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Q9Z2W0 (DNPEP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Aspartyl aminopeptidase

EC=3.4.11.21
Gene names
Name:Dnpep
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism By similarity.

Catalytic activity

Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

One of the zinc ions is readily exchangeable with other divalent cations such as manganese, which strongly stimulates the enzymatic activity By similarity.

Subunit structure

Tetrahedron-shaped homododecamer built from six homodimers By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the peptidase M18 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Aspartyl aminopeptidase
PRO_0000173452

Sites

Metal binding921Zinc 1 By similarity
Metal binding2621Zinc 1 By similarity
Metal binding2621Zinc 2 By similarity
Metal binding3001Zinc 2 By similarity
Metal binding3441Zinc 1 By similarity
Metal binding4381Zinc 2 By similarity
Binding site1681Substrate By similarity
Binding site2991Substrate By similarity
Binding site3441Substrate By similarity
Binding site3471Substrate By similarity
Binding site3721Substrate By similarity
Binding site3791Substrate By similarity

Experimental info

Sequence conflict611K → N in AAD01212. Ref.1
Sequence conflict3641L → S in AAD01212. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z2W0 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0350CC27C4A5AC8E

FASTA47352,207
        10         20         30         40         50         60 
MAMNGRARKE AIQATARELL KFVNRSPSPF HVVAECRSRL LQAGFRELKE TEGWDIVPEN 

        70         80         90        100        110        120 
KYFLTRNSSS IIAFAVGGQY VPGNGFSLIG AHTDSPCLRV KRKSRRSQVG YHQVGVETYG 

       130        140        150        160        170        180 
GGIWSTWFDR DLTLAGRVII KCPTSGRLEQ RLVHIERPIL RIPHLAIHLQ RNINENFGPN 

       190        200        210        220        230        240 
TEIHLVPILA TAVQEELEKG TPEPGPLGAT DERHHSVLMS LLCTHLGLSP DSIMEMELCL 

       250        260        270        280        290        300 
ADTQPAVLGG AYEEFIFAPR LDNLHSCFCA LQALIDSCAS PASLARDPHV RMVTLYDNEE 

       310        320        330        340        350        360 
VGSESAQGAQ SLLTELILRR ISASPQRLTA FEEAIPKSFM ISADMAHAVH PNYSDKHEEN 

       370        380        390        400        410        420 
HRPLFHKGPV IKVNSKQRYA SNAVSESMIR EVAGQVGVPL QDLMVRNDSP CGTTIGPILA 

       430        440        450        460        470 
SRLGLRVLDL GSPQLAMHSI RETACTTGVL QTLTLFKGFF ELFPSVSRNL LVD 

« Hide

References

« Hide 'large scale' references
[1]"Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase."
Wilk S., Wilk E., Magnusson R.P.
J. Biol. Chem. 273:15961-15970(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Mammary gland.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Strain: C57BL/6.
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF005051 mRNA. Translation: AAD01212.1.
AK166276 mRNA. Translation: BAE38675.1.
CH466548 Genomic DNA. Translation: EDL00396.1.
CH466548 Genomic DNA. Translation: EDL00398.1.
CH466548 Genomic DNA. Translation: EDL00400.1.
CH466548 Genomic DNA. Translation: EDL00401.1.
BC092232 mRNA. Translation: AAH92232.1.
CCDSCCDS15070.1.
RefSeqNP_001104301.1. NM_001110831.1.
NP_058574.3. NM_016878.4.
XP_006496468.1. XM_006496405.1.
XP_006496469.1. XM_006496406.1.
UniGeneMm.24680.

3D structure databases

ProteinModelPortalQ9Z2W0.
SMRQ9Z2W0. Positions 5-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Z2W0. 2 interactions.
MINTMINT-4093364.
STRING10090.ENSMUSP00000070821.

Protein family/group databases

MEROPSM18.002.

PTM databases

PhosphoSiteQ9Z2W0.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2W0.

Proteomic databases

MaxQBQ9Z2W0.
PaxDbQ9Z2W0.
PRIDEQ9Z2W0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066668; ENSMUSP00000070821; ENSMUSG00000026209.
ENSMUST00000113605; ENSMUSP00000109235; ENSMUSG00000026209.
GeneID13437.
KEGGmmu:13437.
UCSCuc007bot.2. mouse.

Organism-specific databases

CTD23549.
MGIMGI:1278328. Dnpep.

Phylogenomic databases

eggNOGCOG1362.
GeneTreeENSGT00390000003164.
HOGENOMHOG000253244.
HOVERGENHBG051386.
InParanoidQ56A00.
KOK01267.
OMAIVKCPTS.
OrthoDBEOG789CB1.
TreeFamTF300487.

Gene expression databases

ArrayExpressQ9Z2W0.
BgeeQ9Z2W0.
CleanExMM_DNPEP.
GenevestigatorQ9Z2W0.

Family and domain databases

Gene3D2.30.250.10. 1 hit.
InterProIPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSPR00932. AMINO1PTASE.
ProtoNetSearch...

Other

ChiTaRSDNPEP. mouse.
NextBio283883.
PROQ9Z2W0.
SOURCESearch...

Entry information

Entry nameDNPEP_MOUSE
AccessionPrimary (citable) accession number: Q9Z2W0
Secondary accession number(s): Q56A00
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 98 of the entry and version 2 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

MGD cross-references

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