O42630 (CARP_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar protease A
EC=3.4.23.25

Alternative name(s):
Aspartic endopeptidase pep2
Aspartic protease pep2

Gene names

Name:	pep2
ORF Names:	AFUA_3G11400

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

General annotation (Comments)

Function	Vacuolar aspartic endopeptidase which is probably also secreted and contributes to virulence. Ref.1
Catalytic activity	Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.
Subcellular location	Vacuole lumen. Secreted Probable Ref.1.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Secreted Vacuole
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome 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 region Inferred from electronic annotation. Source: UniProtKB-SubCell vacuolar lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18
	Propeptide	19 – 70	52	Activation peptide		PRO_5000147257
	Chain	71 – 398	328	Vacuolar protease A		PRO_5000147258
Sites
	Active site	103	1	By similarity
	Active site	287	1	By similarity
Amino acid modifications
	Glycosylation	138	1	N-linked (GlcNAc...) Potential
	Glycosylation	338	1	N-linked (GlcNAc...) Potential
	Disulfide bond	116 ↔ 121		By similarity
	Disulfide bond	321 ↔ 354		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O42630 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 52741DFEDBEEAF3B	FASTA	398	43,355
	10 20 30 40 50 60 MKSTSLLTAS VLLGSASAAV HKLKLNKVPL DEQLYTHNID AHVRALGQKY MGIRPNVHQE 70 80 90 100 110 120 LLEENSLNDM SRHDVLVDNF LNAQYFSEIS LGTPPQKFKV VLDTGSSNLW VPGSDCSSIA 130 140 150 160 170 180 CFLHNKYDSS ASSTYKANGT EFAIKYGSGE LSGFVSQDTL QIGDLKVVKQ DFAEATNEPG 190 200 210 220 230 240 LAFAFGRFDG ILGLGYDTIS VNKIVPPFYN MLDQGLLDEP VFAFYLGDTN KEGDNSEASF 250 260 270 280 290 300 GGVDKNHYTG ELTKIPLRRK AYWEVDFDAI ALGDNVAELE NTGIILDTGT SLIALPSTLA 310 320 330 340 350 360 DLLNKEIGAK KGFTGQYSIE CDKRDSLPDL TFTLAGHNFT IGPYDYTLEV QGSCISSFMG 370 380 390 MDFPEPVGPL AILGDAFLRK WYSVYDLGNN AVGLAKAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and targeted deletion of PEP2 which encodes a novel aspartic proteinase from Aspergillus fumigatus." Reichard U., Cole G.T., Ruechel R., Monod M. Int. J. Med. Microbiol. 290:85-96(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, FUNCTION. Strain: D141.
[2]	"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.
[3]	"Genes and molecules involved in Aspergillus fumigatus virulence." Rementeria A., Lopez-Molina N., Ludwig A., Vivanco A.B., Bikandi J., Ponton J., Garaizar J. Rev. Iberoam. Micol. 22:1-23(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VIRULENCE FACTOR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ132504 Genomic DNA. Translation: CAA10674.1. Y15744 mRNA. Translation: CAA75754.1. AAHF01000002 Genomic DNA. Translation: EAL92441.1.
RefSeq	XP_754479.1. XM_749386.1.
3D structure databases
HSSP	HSSP built from PDB template 1FMU based on UniProtKB P07267.
ProteinModelPortal	O42630.
SMR	O42630. Positions 73-397.
ModBase	Search...
Protein-protein interaction databases
STRING	5085.CADAFUAP00005075.
Protein family/group databases
MEROPS	A01.018.
Proteomic databases
PRIDE	O42630.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00005075; CADAFUAP00005075; CADAFUAG00005075.
GeneID	3512540.
KEGG	afm:AFUA_3G11400.
Phylogenomic databases
eggNOG	NOG248684.
HOGENOM	HOG000197681.
KO	K01381.
OMA	SGAMEGY.
OrthoDB	EOG4PVS7C.
Family and domain databases
Gene3D	2.40.70.10. 2 hits.
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. [Graphical view]
PANTHER	PTHR13683. PTHR13683. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
SUPFAM	SSF50630. Pept_Aspartic. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARP_ASPFU

Accession

Primary (citable) accession number: O42630
Secondary accession number(s): Q4WY12

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 3, 2009
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program