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Protein

Aspartyl aminopeptidase

Gene

Dnpep

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc 1By similarity
Binding sitei168 – 1681SubstrateBy similarity
Metal bindingi262 – 2621Zinc 1By similarity
Metal bindingi262 – 2621Zinc 2By similarity
Binding sitei299 – 2991SubstrateBy similarity
Metal bindingi300 – 3001Zinc 2By similarity
Metal bindingi344 – 3441Zinc 1By similarity
Binding sitei344 – 3441SubstrateBy similarity
Binding sitei347 – 3471SubstrateBy similarity
Binding sitei372 – 3721SubstrateBy similarity
Binding sitei379 – 3791SubstrateBy similarity
Metal bindingi438 – 4381Zinc 2By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.11.21. 3474.

Protein family/group databases

MEROPSiM18.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartyl aminopeptidase (EC:3.4.11.21)
Gene namesi
Name:Dnpep
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1278328. Dnpep.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: MGI
  2. cytoplasm Source: MGI
  3. nucleoplasm Source: MGI
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Aspartyl aminopeptidasePRO_0000173452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Z2W0.
PaxDbiQ9Z2W0.
PRIDEiQ9Z2W0.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2W0.

PTM databases

PhosphoSiteiQ9Z2W0.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9Z2W0.
CleanExiMM_DNPEP.
ExpressionAtlasiQ9Z2W0. baseline and differential.
GenevestigatoriQ9Z2W0.

Interactioni

Subunit structurei

Tetrahedron-shaped homododecamer built from six homodimers.By similarity

Protein-protein interaction databases

IntActiQ9Z2W0. 2 interactions.
MINTiMINT-4093364.
STRINGi10090.ENSMUSP00000070821.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2W0.
SMRiQ9Z2W0. Positions 5-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M18 family.Curated

Phylogenomic databases

eggNOGiCOG1362.
GeneTreeiENSGT00390000003164.
HOGENOMiHOG000253244.
HOVERGENiHBG051386.
InParanoidiQ9Z2W0.
KOiK01267.
OMAiDDWDLQP.
OrthoDBiEOG789CB1.
TreeFamiTF300487.

Family and domain databases

Gene3Di2.30.250.10. 1 hit.
InterProiIPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamiPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSiPR00932. AMINO1PTASE.

Sequencei

Sequence statusi: Complete.

Q9Z2W0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMNGRARKE AIQATARELL KFVNRSPSPF HVVAECRSRL LQAGFRELKE
60 70 80 90 100
TEGWDIVPEN KYFLTRNSSS IIAFAVGGQY VPGNGFSLIG AHTDSPCLRV
110 120 130 140 150
KRKSRRSQVG YHQVGVETYG GGIWSTWFDR DLTLAGRVII KCPTSGRLEQ
160 170 180 190 200
RLVHIERPIL RIPHLAIHLQ RNINENFGPN TEIHLVPILA TAVQEELEKG
210 220 230 240 250
TPEPGPLGAT DERHHSVLMS LLCTHLGLSP DSIMEMELCL ADTQPAVLGG
260 270 280 290 300
AYEEFIFAPR LDNLHSCFCA LQALIDSCAS PASLARDPHV RMVTLYDNEE
310 320 330 340 350
VGSESAQGAQ SLLTELILRR ISASPQRLTA FEEAIPKSFM ISADMAHAVH
360 370 380 390 400
PNYSDKHEEN HRPLFHKGPV IKVNSKQRYA SNAVSESMIR EVAGQVGVPL
410 420 430 440 450
QDLMVRNDSP CGTTIGPILA SRLGLRVLDL GSPQLAMHSI RETACTTGVL
460 470
QTLTLFKGFF ELFPSVSRNL LVD
Length:473
Mass (Da):52,207
Last modified:July 27, 2011 - v2
Checksum:i0350CC27C4A5AC8E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611K → N in AAD01212 (PubMed:9632644).Curated
Sequence conflicti364 – 3641L → S in AAD01212 (PubMed:9632644).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15070.1.
RefSeqiNP_001104301.1. NM_001110831.1.
NP_058574.3. NM_016878.4.
XP_006496468.1. XM_006496405.1.
XP_006496469.1. XM_006496406.1.
UniGeneiMm.24680.

Genome annotation databases

EnsembliENSMUST00000066668; ENSMUSP00000070821; ENSMUSG00000026209.
ENSMUST00000113605; ENSMUSP00000109235; ENSMUSG00000026209.
ENSMUST00000187836; ENSMUSP00000139739; ENSMUSG00000026209.
GeneIDi13437.
KEGGimmu:13437.
UCSCiuc007bot.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15070.1.
RefSeqiNP_001104301.1. NM_001110831.1.
NP_058574.3. NM_016878.4.
XP_006496468.1. XM_006496405.1.
XP_006496469.1. XM_006496406.1.
UniGeneiMm.24680.

3D structure databases

ProteinModelPortaliQ9Z2W0.
SMRiQ9Z2W0. Positions 5-473.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z2W0. 2 interactions.
MINTiMINT-4093364.
STRINGi10090.ENSMUSP00000070821.

Protein family/group databases

MEROPSiM18.002.

PTM databases

PhosphoSiteiQ9Z2W0.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2W0.

Proteomic databases

MaxQBiQ9Z2W0.
PaxDbiQ9Z2W0.
PRIDEiQ9Z2W0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066668; ENSMUSP00000070821; ENSMUSG00000026209.
ENSMUST00000113605; ENSMUSP00000109235; ENSMUSG00000026209.
ENSMUST00000187836; ENSMUSP00000139739; ENSMUSG00000026209.
GeneIDi13437.
KEGGimmu:13437.
UCSCiuc007bot.2. mouse.

Organism-specific databases

CTDi23549.
MGIiMGI:1278328. Dnpep.

Phylogenomic databases

eggNOGiCOG1362.
GeneTreeiENSGT00390000003164.
HOGENOMiHOG000253244.
HOVERGENiHBG051386.
InParanoidiQ9Z2W0.
KOiK01267.
OMAiDDWDLQP.
OrthoDBiEOG789CB1.
TreeFamiTF300487.

Enzyme and pathway databases

BRENDAi3.4.11.21. 3474.

Miscellaneous databases

NextBioi283883.
PROiQ9Z2W0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2W0.
CleanExiMM_DNPEP.
ExpressionAtlasiQ9Z2W0. baseline and differential.
GenevestigatoriQ9Z2W0.

Family and domain databases

Gene3Di2.30.250.10. 1 hit.
InterProiIPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamiPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSiPR00932. AMINO1PTASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase."
    Wilk S., Wilk E., Magnusson R.P.
    J. Biol. Chem. 273:15961-15970(1997) [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.
    , 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(2004) [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 (JUN-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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Eye.

Entry informationi

Entry nameiDNPEP_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2W0
Secondary accession number(s): Q56A00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.