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Beta-Ala-His dipeptidase (EC 3.4.13.20) (CNDP dipeptidase 1) (Carnosine dipeptidase 1) (Glutamate carboxypeptidase-like protein 2) (Serum carnosinase)

 CNDP1_HUMAN             Reviewed;         507 AA.
Q96KN2; Q14D40; Q17S05; Q2TBG0; Q6UWK2; Q9BT98;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
28-FEB-2018, entry version 139.
RecName: Full=Beta-Ala-His dipeptidase;
EC=3.4.13.20;
AltName: Full=CNDP dipeptidase 1;
AltName: Full=Carnosine dipeptidase 1;
AltName: Full=Glutamate carboxypeptidase-like protein 2;
AltName: Full=Serum carnosinase;
Flags: Precursor;
Name=CNDP1; Synonyms=CN1, CPGL2; ORFNames=UNQ1915/PRO4380;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-113.
TISSUE=Brain;
Chen J.M., Barrett A.J.;
"Cloning and sequencing of a second human homologue of glutamate
carboxypeptidase in peptidase family M20.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], POLYMORPHISM, AND VARIANTS LEU-20 INS AND
VAL-113.
PubMed=16046297; DOI=10.2337/diabetes.54.8.2320;
Janssen B., Hohenadel D., Brinkkoetter P., Peters V., Rind N.,
Fischer C., Rychlik I., Cerna M., Romzova M., de Heer E., Baelde H.,
Bakker S.J., Zirie M., Rondeau E., Mathieson P., Saleem M.A.,
Meyer J., Koppel H., Sauerhoefer S., Bartram C.R., Nawroth P.,
Hammes H.P., Yard B.A., Zschocke J., van der Woude F.J.;
"Carnosine as a protective factor in diabetic nephropathy: association
with a leucine repeat of the carnosinase gene CNDP1.";
Diabetes 54:2320-2327(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-113.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-20 INS AND
VAL-113.
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
CHARACTERIZATION, SUBUNIT, AND CATALYTIC ACTIVITY.
PubMed=7116644; DOI=10.1016/0009-8981(82)90166-8;
Lenney J.F., George R.P., Weiss A.M., Kucera C.M., Chan P.W.,
Rinzler G.S.;
"Human serum carnosinase: characterization, distinction from cellular
carnosinase, and activation by cadmium.";
Clin. Chim. Acta 123:221-231(1982).
[7]
TISSUE SPECIFICITY.
PubMed=6616870; DOI=10.1016/0009-8981(83)90243-7;
Lenney J.F., Peppers S.C., Kucera C.M., Sjaastad O.;
"Homocarnosinosis: lack of serum carnosinase is the defect probably
responsible for elevated brain and CSF homocarnosine.";
Clin. Chim. Acta 132:157-165(1983).
[8]
BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
AND MUTAGENESIS OF HIS-132; ASP-165 AND GLU-200.
PubMed=12473676; DOI=10.1074/jbc.M209764200;
Teufel M., Saudek V., Ledig J.P., Bernhardt A., Boularand S.,
Carreau A., Cairns N.J., Carter C., Cowley D.J., Duverger D.,
Ganzhorn A.J., Guenet C., Heintzelmann B., Laucher V., Sauvage C.,
Smirnova T.;
"Sequence identification and characterization of human carnosinase and
a closely related non-specific dipeptidase.";
J. Biol. Chem. 278:6521-6531(2003).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-322 AND ASN-382.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[10]
X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 27-507 IN COMPLEX WITH ZINC
IONS, AND COFACTOR.
Structural genomics consortium (SGC);
"Crystal structure of human carnosine dipeptidase 1.";
Submitted (JUL-2011) to the PDB data bank.
-!- CATALYTIC ACTIVITY: Preferential hydrolysis of the beta-Ala-|-His
dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and
other dipeptides including homocarnosine.
{ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:7116644}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|Ref.10};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|Ref.10};
-!- ENZYME REGULATION: Inhibited by the metal chelator 1,10-o-
phenantrolin. The inhibitory concentration 50% (IC(50)) is 5 uM.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.27 uM for carnosine (at 30 degrees Celsius and in the
absence of cadmium ions) {ECO:0000269|PubMed:12473676};
KM=11.00 uM for carnosine (at 30 degrees Celsius and in the
presence of 200 uM cadmium ions) {ECO:0000269|PubMed:12473676};
KM=0.20 uM for homocarnosine (at 30 degrees Celsius and in the
absence of cadmium ions) {ECO:0000269|PubMed:12473676};
KM=1.0 uM for homocarnosine (at 30 degrees Celsius and in the
presence of 200 uM cadmium ions) {ECO:0000269|PubMed:12473676};
Note=1 hour incubation in 50 mM Tris-HCl, pH 7.5.;
pH dependence:
Optimum pH is 8.5. {ECO:0000269|PubMed:12473676};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7116644,
ECO:0000269|Ref.10}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Found in serum and adult nervous central
system. Absent in serum from patients with homocarnosinosis.
{ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:6616870}.
-!- POLYMORPHISM: The number of trinucleotide (CTG) repeat varies
among different alleles leading to insertion of Leu residues in
the signal peptide. The allele with 5 leucines (as shown in the
reference entry) is known as the Mannheim allele. Diabetic
patients with the CNDP1 Mannheim allele are less susceptible for
nephropathy. {ECO:0000269|PubMed:16046297}.
-!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ417564; CAD10388.1; -; mRNA.
EMBL; AY358756; AAQ89116.1; -; mRNA.
EMBL; BC004271; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC110295; AAI10296.1; -; mRNA.
EMBL; BC113512; AAI13513.1; -; mRNA.
EMBL; BC117122; AAI17123.1; -; mRNA.
CCDS; CCDS12007.1; -.
RefSeq; NP_116038.4; NM_032649.5.
UniGene; Hs.400613; -.
PDB; 3DLJ; X-ray; 2.26 A; A/B=27-507.
PDBsum; 3DLJ; -.
ProteinModelPortal; Q96KN2; -.
SMR; Q96KN2; -.
BioGrid; 124230; 16.
STRING; 9606.ENSP00000351682; -.
MEROPS; M20.006; -.
iPTMnet; Q96KN2; -.
PhosphoSitePlus; Q96KN2; -.
BioMuta; CNDP1; -.
DMDM; 317373563; -.
PaxDb; Q96KN2; -.
PeptideAtlas; Q96KN2; -.
PRIDE; Q96KN2; -.
DNASU; 84735; -.
Ensembl; ENST00000358821; ENSP00000351682; ENSG00000150656.
GeneID; 84735; -.
KEGG; hsa:84735; -.
UCSC; uc002llq.5; human.
CTD; 84735; -.
DisGeNET; 84735; -.
EuPathDB; HostDB:ENSG00000150656.14; -.
GeneCards; CNDP1; -.
HGNC; HGNC:20675; CNDP1.
HPA; HPA008933; -.
MIM; 609064; gene.
neXtProt; NX_Q96KN2; -.
PharmGKB; PA134907547; -.
eggNOG; KOG2276; Eukaryota.
eggNOG; COG0624; LUCA.
HOGENOM; HOG000216709; -.
HOVERGEN; HBG051103; -.
InParanoid; Q96KN2; -.
KO; K05604; -.
OrthoDB; EOG091G05RU; -.
PhylomeDB; Q96KN2; -.
TreeFam; TF300633; -.
BioCyc; MetaCyc:HS07681-MONOMER; -.
BRENDA; 3.4.13.20; 2681.
SABIO-RK; Q96KN2; -.
ChiTaRS; CNDP1; human.
EvolutionaryTrace; Q96KN2; -.
GeneWiki; CNDP1; -.
GenomeRNAi; 84735; -.
PRO; PR:Q96KN2; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000150656; -.
CleanEx; HS_CNDP1; -.
ExpressionAtlas; Q96KN2; baseline and differential.
Genevisible; Q96KN2; HS.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0016805; F:dipeptidase activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; IDA:MGI.
GO; GO:0032268; P:regulation of cellular protein metabolic process; IDA:MGI.
CDD; cd05676; M20_dipept_like_CNDP; 1.
InterPro; IPR001261; ArgE/DapE_CS.
InterPro; IPR017153; CNDP/DUG1.
InterPro; IPR002933; Peptidase_M20.
InterPro; IPR011650; Peptidase_M20_dimer.
Pfam; PF07687; M20_dimer; 1.
Pfam; PF01546; Peptidase_M20; 1.
PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
1: Evidence at protein level;
3D-structure; Carboxypeptidase; Complete proteome; Glycoprotein;
Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein;
Polymorphism; Protease; Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 507 Beta-Ala-His dipeptidase.
/FTId=PRO_0000026809.
ACT_SITE 134 134 {ECO:0000250}.
ACT_SITE 199 199 Proton acceptor. {ECO:0000250}.
METAL 132 132 Zinc 2.
METAL 165 165 Zinc 1.
METAL 165 165 Zinc 2.
METAL 200 200 Zinc 1.
METAL 228 228 Zinc 2.
METAL 478 478 Zinc 1.
MOD_RES 219 219 Phosphoserine.
{ECO:0000250|UniProtKB:Q66HG3}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
VARIANT 6 6 G -> R (in dbSNP:rs11151964).
/FTId=VAR_027147.
VARIANT 20 20 L -> LL. {ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16046297}.
/FTId=VAR_027148.
VARIANT 113 113 I -> V (in dbSNP:rs4263028).
{ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16046297,
ECO:0000269|Ref.1}.
/FTId=VAR_027149.
MUTAGEN 132 132 H->A: Loss of activity.
{ECO:0000269|PubMed:12473676}.
MUTAGEN 165 165 D->A: Loss of activity.
{ECO:0000269|PubMed:12473676}.
MUTAGEN 200 200 E->A: Loss of activity.
{ECO:0000269|PubMed:12473676}.
CONFLICT 155 155 D -> G (in Ref. 1; CAD10388 and 5;
AAI10296). {ECO:0000305}.
CONFLICT 237 237 P -> L (in Ref. 1; CAD10388).
{ECO:0000305}.
CONFLICT 272 272 P -> L (in Ref. 1; CAD10388).
{ECO:0000305}.
HELIX 35 44 {ECO:0000244|PDB:3DLJ}.
HELIX 46 57 {ECO:0000244|PDB:3DLJ}.
STRAND 62 65 {ECO:0000244|PDB:3DLJ}.
HELIX 68 87 {ECO:0000244|PDB:3DLJ}.
STRAND 91 95 {ECO:0000244|PDB:3DLJ}.
STRAND 99 101 {ECO:0000244|PDB:3DLJ}.
STRAND 107 109 {ECO:0000244|PDB:3DLJ}.
STRAND 113 118 {ECO:0000244|PDB:3DLJ}.
STRAND 126 132 {ECO:0000244|PDB:3DLJ}.
HELIX 140 142 {ECO:0000244|PDB:3DLJ}.
STRAND 152 154 {ECO:0000244|PDB:3DLJ}.
STRAND 157 160 {ECO:0000244|PDB:3DLJ}.
TURN 161 166 {ECO:0000244|PDB:3DLJ}.
HELIX 167 182 {ECO:0000244|PDB:3DLJ}.
STRAND 188 197 {ECO:0000244|PDB:3DLJ}.
HELIX 199 201 {ECO:0000244|PDB:3DLJ}.
TURN 202 205 {ECO:0000244|PDB:3DLJ}.
HELIX 206 213 {ECO:0000244|PDB:3DLJ}.
TURN 214 217 {ECO:0000244|PDB:3DLJ}.
STRAND 223 226 {ECO:0000244|PDB:3DLJ}.
STRAND 238 243 {ECO:0000244|PDB:3DLJ}.
STRAND 245 255 {ECO:0000244|PDB:3DLJ}.
TURN 262 264 {ECO:0000244|PDB:3DLJ}.
HELIX 272 280 {ECO:0000244|PDB:3DLJ}.
TURN 293 298 {ECO:0000244|PDB:3DLJ}.
HELIX 304 311 {ECO:0000244|PDB:3DLJ}.
HELIX 317 324 {ECO:0000244|PDB:3DLJ}.
HELIX 334 342 {ECO:0000244|PDB:3DLJ}.
STRAND 346 355 {ECO:0000244|PDB:3DLJ}.
STRAND 358 360 {ECO:0000244|PDB:3DLJ}.
STRAND 367 377 {ECO:0000244|PDB:3DLJ}.
HELIX 383 399 {ECO:0000244|PDB:3DLJ}.
STRAND 404 415 {ECO:0000244|PDB:3DLJ}.
HELIX 425 438 {ECO:0000244|PDB:3DLJ}.
STRAND 443 449 {ECO:0000244|PDB:3DLJ}.
HELIX 452 460 {ECO:0000244|PDB:3DLJ}.
STRAND 483 485 {ECO:0000244|PDB:3DLJ}.
HELIX 486 504 {ECO:0000244|PDB:3DLJ}.
SEQUENCE 507 AA; 56706 MW; 756CCD872996F192 CRC64;
MDPKLGRMAA SLLAVLLLLL ERGMFSSPSP PPALLEKVFQ YIDLHQDEFV QTLKEWVAIE
SDSVQPVPRF RQELFRMMAV AADTLQRLGA RVASVDMGPQ QLPDGQSLPI PPIILAELGS
DPTKGTVCFY GHLDVQPADR GDGWLTDPYV LTEVDGKLYG RGATDNKGPV LAWINAVSAF
RALEQDLPVN IKFIIEGMEE AGSVALEELV EKEKDRFFSG VDYIVISDNL WISQRKPAIT
YGTRGNSYFM VEVKCRDQDF HSGTFGGILH EPMADLVALL GSLVDSSGHI LVPGIYDEVV
PLTEEEINTY KAIHLDLEEY RNSSRVEKFL FDTKEEILMH LWRYPSLSIH GIEGAFDEPG
TKTVIPGRVI GKFSIRLVPH MNVSAVEKQV TRHLEDVFSK RNSSNKMVVS MTLGLHPWIA
NIDDTQYLAA KRAIRTVFGT EPDMIRDGST IPIAKMFQEI VHKSVVLIPL GAVDDGEHSQ
NEKINRWNYI EGTKLFAAFF LEMAQLH


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