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Protein

Glutamyl aminopeptidase

Gene

Enpep

Organism
Rattus norvegicus (Rat)
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. Isoform 1 has aminopeptidase activity while isoform 2 does not.

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151SubstrateBy similarity
Metal bindingi385 – 3851Zinc; catalyticPROSITE-ProRule annotation
Active sitei386 – 3861Proton acceptorPROSITE-ProRule annotation
Metal bindingi389 – 3891Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi408 – 4081Zinc; catalyticPROSITE-ProRule annotation
Sitei471 – 4711Transition state stabilizerBy similarity

GO - Molecular functioni

  • aminopeptidase activity Source: RGD
  • metalloaminopeptidase activity Source: UniProtKB
  • peptide binding Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

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
CD_antigen: CD249
Gene namesi
Name:Enpep
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621228. Enpep.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1818CytoplasmicSequence analysisAdd
BLAST
Transmembranei19 – 3921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini40 – 945906ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • vesicle lumen Source: RGD
  • vesicle membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 945945Glutamyl aminopeptidasePRO_0000095098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence analysis
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence analysis
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence analysis
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence analysis
Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence analysis
Glycosylationi584 – 5841N-linked (GlcNAc...)Sequence analysis
Glycosylationi601 – 6011N-linked (GlcNAc...)Sequence analysis
Glycosylationi640 – 6401N-linked (GlcNAc...)Sequence analysis
Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence analysis
Glycosylationi754 – 7541N-linked (GlcNAc...)Sequence analysis
Glycosylationi766 – 7661N-linked (GlcNAc...)Sequence analysis
Glycosylationi792 – 7921N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP50123.
PRIDEiP50123.

Expressioni

Tissue specificityi

Highest expression in kidney proximal tubules and ileum enterocytes. High expression also detected in liver and pituitary. Lower levels in heart, adrenal gland and brain. Not detected in aorta, lung or spleen. In heart, higher levels in ventricle than in atrium. Also expressed in glomerular mesangial cells.4 Publications

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

IntActiP50123. 1 interaction.
STRINGi10116.ENSRNOP00000064188.

Structurei

3D structure databases

ProteinModelPortaliP50123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni349 – 3535Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOVERGENiHBG006616.
InParanoidiP50123.
KOiK11141.
PhylomeDBiP50123.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P50123-1) [UniParc]FASTAAdd to basket

Also known as: APAL

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNFAEEEPSK KYCIKGKHVA IICATVVAVG LIVGLSVGLT RSCEPGTTPA
60 70 80 90 100
PSNPPPHTST ALPPQDQNVC PDSDDESGEW KNFRLPDFIQ PVHYDLEVKV
110 120 130 140 150
LMEEDRYTGI VSISVNLSKD TRDLWLHIRE TRITKLPELR RPSGEQVPIR
160 170 180 190 200
RCFEYKKQEY VVIQAEEDLA ATSGDSVYRL TIEFEGWLNG SLVGFYRTTY
210 220 230 240 250
TEDGQTKSIA ATDHEPTDAR KSFPCFDEPN KKATYNISLI HPKEYSALSN
260 270 280 290 300
MPVEKKETLD NDWKKTTFMK SVPMSTYLVC FAVHQFTSIQ RTSRSGKPLT
310 320 330 340 350
VYVQPNQKQT AEYAANITKA VFDFFEDYFA MEYSLPKLDK IAIPDFGTGA
360 370 380 390 400
MENWGLVTYR ETNLLYDPLL SASSNQQRVA SVVAHELVHQ WFGNIVTMDW
410 420 430 440 450
WDDLWLNEGF ASFFEFLGVN HAEADWQMLS QVLLEDVLPV QEDDSLMSSH
460 470 480 490 500
PVVVTVSTPA EITSVFDGIS YSKGASILRM LQDWITPEKF QKGCQIYLEN
510 520 530 540 550
FKFKNAKTSD FWDSLEKASN QPVKEVMDTW TSQMGYPVVT VSGKQNVTQK
560 570 580 590 600
RFLLDYKADP SQPPSALGYT WNIPIKWTEN GNSNITVYYR SNREGITLNA
610 620 630 640 650
NLSGDGFLKI NPDHIGFYRV NYEAETWDWI AETLSSNHMN FSSADRSSFI
660 670 680 690 700
DDAFALARAQ LLDYEKALNL TRYLTSEKDF LPWERVISAV SYIISMFEDD
710 720 730 740 750
RELYPLIETY FRSQVKPIAD SLGWQDTGSH ITKLLRASVL GFACKMGAGE
760 770 780 790 800
ALGNASQLFE AWLKGNESIP VNLRLLVYRY GMQNSGNEAA WNYTLEQYQK
810 820 830 840 850
TSLAQEKEKL LYGLASVKDV TLLARYLEML KDPNIIKTQD VFTVIRYISY
860 870 880 890 900
NSYGKSMAWN WIQLNWDYLV NRFTINDRYL GRIVTIAEPF NTELQLWQMQ
910 920 930 940
SFFAKYPNAG AGAKPREQVL ETVKNNIEWL KLNRKSISEW FTSMP
Length:945
Mass (Da):107,995
Last modified:July 25, 2003 - v2
Checksum:i5A74F1A537DC5937
GO
Isoform 2 (identifier: P50123-2) [UniParc]FASTAAdd to basket

Also known as: APAS

The sequence of this isoform differs from the canonical sequence as follows:
     569-573: YTWNI → NHFEC
     574-945: Missing.

Show »
Length:573
Mass (Da):64,959
Checksum:i74E326B115475340
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561K → E in AAF66704 (PubMed:10978538).Curated
Sequence conflicti256 – 2561K → E in AAF66710 (PubMed:10978538).Curated
Sequence conflicti306 – 3061N → K in AAF66704 (PubMed:10978538).Curated
Sequence conflicti306 – 3061N → K in AAF66710 (PubMed:10978538).Curated
Sequence conflicti748 – 7481A → D in AAF66704 (PubMed:10978538).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei569 – 5735YTWNI → NHFEC in isoform 2. 1 PublicationVSP_007844
Alternative sequencei574 – 945372Missing in isoform 2. 1 PublicationVSP_007845Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146044 mRNA. Translation: AAF66704.1.
AF146518 mRNA. Translation: AAF66710.1.
BC066663 mRNA. Translation: AAH66663.1.
AF214568 mRNA. Translation: AAF37622.1.
RefSeqiNP_071587.2. NM_022251.2.
UniGeneiRn.162610.

Genome annotation databases

GeneIDi64017.
KEGGirno:64017.
UCSCiRGD:621228. rat. [P50123-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146044 mRNA. Translation: AAF66704.1.
AF146518 mRNA. Translation: AAF66710.1.
BC066663 mRNA. Translation: AAH66663.1.
AF214568 mRNA. Translation: AAF37622.1.
RefSeqiNP_071587.2. NM_022251.2.
UniGeneiRn.162610.

3D structure databases

ProteinModelPortaliP50123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP50123. 1 interaction.
STRINGi10116.ENSRNOP00000064188.

Protein family/group databases

MEROPSiM01.003.

Proteomic databases

PaxDbiP50123.
PRIDEiP50123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64017.
KEGGirno:64017.
UCSCiRGD:621228. rat. [P50123-1]

Organism-specific databases

CTDi2028.
RGDi621228. Enpep.

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOVERGENiHBG006616.
InParanoidiP50123.
KOiK11141.
PhylomeDBiP50123.

Miscellaneous databases

NextBioi612602.
PROiP50123.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Aminopeptidase-A. I. cDNA cloning and expression and localization in rat tissues."
    Troyanovskaya M., Jayaraman G., Song L., Healy D.P.
    Am. J. Physiol. 278:R413-R424(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "Molecular cloning and expression of aminopeptidase A isoforms from rat hippocampus."
    Lee H.-J., Tomioka M., Takaki Y., Masumoto H., Saido T.C.
    Biochim. Biophys. Acta 1493:273-278(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  3. "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] (ISOFORM 1).
    Tissue: Prostate.
  4. "Rat kidney glutamyl aminopeptidase (aminopeptidase A): molecular identity and cellular localization."
    Song L., Ye M., Troyanovskaya M., Wilk E., Wilk S., Healy D.P.
    Am. J. Physiol. 267:F546-F557(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 265-397, PROTEIN SEQUENCE OF 714-731 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Kidney.
  5. "Expression of aminopeptidase A, an angiotensinase, in glomerular mesangial cells."
    Troyanovskaya M., Song L., Jayaraman G., Healy D.P.
    Hypertension 27:518-522(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 482-606 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Kidney.

Entry informationi

Entry nameiAMPE_RAT
AccessioniPrimary (citable) accession number: P50123
Secondary accession number(s): Q64200
, Q9JLQ7, Q9JLQ9, Q9QV24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 25, 2003
Last modified: May 11, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.