ID   DPEP3_RAT               Reviewed;         488 AA.
AC   Q5U2X4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Dipeptidase 3;
DE   Flags: Precursor;
GN   Name=Dpep3;
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
CC   -!- FUNCTION: Lacks dipeptidase activity and is unable to hydrolyze
CC       cystinyl-bis-glycine, leukotriene D4 and the beta-lactam antibiotic
CC       imipenem (By similarity). The absence of activity may be due to the
CC       inability of serine (instead of aspartate found in DPEP1/2) at position
CC       356 to function as the acid/base catalyst and activate the nucleophilic
CC       water/hydroxide (By similarity). {ECO:0000250|UniProtKB:Q9H4B8}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC       TEX101; co-localized on the cell surface of spermatocytes, spermatids,
CC       and testicular spermatozoa, co-localized only in cytoplasmic droplets
CC       of caput and corpus epididymal sperm (By similarity).
CC       {ECO:0000250|UniProtKB:Q9DA79, ECO:0000255|PROSITE-ProRule:PRU10073}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9DA79}; Lipid-
CC       anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9DA79}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}.
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DR   EMBL; BC085826; AAH85826.1; -; mRNA.
DR   RefSeq; NP_001008384.1; NM_001008383.1.
DR   RefSeq; XP_006255579.1; XM_006255517.3.
DR   RefSeq; XP_008770743.1; XM_008772521.1.
DR   AlphaFoldDB; Q5U2X4; -.
DR   SMR; Q5U2X4; -.
DR   STRING; 10116.ENSRNOP00000026809; -.
DR   MEROPS; M19.011; -.
DR   GlyGen; Q5U2X4; 1 site.
DR   PaxDb; Q5U2X4; -.
DR   Ensembl; ENSRNOT00000026809; ENSRNOP00000026809; ENSRNOG00000019757.
DR   GeneID; 364994; -.
DR   KEGG; rno:364994; -.
DR   UCSC; RGD:1305484; rat.
DR   CTD; 64180; -.
DR   RGD; 1305484; Dpep3.
DR   eggNOG; KOG4127; Eukaryota.
DR   GeneTree; ENSGT00940000162331; -.
DR   HOGENOM; CLU_031404_4_1_1; -.
DR   InParanoid; Q5U2X4; -.
DR   OMA; EEVQNSC; -.
DR   OrthoDB; 1272387at2759; -.
DR   PhylomeDB; Q5U2X4; -.
DR   TreeFam; TF324523; -.
DR   Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   Reactome; R-RNO-5423646; Aflatoxin activation and detoxification.
DR   PRO; PR:Q5U2X4; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000019757; Expressed in testis and 12 other tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016805; F:dipeptidase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR   GO; GO:0006508; P:proteolysis; ISO:RGD.
DR   CDD; cd01301; rDP_like; 1.
DR   InterPro; IPR000180; Dipep_AS.
DR   InterPro; IPR028531; Dpep2/3.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008257; Pept_M19.
DR   PANTHER; PTHR10443; PTHR10443; 1.
DR   PANTHER; PTHR10443:SF14; PTHR10443:SF14; 1.
DR   Pfam; PF01244; Peptidase_M19; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1.
DR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..459
FT                   /note="Dipeptidase 3"
FT                   /id="PRO_0000231615"
FT   PROPEP          460..487
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P16444"
FT                   /id="PRO_0000231616"
FT   REGION          41..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           459
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        143..222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   DISULFID        294..326
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   DISULFID        431
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
SQ   SEQUENCE   488 AA;  53370 MW;  E22FCAC7902144C5 CRC64;
     MQPTGPEGPR ALSLRPLGHR LSLLGVLLII PSLWVTCNQT TPSLSSAPTS PGASSAMTTP
     GIPNDTTTSG VTSDPRLREQ ALALMRDFPL VDGHNDLPLL LRELFQNKLQ DVNLHNFTRG
     QTSLDRLRDG LVGAQFWSAY IPCQTQDRDA VRVALEQIDL IRRMCSAYPE LELVTSADGL
     NSTQKLACLI GLEGGHSLDT SLAVLRSFYE LGVRYLTLTF TCSTPWAESA TKFRHHFYTN
     ISGLTSFGEK VVEEMNRIGM MIDLSHASDT LVKQTLEASR APVIFSHSAA RSVCDNLLNV
     PDDILQLLKK NGGIVMVTLS MGVLQCSLLA NVSTVADHFD HIRTVIGSEF IGIGGSYDGS
     GRFPQGLEDV STYPVLLEEL LRRGWGEQEL QGVLRGNLLR VFRQVEQVRE KSLGQSPVEV
     VFPERQQSST CHSHLLPQSQ DAHLKVTKLP SSQVLQRASK APPCPLLGLV AAVTSPAFTL
     WLCCSGHR