Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q07075 (AMPE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | 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:
Glutamyl aminopeptidase

Short name=EAP
EC=3.4.11.7
Alternative name(s):
Aminopeptidase A
Short name=AP-A
Differentiation antigen gp160
CD_antigen=CD249
Gene names
Name:ENPEP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length957 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer; disulfide-linked.

Subcellular location

Membrane; Single-pass type II membrane protein.

Tissue specificity

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

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

angiotensin catabolic process in blood

Non-traceable author statement PubMed 19608358. Source: UniProtKB

angiotensin maturation

Traceable author statement. Source: Reactome

cell migration

Inferred from direct assay PubMed 14998491. Source: MGI

cell proliferation

Non-traceable author statement Ref.1. Source: UniProtKB

cell-cell signaling

Non-traceable author statement Ref.1. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

glomerulus development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of systemic arterial blood pressure by renin-angiotensin

Inferred from direct assay PubMed 19608358. Source: UniProtKB

   Cellular_componentapical part of cell

Inferred from sequence or structural similarity. Source: UniProtKB

apical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

brush border

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

external side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of plasma membrane

Non-traceable author statement Ref.2. Source: UniProtKB

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionaminopeptidase activity

Inferred from direct assay Ref.2. Source: UniProtKB

metalloaminopeptidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

metallopeptidase activity

Inferred from experiment. Source: Reactome

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 957957Glutamyl aminopeptidase
PRO_0000095095

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 3921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain40 – 957918Extracellular Potential
Region357 – 3615Substrate binding By similarity

Sites

Active site3941Proton acceptor By similarity
Metal binding3931Zinc; catalytic By similarity
Metal binding3971Zinc; catalytic By similarity
Metal binding4161Zinc; catalytic By similarity
Binding site2231Substrate By similarity
Site4791Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Ref.6
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Ref.6
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation5541N-linked (GlcNAc...) Potential
Glycosylation5891N-linked (GlcNAc...) Potential
Glycosylation5971N-linked (GlcNAc...) Potential
Glycosylation6071N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation6101N-linked (GlcNAc...) Ref.6
Glycosylation6781N-linked (GlcNAc...) Potential
Glycosylation7631N-linked (GlcNAc...) Ref.6
Glycosylation7731N-linked (GlcNAc...) Ref.6
Glycosylation8011N-linked (GlcNAc...) Potential
Glycosylation8281N-linked (GlcNAc...) Potential

Natural variations

Natural variant2131Q → R. Ref.1 Ref.2 Ref.3 Ref.4
Corresponds to variant rs10004516 [ dbSNP | Ensembl ].
VAR_030359
Natural variant2181V → A. Ref.1
Corresponds to variant rs1126483 [ dbSNP | Ensembl ].
VAR_030360
Natural variant4371R → H.
Corresponds to variant rs34949711 [ dbSNP | Ensembl ].
VAR_057056
Natural variant8611S → R.
Corresponds to variant rs35812243 [ dbSNP | Ensembl ].
VAR_057057
Natural variant8871R → T in a breast cancer sample; somatic mutation. Ref.8
VAR_036047

Secondary structure

.............................................................................................................................................. 957
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07075 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: AB6407432A45A7C6

FASTA957109,244
        10         20         30         40         50         60 
MNFAEREGSK RYCIQTKHVA ILCAVVVGVG LIVGLAVGLT RSCDSSGDGG PGTAPAPSHL 

        70         80         90        100        110        120 
PSSTASPSGP PAQDQDICPA SEDESGQWKN FRLPDFVNPV HYDLHVKPLL EEDTYTGTVS 

       130        140        150        160        170        180 
ISINLSAPTR YLWLHLRETR ITRLPELKRP SGDQVQVRRC FEYKKQEYVV VEAEEELTPS 

       190        200        210        220        230        240 
SGDGLYLLTM EFAGWLNGSL VGFYRTTYTE NGQVKSIVAT DHEPTDARKS FPCFDEPNKK 

       250        260        270        280        290        300 
ATYTISITHP KEYGALSNMP VAKEESVDDK WTRTTFEKSV PMSTYLVCFA VHQFDSVKRI 

       310        320        330        340        350        360 
SNSGKPLTIY VQPEQKHTAE YAANITKSVF DYFEEYFAMN YSLPKLDKIA IPDFGTGAME 

       370        380        390        400        410        420 
NWGLITYRET NLLYDPKESA SSNQQRVATV VAHELVHQWF GNIVTMDWWE DLWLNEGFAS 

       430        440        450        460        470        480 
FFEFLGVNHA ETDWQMRDQM LLEDVLPVQE DDSLMSSHPI IVTVTTPDEI TSVFDGISYS 

       490        500        510        520        530        540 
KGSSILRMLE DWIKPENFQK GCQMYLEKYQ FKNAKTSDFW AALEEASRLP VKEVMDTWTR 

       550        560        570        580        590        600 
QMGYPVLNVN GVKNITQKRF LLDPRANPSQ PPSDLGYTWN IPVKWTEDNI TSSVLFNRSE 

       610        620        630        640        650        660 
KEGITLNSSN PSGNAFLKIN PDHIGFYRVN YEVATWDSIA TALSLNHKTF SSADRASLID 

       670        680        690        700        710        720 
DAFALARAQL LDYKVALNLT KYLKREENFL PWQRVISAVT YIISMFEDDK ELYPMIEEYF 

       730        740        750        760        770        780 
QGQVKPIADS LGWNDAGDHV TKLLRSSVLG FACKMGDREA LNNASSLFEQ WLNGTVSLPV 

       790        800        810        820        830        840 
NLRLLVYRYG MQNSGNEISW NYTLEQYQKT SLAQEKEKLL YGLASVKNVT LLSRYLDLLK 

       850        860        870        880        890        900 
DTNLIKTQDV FTVIRYISYN SYGKNMAWNW IQLNWDYLVN RYTLNNRNLG RIVTIAEPFN 

       910        920        930        940        950 
TELQLWQMES FFAKYPQAGA GEKPREQVLE TVKNNIEWLK QHRNTIREWF FNLLESG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the human kidney differentiation antigen gp160: human aminopeptidase A."
Nanus D.M., Engelstein D., Gastl G.A., Gluck L., Vidal M.J., Morrison M., Finstad C.L., Bander N.H., Albino A.P.
Proc. Natl. Acad. Sci. U.S.A. 90:7069-7073(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 242-251; 300-316 AND 369-377, VARIANTS ARG-213 AND ALA-218.
Tissue: Kidney cortex.
[2]"cDNA cloning and expression of human glutamyl aminopeptidase (aminopeptidase A)."
Li L., Wang J., Cooper M.D.
Genomics 17:657-664(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-213.
Tissue: Kidney.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-213.
[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], VARIANT ARG-213.
Tissue: Placenta.
[5]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-607.
Tissue: Plasma.
[6]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124; ASN-324; ASN-607; ASN-610; ASN-763 AND ASN-773.
Tissue: Liver.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-887.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3691.1.
PIRA47531.
RefSeqNP_001968.3. NM_001977.3.
UniGeneHs.435765.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ07075.
SMRQ07075. Positions 76-954.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ07075. 3 interactions.
STRING9606.ENSP00000265162.

Chemistry

ChEMBLCHEMBL3439.
DrugBankDB00142. L-Glutamic Acid.

Protein family/group databases

MEROPSM01.003.

PTM databases

PhosphoSiteQ07075.

Polymorphism databases

DMDM296439445.

Proteomic databases

MaxQBQ07075.
PaxDbQ07075.
PRIDEQ07075.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265162; ENSP00000265162; ENSG00000138792.
GeneID2028.
KEGGhsa:2028.
UCSCuc003iab.4. human.

Organism-specific databases

CTD2028.
GeneCardsGC04P111286.
H-InvDBHIX0024609.
HGNCHGNC:3355. ENPEP.
HPAHPA005128.
MIM138297. gene.
neXtProtNX_Q07075.
PharmGKBPA27790.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0308.
HOGENOMHOG000106482.
HOVERGENHBG006616.
InParanoidQ07075.
KOK11141.
OMANPVHYDL.
OrthoDBEOG754HNR.
PhylomeDBQ07075.
TreeFamTF300395.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

BgeeQ07075.
CleanExHS_ENPEP.
GenevestigatorQ07075.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi2028.
NextBio8213.
PROQ07075.
SOURCESearch...

Entry information

Entry nameAMPE_HUMAN
AccessionPrimary (citable) accession number: Q07075
Secondary accession number(s): Q504U2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries