ID J3QKT2_HUMAN Unreviewed; 249 AA.
AC J3QKT2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
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};
DE Flags: Fragment;
GN Name=CNDP2 {ECO:0000313|Ensembl:ENSP00000463222.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000463222.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000463222.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., O'Neill K., Piqani B., Smith C.L., Talamas J.A.,
RA Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q.,
RA Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [2] {ECO:0007829|PubMed:19608861}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [3] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4] {ECO:0007829|PubMed:22223895}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [5] {ECO:0007829|PubMed:22814378}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7] {ECO:0000313|Ensembl:ENSP00000463222.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; AC009704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; J3QKT2; -.
DR SMR; J3QKT2; -.
DR MassIVE; J3QKT2; -.
DR MaxQB; J3QKT2; -.
DR PeptideAtlas; J3QKT2; -.
DR Antibodypedia; 23332; 457 antibodies from 31 providers.
DR Ensembl; ENST00000583785.5; ENSP00000463222.1; ENSG00000133313.15.
DR UCSC; uc060qcs.1; human.
DR HGNC; HGNC:24437; CNDP2.
DR VEuPathDB; HostDB:ENSG00000133313; -.
DR GeneTree; ENSGT00940000156500; -.
DR HOGENOM; CLU_1117895_0_0_1; -.
DR OMA; HITIPGF; -.
DR ChiTaRS; CNDP2; human.
DR Proteomes; UP000005640; Chromosome 18.
DR Bgee; ENSG00000133313; Expressed in adult mammalian kidney and 198 other cell types or tissues.
DR ExpressionAtlas; J3QKT2; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR002933; Peptidase_M20.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF11; CYTOSOLIC NON-SPECIFIC DIPEPTIDASE; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Proteomics identification {ECO:0007829|EPD:J3QKT2,
KW ECO:0007829|MaxQB:J3QKT2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT NON_TER 249
FT /evidence="ECO:0000313|Ensembl:ENSP00000463222.1"
SQ SEQUENCE 249 AA; 27710 MW; AD583B7CCCB5535D CRC64;
MAALTTLFKY IDENQDRYIK KLAKWVAIQS VSAWPEKRGE IRRMMEVAAA DVKQLGGSVE
LVDIGKQKLP DGSEIPLPPI LLGRLGSDPQ KKTVCIYGHL DVQPAALEDG WDSEPFTLVE
RDGKLYGRGS TDDKGPVAGW INALEAYQKT GQEIPVNVRF CLEGMEESGS EGLDELIFAR
KDTFFKDVDY VCISDNYWLG KKKPCITYGL RGICYFFIEV ECSNKDLHSG VYGGSVHEAM
TDLILLMGS
//
