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Q9D1A2 (CNDP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic non-specific dipeptidase

EC=3.4.13.18
Alternative name(s):
CNDP dipeptidase 2
Glutamate carboxypeptidase-like protein 1
Gene names
Name:Cndp2
Synonyms:Cn2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes a variety of dipeptides including L-carnosine. Has a strong preference for Cys-Gly By similarity.

Catalytic activity

Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids. Ref.5

Cofactor

Binds 2 manganese ions per subunit. Ref.5 Ref.6

Enzyme regulation

Inhibited by bestatin. Ref.5

Subunit structure

Homodimer By similarity. Ref.6

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in the parafascicular nucleus of the thalamus, tuberomammillary nucleus of the hypothalamus and the mitral cell layer of the olfactory bulb. Ref.5

Sequence similarities

Belongs to the peptidase M20A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 475474Cytosolic non-specific dipeptidase
PRO_0000185273

Regions

Region166 – 1672Substrate binding

Sites

Active site1011 By similarity
Active site1661Proton acceptor By similarity
Metal binding991Manganese 2
Metal binding1321Manganese 1
Metal binding1321Manganese 2
Metal binding1671Manganese 1
Metal binding1951Manganese 2
Metal binding4451Manganese 1
Binding site1951Substrate; via carbonyl oxygen
Binding site2281Substrate; shared with homodimeric partner
Binding site3301Substrate; shared with homodimeric partner
Binding site3431Substrate
Binding site4171Substrate; via amide nitrogen and carbonyl oxygen
Binding site4451Substrate
Site2281Important for catalytic activity

Experimental info

Mutagenesis2281H → A: Loss of activity. Ref.6
Sequence conflict451M → I in BAE31451. Ref.2
Sequence conflict1051A → T in BAE42789. Ref.2
Sequence conflict3571V → A in BAB21596. Ref.1

Secondary structure

........................................................................... 475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9D1A2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 086950275A698500

FASTA47552,767
        10         20         30         40         50         60 
MSALKAVFQY IDENQDRYVK KLAEWVAIQS VSAWPEKRGE IRRMMEVAAA DVQRLGGSVE 

        70         80         90        100        110        120 
LVDIGKQKLP DGSEIPLPPI LLGKLGSDPQ KKTVCIYGHL DVQPAALEDG WDSEPFTLVE 

       130        140        150        160        170        180 
REGKLYGRGS TDDKGPVAGW MNALEAYQKT GQEIPVNLRF CLEGMEESGS EGLDELIFAQ 

       190        200        210        220        230        240 
KDKFFKDVDY VCISDNYWLG KNKPCITYGL RGICYFFIEV ECSDKDLHSG VYGGSVHEAM 

       250        260        270        280        290        300 
TDLISLMGCL VDKKGKILIP GINDAVAPVT DEEHALYDHI DFDMEEFAKD VGAETLLHSC 

       310        320        330        340        350        360 
KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPDMIP EVVSEQVSSY 

       370        380        390        400        410        420 
LSKKFAELQS PNKFKVYMGH GGKPWVSDFN HPHYQAGRRA LKTVFGVEPD LTREGGSIPV 

       430        440        450        460        470 
TLTFQEATGK NVMLLPVGSA DDGAHSQNEK LNRLNYIEGT KMLAAYLYEV SQLKN 

« Hide

References

« Hide 'large scale' references
[1]"Novel mouse gene differentially expressed in kidney."
Yoshikawa T., Nagasugi Y., Sugano S., Hashimoto K., Masuho Y., Seki N.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c, C57BL/6J and NOD.
Tissue: Bone marrow macrophage, Embryonic heart, Heart and Spleen.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[4]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 6-17; 311-329 AND 414-430, MASS SPECTROMETRY.
Tissue: Hippocampus.
[5]"Identification and characterization of a mouse dipeptidase that hydrolyzes L-carnosine."
Otani H., Okumura N., Hashida-Okumura A., Nagai K.
J. Biochem. 137:167-175(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[6]"Structural basis for substrate recognition and hydrolysis by mouse carnosinase CN2."
Unno H., Yamashita T., Ujita S., Okumura N., Otani H., Okumura A., Nagai K., Kusunoki M.
J. Biol. Chem. 283:27289-27299(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MANGANESE AND BESTATIN, MUTAGENESIS OF HIS-228, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB046738 mRNA. Translation: BAB21596.1.
AK003779 mRNA. Translation: BAB22991.1.
AK151013 mRNA. Translation: BAE30033.1.
AK152729 mRNA. Translation: BAE31451.1.
AK168029 mRNA. Translation: BAE40014.1.
AK168652 mRNA. Translation: BAE40509.1.
AK172034 mRNA. Translation: BAE42789.1.
BC005532 mRNA. Translation: AAH05532.1.
RefSeqNP_075638.2. NM_023149.3.
UniGeneMm.29646.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZOFX-ray2.30A/B1-475[»]
2ZOGX-ray1.70A/B1-475[»]
ProteinModelPortalQ9D1A2.
SMRQ9D1A2. Positions 1-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D1A2. 2 interactions.
MINTMINT-1855384.
STRING10090.ENSMUSP00000025546.

Protein family/group databases

MEROPSM20.005.

PTM databases

PhosphoSiteQ9D1A2.

2D gel databases

REPRODUCTION-2DPAGEQ9D1A2.

Proteomic databases

PaxDbQ9D1A2.
PRIDEQ9D1A2.

Protocols and materials databases

DNASU66054.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025546; ENSMUSP00000025546; ENSMUSG00000024644.
ENSMUST00000168419; ENSMUSP00000128696; ENSMUSG00000024644.
GeneID66054.
KEGGmmu:66054.
UCSCuc008fut.1. mouse.

Organism-specific databases

CTD55748.
MGIMGI:1913304. Cndp2.

Phylogenomic databases

eggNOGCOG0624.
GeneTreeENSGT00390000009682.
HOGENOMHOG000216709.
HOVERGENHBG051103.
InParanoidQ3U7B9.
KOK08660.
OMADYALVCD.
OrthoDBEOG7JHM55.
TreeFamTF300633.

Gene expression databases

ArrayExpressQ9D1A2.
BgeeQ9D1A2.
CleanExMM_CNDP2.
GenevestigatorQ9D1A2.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
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.
PROSITEPS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9D1A2.
NextBio320490.
PROQ9D1A2.
SOURCESearch...

Entry information

Entry nameCNDP2_MOUSE
AccessionPrimary (citable) accession number: Q9D1A2
Secondary accession number(s): Q3TA80 expand/collapse secondary AC list , Q3TI32, Q3U7B9, Q99PV1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 2001
Last modified: March 19, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot