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Database: UniProt
Entry: F7EVX6_MACMU
LinkDB: F7EVX6_MACMU
Original site: F7EVX6_MACMU 
ID   F7EVX6_MACMU            Unreviewed;       478 AA.
AC   F7EVX6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Cytosolic non-specific dipeptidase {ECO:0000256|ARBA:ARBA00041164};
DE            EC=3.4.13.18 {ECO:0000256|ARBA:ARBA00038976};
DE   AltName: Full=CNDP dipeptidase 2 {ECO:0000256|ARBA:ARBA00042010};
DE   AltName: Full=Threonyl dipeptidase {ECO:0000256|ARBA:ARBA00041744};
GN   Name=CNDP1 {ECO:0000313|Ensembl:ENSMMUP00000011721.4,
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:ENSMMUP00000011721.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000011721.4, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000011721.4,
RC   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:ENSMMUP00000011721.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000011721.4};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036214};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66725;
CC         Evidence={ECO:0000256|ARBA:ARBA00036214};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66726;
CC         Evidence={ECO:0000256|ARBA:ARBA00036214};
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:0000256|ARBA:ARBA00023673};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC         Evidence={ECO:0000256|ARBA:ARBA00023673};
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:0000256|ARBA:ARBA00036410};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67373;
CC         Evidence={ECO:0000256|ARBA:ARBA00036410};
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:0000256|ARBA:ARBA00036500};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67365;
CC         Evidence={ECO:0000256|ARBA:ARBA00036500};
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:0000256|ARBA:ARBA00036626};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67361;
CC         Evidence={ECO:0000256|ARBA:ARBA00036626};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of dipeptides, preferentially hydrophobic
CC         dipeptides including prolyl amino acids.; EC=3.4.13.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00036421};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   AlphaFoldDB; F7EVX6; -.
DR   MEROPS; M20.005; -.
DR   Ensembl; ENSMMUT00000012498.4; ENSMMUP00000011721.4; ENSMMUG00000008942.4.
DR   VEuPathDB; HostDB:ENSMMUG00000008942; -.
DR   VGNC; VGNC:71257; CNDP1.
DR   GeneTree; ENSGT00940000160484; -.
DR   HOGENOM; CLU_029469_3_0_1; -.
DR   Proteomes; UP000006718; Chromosome 18.
DR   Bgee; ENSMMUG00000008942; Expressed in adult mammalian kidney and 22 other cell types or tissues.
DR   ExpressionAtlas; F7EVX6; baseline.
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; IEA:UniProtKB-KW.
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:SF11; CYTOSOLIC NON-SPECIFIC 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protease {ECO:0000256|ARBA:ARBA00022645};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT   DOMAIN          208..367
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT   BINDING         99
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         132
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         132
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         417
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         445
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         445
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   SITE            228
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-4"
SQ   SEQUENCE   478 AA;  53207 MW;  C102F794EF4BF15D CRC64;
     MAALTTLFKY IDENQDRYIK KLAKWVAIQS VSAWPEKRGE IRRMMEVAAA DVKQLGGSVE
     LVDIGKQKLP DGSEIPLPPI LLGKLGSDPQ KKTVCIYGHL DVQPAALEDG WDSEPFTLVE
     RDGKLYGRGS TDDKGPVAGW INALEAYQKT DQEIPVNVRF CLEGMEESGS EGLDELIFAQ
     KDTFFKDVDY VCISDNYWLG KKKPCITYGL RGICYFFIEV ECSNKDLHSG VYGGSVHEAM
     TDLILLMGSL VDKRGNILIP GINEAVAAVT EEEHKLYDDI DFDIEEFAKD VGAQILLHNN
     KKDILMHRWR FPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPNMTP EVVSEQVTSY
     LTKKFAELHS PNEFKVYMGH GGKPWVTDCS HPHYVAGRRA MKTVFGVEAD LTREGGSIPV
     TLTFQEATGK NIMLLPMGSA DDGAHSQNEK LNRLRPCWPC CCCWREACSP HTPCPRRC
//
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