ID   PEP1_ASPNG              Reviewed;          24 AA.
AC   P55749;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Carboxypeptidase 1;
DE            EC=3.4.16.-;
DE   AltName: Full=Carboxypeptidase I;
DE            Short=CPD-I;
DE   Flags: Fragment;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=1637154; DOI=10.1128/aem.58.7.2144-2152.1992;
RA   Dal Degan F., Ribadeau-Dumas B., Breddam K.;
RT   "Purification and characterization of two serine carboxypeptidases from
RT   Aspergillus niger and their use in C-terminal sequencing of proteins and
RT   peptide synthesis.";
RL   Appl. Environ. Microbiol. 58:2144-2152(1992).
CC   -!- FUNCTION: Removes acidic, neutral and basic amino acids as well as
CC       proline from the C-terminal position. Digests preferentially peptides
CC       containing a hydrophobic residue in P1' position, as well as arginine,
CC       lysine or phenylalanine in P1 position of ester substrate. Catalyzes
CC       also peptide synthesis.
CC   -!- ACTIVITY REGULATION: Inhibited by DFP.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4. Unstable above pH 8.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Contains both N- and O-linked sugar chains. The N-linked
CC       oligosaccharides are unique structures of Man(10)GlcNAc(2) and
CC       Man(11)GlcNAc(2). Deglycosylation does neither affect catalytic
CC       activity, pH, thermal stability, or resistance to proteolysis of the
CC       enzyme.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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   AlphaFoldDB; P55749; -.
DR   STRING; 5061.CADANGAP00001927; -.
DR   ESTHER; aspsa-peps; Carboxypeptidase_S10.
DR   eggNOG; KOG1282; Eukaryota.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Protease; Secreted.
FT   CHAIN           1..>24
FT                   /note="Carboxypeptidase 1"
FT                   /id="PRO_0000120565"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   UNSURE          3
FT   UNSURE          11
FT   NON_TER         24
SQ   SEQUENCE   24 AA;  2623 MW;  B7F183DEF6DBA6C2 CRC64;
     LTNKTARFLV NGTSIPEVDF DVGE