AMPN_BOVIN
ID AMPN_BOVIN Reviewed; 965 AA.
AC P79098; Q3MHR1;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Aminopeptidase N {ECO:0000305};
DE Short=AP-N;
DE Short=bAPN;
DE EC=3.4.11.2 {ECO:0000250|UniProtKB:P15144};
DE AltName: Full=Alanyl aminopeptidase;
DE AltName: Full=Aminopeptidase M;
DE Short=AP-M;
DE AltName: Full=Microsomal aminopeptidase;
DE AltName: CD_antigen=CD13;
GN Name=ANPEP; Synonyms=APN;
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 648-838.
RC TISSUE=Intestine;
RX PubMed=8985407; DOI=10.1128/jvi.71.1.734-737.1997;
RA Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.;
RT "Interspecies aminopeptidase-N chimeras reveal species-specific receptor
RT recognition by canine coronavirus, feline infectious peritonitis virus, and
RT transmissible gastroenteritis virus.";
RL J. Virol. 71:734-737(1997).
CC -!- FUNCTION: Broad specificity aminopeptidase which plays a role in the
CC final digestion of peptides generated from hydrolysis of proteins by
CC gastric and pancreatic proteases. Also involved in the processing of
CC various peptides including peptide hormones, such as angiotensin III
CC and IV, neuropeptides, and chemokines. May also be involved the
CC cleavage of peptides bound to major histocompatibility complex class II
CC molecules of antigen presenting cells. May have a role in angiogenesis
CC and promote cholesterol crystallization. May have a role in amino acid
CC transport by acting as binding partner of amino acid transporter
CC SLC6A19 and regulating its activity (By similarity).
CC {ECO:0000250|UniProtKB:P15144, ECO:0000250|UniProtKB:P97449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000250|UniProtKB:P15144};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15144};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15144};
CC -!- SUBUNIT: Homodimer. Interacts with SLC6A19 (By similarity).
CC {ECO:0000250|UniProtKB:P15144, ECO:0000250|UniProtKB:P97449}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15144};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}.
CC Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.
CC -!- PTM: May undergo proteolysis and give rise to a soluble form.
CC {ECO:0000250|UniProtKB:P15144}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; BC105142; AAI05143.1; -; mRNA.
DR EMBL; X98240; CAA66896.1; -; mRNA.
DR RefSeq; NP_001068612.1; NM_001075144.1.
DR AlphaFoldDB; P79098; -.
DR SMR; P79098; -.
DR STRING; 9913.ENSBTAP00000022456; -.
DR ChEMBL; CHEMBL2010632; -.
DR MEROPS; M01.001; -.
DR PaxDb; P79098; -.
DR PRIDE; P79098; -.
DR GeneID; 404191; -.
DR KEGG; bta:404191; -.
DR CTD; 290; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; P79098; -.
DR OrthoDB; 110058at2759; -.
DR PRO; PR:P79098; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
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 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; Angiogenesis; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Receptor; Reference proteome; Signal-anchor;
KW Sulfation; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..965
FT /note="Aminopeptidase N"
FT /id="PRO_0000095078"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT TRANSMEM 9..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..965
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT REGION 33..65
FT /note="Cytosolic Ser/Thr-rich junction"
FT REGION 40..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..965
FT /note="Metalloprotease"
FT COMPBIAS 42..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 349..353
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 474
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT MOD_RES 173
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 416
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
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 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 760..767
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT DISULFID 797..833
FT /evidence="ECO:0000250|UniProtKB:P15144"
SQ SEQUENCE 965 AA; 109276 MW; C730910D173879A8 CRC64;
MAKGFYISKA LGILAILLGV AAVATIIALS VVYAQEKNKN AERGTAAPTS PTGPTTTSAT
TLDQSKPWNR YRLPTTLLPD SYRVTLRPYL TPNNNGLYIF TGSSTVRFTC KEPTDVIIIH
SKKLNYTQHS GHLAALKGVG DTQAPEIDRT ELVLLTEYLV VHLKSSLEAG KTYEMETTFQ
GELADDLAGF YRSEYMDGNV KKVLATTQMQ STDARKSFPC FDEPAMKATF NITLIHPKDL
TALSNMPPKG PSVPFDGDSN WSVTEFETTP VMSTYLLAYI VSEFTSVESV APNDVQIRIW
ARPKATADNH GLYALNVTGP ILNFFANHYN TAYPLPKSDQ IALPDFNAGA MENWGLVTYR
ENALLYDPQS SSSSNKERVV TVIAHELAHQ WFGNLVTLAW WNDLWLNEGF ASYVEYLGAD
YAEPTWNLKD LMVPNDVYSV MAVDALVTSH PLTTPANEVN TPAQISEMFD TISYSKGASV
IRMLSNFLTE DLFKKGLASY LQTFAYQNTT YLNLWEHLQM AVENQLSIRL PDTVSAIMDR
WTLQMGFPVI TVDTNTGTIS QKHFLLDPNS TVTRPSQFNY LWIVPISSIR NGQPQEHYWL
RGEERNQNEL FKAAADDWVL LNINVTGYYQ VNYDENNWKK IQNQLMSRRE NIPVINRAQV
IYDSFNLASA HMVPVTLALN NTLFLKNEME YMPWQAAVSS LNYFKLMFDR TEVYGPMQNY
LKNQVEPIFL YFENLTKNWT EIPENLMDQY SEINAISTAC SNGLPKCEEL AKTLFNQWMN
NPNVNPIDPN LRSTIYCNAI AQGGQEEWDF AWNQLQQAEL VNEADKLRSA LACTNHVWLL
NRYLSYTLNP DLIRKQDATS TITSIASNVI GQSLAWDFIR SNWKKLFEDY GGGSFSFSNL
IQGVTRRFST EFELQQLEEF KENNMDVGFG SGTRALEQAL EKTKANINWV KENKEVVLNW
FKDHS
