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Dipeptidase 1 (EC 3.4.13.19) (Microsomal dipeptidase) (Renal dipeptidase)

 DPEP1_PIG               Reviewed;         409 AA.
P22412;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
05-DEC-2018, entry version 135.
RecName: Full=Dipeptidase 1;
EC=3.4.13.19;
AltName: Full=Microsomal dipeptidase;
AltName: Full=Renal dipeptidase;
Flags: Precursor;
Name=DPEP1; Synonyms=RDP;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
GLYCOSYLATION AT ASN-57.
TISSUE=Kidney cortex;
PubMed=2173907; DOI=10.1042/bj2710755;
Rached E., Hooper N.M., James P., Semenza G., Turner A.J., Mantei N.;
"cDNA cloning and expression in Xenopus laevis oocytes of pig renal
dipeptidase, a glycosyl-phosphatidylinositol-anchored ectoenzyme.";
Biochem. J. 271:755-760(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Satoh S., Koyama S., Ohtuka K., Keida Y., Niwa M., Kohsaka M.;
"Purification and cDNA cloning for porcine renal dipeptidase.";
Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 17-39.
PubMed=2137335; DOI=10.1042/bj2650429;
Hooper N.M., Keen J.N., Turner A.J.;
"Characterization of the glycosyl-phosphatidylinositol-anchored human
renal dipeptidase reveals that it is more extensively glycosylated
than the pig enzyme.";
Biochem. J. 265:429-433(1990).
[4]
INTERCHAIN DISULFIDE BOND.
PubMed=8823187; DOI=10.1021/bi961193z;
Keynan S., Habgood N.T., Hooper N.M., Turner A.J.;
"Site-directed mutagenesis of conserved cysteine residues in porcine
membrane dipeptidase. Cys-361 alone is involved in disulfide-linked
dimerization.";
Biochemistry 35:12511-12517(1996).
[5]
GPI-ANCHOR AT SER-384, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16689534; DOI=10.1021/ac0517949;
Omaetxebarria M.J., Hagglund P., Elortza F., Hooper N.M.,
Arizmendi J.M., Jensen O.N.;
"Isolation and characterization of glycosylphosphatidylinositol-
anchored peptides by hydrophilic interaction chromatography and MALDI
tandem mass spectrometry.";
Anal. Chem. 78:3335-3341(2006).
-!- FUNCTION: Hydrolyzes a wide range of dipeptides. Implicated in the
renal metabolism of glutathione and its conjugates. Converts
leukotriene D4 to leukotriene E4; it may play an important role in
the regulation of leukotriene activity.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of dipeptides.; EC=3.4.13.19;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10073};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
-!- ACTIVITY REGULATION: Inhibited by L-penicillamine. {ECO:0000250}.
-!- SUBUNIT: Homodimer; disulfide-linked.
-!- SUBCELLULAR LOCATION: Apical cell membrane; Lipid-anchor, GPI-
anchor. Cell projection, microvillus membrane; Lipid-anchor, GPI-
anchor. Note=Brush border membrane.
-!- SIMILARITY: Belongs to the metallo-dependent hydrolases
superfamily. Peptidase M19 family. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
-----------------------------------------------------------------------
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EMBL; X53730; CAA37762.1; -; mRNA.
EMBL; D13142; BAA02433.1; -; mRNA.
PIR; JS0759; JS0759.
RefSeq; NP_999273.1; NM_214108.1.
UniGene; Ssc.315; -.
ProteinModelPortal; P22412; -.
SMR; P22412; -.
STRING; 9823.ENSSSCP00000019823; -.
BindingDB; P22412; -.
ChEMBL; CHEMBL2626; -.
MEROPS; M19.001; -.
iPTMnet; P22412; -.
PaxDb; P22412; -.
PeptideAtlas; P22412; -.
PRIDE; P22412; -.
GeneID; 397196; -.
KEGG; ssc:397196; -.
CTD; 1800; -.
eggNOG; KOG4127; Eukaryota.
eggNOG; COG2355; LUCA.
HOVERGEN; HBG002339; -.
InParanoid; P22412; -.
KO; K01273; -.
BioCyc; MetaCyc:MONOMER-9981; -.
PRO; PR:P22412; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:InterPro.
GO; GO:0034235; F:GPI anchor binding; IDA:UniProtKB.
GO; GO:0070573; F:metallodipeptidase activity; ISS:UniProtKB.
GO; GO:0072341; F:modified amino acid binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0016999; P:antibiotic metabolic process; ISS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
GO; GO:0071732; P:cellular response to nitric oxide; IDA:UniProtKB.
GO; GO:0006507; P:GPI anchor release; IDA:UniProtKB.
GO; GO:0050667; P:homocysteine metabolic process; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
CDD; cd01301; rDP_like; 1.
InterPro; IPR000180; Dipep_AS.
InterPro; IPR028536; Dpep1.
InterPro; IPR032466; Metal_Hydrolase.
InterPro; IPR008257; Pept_M19.
PANTHER; PTHR10443; PTHR10443; 1.
PANTHER; PTHR10443:SF12; PTHR10443:SF12; 1.
Pfam; PF01244; Peptidase_M19; 1.
SUPFAM; SSF51556; SSF51556; 1.
PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1.
PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
1: Evidence at protein level;
Cell membrane; Cell projection; Complete proteome; Dipeptidase;
Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease;
Protease; Reference proteome; Signal; Zinc.
SIGNAL 1 16 {ECO:0000269|PubMed:2137335}.
CHAIN 17 384 Dipeptidase 1.
/FTId=PRO_0000018656.
PROPEP 385 409 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000018657.
METAL 36 36 Zinc 1; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
METAL 38 38 Zinc 1; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
METAL 141 141 Zinc 1; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
METAL 141 141 Zinc 2; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
METAL 214 214 Zinc 2; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
METAL 235 235 Zinc 2; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
BINDING 168 168 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
BINDING 246 246 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
BINDING 304 304 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
LIPID 384 384 GPI-anchor amidated serine.
{ECO:0000269|PubMed:16689534}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2173907}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 87 170 {ECO:0000255|PROSITE-ProRule:PRU10073}.
DISULFID 242 274 {ECO:0000255|PROSITE-ProRule:PRU10073}.
DISULFID 377 377 Interchain.
SEQUENCE 409 AA; 44700 MW; 926B7F0044FA055F CRC64;
MWTSWWLWPL VAVCAADQFR DLAVRIMQDT PVIDGHNDLP WQLLNLFNNQ LQDPGANLSS
LAHTHTNIPK LKAGFVGGQF WSAYVPCDTQ NRDAVKRTLE QIDVIQRMCQ AYPETFACVT
SSTGIRQAFR EGKVASLVGV EGGHSIDSSL GVLRALYHLG MRYMTLTHSC NTPWADNWLV
DTGDDKAQSQ GLSHFGQSVV KEMNRLGVMI DLAHVSVATM RAALKLSQAP VIFSHSSAYS
LCPHRRNVPD DVLQLVKETG SLVMVNFYND YVSCSAKANL SQVADHLDHI KKVAGAAAVG
FGGDYDGVSR VPSGLEDVSK YPDLVAELLR RQWTEAEVRG ALADNLLRVF EAVEQASNHA
QVPGEEPIPL GQLEASCRTN YGYSAAPSLH LPPGSLLASL VPLLLLSLP


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