ID B6HU56_PENRW Unreviewed; 505 AA.
AC B6HU56;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=penicillopepsin {ECO:0000256|ARBA:ARBA00013206};
DE EC=3.4.23.20 {ECO:0000256|ARBA:ARBA00013206};
GN ORFNames=Pc22g18210 {ECO:0000313|EMBL:CAP99109.1}, PCH_Pc22g18210
GN {ECO:0000313|EMBL:CAP99109.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP99109.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP99109.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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 can also activate
CC trypsinogen and hydrolyze the B chain of insulin between positions
CC 'Gly-20' and 'Glu-21'. {ECO:0000256|ARBA:ARBA00002983}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity similar to that
CC of pepsin A, preferring hydrophobic residues at P1 and P1', but also
CC cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and
CC activates trypsinogen.; EC=3.4.23.20;
CC Evidence={ECO:0000256|ARBA:ARBA00000043};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; AM920437; CAP99109.1; -; Genomic_DNA.
DR RefSeq; XP_002565726.1; XM_002565680.1.
DR AlphaFoldDB; B6HU56; -.
DR STRING; 500485.B6HU56; -.
DR MEROPS; A01.077; -.
DR GeneID; 8312838; -.
DR KEGG; pcs:Pc22g18210; -.
DR VEuPathDB; FungiDB:PCH_Pc22g18210; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_10_0_1; -.
DR OMA; AFYPWEL; -.
DR OrthoDB; 3087283at2759; -.
DR BioCyc; PCHR:PC22G18210-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c22.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..505
FT /note="penicillopepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002843776"
FT DOMAIN 106..414
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 432..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 137..142
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 505 AA; 54123 MW; 3387F8AC8F771202 CRC64;
MRLSSCLVFI AGISGVHAFY PWELRMKLST ETTVKRRFVP WTLIGAKSDD STDSTDTSNA
ANRKPFTLDL KKVPVRRDHV YKIVESHKPS LADSAPLHQD GTDYSYFSPV YVGSQKQEMW
MAIDTGAPNT WVFDSKCTEP VCIHHHTFDR SASTSFTTDN LAFSLFYGSG KIDGKMGKDT
LSIAGLEVLQ TFGLANNASE TFESYPFDGI LGLGRSHTSG WNLPSFMDLV AEKKLIKSNL
VGFSLSRSED NHKDGEINFG DVDTTKFDGT ISYTATNDKN WNIPLDDAYV NGQSCNFSGR
TATIDTGTTY LLIPPADAKA LFSLVPDSSQ QPDNPNNYLI PCNSTATIEF EFSGVKYNIS
PKDYVGNPEP EGSDYCISTI VGYASNGADW LVGDVFLKNV YTVFDFDNGQ VGFGALASAS
ASASALKSNL DPSSTSSSSS SSPPQGNGTF TAPLVTGTAA STADATSSSS PASSAMATVS
GSSASHLVHG ISWSMLTVMI AAFAV
//