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Q9D1A2

- CNDP2_MOUSE

UniProt

Q9D1A2 - CNDP2_MOUSE

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Protein

Cytosolic non-specific dipeptidase

Gene

Cndp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.1 Publication

Cofactori

Binds 2 manganese ions per subunit.2 Publications

Enzyme regulationi

Inhibited by bestatin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991Manganese 21 Publication
Active sitei101 – 1011By similarity
Metal bindingi132 – 1321Manganese 11 Publication
Metal bindingi132 – 1321Manganese 21 Publication
Active sitei166 – 1661Proton acceptorBy similarity
Metal bindingi167 – 1671Manganese 11 Publication
Metal bindingi195 – 1951Manganese 21 Publication
Binding sitei195 – 1951Substrate; via carbonyl oxygen
Binding sitei228 – 2281Substrate; shared with homodimeric partner
Sitei228 – 2281Important for catalytic activity
Binding sitei330 – 3301Substrate; shared with homodimeric partner
Binding sitei343 – 3431Substrate
Binding sitei417 – 4171Substrate; via amide nitrogen and carbonyl oxygen
Metal bindingi445 – 4451Manganese 11 Publication
Binding sitei445 – 4451Substrate

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB-KW
  2. dipeptidase activity Source: MGI
  3. metal ion binding Source: UniProtKB-KW
  4. metallopeptidase activity Source: UniProtKB-KW
  5. peptidase activity Source: MGI
  6. tripeptidase activity Source: InterPro

GO - Biological processi

  1. proteolysis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_202492. Sulfur amino acid metabolism.
REACT_210980. Glutathione synthesis and recycling.

Protein family/group databases

MEROPSiM20.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic non-specific dipeptidase (EC:3.4.13.18)
Alternative name(s):
CNDP dipeptidase 2
Glutamate carboxypeptidase-like protein 1
Gene namesi
Name:Cndp2
Synonyms:Cn2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1913304. Cndp2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi228 – 2281H → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 475474Cytosolic non-specific dipeptidasePRO_0000185273Add
BLAST

Proteomic databases

MaxQBiQ9D1A2.
PaxDbiQ9D1A2.
PRIDEiQ9D1A2.

2D gel databases

REPRODUCTION-2DPAGEQ9D1A2.

PTM databases

PhosphoSiteiQ9D1A2.

Expressioni

Tissue specificityi

Highly expressed in the parafascicular nucleus of the thalamus, tuberomammillary nucleus of the hypothalamus and the mitral cell layer of the olfactory bulb.1 Publication

Gene expression databases

BgeeiQ9D1A2.
CleanExiMM_CNDP2.
ExpressionAtlasiQ9D1A2. baseline and differential.
GenevestigatoriQ9D1A2.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi211181. 1 interaction.
IntActiQ9D1A2. 2 interactions.
MINTiMINT-1855384.
STRINGi10090.ENSMUSP00000025546.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312
Helixi15 – 2713
Helixi35 – 373
Helixi38 – 5417
Beta strandi58 – 625
Beta strandi66 – 683
Beta strandi74 – 763
Beta strandi80 – 856
Beta strandi93 – 997
Helixi107 – 1093
Beta strandi119 – 1213
Beta strandi124 – 1274
Turni128 – 1336
Helixi134 – 14916
Beta strandi155 – 16410
Helixi166 – 1683
Helixi173 – 1797
Turni180 – 1878
Beta strandi190 – 1934
Beta strandi199 – 2035
Beta strandi205 – 2106
Beta strandi212 – 22110
Helixi229 – 2324
Turni233 – 2353
Helixi239 – 2479
Turni260 – 2656
Helixi271 – 2766
Helixi284 – 2907
Helixi301 – 3099
Beta strandi313 – 32210
Beta strandi325 – 3273
Beta strandi334 – 34411
Helixi350 – 36617
Beta strandi372 – 38211
Helixi392 – 40514
Beta strandi410 – 4167
Helixi420 – 4289
Beta strandi430 – 4345
Beta strandi450 – 4523
Helixi453 – 47220

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZOFX-ray2.30A/B1-475[»]
2ZOGX-ray1.70A/B1-475[»]
ProteinModelPortaliQ9D1A2.
SMRiQ9D1A2. Positions 1-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D1A2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 1672Substrate binding

Sequence similaritiesi

Belongs to the peptidase M20A family.Curated

Phylogenomic databases

eggNOGiCOG0624.
GeneTreeiENSGT00390000009682.
HOGENOMiHOG000216709.
HOVERGENiHBG051103.
InParanoidiQ9D1A2.
KOiK08660.
OMAiTDGAHSI.
OrthoDBiEOG7JHM55.
PhylomeDBiQ9D1A2.
TreeFamiTF300633.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
InterProiIPR001261. ArgE/DapE_CS.
IPR017153. GSH_degradosome_DUG1.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF037242. CNDP_dipeptidase. 1 hit.
PROSITEiPS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D1A2 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSALKAVFQY IDENQDRYVK KLAEWVAIQS VSAWPEKRGE IRRMMEVAAA
60 70 80 90 100
DVQRLGGSVE LVDIGKQKLP DGSEIPLPPI LLGKLGSDPQ KKTVCIYGHL
110 120 130 140 150
DVQPAALEDG WDSEPFTLVE REGKLYGRGS TDDKGPVAGW MNALEAYQKT
160 170 180 190 200
GQEIPVNLRF CLEGMEESGS EGLDELIFAQ KDKFFKDVDY VCISDNYWLG
210 220 230 240 250
KNKPCITYGL RGICYFFIEV ECSDKDLHSG VYGGSVHEAM TDLISLMGCL
260 270 280 290 300
VDKKGKILIP GINDAVAPVT DEEHALYDHI DFDMEEFAKD VGAETLLHSC
310 320 330 340 350
KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPDMIP
360 370 380 390 400
EVVSEQVSSY LSKKFAELQS PNKFKVYMGH GGKPWVSDFN HPHYQAGRRA
410 420 430 440 450
LKTVFGVEPD LTREGGSIPV TLTFQEATGK NVMLLPVGSA DDGAHSQNEK
460 470
LNRLNYIEGT KMLAAYLYEV SQLKN
Length:475
Mass (Da):52,767
Last modified:June 1, 2001 - v1
Checksum:i086950275A698500
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451M → I in BAE31451. (PubMed:16141072)Curated
Sequence conflicti105 – 1051A → T in BAE42789. (PubMed:16141072)Curated
Sequence conflicti357 – 3571V → A in BAB21596. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS29383.1.
RefSeqiNP_001276460.1. NM_001289531.1.
NP_075638.2. NM_023149.3.
UniGeneiMm.29646.

Genome annotation databases

EnsembliENSMUST00000025546; ENSMUSP00000025546; ENSMUSG00000024644.
ENSMUST00000168419; ENSMUSP00000128696; ENSMUSG00000024644.
GeneIDi66054.
KEGGimmu:66054.
UCSCiuc008fut.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS29383.1.
RefSeqi NP_001276460.1. NM_001289531.1.
NP_075638.2. NM_023149.3.
UniGenei Mm.29646.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZOF X-ray 2.30 A/B 1-475 [» ]
2ZOG X-ray 1.70 A/B 1-475 [» ]
ProteinModelPortali Q9D1A2.
SMRi Q9D1A2. Positions 1-474.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 211181. 1 interaction.
IntActi Q9D1A2. 2 interactions.
MINTi MINT-1855384.
STRINGi 10090.ENSMUSP00000025546.

Protein family/group databases

MEROPSi M20.005.

PTM databases

PhosphoSitei Q9D1A2.

2D gel databases

REPRODUCTION-2DPAGE Q9D1A2.

Proteomic databases

MaxQBi Q9D1A2.
PaxDbi Q9D1A2.
PRIDEi Q9D1A2.

Protocols and materials databases

DNASUi 66054.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025546 ; ENSMUSP00000025546 ; ENSMUSG00000024644 .
ENSMUST00000168419 ; ENSMUSP00000128696 ; ENSMUSG00000024644 .
GeneIDi 66054.
KEGGi mmu:66054.
UCSCi uc008fut.1. mouse.

Organism-specific databases

CTDi 55748.
MGIi MGI:1913304. Cndp2.

Phylogenomic databases

eggNOGi COG0624.
GeneTreei ENSGT00390000009682.
HOGENOMi HOG000216709.
HOVERGENi HBG051103.
InParanoidi Q9D1A2.
KOi K08660.
OMAi TDGAHSI.
OrthoDBi EOG7JHM55.
PhylomeDBi Q9D1A2.
TreeFami TF300633.

Enzyme and pathway databases

Reactomei REACT_202492. Sulfur amino acid metabolism.
REACT_210980. Glutathione synthesis and recycling.

Miscellaneous databases

EvolutionaryTracei Q9D1A2.
NextBioi 320490.
PROi Q9D1A2.
SOURCEi Search...

Gene expression databases

Bgeei Q9D1A2.
CleanExi MM_CNDP2.
ExpressionAtlasi Q9D1A2. baseline and differential.
Genevestigatori Q9D1A2.

Family and domain databases

Gene3Di 3.30.70.360. 1 hit.
InterProi IPR001261. ArgE/DapE_CS.
IPR017153. GSH_degradosome_DUG1.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view ]
Pfami PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view ]
PIRSFi PIRSF037242. CNDP_dipeptidase. 1 hit.
PROSITEi PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, IDENTIFICATION BY 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.

Entry informationi

Entry nameiCNDP2_MOUSE
AccessioniPrimary (citable) accession number: Q9D1A2
Secondary accession number(s): Q3TA80
, Q3TI32, Q3U7B9, Q99PV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3