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Dipeptidyl peptidase 3 (EC 3.4.14.4) (Dipeptidyl aminopeptidase III) (Dipeptidyl arylamidase III) (Dipeptidyl peptidase III) (DPP III) (Proctolinase) (Fragments)

 DPP3_BLACR              Reviewed;          73 AA.
P83681;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
31-OCT-2003, sequence version 1.
12-APR-2017, entry version 41.
RecName: Full=Dipeptidyl peptidase 3;
EC=3.4.14.4;
AltName: Full=Dipeptidyl aminopeptidase III;
AltName: Full=Dipeptidyl arylamidase III;
AltName: Full=Dipeptidyl peptidase III;
Short=DPP III;
AltName: Full=Proctolinase;
Flags: Fragments;
Blaberus craniifer (Death's head cockroach).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Polyneoptera; Dictyoptera; Blattodea;
Blaberoidea; Blaberidae; Blaberinae; Blaberus.
NCBI_TaxID=6982 {ECO:0000305};
[1] {ECO:0000305}
PROTEIN SEQUENCE, FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
TISSUE=Hindgut {ECO:0000269|PubMed:11559363};
PubMed=11559363; DOI=10.1046/j.1432-1327.2001.02425.x;
Mazzocco C., Fukasawa K.M., Raymond A.-A., Puiroux J.;
"Purification, partial sequencing and characterization of an insect
membrane dipeptidyl aminopeptidase that degrades the insect
neuropeptide proctolin.";
Eur. J. Biochem. 268:4940-4949(2001).
-!- FUNCTION: Degrades neuropeptide proctolin (RYLPT) by cleavage
between Tyr and Leu residues. {ECO:0000269|PubMed:11559363}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide from a
peptide comprising four or more residues, with broad specificity.
Also acts on dipeptidyl 2-naphthylamides.
{ECO:0000269|PubMed:11559363}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9NY33};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NY33};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.1.;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11559363};
Multi-pass membrane protein {ECO:0000269|PubMed:11559363}.
-!- MISCELLANEOUS: Purified protein is present in 2 isoforms; 76 kDa
and 80 kDa.
-!- SIMILARITY: Belongs to the peptidase M49 family. {ECO:0000305}.
-!- CAUTION: The order of the last peptide shown is unknown.
{ECO:0000305}.
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GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
1: Evidence at protein level;
Aminopeptidase; Direct protein sequencing; Hydrolase; Membrane;
Metalloprotease; Protease; Transmembrane; Zinc.
CHAIN 1 73 Dipeptidyl peptidase 3.
/FTId=PRO_0000078241.
NON_CONS 7 8 {ECO:0000305}.
NON_CONS 14 15 {ECO:0000305}.
NON_CONS 26 27 {ECO:0000305}.
NON_CONS 39 40 {ECO:0000305}.
NON_CONS 44 45 {ECO:0000305}.
NON_CONS 61 62 {ECO:0000305}.
SEQUENCE 73 AA; 8129 MW; 1A16FCB36F5C96D0 CRC64;
FANLVEKTTY FSDKGEFEGF VAMVNKNVTL GNVIPASYKL QVYKTYDATH EGLIQSFVEN
GTEEVPLDGX EXX


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