ID   AMPE_GLOBL              Reviewed;          57 AA.
AC   P0DQU2;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=Aminopeptidase A {ECO:0000303|PubMed:18384831};
DE            Short=AP-A {ECO:0000305};
DE            Short=APA {ECO:0000303|PubMed:18384831};
DE            EC=3.4.11.7 {ECO:0000269|PubMed:18384831};
DE   AltName: Full=Glutamyl aminopeptidase {ECO:0000305};
DE            Short=EAP {ECO:0000305};
DE   Flags: Fragments;
OS   Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=242054;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=18384831; DOI=10.1016/j.toxicon.2008.02.003;
RA   Ogawa Y., Kanai-Azuma M., Akimoto Y., Kawakami H., Yanoshita R.;
RT   "Exosome-like vesicles in Gloydius blomhoffii blomhoffii venom.";
RL   Toxicon 51:984-993(2008).
CC   -!- FUNCTION: Venom protein that cleaves N-terminal acidic residues from
CC       peptides with high potency in presence of calcium (PubMed:18384831). It
CC       may have several roles in venom including alteration of blood pressure
CC       by cleaving circulating angiotensin-2, general degradation of host
CC       tissue, increase of permeability to other venom components, and/or
CC       processing of other toxins in the venom (By similarity)
CC       (PubMed:18384831). {ECO:0000250|UniProtKB:D3UW23,
CC       ECO:0000269|PubMed:18384831}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal glutamate (and to a lesser extent
CC         aspartate) from a peptide.; EC=3.4.11.7;
CC         Evidence={ECO:0000269|PubMed:18384831};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q07075};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q07075};
CC   -!- ACTIVITY REGULATION: Inhibited by the aminopeptidase competitive
CC       inhibitors amastatin (Leu and acidic inhibitor), and bestatin (Leu
CC       inhibitor), by chelating agents EDTA, and 1,10-Phenanthroline, as well
CC       as by Zn(2+) ions. Substrate specificity is modulated by Ca(2+),
CC       Ba(2+), and Mn(2+) ions which enhances the enzymatic activity for
CC       cleavage of acidic residues. {ECO:0000250|UniProtKB:A5HUI5}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q07075}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18384831};
CC       Single-pass type II membrane protein {ECO:0000305|PubMed:18384831}.
CC       Note=Found in the venom as transmembrane proteins in exosome-like
CC       vesicles. {ECO:0000305|PubMed:18384831}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Calcium; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           <1..>57
FT                   /note="Aminopeptidase A"
FT                   /id="PRO_0000455653"
FT   TOPO_DOM        <1..>57
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:18384831"
FT   CARBOHYD        12
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   NON_CONS        8..9
FT                   /evidence="ECO:0000305|PubMed:18384831"
FT   NON_CONS        24..25
FT                   /evidence="ECO:0000305|PubMed:18384831"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000305|PubMed:18384831"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000305|PubMed:18384831"
FT   NON_TER         1
FT                   /evidence="ECO:0000305|PubMed:18384831"
FT   NON_TER         57
FT                   /evidence="ECO:0000305|PubMed:18384831"
SQ   SEQUENCE   57 AA;  6707 MW;  1AD3BC20E13D45C9 CRC64;
     YLTDHYFKVD LNSTVTQQRF LLDPSELAGI TIMQPSDSNI EWLKQYRDDV ATWLENS