ID H3BQS5_HUMAN Unreviewed; 107 AA. AC H3BQS5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 16-JAN-2019, 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=DPEP1 {ECO:0000313|Ensembl:ENSP00000455916}; 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:ENSP00000455916, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000455916, 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:ENSP00000455916} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-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; AC010538; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR jPOST; H3BQS5; -. DR PeptideAtlas; H3BQS5; -. DR PRIDE; H3BQS5; -. DR Ensembl; ENST00000570029; ENSP00000455916; ENSG00000015413. DR UCSC; uc059ypk.1; human. DR EuPathDB; HostDB:ENSG00000015413.9; -. DR HGNC; HGNC:3002; DPEP1. DR OpenTargets; ENSG00000015413; -. DR eggNOG; KOG4127; Eukaryota. DR eggNOG; COG2355; LUCA. DR GeneTree; ENSGT00940000159615; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000015413; Expressed in 101 organ(s), highest expression level in small intestine Peyer's patch. DR ExpressionAtlas; H3BQS5; 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; IPR028536; Dpep1. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR008257; Pept_M19. DR PANTHER; PTHR10443; PTHR10443; 1. DR PANTHER; PTHR10443:SF12; PTHR10443:SF12; 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|PeptideAtlas:H3BQS5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|RuleBase:RU341113}; KW Zinc {ECO:0000256|RuleBase:RU341113}. FT SIGNAL 1 16 {ECO:0000256|RuleBase:RU341113}. FT CHAIN 17 107 Dipeptidase. FT {ECO:0000256|RuleBase:RU341113}. FT /FTId=PRO_5005134184. FT NON_TER 107 107 {ECO:0000313|Ensembl:ENSP00000455916}. SQ SEQUENCE 107 AA; 12491 MW; 65D8F440083CBE72 CRC64; MWSGWWLWPL VAVCTADFFR DEAERIMRDS PVIDGHNDLP WQLLDMFNNR LQDERANLTT LAGTHTNIPK LRAGFVGGQF WSVYTPCDTQ NKDAVRRTLE QMDVVHR //