位置:首页 > 蛋白库 > PEPA_ASPAW
PEPA_ASPAW
ID   PEPA_ASPAW              Reviewed;         394 AA.
AC   P17946; Q7M512;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 107.
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 A {ECO:0000303|PubMed:2182390};
DE            Short=PEPA;
DE   AltName: Full=Aspergillopepsin I;
DE   AltName: Full=Aspergillopeptidase A;
DE   Flags: Precursor;
GN   Name=pepA {ECO:0000303|PubMed:2182390};
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=UVK143F;
RX   PubMed=2182390; DOI=10.1016/0378-1119(90)90274-u;
RA   Berka R.M., Ward M., Wilson L.J., Hayenga K.J., Kodama K.H.,
RA   Carlomagno L.P., Thompson S.A.;
RT   "Molecular cloning and deletion of the gene encoding aspergillopepsin A
RT   from Aspergillus awamori.";
RL   Gene 86:153-162(1990).
RN   [2]
RP   ERRATUM OF PUBMED:2182390.
RX   PubMed=2269444; DOI=10.1016/0378-1119(90)90261-o;
RA   Thompson S.A.;
RL   Gene 96:313-313(1990).
RN   [3]
RP   PRELIMINARY PROTEIN SEQUENCE OF 70-394.
RA   Ostoslavskaya V.I., Revina L.P., Kotlova E.K., Surova I.A., Levin E.D.,
RA   Timokhina E.A., Stepanov V.M.;
RT   "The primary structure of aspergillopepsin A, aspartic proteinase from
RT   Aspergillus awamori. IV. Amino acid sequence of the enzyme.";
RL   Bioorg. Khim. 12:1030-1047(1986).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M34454; AAA78947.1; -; Genomic_DNA.
DR   PIR; PN0090; PN0090.
DR   PIR; PS0140; PS0140.
DR   AlphaFoldDB; P17946; -.
DR   SMR; P17946; -.
DR   MEROPS; A01.016; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Aspartyl protease; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Protease; Secreted; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..69
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:2182390, ECO:0000269|Ref.3"
FT                   /id="PRO_0000025918"
FT   CHAIN           70..394
FT                   /note="Aspergillopepsin-1"
FT                   /id="PRO_0000025919"
FT   DOMAIN          85..391
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        283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   DISULFID        319..354
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   394 AA;  41177 MW;  88C3590218B27819 CRC64;
     MVVFSKTAAL VLGLSSAVSA APAPTRKGFT INQIARPANK TRTINLPGMY ARSLAKFGGT
     VPQSVKEAAS KGSAVTTPQN NDEEYLTPVT VGKSTLHLDF DTGSADLWVF SDELPSSEQT
     GHDLYTPSSS ATKLSGYTWD ISYGDGSSAS GDVYRDTVTV GGVTTNKQAV EAASKISSEF
     VQNTANDGLL GLAFSSINTV QPKAQTTFFD TVKSQLDSPL FAVQLKHDAP GVYDFGYIDD
     SKYTGSITYT DADSSQGYWG FSTDGYSIGD GSSSSSGFSA IADTGTTLIL LDDEIVSAYY
     EQVSGASGET EAGGYVFSCS TNPPDFTVVI GDYKAVVPGK YINYAPISTG SSTCFGGIQS
     NSGLGLSILG DVFLKSQYVV FNSEGPKLGF AAQA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024