ID J3QLL2_HUMAN Unreviewed; 161 AA. AC J3QLL2; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 2. DT 05-DEC-2018, entry version 41. 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:ENSP00000463604}; 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:ENSP00000463604, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000463604, 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:ENSP00000463604} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-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; J3QLL2; -. DR PeptideAtlas; J3QLL2; -. DR PRIDE; J3QLL2; -. DR Ensembl; ENST00000573808; ENSP00000463604; ENSG00000167261. DR UCSC; uc059wcb.1; human. DR EuPathDB; HostDB:ENSG00000167261.13; -. DR HGNC; HGNC:23028; DPEP2. DR OpenTargets; ENSG00000167261; -. DR GeneTree; ENSGT00940000160211; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000167261; Expressed in 125 organ(s), highest expression level in blood. DR ExpressionAtlas; J3QLL2; 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:0008239; F:dipeptidyl-peptidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro. DR InterPro; IPR000180; Dipep_AS. 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; PS00869; RENAL_DIPEPTIDASE_1; 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:J3QLL2, KW ECO:0000213|PeptideAtlas:J3QLL2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|RuleBase:RU341113}; KW Zinc {ECO:0000256|RuleBase:RU341113}. FT SIGNAL 1 18 {ECO:0000256|RuleBase:RU341113}. FT CHAIN 19 161 Dipeptidase. FT {ECO:0000256|RuleBase:RU341113}. FT /FTId=PRO_5005136804. FT NON_TER 161 161 {ECO:0000313|Ensembl:ENSP00000463604}. SQ SEQUENCE 161 AA; 17802 MW; CE136738E45B2C5D CRC64; MKLQTLAVSV TALKFWSAYV PCQTQDRDAL RLTLEQIDLI RRMCASYSEL ELVTSAKALN DTQKLACLIG VEGGHSLDNS LSILRTFYML GVRYLTLTHT CNTPWAESSA KGVHSFYNNI SGLTDFGEKV VAEMNRLGMM VDLSHVSDAV ARRALEVSQA P //