DPP3_MOUSE
ID DPP3_MOUSE Reviewed; 738 AA.
AC Q99KK7; Q8C0I6;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Dipeptidyl peptidase 3;
DE EC=3.4.14.4 {ECO:0000250|UniProtKB:Q9NY33};
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=Enkephalinase B;
GN Name=Dpp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cleaves and degrades bioactive peptides, including
CC angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg-
CC beta-naphthylamide (in vitro). {ECO:0000250|UniProtKB:Q9NY33}.
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:0000250|UniProtKB:Q9NY33};
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, cytosol
CC {ECO:0000250|UniProtKB:Q9NY33}.
CC -!- SIMILARITY: Belongs to the peptidase M49 family. {ECO:0000305}.
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DR EMBL; AK031020; BAC27216.1; -; mRNA.
DR EMBL; AK166842; BAE39063.1; -; mRNA.
DR EMBL; BC004600; AAH04600.1; -; mRNA.
DR CCDS; CCDS29443.1; -.
DR RefSeq; NP_598564.2; NM_133803.2.
DR RefSeq; XP_006531917.1; XM_006531854.3.
DR AlphaFoldDB; Q99KK7; -.
DR SMR; Q99KK7; -.
DR BioGRID; 217313; 6.
DR STRING; 10090.ENSMUSP00000025851; -.
DR MEROPS; M49.001; -.
DR iPTMnet; Q99KK7; -.
DR PhosphoSitePlus; Q99KK7; -.
DR EPD; Q99KK7; -.
DR jPOST; Q99KK7; -.
DR MaxQB; Q99KK7; -.
DR PaxDb; Q99KK7; -.
DR PRIDE; Q99KK7; -.
DR ProteomicsDB; 277491; -.
DR Antibodypedia; 52373; 435 antibodies from 33 providers.
DR DNASU; 75221; -.
DR Ensembl; ENSMUST00000025851; ENSMUSP00000025851; ENSMUSG00000063904.
DR GeneID; 75221; -.
DR KEGG; mmu:75221; -.
DR UCSC; uc008gbo.2; mouse.
DR CTD; 10072; -.
DR MGI; MGI:1922471; Dpp3.
DR VEuPathDB; HostDB:ENSMUSG00000063904; -.
DR eggNOG; KOG3675; Eukaryota.
DR GeneTree; ENSGT00390000007335; -.
DR HOGENOM; CLU_011977_0_0_1; -.
DR InParanoid; Q99KK7; -.
DR OMA; HCQARFA; -.
DR OrthoDB; 1448344at2759; -.
DR PhylomeDB; Q99KK7; -.
DR TreeFam; TF300598; -.
DR BioGRID-ORCS; 75221; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dpp3; mouse.
DR PRO; PR:Q99KK7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q99KK7; protein.
DR Bgee; ENSMUSG00000063904; Expressed in yolk sac and 229 other tissues.
DR ExpressionAtlas; Q99KK7; baseline and differential.
DR Genevisible; Q99KK7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; ISO:MGI.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT CHAIN 2..738
FT /note="Dipeptidyl peptidase 3"
FT /id="PRO_0000078239"
FT ACT_SITE 451
FT /evidence="ECO:0000250|UniProtKB:O55096"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT CONFLICT 348
FT /note="A -> V (in Ref. 2; AAH04600)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="L -> P (in Ref. 2; AAH04600)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="N -> D (in Ref. 2; AAH04600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 82898 MW; E2B6BD91AE9C81EB CRC64;
MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAHHLSRA AWYGGLAVLL QTSPEAPYIY
ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ AFLVYAAGVY SNMGNYKSFG DTKFVPNLPK
DKLGRVILGS KAAQQRPEEV RDLWQTCGDL MFSLEPRLRH LGLGKEGVTT YFSGDCTMED
AKLAQDFLDS QNLSAYNTRL FKVVGQEGKS HYEVRLASVL NTDPALDSEL TSKLKRYEFQ
GNHFQVTRGD YAPILQKVVE HLEKAKAYAA NSHQEQMLAQ YVESFTQGSI EAHKRGSRFW
IQDKGPIVES YIGFIESYRD PFGSRGEFEG FVAMVNKAMS AKFERLVASA EQLLKELPWP
LAFEKDKFLT PDFTSLDVLT FAGSGIPAGI NIPNYDDLRQ TEGFKNVSLG NVLAVAYAAK
REKLTFLEEE DKDLYIRWKG PSFDVQVGLH ELLGHGSGKL FVQDEKGAFN FDKETVINPE
TGEQIQSWYR SGETWDSKFS TIASSYEECR AESVGLYLCL NPQVLEIFGF EGADAEDVIY
VNWLNMVRAG LLALEFYTPE AANWRQAHMQ ARFVILRVLL EAGEGLVTVT PTTGSDGRPD
ARVRLDRSKI RSVGRPALER FLRRLQVLKS TGDVVAGRAL YEGYAAVTDA PPECFLTLRD
TVLLRKESRK LIVQPNTRLE GSEVQLVEYE ASAAGLIRSF CERFPEDGPE LEEVLIQLAA
ADARFWRNQA QEAPPGQA
