DPP2_MOUSE
ID DPP2_MOUSE Reviewed; 506 AA.
AC Q9ET22; Q8R082;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dipeptidyl peptidase 2;
DE EC=3.4.14.2;
DE AltName: Full=Dipeptidyl aminopeptidase II;
DE AltName: Full=Dipeptidyl peptidase 7;
DE AltName: Full=Dipeptidyl peptidase II;
DE Short=DPP II;
DE AltName: Full=Quiescent cell proline dipeptidase;
DE Flags: Precursor;
GN Name=Dpp7; Synonyms=Dpp2, Qpp;
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 [MRNA].
RC STRAIN=129;
RA Bista P., Jaison P.L., Yardley K., Lee H.J., Huber B.T.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
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: Plays an important role in the degradation of some
CC oligopeptides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially
CC when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially
CC tripeptides.; EC=3.4.14.2;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR EMBL; AF285235; AAG01154.1; -; mRNA.
DR EMBL; AL732557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08237.1; -; Genomic_DNA.
DR EMBL; BC027205; AAH27205.1; -; mRNA.
DR CCDS; CCDS15766.1; -.
DR RefSeq; NP_114031.2; NM_031843.2.
DR AlphaFoldDB; Q9ET22; -.
DR SMR; Q9ET22; -.
DR BioGRID; 219972; 20.
DR STRING; 10090.ENSMUSP00000028332; -.
DR ChEMBL; CHEMBL3259501; -.
DR ESTHER; mouse-dpp2; Prolylcarboxypeptidase.
DR MEROPS; S28.002; -.
DR GlyConnect; 2256; 2 N-Linked glycans (2 sites).
DR GlyGen; Q9ET22; 6 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q9ET22; -.
DR PhosphoSitePlus; Q9ET22; -.
DR EPD; Q9ET22; -.
DR jPOST; Q9ET22; -.
DR MaxQB; Q9ET22; -.
DR PaxDb; Q9ET22; -.
DR PeptideAtlas; Q9ET22; -.
DR PRIDE; Q9ET22; -.
DR ProteomicsDB; 277600; -.
DR Antibodypedia; 18905; 297 antibodies from 33 providers.
DR DNASU; 83768; -.
DR Ensembl; ENSMUST00000028332; ENSMUSP00000028332; ENSMUSG00000026958.
DR GeneID; 83768; -.
DR KEGG; mmu:83768; -.
DR UCSC; uc008irq.1; mouse.
DR CTD; 29952; -.
DR MGI; MGI:1933213; Dpp7.
DR VEuPathDB; HostDB:ENSMUSG00000026958; -.
DR eggNOG; KOG2183; Eukaryota.
DR GeneTree; ENSGT00940000159838; -.
DR HOGENOM; CLU_020959_0_0_1; -.
DR InParanoid; Q9ET22; -.
DR OMA; IKGGAHH; -.
DR OrthoDB; 555765at2759; -.
DR PhylomeDB; Q9ET22; -.
DR TreeFam; TF314414; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 83768; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Dpp7; mouse.
DR PRO; PR:Q9ET22; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ET22; protein.
DR Bgee; ENSMUSG00000026958; Expressed in choroid plexus of fourth ventricle and 248 other tissues.
DR Genevisible; Q9ET22; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:1905146; P:lysosomal protein catabolic process; IMP:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.980; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008758; Peptidase_S28.
DR InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR Pfam; PF05577; Peptidase_S28; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasmic vesicle; Glycoprotein; Hydrolase; Lysosome;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..36
FT /evidence="ECO:0000250"
FT /id="PRO_0000027316"
FT CHAIN 37..506
FT /note="Dipeptidyl peptidase 2"
FT /id="PRO_0000027317"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 428
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 453
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 497
FT /note="P -> L (in Ref. 1; AAG01154)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 56254 MW; 3A4ECAA3DD4EF7D4 CRC64;
MNFHPCYPVD HGVPSWILVL LLSLGLCNLQ ARADRVLDPD FHENYFEQYM DHFNFESFGN
KTFGQRFLVS DKFWKMGEGP IFFYTGNEGD IWSFANNSGF MVELAAQQEA LLVFAEHRYY
GKSLPFGVQS TQRGYTQLLT VEQALADFAV LLQALRQDLG VHDAPTIAFG GSYGGMLSAY
MRMKYPHLVA GALAASAPVV AVAGLGDSYQ FFRDVTADFY GQSPKCAQAV RDAFQQIKDL
FLQGAYDTIS QNFGTCQSLS SPKDLTQLFG FARNAFTVLA MMDYPYPTDF LGPLPANPVK
VGCQRLLNEG QRIMGLRALA GLVYNSSGTE PCYDIYRLYQ SCADPTGCGT GSDARAWDYQ
ACTEINLTFD SNNVTDMFPE IPFSEELRQQ YCLDTWGVWP RQDWLQTSFW GGDLKAASNI
IFSNGDLDPW AGGGIQSNLS TSVIAVTIQG GAHHLDLRAS NSEDPPSVVE VRKLESTLIR
EWVAAARLKQ PAMPRWPGPK KQHPSR
