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Protein

Glutamyl aminopeptidase

Gene

ENPEP

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 sitei213 – 2131SubstrateBy similarity
Metal bindingi383 – 3831Zinc; catalyticPROSITE-ProRule annotation
Active sitei384 – 3841Proton acceptorPROSITE-ProRule annotation
Metal bindingi387 – 3871Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi406 – 4061Zinc; catalyticPROSITE-ProRule annotation
Sitei469 – 4691Transition state stabilizerBy similarity

GO - Molecular functioni

  1. metalloaminopeptidase activity Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell migration Source: UniProtKB
  2. cell proliferation Source: UniProtKB
  3. 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

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei15 – 3521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini36 – 942907ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 942942Glutamyl aminopeptidasePRO_0000095097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi557 – 5571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi579 – 5791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi587 – 5871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi597 – 5971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi632 – 6321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi668 – 6681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi753 – 7531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi786 – 7861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi791 – 7911N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ95334.

Miscellaneous databases

PMAP-CutDBQ95334.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009739.

Structurei

3D structure databases

ProteinModelPortaliQ95334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni347 – 3515Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiQ95334.
KOiK11141.

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]

Sequencei

Sequence statusi: Complete.

Q95334-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTDSKRYCI KTKHVAIICA AVVAVGLIVG LSVGLTRSCD SKDGGQGTTQ
60 70 80 90 100
SPSHLPPTSS PPQDQGVCPA SEDESGNWRD FRLPDFINPV HYDLQVKPLL
110 120 130 140 150
EQDTYTGTVN ISINVTSPTQ HLWLHLRETR ITQLPVLWRP SGEQVQVRRC
160 170 180 190 200
FEYKKQEYVV VEAEEELAPN SGEGLYHLTM EFAGWLNGSL VGFYRTTYVE
210 220 230 240 250
KGQIKSIAAT DHEPTDARKS FPCFDEPNKK ATYTISIIHP KEYKALSNMP
260 270 280 290 300
VEKEESVDDI WTQTTFQKSV PMSTYLVCFA VHQFDSVTRT SRSGKPLTIY
310 320 330 340 350
VQPEQKHTAE YAANITKSVF DYFEDYFAME YSLPKLDKIA IPDFGTGAME
360 370 380 390 400
NWGLITYRET NLLYDPNESA SSNQQRVAAV VAHELVHQWF GNIVTMEWWE
410 420 430 440 450
DLWLNEGFAS FFEFLGVDHA EKEWQMRDQI LLEDVLPVQE DDSLISSHPI
460 470 480 490 500
VVTVSTPAEI TSVFDGISYS KGASILRMLE DWITPEKFQK GCQEYLKKFE
510 520 530 540 550
FKNAKTSDFW EALEEASNLP VKEVMDTWTN QMGYPVLNVE DMRIISQKRF
560 570 580 590 600
LLDPNANSSE PHSVFGYTWN IPVRWTNDNE STITIYNRSE TGGITLNSSN
610 620 630 640 650
PNGNAFLKIN PDHIGFYRVN YEVSTWEWIA TNLSLNHKDF STADRASLID
660 670 680 690 700
DAFALARAQL LNYKEALNLT KYLKMEDEYL PWQRVISAVT YIISMFEDDK
710 720 730 740 750
ELYPMIEKYF RDQVKPIADS LGWNDNGDHL TKLLRASVLG FACKMGDSNA
760 770 780 790 800
LNNASHLFEQ WLTGTVSLPV NLRLLVYRYG MQNSGNETSW NYTLKQYQET
810 820 830 840 850
SLAQEKEKLL YGLASVKNVA LLSRYLDLLK DPNVIKSQDV FTVIRYISYN
860 870 880 890 900
SYGKTMAWNW IQLNWEYLVN RYTLNDRNLG RIVTIAEPFN TELQLWQMES
910 920 930 940
FFKRYPEAGA GEKPREQVLE TVKNNIEWLK QNRDTIRDWF FN
Length:942
Mass (Da):108,284
Last modified:February 1, 1997 - v1
Checksum:iC531E639A588EF2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66371 mRNA. Translation: AAB07141.1.
RefSeqiNP_999182.1. NM_214017.1.
UniGeneiSsc.83.

Genome annotation databases

GeneIDi397080.
KEGGissc:397080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66371 mRNA. Translation: AAB07141.1.
RefSeqiNP_999182.1. NM_214017.1.
UniGeneiSsc.83.

3D structure databases

ProteinModelPortaliQ95334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009739.

Chemistry

BindingDBiQ95334.
ChEMBLiCHEMBL4868.

Protein family/group databases

MEROPSiM01.003.

Proteomic databases

PaxDbiQ95334.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397080.
KEGGissc:397080.

Organism-specific databases

CTDi2028.

Phylogenomic databases

eggNOGiCOG0308.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiQ95334.
KOiK11141.

Miscellaneous databases

PMAP-CutDBQ95334.

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

  1. "Proteolytic fragmentation reveals the oligomeric and domain structure of porcine aminopeptidase A."
    Hesp J.R., Hooper N.M.
    Biochemistry 36:3000-3007(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.

Entry informationi

Entry nameiAMPE_PIG
AccessioniPrimary (citable) accession number: Q95334
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 1, 1997
Last modified: January 7, 2015
This is version 92 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

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.