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Q3UP87

- ELNE_MOUSE

UniProt

Q3UP87 - ELNE_MOUSE

Protein

Neutrophil elastase

Gene

Elane

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
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    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. heparin binding Source: Ensembl
    2. serine-type endopeptidase activity Source: MGI

    GO - Biological processi

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

    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: Ensembl
    2. cytoplasm Source: MGI
    3. secretory granule Source: Ensembl

    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.
    GeneTreeiENSGT00700000104045.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiA6H698.
    KOiK01327.
    OMAiLRGGHFC.
    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

    MALGRLSSRT LAAMLLALFL GGPALASEIV GGRPARPHAW PFMASLQRRG    50
    GHFCGATLIA RNFVMSAAHC VNGLNFRSVQ VVLGAHDLRR QERTRQTFSV 100
    QRIFENGFDP SQLLNDIVII QLNGSATINA NVQVAQLPAQ GQGVGDRTPC 150
    LAMGWGRLGT NRPSPSVLQE LNVTVVTNMC RRRVNVCTLV PRRQAGICFG 200
    DSGGPLVCNN LVQGIDSFIR GGCGSGLYPD AFAPVAEFAD WINSIIRSHN 250
    DHLLTHPKDR EGRTN 265
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04962 , U06076 Genomic DNA. Translation: AAB60670.1 .
    AK143710 mRNA. Translation: BAE25510.1 .
    BC145800 mRNA. Translation: AAI45801.1 .
    CCDSi CCDS23994.1.
    PIRi I48679.
    RefSeqi NP_056594.2. NM_015779.2.
    UniGenei Mm.262194.

    3D structure databases

    ProteinModelPortali Q3UP87.
    SMRi Q3UP87. Positions 29-247.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206058. 1 interaction.

    Chemistry

    BindingDBi Q3UP87.
    ChEMBLi CHEMBL5156.

    Protein family/group databases

    MEROPSi S01.131.

    Proteomic databases

    PRIDEi Q3UP87.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000046091 ; ENSMUSP00000038925 ; ENSMUSG00000020125 .
    GeneIDi 50701.
    KEGGi mmu:50701.
    UCSCi uc007gai.1. mouse.

    Organism-specific databases

    CTDi 1991.
    MGIi MGI:2679229. Elane.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00700000104045.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    InParanoidi A6H698.
    KOi K01327.
    OMAi LRGGHFC.
    OrthoDBi EOG7MKW6Q.
    PhylomeDBi Q3UP87.
    TreeFami TF335284.

    Enzyme and pathway databases

    Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    NextBioi 307549.
    PROi Q3UP87.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3UP87.
    CleanExi MM_ELA2.
    Genevestigatori Q3UP87.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 79 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