ID   AXP1_YARLI              Reviewed;         397 AA.
AC   Q92389;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Acid extracellular protease;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=AXP1; Synonyms=AXP; OrderedLocusNames=YALI0B05654g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=148;
RX   PubMed=8885407; DOI=10.1099/13500872-142-10-2913;
RA   Young T.W., Wadeson A., Glover D.J., Quincey R.V., Butlin M.J., Kamei E.A.;
RT   "The extracellular acid protease gene of Yarrowia lipolytica: sequence and
RT   pH-regulated transcription.";
RL   Microbiology 142:2913-2921(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; X97068; CAA65778.1; -; Genomic_DNA.
DR   EMBL; CR382128; CAG82769.1; -; Genomic_DNA.
DR   RefSeq; XP_500538.1; XM_500538.1.
DR   AlphaFoldDB; Q92389; -.
DR   SMR; Q92389; -.
DR   MEROPS; A01.036; -.
DR   EnsemblFungi; CAG82769; CAG82769; YALI0_B05654g.
DR   GeneID; 2907455; -.
DR   KEGG; yli:YALI0B05654g; -.
DR   VEuPathDB; FungiDB:YALI0_B05654g; -.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   InParanoid; Q92389; -.
DR   OMA; ENDSIAC; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR47965; PTHR47965; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..?
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025832"
FT   CHAIN           ?..397
FT                   /note="Acid extracellular protease"
FT                   /id="PRO_0000025833"
FT   DOMAIN          61..378
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        93..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        303..343
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  42081 MW;  BD678814B4B8984F CRC64;
     MQFSLATLTT LLAFVAAAPA NKGFVHAPIK KQSLQAAQSK IPNFASSGPI TAELYNELMA
     YQVQISLGGQ TISASIDTGS EILWVWENDS IACQVDQQDC DTDGSYNPKK SSTSKDTGVP
     FNINYGKGHA DGYLYTDNAV IGGASAPGFK FGVNSGDLSS GGFSMVFGIG VNSDASTSIS
     AQLQKSGEIS RNLYGMSFSD ANLAGTSNDN SEITFGAINT GRYTGSLKTI PRVATQGGYQ
     HFSVSASGKF GDVDLFDNDL VILDSGTTMT YLKSDYYNAF LGGLEDLDIT LSDYSGGWHG
     YPCSENSKIN FTYNFSGKEI TVTGHDLAIP GNAVNSNVDS SVCFMGVDDG GNMNLFGDTF
     LRAIYSVYDL ERDEVSIAQA AHGKPDNYVV ITGDVPN