ID A0A2K5WAU9_MACFA Unreviewed; 830 AA.
AC A0A2K5WAU9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=NPEPPS {ECO:0000313|Ensembl:ENSMFAP00000034244.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000034244.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000034244.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000034244.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR AlphaFoldDB; A0A2K5WAU9; -.
DR Ensembl; ENSMFAT00000008472.2; ENSMFAP00000034244.2; ENSMFAG00000003608.2.
DR VEuPathDB; HostDB:ENSMFAG00000003608; -.
DR GeneTree; ENSGT00940000155246; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000233100; Chromosome 16.
DR Bgee; ENSMFAG00000003608; Expressed in cerebellum and 13 other cell types or tissues.
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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 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 PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 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; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 82..214
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 249..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 489..802
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 322
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 407
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 830 AA; 93581 MW; F5387C7EBFBFC4B4 CRC64;
MASLSMDCSP TFCVPGLWNP FIIFHSRSSR RRRRLHSLGL AAMPEKRPFE RLPADVSPIN
YSLCLKPDLL DFTFEGKLEA AAQIHATGFN YQNEDEKVTL SFPSTLQTGT GTLKIDFVGE
LNDKMKGFYR SKYTTPSGEV RYAAVTQFEA TDARRAFPCW DEPAIKATFD ISLVVPKDRV
ALSNMNVIDR KPYPDDENLV EVKFARTPVM STYLVAFVVG EYDFVETRSK DGVCVRVYTP
VGKAEQGKFA LEVAAKTLPF YKDYFNVPYP LPKIDLIAIA DFAAGAMENW GLVTYRETAL
LIDPKNSCSS SRQWVALVVG HELAHQWFGN LVTMEWWTHL WLNEGFASWI EYLCVDHCFP
EYDIWTQFVS ADYTRAQELD ALDNSHPIEV SVGHPSEVDE IFDAISYSKG ASVIRMLHDY
IGDKDFKKGM NMYLTKFQQK NAATGEDCPQ WMVPITISTS EDPNQAKLKI LMDKPEMNVV
LKNVKPDQWV KLNLGTVGFY RTQYSSAMLE SLLPGIRDLS LPPVDRLGLQ NDLFSLARAG
IISTVEVLKV MEAFVNEPNY TVWSDLSCNL GILSTLLSHT DFYEEIQEFV KDVFSPIGER
LGWDPKPGEG HLDALLRGLV LGKLGKAGHK ATLEEARRRF KDHVEGKQIL SADLRSPVYL
TVLKHGDGTT LDIMLKLHKQ ADMQEEKNRI ERVLGATLLP DLIQKVLTFA LSEEVRPQDT
VSVIGGVAGG SKHGRKAAWK FIKDNWEELY NRYQGGFLIS RLIKLSVEGF AVDKMAGEVK
AFFESHPAPS AERTIQQCCE NILLNAAWLK RDAESIHQYL LQRKASLPTV
//
