ALP2_ASPFU
ID ALP2_ASPFU Reviewed; 495 AA.
AC P87184; E9QST4; Q4WUP6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Alkaline protease 2;
DE Short=ALP2;
DE EC=3.4.21.63;
DE AltName: Full=Autophagic serine protease alp2;
DE AltName: Allergen=Asp f 18;
DE Flags: Precursor;
GN Name=alp2; ORFNames=AFUA_5G09210;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA], AND FUNCTION.
RC STRAIN=D141;
RX PubMed=11100830; DOI=10.1016/s1438-4221(00)80021-1;
RA Reichard U., Cole G.T., Hill T.W., Ruchel R., Monod M.;
RT "Molecular characterization and influence on fungal development of ALP2, a
RT novel serine proteinase from Aspergillus fumigatus.";
RL Int. J. Med. Microbiol. 290:549-558(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [3]
RP PROTEIN SEQUENCE OF 137-145 AND 168-176, ALLERGEN, AND IGE-BINDING.
RX PubMed=11251631; DOI=10.1046/j.1365-2222.2001.01026.x;
RA Shen H.D., Lin W.L., Tam M.F., Chou H., Wang C.W., Tsai J.J., Wang S.R.,
RA Han S.H.;
RT "Identification of vacuolar serine proteinase as a major allergen of
RT Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence
RT analysis.";
RL Clin. Exp. Allergy 31:295-302(2001).
CC -!- FUNCTION: Alkaline protease that allows assimilation of proteinaceous
CC substrates. Acts as a significant virulence factor in invasive
CC aspergillosis. Required for regular sporulation.
CC {ECO:0000269|PubMed:11100830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity, and of Bz-Arg-
CC OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.; EC=3.4.21.63;
CC -!- ALLERGEN: Acts as a major allergen in patients suffering from extrinsic
CC bronchial asthma. Binds to IgE. {ECO:0000269|PubMed:11251631}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; Y13338; CAA73782.1; -; mRNA.
DR EMBL; AJ243145; CAB45520.1; -; Genomic_DNA.
DR EMBL; AAHF01000003; EAL91680.1; -; Genomic_DNA.
DR RefSeq; XP_753718.1; XM_748625.1.
DR AlphaFoldDB; P87184; -.
DR SMR; P87184; -.
DR STRING; 746128.CADAFUBP00005557; -.
DR Allergome; 3114; Asp f 18.0101.
DR Allergome; 70; Asp f 18.
DR EnsemblFungi; EAL91680; EAL91680; AFUA_5G09210.
DR GeneID; 3510885; -.
DR KEGG; afm:AFUA_5G09210; -.
DR VEuPathDB; FungiDB:Afu5g09210; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR InParanoid; P87184; -.
DR OMA; SNYGKCN; -.
DR OrthoDB; 921536at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblFungi.
DR GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IEA:EnsemblFungi.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Serine protease; Signal; Sporulation; Virulence;
KW Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..136
FT /evidence="ECO:0000269|PubMed:11251631"
FT /id="PRO_0000412304"
FT CHAIN 137..495
FT /note="Alkaline protease 2"
FT /id="PRO_0000412305"
FT DOMAIN 43..136
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 146..452
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 52640 MW; A358FE8D6EE533D2 CRC64;
MKGYLSLSIL PLLVAASPVV VDSIHNGAAP ILSSMNAKEV PDSYIVVFKK HVNAESAAAH
HSWVQDIHSA QNERVELRKR SLFGFGEEAY LGLKNTFDIA GSLVGYSGHF HEDVIEQVRK
HPDVEYIEKD SEVHTMEDPT VEKSAPWGLA RISHRDSLSF GTFNKYLYAS EGGEGVDAYT
IDTGINVDHV DFEGRAQWGK TIPTDDEDAD GNGHGTHCSG TIAGRKYGVA KKANLYAVKV
LRSSGSGTMS DVVAGVEWAV KSHLKKVKDA KDGKIKGFKG SVANMSLGGG KSRTLEAAVN
AGVEAGLHFA VAAGNDNADA CNYSPAAAEN PITVGASTLQ DERAYFSNYG KCTDIFAPGL
NILSTWIGSK HAVNTISGTS MASPHIAGLL AYFVSLQPSK DSAFAVDELT PKKLKKDIIA
IATQGALTDI PSDTPNLLAW NGGGSSNYTD IIASGGYKVN ASVKDRFEGL VHKAEKLLTE
ELGAIYSEIH DAAVA
