Alkaline protease 1 precursor - Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)

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P28296 (ORYZ_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alkaline protease 1
Short name=ALP
EC=3.4.21.63

Alternative name(s):
Aspergillopeptidase B
Aspergillus proteinase B
Elastase
Elastinolytic serine proteinase
Oryzin
Allergen=Asp f 13

Gene names

Name:	alp1
Synonyms:	alk1, alp
ORF Names:	AFUA_4G11800

Organism

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

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	403 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 alkaline protease that allows assimilation of proteinaceous substrates. Acts as a significant virulence factor in invasive aspergillosis. Involved in immune evasion from the human and mice complement systems during infection. Efficiently cleaves important components of the complement cascade such as such as C3, C4, C5, and C1q, as well as IgG, which leads to down-regulation of complement activation at the hyphal surface. Ref.2 Ref.7 Ref.8
Catalytic activity	Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.
Subcellular location	Secreted Ref.2 Ref.4 Ref.7 Ref.8.
Induction	Expression is controlled by the prtT transcription factor. Ref.5 Ref.6
Allergenic properties	Causes an allergic reaction in human. Binds to IgE via three immunodominant epitopes localized at the C-terminal part.
Sequence similarities	Belongs to the peptidase S8 family. Contains 1 peptidase S8 domain.
Biophysicochemical properties	pH dependence: Optimum pH is 7-8. Ref.2

Ontologies

Keywords
Biological process	Virulence
Cellular component	Secreted
Disease	Allergen
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	active evasion of host immune response via regulation of host complement system Inferred from direct assay Ref.8. Source: UniProtKB negative regulation of catalytic activity Inferred from electronic annotation. Source: InterPro pathogenesis Inferred from direct assay Ref.8. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from direct assay Ref.4 Ref.7. Source: UniProtKB
Molecular function	IgE binding Inferred from direct assay Ref.4. Source: UniProtKB identical protein binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity 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 – 21

By similarity

Propeptide

22 – 101

PRO_0000027082

Chain

102 – 403

302

Alkaline protease 1

PRO_0000027083

Sites

Active site

162

Charge relay system By similarity

Active site

193

Charge relay system By similarity

Active site

349

Charge relay system By similarity

Amino acid modifications

Glycosylation

253

N-linked (GlcNAc...) Potential

Glycosylation

307

N-linked (GlcNAc...) Potential

Glycosylation

367

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

106 – 107

SA → RG in CAA77666. Ref.1

Sequence conflict

295

A → R in AAB07672. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P28296 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 2D900D1AE22CDD4A
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FASTA

403

42,190

        10         20         30         40         50         60 
MLSIKRTLLL LGAVLPAVFG APVQETRRAA QKIPGKYIVT FKPGTDTATI ESHTLWATDL 

        70         80         90        100        110        120 
HKRNLERRDT TSGEPPVGIE KSYKIKDFAA YAGSFDDATI EEIRKSADVA HVEEDQIWYL 

       130        140        150        160        170        180 
DALTTQKGAP WGLGSISHKG QASTDYIYDT SAGAGTYAYV VDSGINVNHV EFESRASLAY 

       190        200        210        220        230        240 
NAAGGSHVDS IGHGTHVAGT IGGKTYGVAK KTNLLSVKVF QGESSSTSII LDGFNWAVND 

       250        260        270        280        290        300 
IVSKGRTKKA AINMSLGGGY SYAFNNAVEN AFDEGVLSVV AAGNENSDAS NTSPASAPNA 

       310        320        330        340        350        360 
LTVAAINKSN ARASFSNYGS VVDIFAPGQD ILSAWIGSTT ATNTISGTSM ATPHIVGLSV 

       370        380        390        400 
YLMGLENLSG PAAVTARIKE LATNGVVTNV KGSPNKLAYN GNA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatus." Jaton-Ogay K., Suter M., Crameri R., Falchetto R., Fatih A., Monod M. FEMS Microbiol. Lett. 71:163-168(1992) [PubMed: 1601287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Evidence for possible involvement of an elastolytic serine protease in aspergillosis." Kolattukudy P.E., Lee J.D., Rogers L.M., Zimmerman P., Ceselski S., Fox B., Stein B., Copelan E.A. Infect. Immun. 61:2357-2368(1993) [PubMed: 8500876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 126-158, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[3]	"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. Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[4]	"Identification and expression of an allergen Asp f 13 from Aspergillus fumigatus and epitope mapping using human IgE antibodies and rabbit polyclonal antibodies." Chow L.P., Liu S.L., Yu C.J., Liao H.K., Tsai J.J., Tang T.K. Biochem. J. 346:423-431(2000) [PubMed: 10677362] [Abstract] Cited for: PROTEIN SEQUENCE OF 102-112, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, IGE-BINDING.
[5]	"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: 19564390] [Abstract] Cited for: INDUCTION.
[6]	"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: 19564385] [Abstract] Cited for: INDUCTION.
[7]	"Secreted Aspergillus fumigatus protease Alp1 degrades human complement proteins C3, C4, and C5." Behnsen J., Lessing F., Schindler S., Wartenberg D., Jacobsen I.D., Thoen M., Zipfel P.F., Brakhage A.A. Infect. Immun. 78:3585-3594(2010) [PubMed: 20498262] [Abstract] Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY, FUNCTION.
[8]	"Secretion of a fungal protease represents a complement evasion mechanism in cerebral aspergillosis." Rambach G., Dum D., Mohsenipour I., Hagleitner M., Wurzner R., Lass-Florl C., Speth C. Mol. Immunol. 47:1438-1449(2010) [PubMed: 20303595] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z11580 Genomic DNA. Translation: CAA77666.1. M99420 Genomic DNA. Translation: AAB07672.1. AAHF01000005 Genomic DNA. Translation: EAL89613.1.
PIR	S22184.
RefSeq	XP_751651.1. XM_746558.1.
3D structure databases
ProteinModelPortal	P28296.
ModBase	Search...
Protein family/group databases
Allergome	3111. Asp f 13.0101. 66. Asp f 13.
MEROPS	S08.053.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00008008; CADAFUAP00008008; CADAFUAG00008008.
GeneID	3509271.
GenomeReviews	Gene locus alp1 in contig CM000172_GR.
KEGG	afm:AFUA_4G11800.
Phylogenomic databases
GeneTree	EFGT00050000001578.
HOGENOM	HBG752219.
OMA	DILSAWI.
OrthoDB	EOG437VPD.
Family and domain databases
InterPro	IPR000209. Peptidase_S8/S53. IPR023827. Peptidase_S8_Asp-AS. IPR022398. Peptidase_S8_His-AS. IPR023828. Peptidase_S8_Ser-AS. IPR015500. Peptidase_S8_subtilisin-rel. IPR009020. Prot_inh_propept. IPR010259. Prot_inh_S8A. [Graphical view]
Gene3D	G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
PANTHER	PTHR10795. SubtilSerProt. 1 hit.
Pfam	PF05922. Inhibitor_I9. 1 hit. PF00082. Peptidase_S8. 1 hit. [Graphical view]
PRINTS	PR00723. SUBTILISIN.
SUPFAM	SSF52743. Pept_S8_S53. 1 hit. SSF54897. Prot_inh_propept. 1 hit.
PROSITE	PS00136. SUBTILASE_ASP. 1 hit. PS00137. SUBTILASE_HIS. 1 hit. PS00138. SUBTILASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ORYZ_ASPFU

Accession

Primary (citable) accession number: P28296
Secondary accession number(s): Q4WQ71

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 6, 2005
Last modified:	December 14, 2011
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents