Q07075 (AMPE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	957 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis 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 proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	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 integral to plasma membrane Non-traceable author statement Ref.2. Source: UniProtKB
Molecular_function	metalloaminopeptidase activity Inferred from direct assay Ref.1. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 957	957	Glutamyl aminopeptidase		PRO_0000095095
Regions
	Topological domain	1 – 18	18	Cytoplasmic Potential
	Transmembrane	19 – 39	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	40 – 957	918	Extracellular Potential
	Region	357 – 361	5	Substrate binding By similarity
Sites
	Active site	394	1	Proton acceptor By similarity
	Metal binding	393	1	Zinc; catalytic By similarity
	Metal binding	397	1	Zinc; catalytic By similarity
	Metal binding	416	1	Zinc; catalytic By similarity
	Binding site	223	1	Substrate By similarity
	Site	479	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	124	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	197	1	N-linked (GlcNAc...) Potential
	Glycosylation	324	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	340	1	N-linked (GlcNAc...) Potential
	Glycosylation	554	1	N-linked (GlcNAc...) Potential
	Glycosylation	589	1	N-linked (GlcNAc...) Potential
	Glycosylation	597	1	N-linked (GlcNAc...) Potential
	Glycosylation	607	1	N-linked (GlcNAc...) Ref.5 Ref.6
	Glycosylation	610	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	678	1	N-linked (GlcNAc...) Potential
	Glycosylation	763	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	773	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	801	1	N-linked (GlcNAc...) Potential
	Glycosylation	828	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	213	1	Q → R. Ref.1 Ref.2 Ref.3 Ref.4 Corresponds to variant rs10004516 [ dbSNP | Ensembl ].		VAR_030359
	Natural variant	218	1	V → A. Ref.1 Corresponds to variant rs1126483 [ dbSNP | Ensembl ].		VAR_030360
	Natural variant	437	1	R → H. Corresponds to variant rs34949711 [ dbSNP | Ensembl ].		VAR_057056
	Natural variant	861	1	S → R. Corresponds to variant rs35812243 [ dbSNP | Ensembl ].		VAR_057057
	Natural variant	887	1	R → T in a breast cancer sample; somatic mutation. Ref.8		VAR_036047

Sequences

	Sequence		Length	Mass (Da)
	Q07075 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: AB6407432A45A7C6	FASTA	957	109,244
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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. , 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.
IPI	IPI00014375.
PIR	A47531.
RefSeq	NP_001968.3. NM_001977.3.
UniGene	Hs.435765.
3D structure databases
ProteinModelPortal	Q07075.
SMR	Q07075. Positions 80-950.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q07075. 3 interactions.
STRING	9606.ENSP00000265162.
Protein family/group databases
MEROPS	M01.003.
PTM databases
PhosphoSite	Q07075.
Polymorphism databases
DMDM	296439445.
Proteomic databases
PaxDb	Q07075.
PRIDE	Q07075.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265162; ENSP00000265162; ENSG00000138792.
GeneID	2028.
KEGG	hsa:2028.
UCSC	uc003iab.4. human.
Organism-specific databases
CTD	2028.
GeneCards	GC04P111286.
H-InvDB	HIX0024609.
HGNC	HGNC:3355. ENPEP.
HPA	HPA005128.
MIM	138297. gene.
neXtProt	NX_Q07075.
PharmGKB	PA27790.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0308.
HOGENOM	HOG000106482.
HOVERGEN	HBG006616.
InParanoid	Q07075.
KO	K11141.
OMA	KHTAEYA.
OrthoDB	EOG4GF3DJ.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
Bgee	Q07075.
CleanEx	HS_ENPEP.
Genevestigator	Q07075.
GermOnline	ENSG00000138792. Homo sapiens.
Family and domain databases
InterPro	IPR024571. DUF3358. IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. [Graphical view]
PANTHER	PTHR11533. PTHR11533. 1 hit.
Pfam	PF11838. DUF3358. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL3439.
DrugBank	DB00142. L-Glutamic Acid.
GenomeRNAi	2028.
NextBio	8213.
SOURCE	Search...

Entry information

Entry name

AMPE_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.