Skip Header

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

Q3UP87

- ELNE_MOUSE

UniProt

Q3UP87 - ELNE_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Neutrophil elastase

Gene

Elane

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. heparin binding Source: Ensembl
  2. RNA polymerase II transcription corepressor activity Source: Ensembl
  3. 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
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: Ensembl
  2. cytoplasm Source: MGI
  3. extracellular vesicular exosome Source: Ensembl
  4. secretory granule Source: Ensembl
  5. transcriptional repressor complex Source: Ensembl
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.
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

        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 .
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 ENSGT00760000118895.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi Q3UP87.
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

« 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: October 29, 2014
This is version 80 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