DPP3_DROME
ID DPP3_DROME Reviewed; 786 AA.
AC Q9VHR8; Q8IHE9; Q961F1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Dipeptidyl peptidase 3;
DE EC=3.4.14.4;
DE AltName: Full=Dipeptidyl aminopeptidase III;
DE Short=Dipeptidyl arylamidase III;
DE AltName: Full=Dipeptidyl peptidase III;
DE Short=DPP III;
GN Name=DppIII; ORFNames=CG7415;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Berkeley; TISSUE=Embryo, Head, and Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP IDENTIFICATION (ISOFORM 2).
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).
RN [5]
RP FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=12846841; DOI=10.1046/j.1432-1033.2003.03689.x;
RA Mazzocco C., Fukasawa K.M., Auguste P., Puiroux J.;
RT "Characterization of a functionally expressed dipeptidyl aminopeptidase III
RT from Drosophila melanogaster.";
RL Eur. J. Biochem. 270:3074-3082(2003).
CC -!- FUNCTION: Degrades neuropeptide proctolin (RYLPT) by cleavage between
CC Tyr and Leu residues. {ECO:0000269|PubMed:12846841}.
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:12846841};
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: [Isoform 1]: Membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:12846841}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:12846841}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q9VHR8-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9VHR8-2; Sequence=VSP_007939;
CC -!- SIMILARITY: Belongs to the peptidase M49 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93049.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF54232.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14313.1; -; Genomic_DNA.
DR EMBL; AY051625; AAK93049.1; ALT_INIT; mRNA.
DR EMBL; BT001283; AAN71039.1; -; mRNA.
DR EMBL; BT001401; AAN71156.1; -; mRNA.
DR EMBL; BT001402; AAN71157.1; -; mRNA.
DR EMBL; BT001639; AAN71394.1; -; mRNA.
DR RefSeq; NP_731237.1; NM_169217.3. [Q9VHR8-1]
DR RefSeq; NP_731238.1; NM_169218.3. [Q9VHR8-2]
DR AlphaFoldDB; Q9VHR8; -.
DR SMR; Q9VHR8; -.
DR BioGRID; 66177; 3.
DR IntAct; Q9VHR8; 1.
DR STRING; 7227.FBpp0081331; -.
DR MEROPS; M49.A01; -.
DR PaxDb; Q9VHR8; -.
DR PRIDE; Q9VHR8; -.
DR DNASU; 40996; -.
DR EnsemblMetazoa; FBtr0081840; FBpp0081330; FBgn0037580. [Q9VHR8-2]
DR EnsemblMetazoa; FBtr0081841; FBpp0081331; FBgn0037580. [Q9VHR8-1]
DR GeneID; 40996; -.
DR KEGG; dme:Dmel_CG7415; -.
DR CTD; 40996; -.
DR FlyBase; FBgn0037580; DppIII.
DR VEuPathDB; VectorBase:FBgn0037580; -.
DR eggNOG; KOG3675; Eukaryota.
DR GeneTree; ENSGT00390000007335; -.
DR InParanoid; Q9VHR8; -.
DR OMA; HCQARFA; -.
DR PhylomeDB; Q9VHR8; -.
DR BRENDA; 3.4.14.4; 1994.
DR BioGRID-ORCS; 40996; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40996; -.
DR PRO; PR:Q9VHR8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037580; Expressed in oocyte and 29 other tissues.
DR ExpressionAtlas; Q9VHR8; baseline and differential.
DR Genevisible; Q9VHR8; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:FlyBase.
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; IDA:FlyBase.
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 2: Evidence at transcript level;
KW Alternative splicing; Aminopeptidase; Cell membrane; Cytoplasm; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..786
FT /note="Dipeptidyl peptidase 3"
FT /id="PRO_0000078242"
FT TOPO_DOM 1..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..594
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 507
FT /evidence="ECO:0000250|UniProtKB:O55096"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT VAR_SEQ 1..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007939"
SQ SEQUENCE 786 AA; 89194 MW; C13B945177F9D2D7 CRC64;
MFWLRGLQRS RQQLNRLCHF RSRLNYGTSP SIRSVQPSIS RSLGFCSSLV RYSCSTNLPQ
PAEMASKTAH FVLPNTQPIA DLDCKSAFEN LTEKEKLYAH HFSQASWDGG LIALIQSSPE
APLIFSLLHR IFLAEKIPVL RAKALEAGVS ADDFTAFLVY ACGVFANAGN YKGMGDSKIV
PNLSEKQFET IVKASAAYSD EPRVGKIFEK VKNLIYALES RNEILGFAPD GITTYWSDNC
TKEDSEIVNA WLTSKRIEPY MCRTFKIVEN GQTVYDVKLG SVAESTQDGI TLPLEEYNGN
KFRVTRGDYQ KLLQRVNQHL LQAQKYAANE NESKMIEHYV RSFEQGSLDE HKNGSRWWIK
DKGPVIETYI GFIETYRDPA GGRAEFEGFV AMVNKESSAK FSELVNRAEK LIEYLPWTEP
YEKDSYLKPD FTSLDVLTFA GSGVPAGINI PNYDEIRQDE GFKNVSLGNV LANINRKDPI
PFLTEEDQTL MKEYKVKAFE VQVGLHELLG HGSGKLFRID ENGVYNFDKE NTKNLVTGEP
ITKWYLPGET YDTKFGAIGS SYEECRAEAV GLYLSLQRDI LEIFGFKDKA EQDNIIYVNW
LSLIWNGMGV ALEMFNPKSK LWLQAHSRAR FVIMKVLLEA GEGLVKVEET EKGKNLLLTV
DRSKIDTVGR KALGDFLTKL QVYKSTADIE AASKMYEHYS KVDESGSHPW AKWRDICLAH
KKPRMILVQA NTAIGQDQKV QLKTYEPTHE GYIQSWVERY PNTDIDDLLE SIVEKDKKYF
PTAFNN
