CARP_ASPFU
ID CARP_ASPFU Reviewed; 398 AA.
AC O42630; Q4WY12;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Vacuolar protease A;
DE EC=3.4.23.25;
DE AltName: Full=Aspartic endopeptidase pep2;
DE AltName: Full=Aspartic protease pep2;
DE Flags: Precursor;
GN Name=pep2; ORFNames=AFUA_3G11400;
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 DNA / MRNA], SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC STRAIN=D141;
RX PubMed=11043985; DOI=10.1016/s1438-4221(00)80111-3;
RA Reichard U., Cole G.T., Ruechel R., Monod M.;
RT "Molecular cloning and targeted deletion of PEP2 which encodes a novel
RT aspartic proteinase from Aspergillus fumigatus.";
RL Int. J. Med. Microbiol. 290:85-96(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 VIRULENCE FACTOR.
RX PubMed=15813678; DOI=10.1016/s1130-1406(05)70001-2;
RA Rementeria A., Lopez-Molina N., Ludwig A., Vivanco A.B., Bikandi J.,
RA Ponton J., Garaizar J.;
RT "Genes and molecules involved in Aspergillus fumigatus virulence.";
RL Rev. Iberoam. Micol. 22:1-23(2005).
CC -!- FUNCTION: Vacuolar aspartic endopeptidase which is probably also
CC secreted and contributes to virulence. {ECO:0000269|PubMed:11043985}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate.
CC Does not act on esters of Tyr or Arg.; EC=3.4.23.25;
CC -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:11043985}.
CC Secreted {ECO:0000305|PubMed:11043985}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AJ132504; CAA10674.1; -; Genomic_DNA.
DR EMBL; Y15744; CAA75754.1; -; mRNA.
DR EMBL; AAHF01000002; EAL92441.1; -; Genomic_DNA.
DR RefSeq; XP_754479.1; XM_749386.1.
DR AlphaFoldDB; O42630; -.
DR SMR; O42630; -.
DR STRING; 746128.CADAFUBP00003699; -.
DR MEROPS; A01.018; -.
DR PRIDE; O42630; -.
DR EnsemblFungi; EAL92441; EAL92441; AFUA_3G11400.
DR GeneID; 3512540; -.
DR KEGG; afm:AFUA_3G11400; -.
DR VEuPathDB; FungiDB:Afu3g11400; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; O42630; -.
DR OMA; DKSHYTG; -.
DR OrthoDB; 1619495at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05488; Proteinase_A_fungi; 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; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal; Vacuole; Virulence; Zymogen.
FT SIGNAL 1..18
FT PROPEP 19..70
FT /note="Activation peptide"
FT /id="PRO_5000147257"
FT CHAIN 71..398
FT /note="Vacuolar protease A"
FT /id="PRO_5000147258"
FT DOMAIN 85..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..121
FT /evidence="ECO:0000250"
FT DISULFID 321..354
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 43355 MW; 52741DFEDBEEAF3B CRC64;
MKSTSLLTAS VLLGSASAAV HKLKLNKVPL DEQLYTHNID AHVRALGQKY MGIRPNVHQE
LLEENSLNDM SRHDVLVDNF LNAQYFSEIS LGTPPQKFKV VLDTGSSNLW VPGSDCSSIA
CFLHNKYDSS ASSTYKANGT EFAIKYGSGE LSGFVSQDTL QIGDLKVVKQ DFAEATNEPG
LAFAFGRFDG ILGLGYDTIS VNKIVPPFYN MLDQGLLDEP VFAFYLGDTN KEGDNSEASF
GGVDKNHYTG ELTKIPLRRK AYWEVDFDAI ALGDNVAELE NTGIILDTGT SLIALPSTLA
DLLNKEIGAK KGFTGQYSIE CDKRDSLPDL TFTLAGHNFT IGPYDYTLEV QGSCISSFMG
MDFPEPVGPL AILGDAFLRK WYSVYDLGNN AVGLAKAK
