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Dipeptidase 1 (EC 3.4.13.19) (Microsomal dipeptidase)

 DPEP1_SHEEP             Reviewed;         410 AA.
P43477;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 108.
RecName: Full=Dipeptidase 1;
EC=3.4.13.19;
AltName: Full=Microsomal dipeptidase;
Flags: Precursor;
Name=DPEP1;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-56, FUNCTION, AND
TISSUE SPECIFICITY.
TISSUE=Lung;
PubMed=8054366; DOI=10.1016/0925-4439(94)90046-9;
An S., Schmidt F.J., Campbell B.J.;
"Molecular cloning of sheep lung dipeptidase: a glycosyl
phosphatidylinositol-anchored ectoenzyme that converts leukotriene D4
to leukotriene E4.";
Biochim. Biophys. Acta 1226:337-340(1994).
-!- 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. In lung tissue, it may
terminate or significantly reduce the leukotriene induced signal
for bronchospasm. {ECO:0000269|PubMed:8054366}.
-!- CATALYTIC ACTIVITY: Hydrolysis of dipeptides.
{ECO:0000255|PROSITE-ProRule:PRU10073}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
-!- ENZYME 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.
-!- TISSUE SPECIFICITY: Expressed in lung, kidney and intestinal
tissues. {ECO:0000269|PubMed:8054366}.
-!- SIMILARITY: Belongs to the metallo-dependent hydrolases
superfamily. Peptidase M19 family. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
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EMBL; L27113; AAA21725.1; -; mRNA.
ProteinModelPortal; P43477; -.
SMR; P43477; -.
MEROPS; M19.001; -.
HOVERGEN; HBG002339; -.
Proteomes; UP000002356; 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:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS: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; ISS: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; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0071732; P:cellular response to nitric oxide; ISS: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:0000250}.
CHAIN 17 384 Dipeptidase 1.
/FTId=PRO_0000018662.
PROPEP 385 410 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000018663.
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:0000250}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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. {ECO:0000255|PROSITE-
ProRule:PRU10073}.
CONFLICT 42 42 A -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
SEQUENCE 410 AA; 45096 MW; AA818C8B8BB91F31 CRC64;
MWTGWWLWPL VAVCTADQFR DNAVRLMQST PVIDGHNDLP WALLKKFNNQ LQDPRANLTS
LNSTHTNIPK LKAGFVGAQF WSAYTPCDTQ NKDSVKRTVE QIDVIQRMCQ LYPETFLCVT
DSAGIQQAFQ EGKVASLVGV EGGHSIDSSL GVLRALYHLG MRYLTLTHSC NTPWADNWLV
DTGEDKAQSQ GLSSFGQSVV KEMNRLGIII DLAHVSVATM EAALQLSKAP VIFSHSSAYS
LCHHRRNVPD HVLQLVKQTG SLVMVNFYND YVSCKAEANL SQVADHLDYI KKVAGAGAVG
FGGDYDGVSR LPSGLEDVSK YPDLVAELLR RQWTEEEVRG ALAENLLRVF KAVEQASDHK
QAPGEEPIPL GQLEASCRTK YGYSGTPSLH LQPGSLLASL VTLLLSLCLL


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