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Reviewed, UniProtKB/Swiss-Prot Q66HG3 (CNDP1_RAT)

Last modified November 3, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Beta-Ala-His dipeptidase
    EC=3.4.13.20
Alternative name(s):
    Carnosine dipeptidase 1
    CNDP dipeptidase 1
Gene names
Name: Cndp1
Synonyms: Cn1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer By similarity.

Tissue specificity

Detected exclusively in kidney. Ref.2

Sequence similarities

Belongs to the peptidase M20A family.

Caution

In contrast to human counterpart, it lacks a signal sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Beta-Ala-His dipeptidase
PRO_0000250531

Sites

Active site1091 By similarity
Active site1741Proton acceptor By similarity
Metal binding1071Zinc 2 By similarity
Metal binding1401Zinc 1 By similarity
Metal binding1401Zinc 2 By similarity
Metal binding1751Zinc 1 By similarity
Metal binding2031Zinc 2 By similarity
Metal binding4531Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66HG3-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: EF8DAE8C15BF06F5

FASTA49254,928
        10         20         30         40         50         60 
MLSPPHSGTL EKLFQYIDLH QDEFVQTLKE WVAIESDSVQ PMPRLRQELF RMMALAADKL 

        70         80         90        100        110        120 
RNLGARVDSV DLGSQQMPDG QSLPTPPIIL AELGNDPKKP SVCFYGHLDV QPAQKEDGWL 

       130        140        150        160        170        180 
TDPYTLTEVD GKLYGRGATD NKGPVLAWIN AVSTFRALQQ DLPVNVKFIL EGMEEAGSVA 

       190        200        210        220        230        240 
LEELVKREKD NFFSGVDYIV ISDNLWLSQK KPALTCGTRG NCYFTVEVKC RDQDFHSGTF 

       250        260        270        280        290        300 
GGILNEPMAD LVALLGSLVD SSGHILVPGI YDQMAPITEE EKTMYENIDL DLEEYQKSSR 

       310        320        330        340        350        360 
VERFLFDTKE ELLTHLWRYP SLSIHGIEGA FDEPGTKTVI PGRVLGKFSI RLVPHMTPSV 

       370        380        390        400        410        420 
VETQVTQHLE AVFSKRNSFN KMAVSMVLGL QPWTANINGT QYLAARRAIQ TVFGVDPDMI 

       430        440        450        460        470        480 
QDGSTIPIAK IFQDITQKSV MMLPLGAVDD GEHSQNEKIN RWNYIQGSKL FAAFFLELSK 

       490 
LHSGQQVPSG AF 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[2]"Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase."
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.
J. Biol. Chem. 278:6521-6531(2003) [PubMed: 12473676] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

BC081877 mRNA. Translation: AAH81877.1.
IPIIPI00367063.
RefSeqNP_001007688.1.
UniGeneRn.15548

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ66HG3.

Genome annotation databases

EnsemblENSRNOT00000034970; ENSRNOP00000034652; ENSRNOG00000027739; Rattus norvegicus. [Genome view]
GeneID307212.
KEGGrno:307212.
NMPDRfig|10116.3.peg.14472.
UCSCNM_001007687. rat.

Organism-specific databases

CTD307212.
RGD1359493. Cndp1.

Phylogenomic databases

HOVERGENQ66HG3.
OMAKDRFFSS.

Enzyme and pathway databases

BRENDA3.4.13.20. 248.

Gene expression databases

ArrayExpressQ66HG3.
GenevestigatorQ66HG3.
GermOnlineENSRNOG00000027739. Rattus norvegicus.

Family and domain databases

InterProIPR001261. ArgE/DapE_CS.
IPR017153. GSH_degradosome_DUG1.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF037242. CNDP_dipeptidase. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. False negative.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio657098.

Entry information

Entry nameCNDP1_RAT
AccessionPrimary (citable) accession number: Q66HG3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 11, 2004
Last modified: November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents