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Protein

Neutrophil elastase

Gene

Elane

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Charge relay systemBy similarity
Active sitei116 – 1161Charge relay systemBy similarity
Active sitei202 – 2021Charge relay systemBy similarity

GO - Molecular functioni

  1. cytokine binding Source: MGI
  2. endopeptidase activity Source: MGI
  3. heparin binding Source: MGI
  4. peptidase activity Source: MGI
  5. protease binding Source: MGI
  6. RNA polymerase II transcription corepressor activity Source: MGI
  7. serine-type endopeptidase activity Source: MGI

GO - Biological processi

  1. acute inflammatory response to antigenic stimulus Source: MGI
  2. defense response to bacterium Source: MGI
  3. defense response to fungus Source: MGI
  4. leukocyte migration Source: MGI
  5. negative regulation of chemokine biosynthetic process Source: MGI
  6. negative regulation of growth of symbiont in host Source: MGI
  7. negative regulation of interleukin-8 biosynthetic process Source: MGI
  8. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  9. neutrophil mediated killing of fungus Source: MGI
  10. phagocytosis Source: MGI
  11. positive regulation of immune response Source: MGI
  12. positive regulation of interleukin-8 biosynthetic process Source: MGI
  13. positive regulation of smooth muscle cell proliferation Source: MGI
  14. proteolysis Source: MGI
  15. response to lipopolysaccharide Source: MGI
  16. response to UV Source: MGI
  17. response to yeast Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:2679229. Elane.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: MGI
  2. cytoplasm Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. secretory granule Source: MGI
  5. transcriptional repressor complex Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 265239Neutrophil elastasePRO_0000228686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 70PROSITE-ProRule annotation
Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi150 ↔ 208PROSITE-ProRule annotation
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi180 ↔ 187PROSITE-ProRule annotation
Disulfide bondi198 ↔ 223PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ3UP87.

Expressioni

Gene expression databases

BgeeiQ3UP87.
CleanExiMM_ELA2.
GenevestigatoriQ3UP87.

Interactioni

Subunit structurei

Interacts with NOTCH2NL.By similarity

Protein-protein interaction databases

BioGridi206058. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ3UP87.
SMRiQ3UP87. Positions 29-247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 247219Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiQ3UP87.
KOiK01327.
OMAiAQFANWI.
OrthoDBiEOG7MKW6Q.
PhylomeDBiQ3UP87.
TreeFamiTF335284.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261A → P in AAB60670. (PubMed:8035830)Curated
Sequence conflicti68 – 681A → V in AAB60670. (PubMed:8035830)Curated
Sequence conflicti102 – 1021R → G in AAB60670. (PubMed:8035830)Curated
Sequence conflicti181 – 1811R → P in AAB60670. (PubMed:8035830)Curated
Sequence conflicti236 – 2361A → G in AAB60670. (PubMed:8035830)Curated
Sequence conflicti239 – 2391A → V in AAB60670. (PubMed:8035830)Curated
Sequence conflicti248 – 2481S → R in AAB60670. (PubMed:8035830)Curated
Sequence conflicti261 – 2611E → R in AAB60670. (PubMed:8035830)Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ3UP87.
SMRiQ3UP87. Positions 29-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206058. 1 interaction.

Chemistry

BindingDBiQ3UP87.
ChEMBLiCHEMBL5156.

Protein family/group databases

MEROPSiS01.131.

Proteomic databases

PRIDEiQ3UP87.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1991.
MGIiMGI:2679229. Elane.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiQ3UP87.
KOiK01327.
OMAiAQFANWI.
OrthoDBiEOG7MKW6Q.
PhylomeDBiQ3UP87.
TreeFamiTF335284.

Enzyme and pathway databases

ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

NextBioi307549.
PROiQ3UP87.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UP87.
CleanExiMM_ELA2.
GenevestigatoriQ3UP87.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiELNE_MOUSE
AccessioniPrimary (citable) accession number: Q3UP87
Secondary accession number(s): A6H698, Q61515
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 11, 2005
Last modified: February 4, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.