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Q95334

- AMPE_PIG

UniProt

Q95334 - AMPE_PIG

Protein

Glutamyl aminopeptidase

Gene

ENPEP

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    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

    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: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1414CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini36 – 942907ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei15 – 3521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    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

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    MSTDSKRYCI KTKHVAIICA AVVAVGLIVG LSVGLTRSCD SKDGGQGTTQ    50
    SPSHLPPTSS PPQDQGVCPA SEDESGNWRD FRLPDFINPV HYDLQVKPLL 100
    EQDTYTGTVN ISINVTSPTQ HLWLHLRETR ITQLPVLWRP SGEQVQVRRC 150
    FEYKKQEYVV VEAEEELAPN SGEGLYHLTM EFAGWLNGSL VGFYRTTYVE 200
    KGQIKSIAAT DHEPTDARKS FPCFDEPNKK ATYTISIIHP KEYKALSNMP 250
    VEKEESVDDI WTQTTFQKSV PMSTYLVCFA VHQFDSVTRT SRSGKPLTIY 300
    VQPEQKHTAE YAANITKSVF DYFEDYFAME YSLPKLDKIA IPDFGTGAME 350
    NWGLITYRET NLLYDPNESA SSNQQRVAAV VAHELVHQWF GNIVTMEWWE 400
    DLWLNEGFAS FFEFLGVDHA EKEWQMRDQI LLEDVLPVQE DDSLISSHPI 450
    VVTVSTPAEI TSVFDGISYS KGASILRMLE DWITPEKFQK GCQEYLKKFE 500
    FKNAKTSDFW EALEEASNLP VKEVMDTWTN QMGYPVLNVE DMRIISQKRF 550
    LLDPNANSSE PHSVFGYTWN IPVRWTNDNE STITIYNRSE TGGITLNSSN 600
    PNGNAFLKIN PDHIGFYRVN YEVSTWEWIA TNLSLNHKDF STADRASLID 650
    DAFALARAQL LNYKEALNLT KYLKMEDEYL PWQRVISAVT YIISMFEDDK 700
    ELYPMIEKYF RDQVKPIADS LGWNDNGDHL TKLLRASVLG FACKMGDSNA 750
    LNNASHLFEQ WLTGTVSLPV NLRLLVYRYG MQNSGNETSW NYTLKQYQET 800
    SLAQEKEKLL YGLASVKNVA LLSRYLDLLK DPNVIKSQDV FTVIRYISYN 850
    SYGKTMAWNW IQLNWEYLVN RYTLNDRNLG RIVTIAEPFN TELQLWQMES 900
    FFKRYPEAGA GEKPREQVLE TVKNNIEWLK QNRDTIRDWF FN 942
    Length:942
    Mass (Da):108,284
    Last modified:February 1, 1997 - v1
    Checksum:iC531E639A588EF2E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66371 mRNA. Translation: AAB07141.1 .
    RefSeqi NP_999182.1. NM_214017.1.
    UniGenei Ssc.83.

    3D structure databases

    ProteinModelPortali Q95334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000009739.

    Chemistry

    BindingDBi Q95334.
    ChEMBLi CHEMBL4868.

    Protein family/group databases

    MEROPSi M01.003.

    Proteomic databases

    PaxDbi Q95334.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397080.
    KEGGi ssc:397080.

    Organism-specific databases

    CTDi 2028.

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000106482.
    HOVERGENi HBG006616.
    KOi K11141.

    Miscellaneous databases

    PMAP-CutDB Q95334.

    Family and domain databases

    InterProi IPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    Pfami PF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 89 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