ID   DPP3_BLACR              Reviewed;          73 AA.
AC   P83681;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Dipeptidyl peptidase 3;
DE            EC=3.4.14.4;
DE   AltName: Full=Dipeptidyl aminopeptidase III;
DE   AltName: Full=Dipeptidyl arylamidase III;
DE   AltName: Full=Dipeptidyl peptidase III;
DE            Short=DPP III;
DE   AltName: Full=Proctolinase;
DE   Flags: Fragments;
OS   Blaberus craniifer (Death's head cockroach).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blaberidae;
OC   Blaberinae; Blaberus.
OX   NCBI_TaxID=6982 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Hindgut {ECO:0000269|PubMed:11559363};
RX   PubMed=11559363; DOI=10.1046/j.1432-1327.2001.02425.x;
RA   Mazzocco C., Fukasawa K.M., Raymond A.-A., Puiroux J.;
RT   "Purification, partial sequencing and characterization of an insect
RT   membrane dipeptidyl aminopeptidase that degrades the insect neuropeptide
RT   proctolin.";
RL   Eur. J. Biochem. 268:4940-4949(2001).
CC   -!- FUNCTION: Degrades neuropeptide proctolin (RYLPT) by cleavage between
CC       Tyr and Leu residues. {ECO:0000269|PubMed:11559363}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide from a peptide comprising
CC         four or more residues, with broad specificity. Also acts on
CC         dipeptidyl 2-naphthylamides.; EC=3.4.14.4;
CC         Evidence={ECO:0000269|PubMed:11559363};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9NY33};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NY33};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.1.;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11559363}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:11559363}.
CC   -!- MISCELLANEOUS: Purified protein is present in 2 isoforms; 76 kDa and 80
CC       kDa.
CC   -!- SIMILARITY: Belongs to the peptidase M49 family. {ECO:0000305}.
CC   -!- CAUTION: The order of the last peptide shown is unknown. {ECO:0000305}.
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DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Direct protein sequencing; Hydrolase; Membrane;
KW   Metalloprotease; Protease; Transmembrane; Zinc.
FT   CHAIN           1..73
FT                   /note="Dipeptidyl peptidase 3"
FT                   /id="PRO_0000078241"
FT   NON_CONS        7..8
FT                   /evidence="ECO:0000305"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000305"
FT   NON_CONS        26..27
FT                   /evidence="ECO:0000305"
FT   NON_CONS        39..40
FT                   /evidence="ECO:0000305"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000305"
FT   NON_CONS        61..62
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   73 AA;  8129 MW;  1A16FCB36F5C96D0 CRC64;
     FANLVEKTTY FSDKGEFEGF VAMVNKNVTL GNVIPASYKL QVYKTYDATH EGLIQSFVEN
     GTEEVPLDGX EXX