Glutamyl aminopeptidase - Sus scrofa (Pig)

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Q95334 (AMPE_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
CD_antigen=CD249

Gene names

Name:

ENPEP

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	942 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1
Subcellular location	Membrane; Single-pass type II membrane protein.
Sequence similarities	Belongs to the peptidase M1 family.

Ontologies

Keywords
Cellular component	Membrane
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 Reference proteome
Gene Ontology (GO)
Biological_process	cell migration Inferred from sequence or structural similarity. Source: UniProtKB cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of systemic arterial blood pressure by renin-angiotensin Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metalloaminopeptidase activity Inferred from sequence or structural similarity. 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

942

Glutamyl aminopeptidase

PRO_0000095097

Regions

Topological domain

14

Cytoplasmic Potential

Transmembrane

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

907

Extracellular Potential

Region

5

Substrate binding By similarity

Sites

Active site

1

Proton acceptor By similarity

Metal binding

1

Zinc; catalytic By similarity

Metal binding

1

Zinc; catalytic By similarity

Metal binding

1

Zinc; catalytic By similarity

Binding site

1

Substrate By similarity

Site

1

Transition state stabilizer By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q95334 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: C531E639A588EF2E
Show »

942

108,284

        10         20         30         40         50         60 
MSTDSKRYCI KTKHVAIICA AVVAVGLIVG LSVGLTRSCD SKDGGQGTTQ SPSHLPPTSS 

        70         80         90        100        110        120 
PPQDQGVCPA SEDESGNWRD FRLPDFINPV HYDLQVKPLL EQDTYTGTVN ISINVTSPTQ 

       130        140        150        160        170        180 
HLWLHLRETR ITQLPVLWRP SGEQVQVRRC FEYKKQEYVV VEAEEELAPN SGEGLYHLTM 

       190        200        210        220        230        240 
EFAGWLNGSL VGFYRTTYVE KGQIKSIAAT DHEPTDARKS FPCFDEPNKK ATYTISIIHP 

       250        260        270        280        290        300 
KEYKALSNMP VEKEESVDDI WTQTTFQKSV PMSTYLVCFA VHQFDSVTRT SRSGKPLTIY 

       310        320        330        340        350        360 
VQPEQKHTAE YAANITKSVF DYFEDYFAME YSLPKLDKIA IPDFGTGAME NWGLITYRET 

       370        380        390        400        410        420 
NLLYDPNESA SSNQQRVAAV VAHELVHQWF GNIVTMEWWE DLWLNEGFAS FFEFLGVDHA 

       430        440        450        460        470        480 
EKEWQMRDQI LLEDVLPVQE DDSLISSHPI VVTVSTPAEI TSVFDGISYS KGASILRMLE 

       490        500        510        520        530        540 
DWITPEKFQK GCQEYLKKFE FKNAKTSDFW EALEEASNLP VKEVMDTWTN QMGYPVLNVE 

       550        560        570        580        590        600 
DMRIISQKRF LLDPNANSSE PHSVFGYTWN IPVRWTNDNE STITIYNRSE TGGITLNSSN 

       610        620        630        640        650        660 
PNGNAFLKIN PDHIGFYRVN YEVSTWEWIA TNLSLNHKDF STADRASLID DAFALARAQL 

       670        680        690        700        710        720 
LNYKEALNLT KYLKMEDEYL PWQRVISAVT YIISMFEDDK ELYPMIEKYF RDQVKPIADS 

       730        740        750        760        770        780 
LGWNDNGDHL TKLLRASVLG FACKMGDSNA LNNASHLFEQ WLTGTVSLPV NLRLLVYRYG 

       790        800        810        820        830        840 
MQNSGNETSW NYTLKQYQET SLAQEKEKLL YGLASVKNVA LLSRYLDLLK DPNVIKSQDV 

       850        860        870        880        890        900 
FTVIRYISYN SYGKTMAWNW IQLNWEYLVN RYTLNDRNLG RIVTIAEPFN TELQLWQMES 

       910        920        930        940 
FFKRYPEAGA GEKPREQVLE TVKNNIEWLK QNRDTIRDWF FN

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U66371 mRNA. Translation: AAB07141.1.
RefSeq	NP_999182.1. NM_214017.1.
UniGene	Ssc.83.
3D structure databases
ProteinModelPortal	Q95334.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000009739.
Protein family/group databases
MEROPS	M01.003.
Proteomic databases
PaxDb	Q95334.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397080.
KEGG	ssc:397080.
Organism-specific databases
CTD	2028.
Phylogenomic databases
eggNOG	COG0308.
HOGENOM	HOG000106482.
HOVERGEN	HBG006616.
KO	K11141.
OrthoDB	EOG4GF3DJ.
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
BindingDB	Q95334.
ChEMBL	CHEMBL4868.
PMAP-CutDB	Q95334.

Entry information

Entry name

AMPE_PIG

Accession

Primary (citable) accession number: Q95334

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents