CNDP2_BOVIN
ID CNDP2_BOVIN Reviewed; 475 AA.
AC Q3ZC84;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Cytosolic non-specific dipeptidase;
DE EC=3.4.13.18 {ECO:0000250|UniProtKB:Q96KP4, ECO:0000250|UniProtKB:Q9D1A2};
DE AltName: Full=CNDP dipeptidase 2;
DE AltName: Full=Threonyl dipeptidase {ECO:0000250|UniProtKB:Q9D1A2};
GN Name=CNDP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the peptide bond hydrolysis in dipeptides,
CC displaying a non-redundant activity toward threonyl dipeptides.
CC Mediates threonyl dipeptide catabolism in a tissue-specific way (By
CC similarity). Has high dipeptidase activity toward cysteinylglycine, an
CC intermediate metabolite in glutathione metabolism. Metabolizes N-
CC lactoyl-amino acids, both through hydrolysis to form lactic acid and
CC amino acids, as well as through their formation by reverse proteolysis.
CC Plays a role in the regulation of cell cycle arrest and apoptosis (By
CC similarity). {ECO:0000250|UniProtKB:Q96KP4,
CC ECO:0000250|UniProtKB:Q9D1A2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of dipeptides, preferentially hydrophobic
CC dipeptides including prolyl amino acids.; EC=3.4.13.18;
CC Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-threonyl-L-threonine = 2 L-threonine;
CC Xref=Rhea:RHEA:67360, ChEBI:CHEBI:15377, ChEBI:CHEBI:57926,
CC ChEBI:CHEBI:169953; Evidence={ECO:0000250|UniProtKB:Q9D1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67361;
CC Evidence={ECO:0000250|UniProtKB:Q9D1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-threonyl-L-serine = L-serine + L-threonine;
CC Xref=Rhea:RHEA:67364, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57926, ChEBI:CHEBI:169954;
CC Evidence={ECO:0000250|UniProtKB:Q9D1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67365;
CC Evidence={ECO:0000250|UniProtKB:Q9D1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-seryl-L-threonine = L-serine + L-threonine;
CC Xref=Rhea:RHEA:67372, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57926, ChEBI:CHEBI:169955;
CC Evidence={ECO:0000250|UniProtKB:Q9D1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67373;
CC Evidence={ECO:0000250|UniProtKB:Q9D1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanyl-L-cysteine = L-alanine + L-cysteine;
CC Xref=Rhea:RHEA:67380, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:169958;
CC Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67381;
CC Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + L-phenylalanine = H2O + N-[(S)-lactoyl]-L-
CC phenylalanine; Xref=Rhea:RHEA:66724, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:58095, ChEBI:CHEBI:167456;
CC Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66725;
CC Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66726;
CC Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q96KP4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96KP4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96KP4}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; BC102835; AAI02836.1; -; mRNA.
DR RefSeq; NP_001030280.1; NM_001035108.1.
DR RefSeq; XP_005223983.1; XM_005223926.2.
DR RefSeq; XP_005223984.1; XM_005223927.3.
DR AlphaFoldDB; Q3ZC84; -.
DR SMR; Q3ZC84; -.
DR STRING; 9913.ENSBTAP00000031070; -.
DR MEROPS; M20.005; -.
DR PaxDb; Q3ZC84; -.
DR PeptideAtlas; Q3ZC84; -.
DR PRIDE; Q3ZC84; -.
DR Ensembl; ENSBTAT00000031107; ENSBTAP00000031070; ENSBTAG00000009841.
DR GeneID; 512626; -.
DR KEGG; bta:512626; -.
DR CTD; 55748; -.
DR VEuPathDB; HostDB:ENSBTAG00000009841; -.
DR VGNC; VGNC:27494; CNDP2.
DR eggNOG; KOG2276; Eukaryota.
DR GeneTree; ENSGT00940000156500; -.
DR HOGENOM; CLU_029469_3_1_1; -.
DR InParanoid; Q3ZC84; -.
DR OMA; HITIPGF; -.
DR OrthoDB; 733473at2759; -.
DR TreeFam; TF300633; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000009841; Expressed in cortex of kidney and 105 other tissues.
DR ExpressionAtlas; Q3ZC84; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0103046; F:alanylglutamate dipeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016805; F:dipeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR017153; CNDP/DUG1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Carboxypeptidase; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome.
FT CHAIN 1..475
FT /note="Cytosolic non-specific dipeptidase"
FT /id="PRO_0000284970"
FT ACT_SITE 101
FT /evidence="ECO:0000250"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96KP4"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96KP4"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96KP4"
FT BINDING 166..167
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96KP4"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96KP4"
FT BINDING 195
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96KP4"
FT BINDING 445
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT SITE 228
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96KP4"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Q0N1"
SQ SEQUENCE 475 AA; 52655 MW; A8A6CEEC0D06B477 CRC64;
MSALTTLFKY VDENQDRYVK KLAEWVAIQS VSAWPEKRGE IRRMMEVAAA DIKQLGGSVQ
LVDIGTQKLP DGSEIPLPPI LLGKLGSDPQ KKTVCIYGHL DVQPAALEDG WDSEPFTLVE
RDGKLFGRGA TDDKGPVAGW INALEAFQKT KQEVPVNVRF CLEGMEESGS EGLDALIFAQ
KDAFFKDVDY VCISDNYWLG KNKPCITYGL RGICYFFIEV ECSDKDLHSG VYGGSVHEAM
TDLIMLMGCL MDKKGKILIP GISEAVAPVT EEELELYDKI DFDLEEYARD VGAGTLLHGC
KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPNMTP EVVSEQVTSY
LTKKFAELHS PNKFKVYMGH GGKPWVSDFN HPHYLAGRRA LKTVFGVEPD LTREGGSIPV
TLTFQEATGK NVMLLPVGSA DDGAHSQNEK LNRRNYIEGT KMLAAYLYEV SQLKD
