 70 80 90 100
GHFCGATLIA RNFVMSAAHC VNGLNFRSVQ VVLGAHDLRR QERTRQTFSV
110 120 130 140 150
QRIFENGFDP SQLLNDIVII QLNGSATINA NVQVAQLPAQ GQGVGDRTPC
160 170 180 190 200
LAMGWGRLGT NRPSPSVLQE LNVTVVTNMC RRRVNVCTLV PRRQAGICFG
210 220 230 240 250
DSGGPLVCNN LVQGIDSFIR GGCGSGLYPD AFAPVAEFAD WINSIIRSHN
260
DHLLTHPKDR EGRTN
Length:265
Mass (Da):28,648
Last modified:October 11, 2005 - v1
Checksum:i666029A299275EB6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26A → P in AAB60670 (PubMed:8035830).Curated1
Sequence conflicti68A → V in AAB60670 (PubMed:8035830).Curated1
Sequence conflicti102R → G in AAB60670 (PubMed:8035830).Curated1
Sequence conflicti181R → P in AAB60670 (PubMed:8035830).Curated1
Sequence conflicti236A → G in AAB60670 (PubMed:8035830).Curated1
Sequence conflicti239A → V in AAB60670 (PubMed:8035830).Curated1
Sequence conflicti248S → R in AAB60670 (PubMed:8035830).Curated1
Sequence conflicti261E → R in AAB60670 (PubMed:8035830).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04962, U06076 Genomic DNA Translation: AAB60670.1
AK143710 mRNA Translation: BAE25510.1
BC145800 mRNA Translation: AAI45801.1
CCDSiCCDS23994.1
PIRiI48679
RefSeqiNP_056594.2, NM_015779.2
UniGeneiMm.262194

Genome annotation databases

EnsembliENSMUST00000046091; ENSMUSP00000038925; ENSMUSG00000020125
GeneIDi50701
KEGGimmu:50701
UCSCiuc007gai.1 mouse

Similar proteinsi

Entry informationi

Entry nameiELNE_MOUSE
AccessioniPrimary (citable) accession number: Q3UP87
Secondary accession number(s): A6H698, Q61515
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 11, 2005
Last modified: June 20, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health