Beta-Ala-His dipeptidase (CNDP1)

The protein contains 507 amino acids for an estimated molecular weight of 56706 Da.

 

No function (updated: Jan. 11, 2011)

Protein identification was indicated in the following studies:

  1. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 96%
Model score: 100
No model available.

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VariantDescription
dbSNP:rs11151964
dbSNP:rs4263028

The reference OMIM entry for this protein is 609064

Carnosine dipeptidase 1; cndp1
Carnosinase 1; cn1
Carnosinase, serum

DESCRIPTION

Carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine) have potential neuroprotective and neurotransmitter functions in the brain. CNDP1, also known as serum carnosinase (EC 3.4.13.20), is distributed in human plasma and brain and degrades carnosine, homocarnosine, and other related peptides (Teufel et al., 2003).

CLONING

Teufel et al. (2003) assembled overlapping ESTs derived from human brain cDNA libraries to obtain full-length CN1. The deduced 508-amino acid protein has a calculated molecular mass of 56.8 kD. CN1 has a typical signal peptide, essential histidine and carboxyl residues in the metal-binding site, and 3 N-glycosylation sites. CN1 shares 49% amino acid identity with CN2 (CNDP2; 169800). Northern blot analysis detected a 2.4-kb transcript in brain and liver and a 4.4-kb transcript in brain. mRNA dot blot analysis detected CN1 expression in the central nervous system of adults and, to a lesser extent, in liver. No expression was detected in fetal brain. The mouse and rat CN1 homologs do not have an N-terminal signal peptide and are expressed exclusively in kidney. Western blot analysis detected multiple protein bands in extracts of plasma and cerebrospinal fluid and 2 bands in cortex and hippocampus. Immunohistochemical analysis detected CN1 in the cytosol of pyramidal neurons in the hippocampus and in large and small neurons of the temporal cortex. In subcortical white matter, CN1 was expressed by small cells, presumably glial cells, and neuronal fibers. Western blot analysis of transfected Chinese hamster ovary (CHO) cells found CN1 secreted to the medium. Size-exclusion chromatography indicated that CN1 formed homodimers of 167 kD. N-glycosidase treatment reduced the apparent molecular mass of reduced monomeric CN1 from 82 kD to 63.7 kD.

GENE FUNCTION

Teufel et al. (2003) found carnosinase activity only in the supernatant of CN1-transfected CHO cells and in human plasma. Point mutation of putative metal-binding residues produced inactive enzymes. The pH optimum of carnosine degradation was between pH 7.5 and 8.5. In a substrate survey, CN1 only degraded carnosine, N-methylcarnosine, ala-his, gly-his, and homocarnosine.

MAPPING

The International Radiation Hybrid Mapping Consortium mapped the CNDP1 gene to chromosome 18 (TMAP WI-15225). ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 609064 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).