ID   DPP2_RAT                Reviewed;         500 AA.
AC   Q9EPB1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, 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;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=Wistar; TISSUE=Kidney;
RX   PubMed=11173530; DOI=10.1093/oxfordjournals.jbchem.a002855;
RA   Araki H., Li Y.-H., Yamamoto Y., Haneda M., Nishi K., Kikkawa R.,
RA   Ohkubo I.;
RT   "Purification, molecular cloning, and immunohistochemical localization of
RT   dipeptidyl peptidase II from the rat kidney and its identity with quiescent
RT   cell proline dipeptidase.";
RL   J. Biochem. 129:279-288(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=Wistar; TISSUE=Kidney;
RX   PubMed=11139392; DOI=10.1042/0264-6021:3530283;
RA   Fukasawa K.M., Fukasawa K., Higaki K., Shiina N., Ohno M., Ito S.,
RA   Otogoto J., Ota N.;
RT   "Cloning and functional expression of rat kidney dipeptidyl peptidase II.";
RL   Biochem. J. 353:283-290(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [4]
RP   PROTEIN SEQUENCE OF 67-72; 123-133; 157-184; 214-225; 264-273; 416-437 AND
RP   459-480, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
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.
CC   -!- SUBCELLULAR LOCATION: Lysosome. Cytoplasmic vesicle {ECO:0000250}.
CC       Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in kidney, but also
CC       expressed in a variety of tissues.
CC   -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR   EMBL; AB048711; BAB13500.1; -; mRNA.
DR   EMBL; AB038232; BAB11691.1; -; mRNA.
DR   EMBL; BC078783; AAH78783.1; -; mRNA.
DR   PIR; JC7668; JC7668.
DR   RefSeq; NP_114179.1; NM_031973.1.
DR   AlphaFoldDB; Q9EPB1; -.
DR   SMR; Q9EPB1; -.
DR   IntAct; Q9EPB1; 1.
DR   STRING; 10116.ENSRNOP00000017271; -.
DR   BindingDB; Q9EPB1; -.
DR   ChEMBL; CHEMBL4352; -.
DR   ESTHER; ratno-dpp2; Prolylcarboxypeptidase.
DR   MEROPS; S28.002; -.
DR   GlyCosmos; Q9EPB1; 6 sites, 2 glycans.
DR   GlyGen; Q9EPB1; 6 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q9EPB1; -.
DR   PhosphoSitePlus; Q9EPB1; -.
DR   jPOST; Q9EPB1; -.
DR   PaxDb; 10116-ENSRNOP00000017271; -.
DR   Ensembl; ENSRNOT00000017271.4; ENSRNOP00000017271.2; ENSRNOG00000012640.4.
DR   Ensembl; ENSRNOT00055000875; ENSRNOP00055000689; ENSRNOG00055000506.
DR   Ensembl; ENSRNOT00060055494; ENSRNOP00060045938; ENSRNOG00060032002.
DR   Ensembl; ENSRNOT00065043513; ENSRNOP00065035701; ENSRNOG00065025256.
DR   GeneID; 83799; -.
DR   KEGG; rno:83799; -.
DR   UCSC; RGD:71073; rat.
DR   AGR; RGD:71073; -.
DR   CTD; 29952; -.
DR   RGD; 71073; Dpp7.
DR   eggNOG; KOG2183; Eukaryota.
DR   GeneTree; ENSGT00940000159838; -.
DR   HOGENOM; CLU_020959_0_0_1; -.
DR   InParanoid; Q9EPB1; -.
DR   OMA; ELYMPMS; -.
DR   OrthoDB; 5488375at2759; -.
DR   PhylomeDB; Q9EPB1; -.
DR   TreeFam; TF314414; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q9EPB1; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000012640; Expressed in adult mammalian kidney and 19 other cell types or tissues.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISO:RGD.
DR   GO; GO:0031982; C:vesicle; ISO:RGD.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:RGD.
DR   GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR   GO; GO:1905146; P:lysosomal protein catabolic process; ISO:RGD.
DR   GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 1.20.120.980; Serine carboxypeptidase S28, SKS domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008758; Peptidase_S28.
DR   InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR   PANTHER; PTHR11010:SF107; DIPEPTIDYL PEPTIDASE 2; 1.
DR   PANTHER; PTHR11010; PROTEASE S28 PRO-X CARBOXYPEPTIDASE-RELATED; 1.
DR   Pfam; PF05577; Peptidase_S28; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   Genevisible; Q9EPB1; RN.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cytoplasmic vesicle; Direct protein sequencing;
KW   Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   PROPEP          34..36
FT                   /id="PRO_0000027318"
FT   CHAIN           37..500
FT                   /note="Dipeptidyl peptidase 2"
FT                   /id="PRO_0000027319"
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"
SQ   SEQUENCE   500 AA;  55114 MW;  401089D282CE1514 CRC64;
     MGLHPCSPVD HGVPSWVLVL LLTLGLCSLQ ATADSVLDPD FRENYFEQYM DHFNFESFSN
     KTFGQRFLVS DKFWKMGEGP IFFYTGNEGD IWSLANNSGF IVELAAQQEA LLVFAEHRYY
     GKSLPFGVQS TQRGYTQLLT VEQALADFAV LLQALRHNLG VQDAPTIAFG GSYGGMLSAY
     MRMKYPHLVA GALAASAPVI AVAGLGNPDQ FFRDVTADFY GQSPKCAQAV RDAFQQIKDL
     FLQGAYDTIS QNFGTCQSLS SPKDLTQLFG FARNAFTVLA MMDYPYPTNF LGPLPANPVK
     VGCERLLSEG QRIMGLRALA GLVYNSSGME PCFDIYQMYQ SCADPTGCGT GSNARAWDYQ
     ACTEINLTFD SNNVTDMFPE IPFSDELRQQ YCLDTWGVWP RPDWLQTSFW GGDLKAASNI
     IFSNGDLDPW AGGGIQRNLS TSIIAVTIQG GAHHLDLRAS NSEDPPSVVE VRKLEATLIR
     EWVAAARLKQ PAEAQWPGPK
//