PEPA_EMENI
ID PEPA_EMENI Reviewed; 386 AA.
AC O93885; C8V2W4; Q5AXU2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Aspergillopepsin-1 {ECO:0000305};
DE EC=3.4.23.18 {ECO:0000250|UniProtKB:Q12567};
DE AltName: Full=Aspartic protease pepA;
DE AltName: Full=Aspergillopepsin I;
DE AltName: Full=Aspergillopeptidase A;
DE AltName: Full=Proctase B;
DE Flags: Precursor;
GN Name=prtB {ECO:0000303|PubMed:10882536}; Synonyms=pepA; ORFNames=AN6888;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=MH2;
RX PubMed=10882536; DOI=10.1006/fgbi.2000.1195;
RA vanKuyk P.A., Cheetham B.F., Katz M.E.;
RT "Analysis of two Aspergillus nidulans genes encoding extracellular
RT proteases.";
RL Fungal Genet. Biol. 29:201-210(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation of
CC proteinaceous substrates. The scissile peptide bond is attacked by a
CC nucleophilic water molecule activated by two aspartic residues in the
CC active site. Shows a broad primary substrate specificity. Favors
CC hydrophobic residues at the P1 and P1' positions, but also accepts a
CC lysine residue in the P1 position, leading to the activation of
CC trypsinogen and chymotrypsinogen A. {ECO:0000250|UniProtKB:Q12567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity. Generally
CC favors hydrophobic residues in P1 and P1', but also accepts Lys in
CC P1, which leads to activation of trypsinogen. Does not clot milk.;
CC EC=3.4.23.18; Evidence={ECO:0000250|UniProtKB:Q12567};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12567}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
CC -!- INDUCTION: Expressed, albeit at a very low level.
CC {ECO:0000269|PubMed:10882536}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
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DR EMBL; AF090736; AAD04378.1; -; Genomic_DNA.
DR EMBL; AACD01000113; EAA58287.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF71666.1; -; Genomic_DNA.
DR RefSeq; XP_664492.1; XM_659400.1.
DR AlphaFoldDB; O93885; -.
DR SMR; O93885; -.
DR STRING; 162425.CADANIAP00007689; -.
DR MEROPS; A01.026; -.
DR EnsemblFungi; CBF71666; CBF71666; ANIA_06888.
DR EnsemblFungi; EAA58287; EAA58287; AN6888.2.
DR GeneID; 2870599; -.
DR KEGG; ani:AN6888.2; -.
DR VEuPathDB; FungiDB:AN6888; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR InParanoid; O93885; -.
DR OMA; YGSGNAK; -.
DR OrthoDB; 1619495at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
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; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..69
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q12567"
FT /id="PRO_0000407048"
FT CHAIN 70..386
FT /note="Aspergillopepsin-1"
FT /id="PRO_0000407049"
FT DOMAIN 85..383
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 311..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 386 AA; 41194 MW; F50654A022D1E6A1 CRC64;
MVVFSKVAAA AFGLSAVASA MPAAPPRQGF TINQLTRAIP KRTINLPAIY ANALSKYGGN
VPPHIQDAMA HGSAVTTPEQ YDVEYLTPVA VGGTTMNLDF DTGSADLWVF SNELPSSQTT
GHSVYKPSDN GTRMSGYSWE ISYGDGSSAG GDVYRDTVTV GGVTAPGQAV EAASHISEQF
TRDQNNDGLL GLAFSSINTV QPKSQTTFFD SVKSQLESPL FAVTLKHQAP GSYDFGYIDQ
SKYTGELTYT DVDNSQGFWM FSATAGETDF DAIADTGTTL IMIDQSIAED YYSQVPLAFN
NFFYGGWTFP CSAELPSFTV TINGYDAVVP GEHIKYAPVT DGSSTCFGGI QDNQGLPFSI
LGDVFLKSQY VVFDSEGPQL GFAPQA
