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Protein

Alkaline protease 2

Gene

alp2

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Alkaline protease that allows assimilation of proteinaceous substrates. Acts as a significant virulence factor in invasive aspergillosis. Required for regular sporulation.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei182 – 1821Charge relay systemBy similarity
Active sitei214 – 2141Charge relay systemBy similarity
Active sitei380 – 3801Charge relay systemBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • asexual sporulation resulting in formation of a cellular spore Source: ASPGD
  • dibasic protein processing Source: EnsemblFungi
  • pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Sporulation, Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline protease 2 (EC:3.4.21.63)
Short name:
ALP2
Alternative name(s):
Autophagic serine protease alp2
Allergen: Asp f 18
Gene namesi
Name:alp2
ORF Names:AFUA_5G09210
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiFungiDB:Afu5g09210.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: ASPGD
Complete GO annotation...

Pathology & Biotechi

Allergenic propertiesi

Acts as a major allergen in patients suffering from extrinsic bronchial asthma. Binds to IgE.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3114. Asp f 18.0101.
70. Asp f 18.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Propeptidei17 – 1361201 PublicationPRO_0000412304Add
BLAST
Chaini137 – 495359Alkaline protease 2PRO_0000412305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence analysis
Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence analysis
Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Zymogen

Interactioni

GO - Molecular functioni

  • IgE binding Source: UniProtKB

Structurei

3D structure databases

ProteinModelPortaliP87184.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini166 – 432267Peptidase S8Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000199176.
InParanoidiP87184.
KOiK01336.
OMAiWIGSKHA.
OrthoDBiEOG7WT4B5.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
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.
PROSITEiPS00137. 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.

P87184-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGYLSLSIL PLLVAASPVV VDSIHNGAAP ILSSMNAKEV PDSYIVVFKK
60 70 80 90 100
HVNAESAAAH HSWVQDIHSA QNERVELRKR SLFGFGEEAY LGLKNTFDIA
110 120 130 140 150
GSLVGYSGHF HEDVIEQVRK HPDVEYIEKD SEVHTMEDPT VEKSAPWGLA
160 170 180 190 200
RISHRDSLSF GTFNKYLYAS EGGEGVDAYT IDTGINVDHV DFEGRAQWGK
210 220 230 240 250
TIPTDDEDAD GNGHGTHCSG TIAGRKYGVA KKANLYAVKV LRSSGSGTMS
260 270 280 290 300
DVVAGVEWAV KSHLKKVKDA KDGKIKGFKG SVANMSLGGG KSRTLEAAVN
310 320 330 340 350
AGVEAGLHFA VAAGNDNADA CNYSPAAAEN PITVGASTLQ DERAYFSNYG
360 370 380 390 400
KCTDIFAPGL NILSTWIGSK HAVNTISGTS MASPHIAGLL AYFVSLQPSK
410 420 430 440 450
DSAFAVDELT PKKLKKDIIA IATQGALTDI PSDTPNLLAW NGGGSSNYTD
460 470 480 490
IIASGGYKVN ASVKDRFEGL VHKAEKLLTE ELGAIYSEIH DAAVA
Length:495
Mass (Da):52,640
Last modified:July 1, 1997 - v1
Checksum:iA358FE8D6EE533D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13338 mRNA. Translation: CAA73782.1.
AJ243145 Genomic DNA. Translation: CAB45520.1.
AAHF01000003 Genomic DNA. Translation: EAL91680.1.
RefSeqiXP_753718.1. XM_748625.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00006386; CADAFUAP00006386; CADAFUAG00006386.
GeneIDi3510885.
KEGGiafm:AFUA_5G09210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13338 mRNA. Translation: CAA73782.1.
AJ243145 Genomic DNA. Translation: CAB45520.1.
AAHF01000003 Genomic DNA. Translation: EAL91680.1.
RefSeqiXP_753718.1. XM_748625.1.

3D structure databases

ProteinModelPortaliP87184.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3114. Asp f 18.0101.
70. Asp f 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00006386; CADAFUAP00006386; CADAFUAG00006386.
GeneIDi3510885.
KEGGiafm:AFUA_5G09210.

Organism-specific databases

EuPathDBiFungiDB:Afu5g09210.

Phylogenomic databases

HOGENOMiHOG000199176.
InParanoidiP87184.
KOiK01336.
OMAiWIGSKHA.
OrthoDBiEOG7WT4B5.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
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.
PROSITEiPS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization and influence on fungal development of ALP2, a novel serine proteinase from Aspergillus fumigatus."
    Reichard U., Cole G.T., Hill T.W., Ruchel R., Monod M.
    Int. J. Med. Microbiol. 290:549-558(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA], 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. "Identification of vacuolar serine proteinase as a major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis."
    Shen H.D., Lin W.L., Tam M.F., Chou H., Wang C.W., Tsai J.J., Wang S.R., Han S.H.
    Clin. Exp. Allergy 31:295-302(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 137-145 AND 168-176, ALLERGEN, IGE-BINDING.

Entry informationi

Entry nameiALP2_ASPFU
AccessioniPrimary (citable) accession number: P87184
Secondary accession number(s): E9QST4, Q4WUP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: July 1, 1997
Last modified: September 16, 2015
This is version 115 of the entry and version 1 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.