P46075 (ELM_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Extracellular metalloproteinase mep
EC=3.4.24.-

Alternative name(s):
Elastinolytic metalloproteinase mep
Fungalysin mep

Gene names

Name:	mep
ORF Names:	AFUA_8G07080

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Neosartorya fumigata

Protein attributes

Sequence length	634 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor By similarity. Catalyzes the hydrolysis of elastin.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Secreted By similarity.
Induction	Expression is controlled by the prtT transcription factor. Ref.6 Ref.7
Sequence similarities	Belongs to the peptidase M36 family.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular space Inferred from electronic annotation. Source: InterPro
Molecular_function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Propeptide	19 – 245	227			PRO_0000029243
	Chain	246 – 634	389	Extracellular metalloproteinase mep		PRO_0000029244
Sites
	Active site	430	1	By similarity
	Metal binding	429	1	Zinc; catalytic By similarity
	Metal binding	433	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	286	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	137	1	Q → K in strain: Isolate 13.
	Natural variant	197	1	A → P in strain: Isolate 13.
	Natural variant	419	1	D → N in strain: Isolate 13.
	Natural variant	448 – 450	3	CLN → SLY in strain: Isolate 13.
	Natural variant	482	1	T → A in strain: Isolate 13.
	Natural variant	529	1	M → I in strain: Isolate 13.
	Natural variant	573	1	L → F in strain: Isolate 13.
	Natural variant	578	1	P → A in strain: Isolate 13.
Experimental info
	Sequence conflict	305	1	S → P in CAA83015. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P46075 [UniParc]. Last modified January 10, 2006. Version 3. Checksum: B9F9A8D83E1FEBBF	FASTA	634	68,708
	10 20 30 40 50 60 MRGLLLAGAL ALPASVFAHP AHQSYGLNRR TVDLNAFRLK SLAKYVNATE TVIEAPSSFA 70 80 90 100 110 120 PFKPQSYVEV ATQHVKMIAP DATFRVVDDH YVGDNGVAHV HFRQTANGLD IDNADFNVNV 130 140 150 160 170 180 GKDGKVFSYG NSFYTGQIPS SAALTKRDFS DPVTALKGTT NTLQLPITVD SASSESTEEK 190 200 210 220 230 240 ESYVFKGVSG TVSDPKAKLV YFVKDDGTLA LAWRVETDID SNWLLTYIDA KSGEEIHGVV 250 260 270 280 290 300 DYVAEADYQV YAWGINDPTE GERTVIKDPW DSVASEFTWI SDGSTNYTTS RGNNGIAQSN 310 320 330 340 350 360 PSGGSSYLNN YRPSSSSLSF KYPYSVSSSP PSSYIDASII QLFYTANIYH DLLYTLGFTE 370 380 390 400 410 420 KAGNFEYNTN GQGGLGNDYV ILNAQDGSGT NNANFATPPD GQPGRMRMYV WTESTPYRDG 430 440 450 460 470 480 SFEAGIVIHE YTHGLSNRLT GGPANSNCLN ALESGGMGEG WSDFMATAIR LKPGDKRSTD 490 500 510 520 530 540 YTMGEWASNR AGGIRQYPYS TSLSTNPLTY TSVNSLNAVH AIGTVWASML YEVLWNLIDK 550 560 570 580 590 600 HGKNDAPKPT LRDGVPTDGK YLAMKLVMDG MALQPCNPNF VQARDAILDA DTALTGGENQ 610 620 630 CEIWTAFAKR GLGAGAKYSS RNRVGSTEVP SGVC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z30424 Genomic DNA. Translation: CAA83015.1. L29566 Genomic DNA. Translation: AAB07708.1. AAHF01000013 Genomic DNA. Translation: EAL85468.1.
PIR	S61435.
RefSeq	XP_747506.1. XM_742413.1.
3D structure databases
ProteinModelPortal	P46075.
ModBase	Search...
Protein family/group databases
Allergome	3123. Asp f 5.0101. 75. Asp f 5.
MEROPS	M36.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00003091; CADAFUAP00003091; CADAFUAG00003091.
GeneID	3504960.
KEGG	afm:AFUA_8G07080.
Phylogenomic databases
eggNOG	NOG78576.
HOGENOM	HOG000159216.
KO	K01417.
OMA	GNFQVNN.
OrthoDB	EOG41CB4D.
Family and domain databases
InterPro	IPR011096. FTP_domain. IPR001842. Peptidase_M36. [Graphical view]
Pfam	PF07504. FTP. 1 hit. PF02128. Peptidase_M36. 1 hit. [Graphical view]
PRINTS	PR00999. FUNGALYSIN.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ELM_ASPFU

Accession

Primary (citable) accession number: P46075
Secondary accession number(s): P46074, Q4WBR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 10, 2006
Last modified:	May 1, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program