ID   DPEP3_HUMAN             Reviewed;         488 AA.
AC   Q9H4B8; B3KQ48; Q6PEZ5; Q6UXE4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Dipeptidase 3;
DE   Flags: Precursor;
GN   Name=DPEP3; ORFNames=UNQ834/PRO1772;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Chen J.M., Fortunato M., Barrett A.J.;
RT   "Cloning and sequencing of a second human homologue of renal membrane
RT   dipeptidase.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS), ABSENCE OF DIPEPTIDASE ACTIVITY,
RP   SUBUNIT, AND MUTAGENESIS OF GLU-196.
RX   PubMed=32325220; DOI=10.1016/j.jsb.2020.107512;
RA   Hayashi K., Longenecker K.L., Koenig P., Prashar A., Hampl J., Stoll V.,
RA   Vivona S.;
RT   "Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment
RT   reveals basis for lack of dipeptidase activity.";
RL   J. Struct. Biol. 211:107512-107512(2020).
CC   -!- FUNCTION: Lacks dipeptidase activity and is unable to hydrolyze
CC       cystinyl-bis-glycine, leukotriene D4 and the beta-lactam antibiotic
CC       imipenem (PubMed:32325220). 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 (PubMed:32325220). A tyrosine (instead of
CC       histidine) at position 269 reduces affinity for the beta zinc and may
CC       cause substrate steric hindrance (PubMed:32325220).
CC       {ECO:0000269|PubMed:32325220}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:32325220). 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       ECO:0000269|PubMed:32325220}.
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=AAH57789.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAG51910.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAC15385.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAW83198.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ291679; CAC15385.1; ALT_INIT; mRNA.
DR   EMBL; AY358390; AAQ88756.1; -; mRNA.
DR   EMBL; AK057401; BAG51910.1; ALT_INIT; mRNA.
DR   EMBL; AC040162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471092; EAW83198.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC057789; AAH57789.1; ALT_INIT; mRNA.
DR   CCDS; CCDS10856.2; -.
DR   RefSeq; NP_001123230.1; NM_001129758.1.
DR   RefSeq; NP_071752.3; NM_022357.3.
DR   PDB; 6VGO; X-ray; 1.82 A; A=1-488.
DR   PDB; 6VGR; X-ray; 2.84 A; A/B=1-488.
DR   PDBsum; 6VGO; -.
DR   PDBsum; 6VGR; -.
DR   AlphaFoldDB; Q9H4B8; -.
DR   SMR; Q9H4B8; -.
DR   BioGRID; 122099; 17.
DR   IntAct; Q9H4B8; 5.
DR   STRING; 9606.ENSP00000500237; -.
DR   MEROPS; M19.004; -.
DR   GlyCosmos; Q9H4B8; 1 site, No reported glycans.
DR   GlyGen; Q9H4B8; 1 site.
DR   iPTMnet; Q9H4B8; -.
DR   PhosphoSitePlus; Q9H4B8; -.
DR   BioMuta; DPEP3; -.
DR   DMDM; 91206587; -.
DR   EPD; Q9H4B8; -.
DR   jPOST; Q9H4B8; -.
DR   MassIVE; Q9H4B8; -.
DR   PaxDb; 9606-ENSP00000268793; -.
DR   PeptideAtlas; Q9H4B8; -.
DR   ProteomicsDB; 80820; -.
DR   ABCD; Q9H4B8; 44 sequenced antibodies.
DR   Antibodypedia; 54982; 109 antibodies from 17 providers.
DR   DNASU; 64180; -.
DR   Ensembl; ENST00000268793.6; ENSP00000268793.5; ENSG00000141096.6.
DR   GeneID; 64180; -.
DR   KEGG; hsa:64180; -.
DR   MANE-Select; ENST00000268793.6; ENSP00000268793.5; NM_001370198.1; NP_001357127.1.
DR   UCSC; uc002evc.5; human.
DR   AGR; HGNC:23029; -.
DR   CTD; 64180; -.
DR   DisGeNET; 64180; -.
DR   GeneCards; DPEP3; -.
DR   HGNC; HGNC:23029; DPEP3.
DR   HPA; ENSG00000141096; Tissue enriched (testis).
DR   MIM; 609926; gene.
DR   neXtProt; NX_Q9H4B8; -.
DR   OpenTargets; ENSG00000141096; -.
DR   PharmGKB; PA134978786; -.
DR   VEuPathDB; HostDB:ENSG00000141096; -.
DR   eggNOG; KOG4127; Eukaryota.
DR   GeneTree; ENSGT00940000162331; -.
DR   HOGENOM; CLU_031404_4_1_1; -.
DR   InParanoid; Q9H4B8; -.
DR   OMA; SRHNVFG; -.
DR   OrthoDB; 5476406at2759; -.
DR   PhylomeDB; Q9H4B8; -.
DR   TreeFam; TF324523; -.
DR   PathwayCommons; Q9H4B8; -.
DR   Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR   Reactome; R-HSA-9664535; LTC4-CYSLTR mediated IL4 production.
DR   SignaLink; Q9H4B8; -.
DR   BioGRID-ORCS; 64180; 14 hits in 1148 CRISPR screens.
DR   GeneWiki; DPEP3; -.
DR   GenomeRNAi; 64180; -.
DR   Pharos; Q9H4B8; Tbio.
DR   PRO; PR:Q9H4B8; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9H4B8; Protein.
DR   Bgee; ENSG00000141096; Expressed in right testis and 90 other cell types or tissues.
DR   ExpressionAtlas; Q9H4B8; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016805; F:dipeptidase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:Ensembl.
DR   CDD; cd01301; rDP_like; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR000180; Dipep_AS.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008257; Pept_M19.
DR   PANTHER; PTHR10443:SF14; DIPEPTIDASE 3; 1.
DR   PANTHER; PTHR10443; MICROSOMAL DIPEPTIDASE; 1.
DR   Pfam; PF01244; Peptidase_M19; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1.
DR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
DR   Genevisible; Q9H4B8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..463
FT                   /note="Dipeptidase 3"
FT                   /id="PRO_0000231609"
FT   PROPEP          464..488
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P16444"
FT                   /id="PRO_0000231610"
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"
FT   MUTAGEN         196
FT                   /note="E->A: Loss of zinc binding."
FT                   /evidence="ECO:0000269|PubMed:32325220"
FT   CONFLICT        48
FT                   /note="Missing (in Ref. 6; AAH57789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="Missing (in Ref. 2; AAQ88756)"
FT                   /evidence="ECO:0000305"
FT   HELIX           79..90
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           100..108
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           127..132
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          135..143
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   TURN            149..152
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           153..170
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           180..185
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          187..196
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           198..201
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           205..213
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          216..221
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           249..261
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           272..281
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          287..291
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   TURN            294..296
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           305..314
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   TURN            324..329
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           335..348
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           351..353
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   STRAND          362..364
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           373..375
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           376..385
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           390..397
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   HELIX           399..414
FT                   /evidence="ECO:0007829|PDB:6VGO"
FT   TURN            415..417
FT                   /evidence="ECO:0007829|PDB:6VGO"
SQ   SEQUENCE   488 AA;  53687 MW;  F14FEE5AFB3F4471 CRC64;
     MQPTGREGSR ALSRRYLRRL LLLLLLLLLR QPVTRAETTP GAPRALSTLG SPSLFTTPGV
     PSALTTPGLT TPGTPKTLDL RGRAQALMRS FPLVDGHNDL PQVLRQRYKN VLQDVNLRNF
     SHGQTSLDRL RDGLVGAQFW SASVSCQSQD QTAVRLALEQ IDLIHRMCAS YSELELVTSA
     EGLNSSQKLA CLIGVEGGHS LDSSLSVLRS FYVLGVRYLT LTFTCSTPWA ESSTKFRHHM
     YTNVSGLTSF GEKVVEELNR LGMMIDLSYA SDTLIRRVLE VSQAPVIFSH SAARAVCDNL
     LNVPDDILQL LKKNGGIVMV TLSMGVLQCN LLANVSTVAD HFDHIRAVIG SEFIGIGGNY
     DGTGRFPQGL EDVSTYPVLI EELLSRSWSE EELQGVLRGN LLRVFRQVEK VREESRAQSP
     VEAEFPYGQL STSCHSHLVP QNGHQATHLE VTKQPTNRVP WRSSNASPYL VPGLVAAATI
     PTFTQWLC
//