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Protein

Neutral protease 2 homolog mep20

Gene

mep20

Organism
Neosartorya fumigata (Aspergillus fumigatus)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine. May be involved in virulence (By similarity).By similarity

Catalytic activityi

Preferential cleavage of bonds with hydrophobic residues in P1'; also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi299Zinc; catalyticPROSITE-ProRule annotation1
Active sitei300PROSITE-ProRule annotation1
Metal bindingi303Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi314Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processVirulence
LigandMetal-binding, Zinc

Protein family/group databases

MEROPSiM35.002

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral protease 2 homolog mep20 (EC:3.4.24.39)
Alternative name(s):
Deuterolysin mep20
Gene namesi
Name:mep20
OrganismiNeosartorya fumigata (Aspergillus fumigatus)
Taxonomic identifieri746128 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000040706420 – 172By similarityAdd BLAST153
ChainiPRO_0000407065173 – 365Neutral protease 2 homolog mep20Add BLAST193

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi73N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi178 ↔ 249By similarity
Disulfide bondi256 ↔ 274By similarity
Glycosylationi351N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ09016
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M35 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR024079 MetalloPept_cat_dom_sf
IPR001384 Peptidase_M35
PfamiView protein in Pfam
PF02102 Peptidase_M35, 1 hit
PRINTSiPR00768 DEUTEROLYSIN
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q09016-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTILASAI LALINGALAL PANTPTLDVT LTQVDNTRIK ATVKNTGNEK
60 70 80 90 100
VTFVHLNFFQ DAAPVKKVSL FRNGTEVEFT GIKRRLLTEG LSDDGLTTLA
110 120 130 140 150
PGGTFEDEFD VASTGDLTEG GTVTIRTDGF VPITTDRKVS GYIPYQSNEL
160 170 180 190 200
EIEVDPAKAA AVPQAIKLLD RRTKVASCSG SRASALSTAL RNAGSLANAA
210 220 230 240 250
ASAASSGSST RFQEYFKTTS RRPENVGGRF RAVGREASSQ SSGKTTYYCN
260 270 280 290 300
DPYGYCDSNT LAYTLPSSNL IANCDIYYSY LPALTSSCHA QDQATTTLHE
310 320 330 340 350
FTHAPAVYSP GTDDYAYGYR ASTALSASQA LLNADTYALF ANGSPLLPLS
360
NHSKCRNTMV WRTLL
Length:365
Mass (Da):39,031
Last modified:November 1, 1996 - v1
Checksum:i61495EA7CF94C345
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24146 Genomic DNA Translation: AAB07644.1
PIRiJC4379

Similar proteinsi

Entry informationi

Entry nameiMEP20_ASPFM
AccessioniPrimary (citable) accession number: Q09016
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 66 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health