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Protein

Extracellular metalloproteinase mep

Gene

mep

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor (By similarity). Catalyzes the hydrolysis of elastin.By similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi429 – 4291Zinc; catalyticPROSITE-ProRule annotation
Active sitei430 – 4301PROSITE-ProRule annotation
Metal bindingi433 – 4331Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM36.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular metalloproteinase mep (EC:3.4.24.-)
Alternative name(s):
Elastinolytic metalloproteinase mep
Fungalysin mep
Gene namesi
Name:mep
ORF Names:AFUA_8G07080
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiFungiDB:Afu8g07080.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei3123. Asp f 5.0101.
75. Asp f 5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 2452271 PublicationPRO_0000029243Add
BLAST
Chaini246 – 634389Extracellular metalloproteinase mepPRO_0000029244Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Zymogen

Expressioni

Inductioni

Expression is controlled by the prtT transcription factor.2 Publications

Structurei

Secondary structure

1
634
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 374Combined sources
Beta strandi44 – 463Combined sources
Helixi48 – 547Combined sources
Helixi67 – 7812Combined sources
Beta strandi83 – 864Combined sources
Beta strandi98 – 1069Combined sources
Beta strandi109 – 12012Combined sources
Beta strandi124 – 1318Combined sources
Helixi142 – 1454Combined sources
Helixi152 – 16312Combined sources
Beta strandi168 – 1758Combined sources
Beta strandi182 – 1909Combined sources
Beta strandi196 – 2038Combined sources
Beta strandi209 – 21810Combined sources
Beta strandi223 – 2319Combined sources
Helixi232 – 2343Combined sources
Beta strandi236 – 2449Combined sources
Beta strandi247 – 2504Combined sources
Helixi258 – 2603Combined sources
Beta strandi264 – 2674Combined sources
Turni272 – 2776Combined sources
Beta strandi288 – 29912Combined sources
Helixi331 – 3344Combined sources
Helixi335 – 35521Combined sources
Turni360 – 3634Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi380 – 3845Combined sources
Beta strandi393 – 3964Combined sources
Beta strandi404 – 4085Combined sources
Beta strandi413 – 4164Combined sources
Helixi420 – 4223Combined sources
Helixi424 – 43916Combined sources
Helixi452 – 47019Combined sources
Helixi485 – 4884Combined sources
Beta strandi494 – 4974Combined sources
Turni503 – 5053Combined sources
Helixi510 – 5156Combined sources
Helixi519 – 54123Combined sources
Beta strandi546 – 5483Combined sources
Beta strandi555 – 5584Combined sources
Helixi559 – 57315Combined sources
Helixi580 – 59516Combined sources
Helixi600 – 60910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4K90X-ray1.80A246-634[»]
B31-245[»]
ProteinModelPortaliP46075.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M36 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000159216.
InParanoidiP46075.
KOiK01417.
OMAiEEAGNFQ.
OrthoDBiEOG7RV9QR.

Family and domain databases

InterProiIPR011096. FTP_domain.
IPR001842. Peptidase_M36.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF02128. Peptidase_M36. 1 hit.
[Graphical view]
PRINTSiPR00999. FUNGALYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P46075-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGLLLAGAL ALPASVFAHP AHQSYGLNRR TVDLNAFRLK SLAKYVNATE
60 70 80 90 100
TVIEAPSSFA PFKPQSYVEV ATQHVKMIAP DATFRVVDDH YVGDNGVAHV
110 120 130 140 150
HFRQTANGLD IDNADFNVNV GKDGKVFSYG NSFYTGQIPS SAALTKRDFS
160 170 180 190 200
DPVTALKGTT NTLQLPITVD SASSESTEEK ESYVFKGVSG TVSDPKAKLV
210 220 230 240 250
YFVKDDGTLA LAWRVETDID SNWLLTYIDA KSGEEIHGVV DYVAEADYQV
260 270 280 290 300
YAWGINDPTE GERTVIKDPW DSVASEFTWI SDGSTNYTTS RGNNGIAQSN
310 320 330 340 350
PSGGSSYLNN YRPSSSSLSF KYPYSVSSSP PSSYIDASII QLFYTANIYH
360 370 380 390 400
DLLYTLGFTE KAGNFEYNTN GQGGLGNDYV ILNAQDGSGT NNANFATPPD
410 420 430 440 450
GQPGRMRMYV WTESTPYRDG SFEAGIVIHE YTHGLSNRLT GGPANSNCLN
460 470 480 490 500
ALESGGMGEG WSDFMATAIR LKPGDKRSTD YTMGEWASNR AGGIRQYPYS
510 520 530 540 550
TSLSTNPLTY TSVNSLNAVH AIGTVWASML YEVLWNLIDK HGKNDAPKPT
560 570 580 590 600
LRDGVPTDGK YLAMKLVMDG MALQPCNPNF VQARDAILDA DTALTGGENQ
610 620 630
CEIWTAFAKR GLGAGAKYSS RNRVGSTEVP SGVC
Length:634
Mass (Da):68,708
Last modified:January 10, 2006 - v3
Checksum:iB9F9A8D83E1FEBBF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti305 – 3051S → P in CAA83015 (PubMed:7715453).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371Q → K in strain: Isolate 13.
Natural varianti197 – 1971A → P in strain: Isolate 13.
Natural varianti419 – 4191D → N in strain: Isolate 13.
Natural varianti448 – 4503CLN → SLY in strain: Isolate 13.
Natural varianti482 – 4821T → A in strain: Isolate 13.
Natural varianti529 – 5291M → I in strain: Isolate 13.
Natural varianti573 – 5731L → F in strain: Isolate 13.
Natural varianti578 – 5781P → A in strain: Isolate 13.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30424 Genomic DNA. Translation: CAA83015.1.
L29566 Genomic DNA. Translation: AAB07708.1.
AAHF01000013 Genomic DNA. Translation: EAL85468.1.
PIRiS61435.
RefSeqiXP_747506.1. XM_742413.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00003091; CADAFUAP00003091; CADAFUAG00003091.
GeneIDi3504960.
KEGGiafm:AFUA_8G07080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30424 Genomic DNA. Translation: CAA83015.1.
L29566 Genomic DNA. Translation: AAB07708.1.
AAHF01000013 Genomic DNA. Translation: EAL85468.1.
PIRiS61435.
RefSeqiXP_747506.1. XM_742413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4K90X-ray1.80A246-634[»]
B31-245[»]
ProteinModelPortaliP46075.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3123. Asp f 5.0101.
75. Asp f 5.
MEROPSiM36.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00003091; CADAFUAP00003091; CADAFUAG00003091.
GeneIDi3504960.
KEGGiafm:AFUA_8G07080.

Organism-specific databases

EuPathDBiFungiDB:Afu8g07080.

Phylogenomic databases

HOGENOMiHOG000159216.
InParanoidiP46075.
KOiK01417.
OMAiEEAGNFQ.
OrthoDBiEOG7RV9QR.

Family and domain databases

InterProiIPR011096. FTP_domain.
IPR001842. Peptidase_M36.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF02128. Peptidase_M36. 1 hit.
[Graphical view]
PRINTSiPR00999. FUNGALYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and disruption of the gene encoding an extracellular metalloprotease of Aspergillus fumigatus."
    Jaton-Ogay K., Paris S., Huerre M., Quadroni M., Falchetto R., Togni G., Latge J.-P., Monod M.
    Mol. Microbiol. 14:917-928(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Delta18.
  2. Sanglard D.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Molecular cloning and sequencing of the cDNA and gene for a novel elastinolytic metalloproteinase from Aspergillus fumigatus and its expression in Escherichia coli."
    Sirakova T.D., Markaryan A., Kolattukudy P.E.
    Infect. Immun. 62:4208-4218(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 530-542.
    Strain: Isolate 13.
  4. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
  5. "Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung."
    Markaryan A., Morozova I., Yu H., Kolattukudy P.E.
    Infect. Immun. 62:2149-2157(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 246-258.
  6. "A regulator of Aspergillus fumigatus extracellular proteolytic activity is dispensable for virulence."
    Bergmann A., Hartmann T., Cairns T., Bignell E.M., Krappmann S.
    Infect. Immun. 77:4041-4050(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "Transcription factor PrtT controls expression of multiple secreted proteases in the human pathogenic mold Aspergillus fumigatus."
    Sharon H., Hagag S., Osherov N.
    Infect. Immun. 77:4051-4060(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiELM_ASPFU
AccessioniPrimary (citable) accession number: P46075
Secondary accession number(s): P46074, Q4WBR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 10, 2006
Last modified: December 9, 2015
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.