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Protein

Alkaline protease 1

Gene

alp1

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 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.3 Publications

Catalytic activityi

Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.

pH dependencei

Optimum pH is 7-8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621Charge relay systemBy similarity
Active sitei193 – 1931Charge relay systemBy similarity
Active sitei349 – 3491Charge relay systemBy similarity

GO - Molecular functioni

  • fibrinogen binding Source: ASPGD
  • IgE binding Source: UniProtKB
  • peptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: InterPro
  • serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  • active evasion of host immune response via regulation of host complement system Source: UniProtKB
  • complement activation Source: ASPGD
  • elastin catabolic process Source: ASPGD
  • pathogenesis Source: UniProtKB
  • protein catabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

Protein family/group databases

MEROPSiS08.053.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline protease 1 (EC:3.4.21.63)
Short name:
ALP
Alternative name(s):
Aspergillopeptidase B
Aspergillus proteinase B
Elastase
Elastinolytic serine proteinase
Oryzin
Allergen: Asp f 13
Gene namesi
Name:alp1
Synonyms:alk1, alp
ORF Names:AFUA_4G11800
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiFungiDB:Afu4g11800.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Binds to IgE via three immunodominant epitopes localized at the C-terminal part.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3111. Asp f 13.0101.
66. Asp f 13.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121By similarityAdd
BLAST
Propeptidei22 – 101801 PublicationPRO_0000027082Add
BLAST
Chaini102 – 403302Alkaline protease 1PRO_0000027083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence analysis
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Zymogen

Expressioni

Inductioni

Expression is controlled by the prtT transcription factor.2 Publications

Interactioni

GO - Molecular functioni

  • fibrinogen binding Source: ASPGD
  • IgE binding Source: UniProtKB

Structurei

3D structure databases

ProteinModelPortaliP28296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 384226Peptidase S8Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000199176.
InParanoidiP28296.
KOiK18549.
OMAiIESHTLW.
OrthoDBiEOG7WT4B5.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
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. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P28296-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSIKRTLLL LGAVLPAVFG APVQETRRAA QKIPGKYIVT FKPGTDTATI
60 70 80 90 100
ESHTLWATDL HKRNLERRDT TSGEPPVGIE KSYKIKDFAA YAGSFDDATI
110 120 130 140 150
EEIRKSADVA HVEEDQIWYL DALTTQKGAP WGLGSISHKG QASTDYIYDT
160 170 180 190 200
SAGAGTYAYV VDSGINVNHV EFESRASLAY NAAGGSHVDS IGHGTHVAGT
210 220 230 240 250
IGGKTYGVAK KTNLLSVKVF QGESSSTSII LDGFNWAVND IVSKGRTKKA
260 270 280 290 300
AINMSLGGGY SYAFNNAVEN AFDEGVLSVV AAGNENSDAS NTSPASAPNA
310 320 330 340 350
LTVAAINKSN ARASFSNYGS VVDIFAPGQD ILSAWIGSTT ATNTISGTSM
360 370 380 390 400
ATPHIVGLSV YLMGLENLSG PAAVTARIKE LATNGVVTNV KGSPNKLAYN

GNA
Length:403
Mass (Da):42,190
Last modified:December 6, 2005 - v2
Checksum:i2D900D1AE22CDD4A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1072SA → RG in CAA77666 (PubMed:1601287).Curated
Sequence conflicti295 – 2951A → R in AAB07672 (PubMed:8500876).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11580 Genomic DNA. Translation: CAA77666.1.
M99420 Genomic DNA. Translation: AAB07672.1.
AAHF01000005 Genomic DNA. Translation: EAL89613.1.
PIRiS22184.
RefSeqiXP_751651.1. XM_746558.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00008008; CADAFUAP00008008; CADAFUAG00008008.
GeneIDi3509271.
KEGGiafm:AFUA_4G11800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11580 Genomic DNA. Translation: CAA77666.1.
M99420 Genomic DNA. Translation: AAB07672.1.
AAHF01000005 Genomic DNA. Translation: EAL89613.1.
PIRiS22184.
RefSeqiXP_751651.1. XM_746558.1.

3D structure databases

ProteinModelPortaliP28296.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3111. Asp f 13.0101.
66. Asp f 13.
MEROPSiS08.053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00008008; CADAFUAP00008008; CADAFUAG00008008.
GeneIDi3509271.
KEGGiafm:AFUA_4G11800.

Organism-specific databases

EuPathDBiFungiDB:Afu4g11800.

Phylogenomic databases

HOGENOMiHOG000199176.
InParanoidiP28296.
KOiK18549.
OMAiIESHTLW.
OrthoDBiEOG7WT4B5.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
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. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.

Entry informationi

Entry nameiORYZ_ASPFU
AccessioniPrimary (citable) accession number: P28296
Secondary accession number(s): Q4WQ71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 6, 2005
Last modified: November 11, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.