ID I3L348_HUMAN Unreviewed; 137 AA. AC I3L348; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 05-DEC-2018, entry version 42. DE RecName: Full=Dipeptidase {ECO:0000256|RuleBase:RU341113}; DE EC=3.4.13.19 {ECO:0000256|RuleBase:RU341113}; DE Flags: Fragment; GN Name=DPEP2 {ECO:0000313|Ensembl:ENSP00000460169}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000460169, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000460169, ECO:0000313|Proteomes:UP000005640} 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., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA 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., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000460169} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of dipeptides.; EC=3.4.13.19; CC Evidence={ECO:0000256|RuleBase:RU341113}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU341113}; CC -!- SUBUNIT: Homodimer; disulfide-linked. CC {ECO:0000256|RuleBase:RU341113}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU341113}; CC Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU341113}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases CC superfamily. Peptidase M19 family. CC {ECO:0000256|RuleBase:RU341113}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC040162; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877614; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3L348; -. DR PeptideAtlas; I3L348; -. DR PRIDE; I3L348; -. DR Ensembl; ENST00000572624; ENSP00000460169; ENSG00000167261. DR UCSC; uc059wcd.1; human. DR EuPathDB; HostDB:ENSG00000167261.13; -. DR HGNC; HGNC:23028; DPEP2. DR OpenTargets; ENSG00000167261; -. DR eggNOG; KOG4127; Eukaryota. DR eggNOG; COG2355; LUCA. DR GeneTree; ENSGT00940000160211; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000167261; Expressed in 125 organ(s), highest expression level in blood. DR ExpressionAtlas; I3L348; baseline and differential. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR028531; Dpep2. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR008257; Pept_M19. DR PANTHER; PTHR10443; PTHR10443; 1. DR PANTHER; PTHR10443:SF9; PTHR10443:SF9; 1. DR Pfam; PF01244; Peptidase_M19; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Dipeptidase {ECO:0000256|RuleBase:RU341113}; KW Disulfide bond {ECO:0000256|RuleBase:RU341113}; KW Glycoprotein {ECO:0000256|RuleBase:RU341113}; KW GPI-anchor {ECO:0000256|RuleBase:RU341113}; KW Hydrolase {ECO:0000256|RuleBase:RU341113}; KW Lipoprotein {ECO:0000256|RuleBase:RU341113}; KW Membrane {ECO:0000256|RuleBase:RU341113}; KW Metal-binding {ECO:0000256|RuleBase:RU341113}; KW Metalloprotease {ECO:0000256|RuleBase:RU341113}; KW Protease {ECO:0000256|RuleBase:RU341113}; KW Proteomics identification {ECO:0000213|MaxQB:I3L348, KW ECO:0000213|PeptideAtlas:I3L348}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|RuleBase:RU341113}; KW Zinc {ECO:0000256|RuleBase:RU341113}. FT SIGNAL 1 32 {ECO:0000256|RuleBase:RU341113}. FT CHAIN 33 137 Dipeptidase. FT {ECO:0000256|RuleBase:RU341113}. FT /FTId=PRO_5009031251. FT NON_TER 137 137 {ECO:0000313|Ensembl:ENSP00000460169}. SQ SEQUENCE 137 AA; 14933 MW; 985B05B0B4FECB3A CRC64; MQPSGLEGPG TFGRWPLLSL LLLLLLLQPV TCAYTTPGPP RALTTLGAPR AHTMPGTYAP STTLSSPSTQ GLQEQARALM RDFPLVDGHN DLPLVLRQVY QKGLQDVNLR NFSYGQTSLD RLRDGLVGAQ FWSAYVP //