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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)DescriptionActionsGraphical viewLength
Metal bindingi90Zinc 11
Binding sitei166SubstrateBy similarity1
Metal bindingi260Zinc 11
Metal bindingi260Zinc 21
Binding sitei297SubstrateBy similarity1
Metal bindingi298Zinc 21
Metal bindingi342Zinc 11
Binding sitei342SubstrateBy similarity1
Binding sitei345SubstrateBy similarity1
Binding sitei370SubstrateBy similarity1
Binding sitei377SubstrateBy similarity1
Metal bindingi436Zinc 21

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002849101 – 471Aspartyl aminopeptidaseAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei199PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ2HJH1.
PeptideAtlasiQ2HJH1.
PRIDEiQ2HJH1.

Expressioni

Gene expression databases

BgeeiENSBTAG00000021514.

Interactioni

Subunit structurei

Tetrahedron-shaped homododecamer built from six homodimers.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000028671.

Structurei

Secondary structure

1471
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 22Combined sources18
Helixi27 – 40Combined sources14
Beta strandi59 – 64Combined sources6
Turni65 – 67Combined sources3
Beta strandi68 – 74Combined sources7
Beta strandi84 – 90Combined sources7
Beta strandi95 – 106Combined sources12
Beta strandi109 – 119Combined sources11
Helixi122 – 125Combined sources4
Beta strandi130 – 139Combined sources10
Turni141 – 143Combined sources3
Beta strandi146 – 152Combined sources7
Helixi165 – 167Combined sources3
Turni169 – 173Combined sources5
Turni179 – 183Combined sources5
Beta strandi186 – 189Combined sources4
Helixi190 – 196Combined sources7
Helixi214 – 224Combined sources11
Helixi228 – 230Combined sources3
Beta strandi231 – 240Combined sources10
Beta strandi245 – 247Combined sources3
Turni248 – 251Combined sources4
Beta strandi253 – 256Combined sources4
Helixi259 – 275Combined sources17
Helixi279 – 284Combined sources6
Beta strandi287 – 295Combined sources9
Helixi297 – 299Combined sources3
Beta strandi303 – 306Combined sources4
Helixi311 – 320Combined sources10
Helixi328 – 332Combined sources5
Helixi333 – 335Combined sources3
Beta strandi337 – 341Combined sources5
Helixi352 – 354Combined sources3
Beta strandi368 – 370Combined sources3
Turni373 – 376Combined sources4
Helixi381 – 394Combined sources14
Beta strandi399 – 401Combined sources3
Helixi413 – 421Combined sources9
Beta strandi424 – 429Combined sources6
Beta strandi431 – 434Combined sources4
Beta strandi437 – 444Combined sources8
Helixi445 – 466Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VARX-ray2.25A3-471[»]
3VATX-ray2.10A3-471[»]
ProteinModelPortaliQ2HJH1.
SMRiQ2HJH1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M18 family.Curated

Phylogenomic databases

eggNOGiKOG2596. Eukaryota.
COG1362. LUCA.
GeneTreeiENSGT00390000003164.
HOGENOMiHOG000253244.
HOVERGENiHBG051386.
InParanoidiQ2HJH1.
KOiK01267.
OMAiPDKHEEH.
OrthoDBiEOG091G06FO.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VARX-ray2.25A3-471[»]
3VATX-ray2.10A3-471[»]
ProteinModelPortaliQ2HJH1.
SMRiQ2HJH1.
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.
OMAiPDKHEEH.
OrthoDBiEOG091G06FO.
TreeFamiTF300487.

Gene expression databases

BgeeiENSBTAG00000021514.

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...

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: November 2, 2016
This is version 75 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.