AMPE_BOVIN
ID AMPE_BOVIN Reviewed; 956 AA.
AC Q32LQ0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glutamyl aminopeptidase;
DE Short=EAP;
DE EC=3.4.11.7;
DE AltName: Full=Aminopeptidase A;
DE Short=AP-A;
DE AltName: CD_antigen=CD249;
GN Name=ENPEP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates central hypertension through its calcium-modulated
CC preference to cleave N-terminal acidic residues from peptides such as
CC angiotensin II. {ECO:0000250|UniProtKB:Q07075}.
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:0000250|UniProtKB:Q07075};
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: Substrate specificity is modulated by calcium
CC which enhances the enzymatic activity for cleavage of acidic residues
CC while reducing its activity with basic residues. Inhibited by
CC aminopeptidase inhibitors amastatin and bestatin.
CC {ECO:0000250|UniProtKB:Q07075}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q07075}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07075};
CC Single-pass type II membrane protein.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; BC109476; AAI09477.1; -; mRNA.
DR RefSeq; NP_001033116.1; NM_001038027.1.
DR AlphaFoldDB; Q32LQ0; -.
DR SMR; Q32LQ0; -.
DR STRING; 9913.ENSBTAP00000010972; -.
DR MEROPS; M01.003; -.
DR PaxDb; Q32LQ0; -.
DR GeneID; 504350; -.
DR KEGG; bta:504350; -.
DR CTD; 2028; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; Q32LQ0; -.
DR OrthoDB; 110058at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; ISS:UniProtKB.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR033508; Aminopeptidase_A.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF242; PTHR11533:SF242; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..956
FT /note="Glutamyl aminopeptidase"
FT /id="PRO_0000278197"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..956
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 48..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q07075"
FT BINDING 359..363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q07075"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 888
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q07075"
FT SITE 223
FT /note="Binds calcium which modulates its enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q07075"
FT SITE 481
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q07075"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 956 AA; 109801 MW; 90DC7FD3E67C1541 CRC64;
MILEERSSWE GSKRYCIKTK HVAIICAVVV AVGLIVGLSV GLTRSCDSTE GMTQGTTQGT
TQAPSHLPPV TSPPEDQGVC PASEDESGGW KDFRLPDFIK PVHYDLEVKP LMEQDTYTGS
VDISINVSSS TRYLWLHLRE TRITRLPVLR RPSGEQVQVR QCFEYKKQEY VVVEAEEELE
PNTGEGPYHL ILEFAGWLNG SLVGFYRTTY VEKGQTKSIA ATDHEPTDAR KSFPCFDEPN
KKATYTISIV HSKEYKALSN MPVEKEESVD DIWSRTTFQK SVPMSTYLVC FAVHQFDSVT
RISNRGIPLT IYVQPEQKHT AEYAANITKS VFDYFEDYFG MSYSLPKLDK IAIPDFGTGA
MENWGLITYR ETNLLYDPDE SASSNKQRVA AVIAHELVHQ WFGNIVTMEW WDDLWLNEGF
ASFFEYLGVA YAEKDWQMRD QMILDDVLPV QEDDSLMSSH PIVVTVATPD EITSVFDGIS
YSKGASILRM LENWITREKF QIGCQNYLKK HKFENAKTSD FWAALEEASN LPVKEVMDTW
TNQMGYPVLN VDNMKNITQK RFLLDPRANA SEPHSAFGYT WNIPIKWTED DEQRITLYNR
SETGGITLES TLSGNAFLKI NPDHIGFYRV NYEVSTWEWI ATNLSVNHTD FSSADRASFI
DDAFALARAQ LLNYKEALNL TKYLKEEKEY LPWHRVISAV TYIISMFEDD KELYPVIEKY
FRDQVKPIAD SLGWNDVGDH LTKLLRASVL GLACKMGDSD ALNNASQLFQ EWLTGTVSLP
VNLRLLVYRY GMQNSGNETS WNYTLEQYQK TSLAQEKEKL LYGLASVKNV TLLSRYLDLL
KDSNLIKTQD VFTVIQYISY NSYGKTMAWN WIQLNWEYLV NRYTLNNRNL GRIVTIAEPF
NTELQLWQIK SFFERYPEAG AGQKPREQVL ETVKNNIEWL KQNRDTIRNW FLDLNG
