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Protein

Glutamyl aminopeptidase

Gene

ENPEP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Appears to have a role in the catabolic pathway of the renin-angiotensin system. Probably plays a role in regulating growth and differentiation of early B-lineage cells.

Catalytic activityi

Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei223SubstrateBy similarity1
Metal bindingi393Zinc; catalyticPROSITE-ProRule annotation1
Active sitei394Proton acceptorPROSITE-ProRule annotation1
Metal bindingi397Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi416Zinc; catalyticPROSITE-ProRule annotation1
Sitei479Transition state stabilizerBy similarity1

GO - Molecular functioni

  • aminopeptidase activity Source: UniProtKB
  • metalloaminopeptidase activity Source: UniProtKB
  • metallopeptidase activity Source: Reactome
  • peptide binding Source: GO_Central
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • angiotensin catabolic process in blood Source: UniProtKB
  • angiotensin maturation Source: Reactome
  • cell-cell signaling Source: UniProtKB
  • cell migration Source: MGI
  • cell proliferation Source: UniProtKB
  • glomerulus development Source: UniProtKB
  • peptide catabolic process Source: GO_Central
  • regulation of systemic arterial blood pressure by renin-angiotensin Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS06560-MONOMER.
ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.

Protein family/group databases

MEROPSiM01.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl aminopeptidase (EC:3.4.11.7)
Short name:
EAP
Alternative name(s):
Aminopeptidase A
Short name:
AP-A
Differentiation antigen gp160
CD_antigen: CD249
Gene namesi
Name:ENPEP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3355. ENPEP.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 18CytoplasmicSequence analysisAdd BLAST18
Transmembranei19 – 39Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini40 – 957ExtracellularSequence analysisAdd BLAST918

GO - Cellular componenti

  • apical part of cell Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • brush border Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • external side of plasma membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2028.
OpenTargetsiENSG00000138792.
PharmGKBiPA27790.

Chemistry databases

ChEMBLiCHEMBL3439.

Polymorphism and mutation databases

BioMutaiENPEP.
DMDMi296439445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000950951 – 957Glutamyl aminopeptidaseAdd BLAST957

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi124N-linked (GlcNAc...)1 Publication1
Glycosylationi197N-linked (GlcNAc...)Sequence analysis1
Glycosylationi324N-linked (GlcNAc...)1 Publication1
Glycosylationi340N-linked (GlcNAc...)Sequence analysis1
Glycosylationi554N-linked (GlcNAc...)Sequence analysis1
Glycosylationi589N-linked (GlcNAc...)Sequence analysis1
Glycosylationi597N-linked (GlcNAc...)Sequence analysis1
Glycosylationi607N-linked (GlcNAc...)2 Publications1
Glycosylationi610N-linked (GlcNAc...)1 Publication1
Glycosylationi678N-linked (GlcNAc...)Sequence analysis1
Glycosylationi763N-linked (GlcNAc...)1 Publication1
Glycosylationi773N-linked (GlcNAc...)1 Publication1
Glycosylationi801N-linked (GlcNAc...)Sequence analysis1
Glycosylationi828N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ07075.
MaxQBiQ07075.
PaxDbiQ07075.
PeptideAtlasiQ07075.
PRIDEiQ07075.

PTM databases

iPTMnetiQ07075.
PhosphoSitePlusiQ07075.

Expressioni

Tissue specificityi

Expressed by epithelial cells of the proximal tubule cells and the glomerulus of the nephron. Also found in a variety of other tissues.

Gene expression databases

BgeeiENSG00000138792.
CleanExiHS_ENPEP.
ExpressionAtlasiQ07075. baseline and differential.
GenevisibleiQ07075. HS.

Organism-specific databases

HPAiHPA005128.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

BioGridi108342. 2 interactors.
IntActiQ07075. 3 interactors.
STRINGi9606.ENSP00000265162.

Chemistry databases

BindingDBiQ07075.

Structurei

Secondary structure

1957
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi87 – 89Combined sources3
Beta strandi90 – 92Combined sources3
Beta strandi97 – 109Combined sources13
Helixi110 – 112Combined sources3
Beta strandi114 – 125Combined sources12
Beta strandi129 – 135Combined sources7
Beta strandi138 – 148Combined sources11
Beta strandi157 – 163Combined sources7
Helixi164 – 166Combined sources3
Beta strandi168 – 177Combined sources10
Beta strandi181 – 183Combined sources3
Beta strandi186 – 195Combined sources10
Beta strandi200 – 210Combined sources11
Beta strandi213 – 221Combined sources9
Turni223 – 226Combined sources4
Helixi227 – 230Combined sources4
Beta strandi241 – 250Combined sources10
Beta strandi253 – 259Combined sources7
Beta strandi261 – 276Combined sources16
Helixi284 – 286Combined sources3
Beta strandi289 – 292Combined sources4
Beta strandi295 – 300Combined sources6
Beta strandi306 – 311Combined sources6
Helixi313 – 319Combined sources7
Helixi320 – 336Combined sources17
Beta strandi342 – 344Combined sources3
Beta strandi346 – 353Combined sources8
Beta strandi355 – 359Combined sources5
Beta strandi364 – 368Combined sources5
Helixi369 – 371Combined sources3
Turni376 – 378Combined sources3
Helixi381 – 397Combined sources17
Turni401 – 403Combined sources3
Beta strandi404 – 408Combined sources5
Helixi409 – 412Combined sources4
Helixi413 – 430Combined sources18
Helixi432 – 434Combined sources3
Helixi436 – 443Combined sources8
Helixi445 – 451Combined sources7
Helixi467 – 472Combined sources6
Helixi476 – 493Combined sources18
Helixi495 – 508Combined sources14
Beta strandi512 – 514Combined sources3
Helixi516 – 527Combined sources12
Helixi531 – 535Combined sources5
Helixi536 – 538Combined sources3
Beta strandi545 – 550Combined sources6
Turni551 – 553Combined sources3
Beta strandi554 – 559Combined sources6
Turni574 – 577Combined sources4
Beta strandi581 – 587Combined sources7
Beta strandi590 – 596Combined sources7
Beta strandi618 – 620Combined sources3
Helixi621 – 623Combined sources3
Beta strandi625 – 630Combined sources6
Helixi633 – 646Combined sources14
Helixi647 – 649Combined sources3
Helixi652 – 667Combined sources16
Helixi673 – 678Combined sources6
Turni679 – 682Combined sources4
Helixi683 – 685Combined sources3
Helixi689 – 705Combined sources17
Turni706 – 708Combined sources3
Helixi712 – 731Combined sources20
Helixi739 – 754Combined sources16
Helixi758 – 771Combined sources14
Turni780 – 782Combined sources3
Helixi783 – 794Combined sources12
Helixi797 – 809Combined sources13
Helixi813 – 823Combined sources11
Helixi829 – 838Combined sources10
Turni842 – 844Combined sources3
Helixi847 – 849Combined sources3
Helixi850 – 858Combined sources9
Helixi863 – 873Combined sources11
Helixi875 – 882Combined sources8
Helixi887 – 891Combined sources5
Helixi892 – 896Combined sources5
Helixi902 – 914Combined sources13
Helixi919 – 921Combined sources3
Helixi922 – 953Combined sources32

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KX7X-ray2.15A76-957[»]
4KX8X-ray2.40A76-957[»]
4KX9X-ray2.25A76-957[»]
4KXAX-ray2.40A76-957[»]
4KXBX-ray2.40A76-957[»]
4KXCX-ray2.40A76-957[»]
4KXDX-ray2.15A76-957[»]
ProteinModelPortaliQ07075.
SMRiQ07075.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni357 – 361Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiQ07075.
KOiK11141.
OMAiQVQVRRC.
OrthoDBiEOG091G01GH.
PhylomeDBiQ07075.
TreeFamiTF300395.

Family and domain databases

InterProiIPR033508. Aminopeptidase_A.
IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PTHR11533:SF188. PTHR11533:SF188. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07075-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFAEREGSK RYCIQTKHVA ILCAVVVGVG LIVGLAVGLT RSCDSSGDGG
60 70 80 90 100
PGTAPAPSHL PSSTASPSGP PAQDQDICPA SEDESGQWKN FRLPDFVNPV
110 120 130 140 150
HYDLHVKPLL EEDTYTGTVS ISINLSAPTR YLWLHLRETR ITRLPELKRP
160 170 180 190 200
SGDQVQVRRC FEYKKQEYVV VEAEEELTPS SGDGLYLLTM EFAGWLNGSL
210 220 230 240 250
VGFYRTTYTE NGQVKSIVAT DHEPTDARKS FPCFDEPNKK ATYTISITHP
260 270 280 290 300
KEYGALSNMP VAKEESVDDK WTRTTFEKSV PMSTYLVCFA VHQFDSVKRI
310 320 330 340 350
SNSGKPLTIY VQPEQKHTAE YAANITKSVF DYFEEYFAMN YSLPKLDKIA
360 370 380 390 400
IPDFGTGAME NWGLITYRET NLLYDPKESA SSNQQRVATV VAHELVHQWF
410 420 430 440 450
GNIVTMDWWE DLWLNEGFAS FFEFLGVNHA ETDWQMRDQM LLEDVLPVQE
460 470 480 490 500
DDSLMSSHPI IVTVTTPDEI TSVFDGISYS KGSSILRMLE DWIKPENFQK
510 520 530 540 550
GCQMYLEKYQ FKNAKTSDFW AALEEASRLP VKEVMDTWTR QMGYPVLNVN
560 570 580 590 600
GVKNITQKRF LLDPRANPSQ PPSDLGYTWN IPVKWTEDNI TSSVLFNRSE
610 620 630 640 650
KEGITLNSSN PSGNAFLKIN PDHIGFYRVN YEVATWDSIA TALSLNHKTF
660 670 680 690 700
SSADRASLID DAFALARAQL LDYKVALNLT KYLKREENFL PWQRVISAVT
710 720 730 740 750
YIISMFEDDK ELYPMIEEYF QGQVKPIADS LGWNDAGDHV TKLLRSSVLG
760 770 780 790 800
FACKMGDREA LNNASSLFEQ WLNGTVSLPV NLRLLVYRYG MQNSGNEISW
810 820 830 840 850
NYTLEQYQKT SLAQEKEKLL YGLASVKNVT LLSRYLDLLK DTNLIKTQDV
860 870 880 890 900
FTVIRYISYN SYGKNMAWNW IQLNWDYLVN RYTLNNRNLG RIVTIAEPFN
910 920 930 940 950
TELQLWQMES FFAKYPQAGA GEKPREQVLE TVKNNIEWLK QHRNTIREWF

FNLLESG
Length:957
Mass (Da):109,244
Last modified:May 18, 2010 - v3
Checksum:iAB6407432A45A7C6
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030359213Q → R.4 PublicationsCorresponds to variant rs10004516dbSNPEnsembl.1
Natural variantiVAR_030360218V → A.1 PublicationCorresponds to variant rs1126483dbSNPEnsembl.1
Natural variantiVAR_057056437R → H.Corresponds to variant rs34949711dbSNPEnsembl.1
Natural variantiVAR_057057861S → R.Corresponds to variant rs35812243dbSNPEnsembl.1
Natural variantiVAR_036047887R → T in a breast cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14721 mRNA. Translation: AAA35522.1.
L12468 mRNA. Translation: AAA16876.1.
AC017068 Genomic DNA. No translation available.
AC098798 Genomic DNA. No translation available.
BC094770 mRNA. Translation: AAH94770.1.
CCDSiCCDS3691.1.
PIRiA47531.
RefSeqiNP_001968.3. NM_001977.3.
UniGeneiHs.435765.

Genome annotation databases

EnsembliENST00000265162; ENSP00000265162; ENSG00000138792.
GeneIDi2028.
KEGGihsa:2028.
UCSCiuc003iab.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14721 mRNA. Translation: AAA35522.1.
L12468 mRNA. Translation: AAA16876.1.
AC017068 Genomic DNA. No translation available.
AC098798 Genomic DNA. No translation available.
BC094770 mRNA. Translation: AAH94770.1.
CCDSiCCDS3691.1.
PIRiA47531.
RefSeqiNP_001968.3. NM_001977.3.
UniGeneiHs.435765.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KX7X-ray2.15A76-957[»]
4KX8X-ray2.40A76-957[»]
4KX9X-ray2.25A76-957[»]
4KXAX-ray2.40A76-957[»]
4KXBX-ray2.40A76-957[»]
4KXCX-ray2.40A76-957[»]
4KXDX-ray2.15A76-957[»]
ProteinModelPortaliQ07075.
SMRiQ07075.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108342. 2 interactors.
IntActiQ07075. 3 interactors.
STRINGi9606.ENSP00000265162.

Chemistry databases

BindingDBiQ07075.
ChEMBLiCHEMBL3439.

Protein family/group databases

MEROPSiM01.003.

PTM databases

iPTMnetiQ07075.
PhosphoSitePlusiQ07075.

Polymorphism and mutation databases

BioMutaiENPEP.
DMDMi296439445.

Proteomic databases

EPDiQ07075.
MaxQBiQ07075.
PaxDbiQ07075.
PeptideAtlasiQ07075.
PRIDEiQ07075.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265162; ENSP00000265162; ENSG00000138792.
GeneIDi2028.
KEGGihsa:2028.
UCSCiuc003iab.5. human.

Organism-specific databases

CTDi2028.
DisGeNETi2028.
GeneCardsiENPEP.
H-InvDBHIX0024609.
HGNCiHGNC:3355. ENPEP.
HPAiHPA005128.
MIMi138297. gene.
neXtProtiNX_Q07075.
OpenTargetsiENSG00000138792.
PharmGKBiPA27790.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiQ07075.
KOiK11141.
OMAiQVQVRRC.
OrthoDBiEOG091G01GH.
PhylomeDBiQ07075.
TreeFamiTF300395.

Enzyme and pathway databases

BioCyciZFISH:HS06560-MONOMER.
ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.

Miscellaneous databases

ChiTaRSiENPEP. human.
GenomeRNAii2028.
PROiQ07075.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138792.
CleanExiHS_ENPEP.
ExpressionAtlasiQ07075. baseline and differential.
GenevisibleiQ07075. HS.

Family and domain databases

InterProiIPR033508. Aminopeptidase_A.
IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PTHR11533:SF188. PTHR11533:SF188. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMPE_HUMAN
AccessioniPrimary (citable) accession number: Q07075
Secondary accession number(s): Q504U2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 18, 2010
Last modified: November 2, 2016
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Peptidase families
    Classification of peptidase families and list of entries
  8. 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.