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Database: UniProt
Entry: A0A1D5RC16_MACMU
LinkDB: A0A1D5RC16_MACMU
Original site: A0A1D5RC16_MACMU 
ID   A0A1D5RC16_MACMU        Unreviewed;       512 AA.
AC   A0A1D5RC16;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Carnosine dipeptidase 1 {ECO:0000313|Ensembl:ENSMMUP00000057858.2};
GN   Name=CNDP1 {ECO:0000313|Ensembl:ENSMMUP00000057858.2,
GN   ECO:0000313|VGNC:VGNC:71257};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000057858.2, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000057858.2}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000057858.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037242-3};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR037242-3};
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   AlphaFoldDB; A0A1D5RC16; -.
DR   SMR; A0A1D5RC16; -.
DR   STRING; 9544.ENSMMUP00000057858; -.
DR   Ensembl; ENSMMUT00000075995.2; ENSMMUP00000057858.2; ENSMMUG00000008942.4.
DR   VEuPathDB; HostDB:ENSMMUG00000008942; -.
DR   VGNC; VGNC:71257; CNDP1.
DR   GeneTree; ENSGT00940000160484; -.
DR   InParanoid; A0A1D5RC16; -.
DR   OMA; CKGNIVM; -.
DR   Proteomes; UP000006718; Chromosome 18.
DR   Bgee; ENSMMUG00000008942; Expressed in adult mammalian kidney and 22 other cell types or tissues.
DR   ExpressionAtlas; A0A1D5RC16; baseline.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:Ensembl.
DR   CDD; cd05676; M20_dipept_like_CNDP; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR017153; CNDP/DUG1.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF1; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|PIRSR:PIRSR037242-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037242-3};
KW   Protease {ECO:0000256|ARBA:ARBA00022645};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..512
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023893739"
FT   DOMAIN          247..404
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT   BINDING         137
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         205
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         233
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         483
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   SITE            266
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-4"
SQ   SEQUENCE   512 AA;  57135 MW;  EC2869A93937AD25 CRC64;
     MGLRSGAITR WRLTAASLLA LLLLLEGGMF SSHSLPPALL EKVFQYIDLH QDEFVQTLKE
     WVAIESDSVQ PVPRFRQELF RMMAVAADTL QRLGARVTSV DMGSQQLPDG QSLPIPPVIL
     AELGNDPTKG TVCFYGHLDV QPADQGDGWL TDPYVLTEVD GKLYGRGATD NKGPVLAWIN
     AVSAFRALEQ DLPVNIKFII EGMEEAGSVA LEELVEKEKN RFFSGVDYIV ISDNLWISQR
     KPAITYGTRG NSYFTVEVKC RDQDFHSGTF GGILHEPMAD LVALLGSLVD SSGHILVPGI
     YDEVAPLTEE EINTYKAIHL DLEEYRNSSR VEKFLFDTKE EILMHLWRYP SLSIHGIEGA
     FDEPGAKTVI PGQVIGKFSI RLVPHMNVSV VEKQVTRHLE DVFSKRNSSN KMVVSMTLGL
     HPWIANVNDT QYLAAKRAIR TVFGTEPDMI RDGSTIPIAK MFQEIVHKSV VLIPLGAVDD
     GEHSQNEKIN RWNYIEGTKL FAAFFLEMAQ LH
//
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