ID   DPEP3_MACFA             Reviewed;         488 AA.
AC   Q4R7M2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Dipeptidase 3;
DE   Flags: Precursor;
GN   Name=DPEP3; ORFNames=QtsA-14814;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 asparagine (instead of aspartate found in DPEP1/2) at
CC       position 359 to function as the acid/base catalyst and activate the
CC       nucleophilic water/hydroxide (By similarity). A tyrosine (instead of
CC       histidine) at position 269 reduces affinity for the beta zinc and may
CC       cause substrate steric hindrance (By similarity).
CC       {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE00900.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB168793; BAE00900.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001306334.1; NM_001319405.1.
DR   AlphaFoldDB; Q4R7M2; -.
DR   SMR; Q4R7M2; -.
DR   STRING; 9541.XP_005592362.1; -.
DR   MEROPS; M19.004; -.
DR   GeneID; 102124306; -.
DR   CTD; 64180; -.
DR   eggNOG; KOG4127; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
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:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Meiosis; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..463
FT                   /note="Dipeptidase 3"
FT                   /id="PRO_0000231611"
FT   PROPEP          464..488
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P16444"
FT                   /id="PRO_0000231612"
FT   REGION          36..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           463
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        146..225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   DISULFID        297..329
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   DISULFID        434
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
SQ   SEQUENCE   488 AA;  53868 MW;  04E628F0DB30BE6C CRC64;
     MQPTGHEGSR ALSRRHLRRL LLLLLLLLLR QPVTRGETTT GAPRALSTLG FPSPFTTPGV
     PSTLTTPGLT TPGTTKTLDL RSRAQALMRD FPLVDGHNDL PQVLRQRYKN VLQDVNLRNF
     SHSQTSLDRL RDGLVGAQFW SASVSCQTQD QTAVRLALEQ IDLIRRMCAS YSELELVTSA
     EGLNSSQKLA CLIGVEGGHS LDSSLSVLRS FYVLGVRYLT LTFTCNTPWA ESSTKFTHHM
     YTNVSGLTSF GEKVVEELNR LGMMIDLSYA SDTLMRRVLE VSRAPVIFSH SAARAVCDNS
     LNVPDDILQL LKKNGGIVMV TLSMGVLQCN LLANVSTVAD HFDHIRAVIG SEFIGIGGNY
     DGAGRFPQGL EDVSTYPVLI EELLSRSWSE KELQGVLRGN LLRVFRQAEK VREESRAQSP
     MEAEFPYGQL STSCHSHLVP QNGHQATHLE VTKWPTNRVP WRSSDASPYL LPGLVAAATF
     PTVIQWLC