ID   DPP3_NEMVE              Reviewed;         729 AA.
AC   A7RZW4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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;
GN   Name=dpp3; ORFNames=v1g183903;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M49 family. {ECO:0000305}.
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DR   EMBL; DS469558; EDO43060.1; -; Genomic_DNA.
DR   RefSeq; XP_001635123.1; XM_001635073.1.
DR   AlphaFoldDB; A7RZW4; -.
DR   SMR; A7RZW4; -.
DR   STRING; 45351.EDO43060; -.
DR   MEROPS; M49.001; -.
DR   PRIDE; A7RZW4; -.
DR   EnsemblMetazoa; EDO43060; EDO43060; NEMVEDRAFT_v1g183903.
DR   eggNOG; KOG3675; Eukaryota.
DR   HOGENOM; CLU_011977_0_0_1; -.
DR   InParanoid; A7RZW4; -.
DR   OMA; HCQARFA; -.
DR   OrthoDB; 1448344at2759; -.
DR   PhylomeDB; A7RZW4; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR005317; Dipeptidyl-peptase3.
DR   InterPro; IPR039461; Peptidase_M49.
DR   PANTHER; PTHR23422; PTHR23422; 1.
DR   Pfam; PF03571; Peptidase_M49; 1.
DR   PIRSF; PIRSF007828; Dipeptidyl-peptidase_III; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Zinc.
FT   CHAIN           1..729
FT                   /note="Dipeptidyl peptidase 3"
FT                   /id="PRO_0000332968"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000250|UniProtKB:O55096"
FT   BINDING         459
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT   BINDING         464
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT   BINDING         517
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NY33"
SQ   SEQUENCE   729 AA;  81659 MW;  E9CE4DAD281A68DE CRC64;
     MAESDFDKTQ YIIPNEANIN FLECRTAFGG LTEKEKCYAH YLYKASWEGA LICLLQTSPE
     APGIFLLFQK LFSSESVGSL KEKALKSSVA PTEEEFTSFL TYVAAFYGNI GNYKSFGDTK
     FIPNLPKEKF QTIVFSSQAY ATNAKSVVTL WSDCCEAMYS LKPKLRQLGF GEQGISTYYS
     SNCNKSDAEF IQGFLKEKNI EGWNTRLFKE INDKGHVTYN LRLASTALSA EDCSAEKKDD
     VASLVKSYEY QGTTVKITRG DYAGLLKKVV DNLIMAKGFA SNENEVAMLD HYVHSFTTGS
     VEAHKDGSRH WIRDKGPVVE TYIGFIESYR DPFGVRAEYE GFVSIVNKSM SAKFADLVSS
     AETLLPQLPW PSSYEKDTFL RPDFTSLDVL GFGSSGIPAG INIPNYDEIR QDEGFKNVSL
     GNVLSAHSAD QKITFLTEED AELYSKLKAP SFEVQVGLHE LLGHGSGKLF IKKPDGSYNF
     DHKSVVNTET GEKIQSWYTE GETWSTKFAE LSSSYEECRA ECVGIYLCLN KDVLRIFGHE
     GAAGDDIVYV NWLNMVRAGL LGLEFYTPEN NKWRQAHMQA RYVILRVLLE AGEQLVQLTR
     IAGSDGKPDI LVTLDRNKIS CVGQPAIGAF LRKLQVFKST ADYASGKDLY DKYSAVDAHF
     LEMRNIVLAR KTPRRMFVQS HTTIQDGVVS LKEFEASASG MIASFIARFP GDDPVLEKLW
     RDDLPYHQY