AMPN_HAECO
ID AMPN_HAECO Reviewed; 972 AA.
AC Q10737;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Aminopeptidase N;
DE Short=AP-N;
DE EC=3.4.11.2;
DE AltName: Full=Membrane glycoprotein H11;
DE AltName: Full=Microsomal aminopeptidase;
OS Haemonchus contortus (Barber pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Trichostrongyloidea; Haemonchidae; Haemonchus.
OX NCBI_TaxID=6289;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9128148; DOI=10.1016/s0167-4838(96)00204-x;
RA Smith T.S., Graham M., Munn E.A., Newton S.E., Knox D.P., Coadwell W.J.,
RA McMichael-Phillips D., Smith H., Smith W.D., Oliver J.J.;
RT "Cloning and characterization of a microsomal aminopeptidase from the
RT intestine of the nematode Haemonchus contortus.";
RL Biochim. Biophys. Acta 1338:295-306(1997).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; X94187; CAA63897.1; -; mRNA.
DR AlphaFoldDB; Q10737; -.
DR SMR; Q10737; -.
DR MEROPS; M01.015; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..972
FT /note="Aminopeptidase N"
FT /id="PRO_0000095087"
FT TOPO_DOM 2..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..972
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 343..347
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 466
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 759..766
FT /evidence="ECO:0000250"
FT DISULFID 804..840
FT /evidence="ECO:0000250"
SQ SEQUENCE 972 AA; 110674 MW; 5964328CC3C80E43 CRC64;
MTSQGRTRTL LNLTPIRLIV ALFLVAAAVG LSIGLTYYFT RKAFDTSEKP GKDDTGGKDK
DNSPSAAELL LPSNIKPLSY DLTIKTYLPG YVDFPPEKNL TFDGRVEISM VVIEPTKSIV
LNSKKISVIP QECELVSGDK KLEIESVKEH PRLEKVEFLI KSQLEKDQQI LLKVGYIGLI
SNSFGGIYQT TYTTPDGTPK IAAVSQNEPI DARRMVPCMD EPKYKANWTV TVIHPKGTKA
VSNGIEVNGD GEISGDWITS KFLTTPRMSS YLLAVMVSEF EYIEGETKTG VRFRIWSRPE
AKKMTQYALQ SGIKCIEFYE DFFDIRFPLK KQDMIALPDF SAGAMENWGL ITYRENSLLY
DDRFYAPMNK QRIARIVAHE LAHQWFGDLV TMKWWDNLWL NEGFARFTEF IGAGQITQDD
ARMRNYFLID VLERALKADS VASSHPLSFR IDKAAEVEEA FDDITYAKGA SVLTMLRALI
GEEKHKHAVS QYLKKFSYSN AEATDLWAVF DEVVTDVEGP DGKPMKTTEF ASQWTTQMGF
PVISVAEFNS TTLKLTQSRY EANKDAVEKE KYRHPKYGFK WDIPLWYQEG DKKEIKRTWL
RRDEPLYLHV SDAGAPFVVN ADRYGFYRQN HDANGWKKII KQLKDNHEVY SPRTRNAIIS
DAFAAAATDA IEYETVFELL NYAEKETEYL PLEIAMSGIS SILKYFGTEP EAKPAQTYMM
NILKPMYEKS SIDFIANNYR NDKLFFQINL QKDVIDMFCA LGSQDCRKKY KKLFDDEVMN
KCRDGQAATE CVRIAAPLRS SVYCYGVKEG GDYASDKVME LYTAETLALE KDFLRLALGC
HKDVTALKGL LLRALDRNSS FVRMQDIPSA FNDVAANPIG GEFIFNFLIE RWPDIIESIG
TKHTYVEKVI PACTSGIRSQ QQIDQLKNLQ KNGMNARQFG AFDKAIERAQ NRVDWIKKHF
QKLAAFFKKA TL
