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Protein

Aspartyl aminopeptidase

Gene

DNPEP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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+Note: Binds 2 Zn2+ ions per subunit.

Enzyme regulationi

One of the zinc ions is readily exchangeable with other divalent cations such as manganese, which strongly stimulates the enzymatic activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901Zinc 1
Binding sitei166 – 1661SubstrateBy similarity
Metal bindingi260 – 2601Zinc 1
Metal bindingi260 – 2601Zinc 2
Binding sitei297 – 2971SubstrateBy similarity
Metal bindingi298 – 2981Zinc 2
Metal bindingi342 – 3421Zinc 1
Binding sitei342 – 3421SubstrateBy similarity
Binding sitei345 – 3451SubstrateBy similarity
Binding sitei370 – 3701SubstrateBy similarity
Binding sitei377 – 3771SubstrateBy similarity
Metal bindingi436 – 4361Zinc 2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM18.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartyl aminopeptidase (EC:3.4.11.21)
Gene namesi
Name:DNPEP
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Aspartyl aminopeptidasePRO_0000284910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ2HJH1.
PeptideAtlasiQ2HJH1.
PRIDEiQ2HJH1.

Interactioni

Subunit structurei

Tetrahedron-shaped homododecamer built from six homodimers.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000028671.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2218Combined sources
Helixi27 – 4014Combined sources
Beta strandi59 – 646Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 747Combined sources
Beta strandi84 – 907Combined sources
Beta strandi95 – 10612Combined sources
Beta strandi109 – 11911Combined sources
Helixi122 – 1254Combined sources
Beta strandi130 – 13910Combined sources
Turni141 – 1433Combined sources
Beta strandi146 – 1527Combined sources
Helixi165 – 1673Combined sources
Turni169 – 1735Combined sources
Turni179 – 1835Combined sources
Beta strandi186 – 1894Combined sources
Helixi190 – 1967Combined sources
Helixi214 – 22411Combined sources
Helixi228 – 2303Combined sources
Beta strandi231 – 24010Combined sources
Beta strandi245 – 2473Combined sources
Turni248 – 2514Combined sources
Beta strandi253 – 2564Combined sources
Helixi259 – 27517Combined sources
Helixi279 – 2846Combined sources
Beta strandi287 – 2959Combined sources
Helixi297 – 2993Combined sources
Beta strandi303 – 3064Combined sources
Helixi311 – 32010Combined sources
Helixi328 – 3325Combined sources
Helixi333 – 3353Combined sources
Beta strandi337 – 3415Combined sources
Helixi352 – 3543Combined sources
Beta strandi368 – 3703Combined sources
Turni373 – 3764Combined sources
Helixi381 – 39414Combined sources
Beta strandi399 – 4013Combined sources
Helixi413 – 4219Combined sources
Beta strandi424 – 4296Combined sources
Beta strandi431 – 4344Combined sources
Beta strandi437 – 4448Combined sources
Helixi445 – 46622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VARX-ray2.25A3-471[»]
3VATX-ray2.10A3-471[»]
ProteinModelPortaliQ2HJH1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M18 family.Curated

Phylogenomic databases

eggNOGiKOG2596. Eukaryota.
COG1362. LUCA.
GeneTreeiENSGT00390000003164.
HOGENOMiHOG000253244.
HOVERGENiHBG051386.
InParanoidiQ2HJH1.
KOiK01267.
OMAiDDWDLQP.
OrthoDBiEOG789CB1.
TreeFamiTF300487.

Family and domain databases

Gene3Di2.30.250.10. 1 hit.
InterProiIPR014720. dsRBD_dom.
IPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamiPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSiPR00932. AMINO1PTASE.

Sequencei

Sequence statusi: Complete.

Q2HJH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRARKEAV QAAARELLKF VNRSPSPFHA VAECRSRLLQ AGFHELKETE
60 70 80 90 100
SWDIKPESKY FLTRNSSTII AFAVGGQYVP GNGFSLIGAH TDSPCLRVKR
110 120 130 140 150
RSRRSQVGFQ QVGVETYGGG IWSTWFDRDL TLAGRVIVKC PTSGRLEQRL
160 170 180 190 200
VHVDRPILRI PHLAIHLQRN VNENFGPNME MHLVPILATS IQEELEKGTP
210 220 230 240 250
EPGPLNATDE RHHSVLTSLL CAHLGLSPED ILEMELCLAD TQPAVLGGAY
260 270 280 290 300
EEFIFAPRLD NLHSCFCALQ ALIDSCSAPA SLAADPHVRM IALYDNEEVG
310 320 330 340 350
SESAQGAQSL LTELVLRRIS ASPQHLTAFE EAIPKSYMIS ADMAHAVHPN
360 370 380 390 400
YLDKHEENHR PLFHKGPVIK VNSKQRYASN AVSEALIREV ASSVGVPLQD
410 420 430 440 450
LMVRNDSPCG TTIGPILASR LGLRVLDLGS PQLAMHSIRE TACTTGVLQT
460 470
ITLFKGFFEL FPSLSRSLLV D
Length:471
Mass (Da):51,828
Last modified:March 21, 2006 - v1
Checksum:i35BD6BBAE2D5158C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC105402 mRNA. Translation: AAI05403.1.
RefSeqiNP_001039417.1. NM_001045952.1.
UniGeneiBt.20307.

Genome annotation databases

EnsembliENSBTAT00000028671; ENSBTAP00000028671; ENSBTAG00000021514.
GeneIDi506882.
KEGGibta:506882.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC105402 mRNA. Translation: AAI05403.1.
RefSeqiNP_001039417.1. NM_001045952.1.
UniGeneiBt.20307.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VARX-ray2.25A3-471[»]
3VATX-ray2.10A3-471[»]
ProteinModelPortaliQ2HJH1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000028671.

Protein family/group databases

MEROPSiM18.002.

Proteomic databases

PaxDbiQ2HJH1.
PeptideAtlasiQ2HJH1.
PRIDEiQ2HJH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000028671; ENSBTAP00000028671; ENSBTAG00000021514.
GeneIDi506882.
KEGGibta:506882.

Organism-specific databases

CTDi23549.

Phylogenomic databases

eggNOGiKOG2596. Eukaryota.
COG1362. LUCA.
GeneTreeiENSGT00390000003164.
HOGENOMiHOG000253244.
HOVERGENiHBG051386.
InParanoidiQ2HJH1.
KOiK01267.
OMAiDDWDLQP.
OrthoDBiEOG789CB1.
TreeFamiTF300487.

Family and domain databases

Gene3Di2.30.250.10. 1 hit.
InterProiIPR014720. dsRBD_dom.
IPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamiPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSiPR00932. AMINO1PTASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  2. "Insights into substrate specificity and metal activation of mammalian tetrahedral aspartyl aminopeptidase."
    Chen Y., Farquhar E.R., Chance M.R., Palczewski K., Kiser P.D.
    J. Biol. Chem. 287:13356-13370(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 3-471, ELECTRON MICROSCOPY (22 ANGSTROMS), ZINC-BINDING SITES, ENZYME REGULATION.

Entry informationi

Entry nameiDNPEP_BOVIN
AccessioniPrimary (citable) accession number: Q2HJH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 21, 2006
Last modified: July 6, 2016
This is version 73 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.