CNDP1_RAT
ID CNDP1_RAT Reviewed; 492 AA.
AC Q66HG3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Beta-Ala-His dipeptidase;
DE EC=3.4.13.20 {ECO:0000250|UniProtKB:Q8BUG2, ECO:0000250|UniProtKB:Q96KN2};
DE AltName: Full=CNDP dipeptidase 1;
DE AltName: Full=Carnosine dipeptidase 1;
GN Name=Cndp1; Synonyms=Cn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=12473676; DOI=10.1074/jbc.m209764200;
RA Teufel M., Saudek V., Ledig J.P., Bernhardt A., Boularand S., Carreau A.,
RA Cairns N.J., Carter C., Cowley D.J., Duverger D., Ganzhorn A.J., Guenet C.,
RA Heintzelmann B., Laucher V., Sauvage C., Smirnova T.;
RT "Sequence identification and characterization of human carnosinase and a
RT closely related non-specific dipeptidase.";
RL J. Biol. Chem. 278:6521-6531(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Catalyzes the peptide bond hydrolysis in Xaa-His dipeptides,
CC displaying the highest activity toward carnosine (beta-alanyl-L-
CC histidine) and anserine (beta-alanyl-3-methyl-histidine).
CC {ECO:0000250|UniProtKB:Q96KN2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential hydrolysis of the beta-Ala-|-His dipeptide
CC (carnosine), and also anserine, Xaa-|-His dipeptides and other
CC dipeptides including homocarnosine.; EC=3.4.13.20;
CC Evidence={ECO:0000250|UniProtKB:Q8BUG2,
CC ECO:0000250|UniProtKB:Q96KN2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carnosine + H2O = beta-alanine + L-histidine;
CC Xref=Rhea:RHEA:59360, ChEBI:CHEBI:15377, ChEBI:CHEBI:57485,
CC ChEBI:CHEBI:57595, ChEBI:CHEBI:57966; EC=3.4.13.20;
CC Evidence={ECO:0000250|UniProtKB:Q8BUG2,
CC ECO:0000250|UniProtKB:Q96KN2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59361;
CC Evidence={ECO:0000250|UniProtKB:Q8BUG2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=anserine + H2O = beta-alanine + N(pros)-methyl-L-histidine;
CC Xref=Rhea:RHEA:59576, ChEBI:CHEBI:15377, ChEBI:CHEBI:57966,
CC ChEBI:CHEBI:58445, ChEBI:CHEBI:143076; EC=3.4.13.20;
CC Evidence={ECO:0000250|UniProtKB:Q96KN2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59577;
CC Evidence={ECO:0000250|UniProtKB:Q96KN2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanyl-L-histidine = L-alanine + L-histidine;
CC Xref=Rhea:RHEA:37283, ChEBI:CHEBI:15377, ChEBI:CHEBI:57595,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:74388;
CC Evidence={ECO:0000250|UniProtKB:Q96KN2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37284;
CC Evidence={ECO:0000250|UniProtKB:Q96KN2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-L-histidine + H2O = glycine + L-histidine;
CC Xref=Rhea:RHEA:67376, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57595, ChEBI:CHEBI:169956;
CC Evidence={ECO:0000250|UniProtKB:Q96KN2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67377;
CC Evidence={ECO:0000250|UniProtKB:Q96KN2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-homocarnosine = 4-aminobutanoate + L-histidine;
CC Xref=Rhea:RHEA:59572, ChEBI:CHEBI:15377, ChEBI:CHEBI:57595,
CC ChEBI:CHEBI:59888, ChEBI:CHEBI:143075; EC=3.4.13.20;
CC Evidence={ECO:0000250|UniProtKB:Q96KN2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59573;
CC Evidence={ECO:0000250|UniProtKB:Q96KN2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q96KN2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96KN2};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96KN2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q96KN2}.
CC -!- TISSUE SPECIFICITY: Detected exclusively in kidney.
CC {ECO:0000269|PubMed:12473676}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
CC -!- CAUTION: In contrast to human counterpart, it lacks a signal sequence.
CC {ECO:0000305}.
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DR EMBL; BC081877; AAH81877.1; -; mRNA.
DR RefSeq; NP_001007688.1; NM_001007687.1.
DR RefSeq; XP_006255071.1; XM_006255009.3.
DR RefSeq; XP_008770357.1; XM_008772135.2.
DR AlphaFoldDB; Q66HG3; -.
DR SMR; Q66HG3; -.
DR STRING; 10116.ENSRNOP00000034652; -.
DR MEROPS; M20.006; -.
DR iPTMnet; Q66HG3; -.
DR PhosphoSitePlus; Q66HG3; -.
DR PaxDb; Q66HG3; -.
DR Ensembl; ENSRNOT00000034970; ENSRNOP00000034652; ENSRNOG00000027739.
DR GeneID; 307212; -.
DR KEGG; rno:307212; -.
DR CTD; 84735; -.
DR RGD; 1359493; Cndp1.
DR eggNOG; KOG2276; Eukaryota.
DR GeneTree; ENSGT00940000160484; -.
DR HOGENOM; CLU_029469_3_1_1; -.
DR InParanoid; Q66HG3; -.
DR OMA; PMNAIPG; -.
DR OrthoDB; 733473at2759; -.
DR PhylomeDB; Q66HG3; -.
DR TreeFam; TF300633; -.
DR PRO; PR:Q66HG3; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000027739; Expressed in adult mammalian kidney and 17 other tissues.
DR Genevisible; Q66HG3; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016805; F:dipeptidase activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; ISO:RGD.
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 1: Evidence at protein level;
KW Carboxypeptidase; Hydrolase; Metal-binding; Metalloprotease;
KW Phosphoprotein; Protease; Reference proteome; Secreted; Zinc.
FT CHAIN 1..492
FT /note="Beta-Ala-His dipeptidase"
FT /id="PRO_0000250531"
FT ACT_SITE 109
FT /evidence="ECO:0000250"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96KN2"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96KN2"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96KN2"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96KN2"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96KN2"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96KN2"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
SQ SEQUENCE 492 AA; 54928 MW; EF8DAE8C15BF06F5 CRC64;
MLSPPHSGTL EKLFQYIDLH QDEFVQTLKE WVAIESDSVQ PMPRLRQELF RMMALAADKL
RNLGARVDSV DLGSQQMPDG QSLPTPPIIL AELGNDPKKP SVCFYGHLDV QPAQKEDGWL
TDPYTLTEVD GKLYGRGATD NKGPVLAWIN AVSTFRALQQ DLPVNVKFIL EGMEEAGSVA
LEELVKREKD NFFSGVDYIV ISDNLWLSQK KPALTCGTRG NCYFTVEVKC RDQDFHSGTF
GGILNEPMAD LVALLGSLVD SSGHILVPGI YDQMAPITEE EKTMYENIDL DLEEYQKSSR
VERFLFDTKE ELLTHLWRYP SLSIHGIEGA FDEPGTKTVI PGRVLGKFSI RLVPHMTPSV
VETQVTQHLE AVFSKRNSFN KMAVSMVLGL QPWTANINGT QYLAARRAIQ TVFGVDPDMI
QDGSTIPIAK IFQDITQKSV MMLPLGAVDD GEHSQNEKIN RWNYIQGSKL FAAFFLELSK
LHSGQQVPSG AF
