ID A0A0M3QXB0_DROBS Unreviewed; 882 AA.
AC A0A0M3QXB0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
DE Flags: Fragment;
GN ORFNames=Dbus_chr3Rg363 {ECO:0000313|EMBL:ALC45613.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC45613.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC45613.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC45613.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; CP012526; ALC45613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3QXB0; -.
DR STRING; 30019.A0A0M3QXB0; -.
DR OMA; DGWAQKE; -.
DR Proteomes; UP000494163; Chromosome 3r sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side 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: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; -; 2.
DR Gene3D; 2.60.40.1910; -; 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:SF284; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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|RuleBase:RU364040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000494163};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..882
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005788337"
FT DOMAIN 33..216
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 247..478
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 559..681
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 412
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ALC45613.1"
SQ SEQUENCE 882 AA; 101941 MW; B378E8A47336D27E CRC64;
WTSKLWLLAT IALIALIGTN GAVDYRLDRS VIPSFYNLSI KLFDHEDNRI FDGSVSIDIQ
TFETNIKEIK LHKDLLDIQG CALYKTGQLV EKIDIARLDY KSETQTLTIP LTDVLIDQVT
YTLNFNYTGH IRTDMSGLYV ADYNNIMLLT HMHGLNARLV LPCFDEPAFK AKFQLHIRRS
SAYQCFSNTK LASTTQESAN RYTDHFEVTP PMSTYLLAFA VSEFKYLGNL SEFAVISQPD
HYMNTEFSYN VGKRLLPAYG ELFEQNYTQL GNEALLFLAS PRFRHSGMEN WGLVIFRDNI
LLQSPGYTDG WSNKETTISV ISHEISHMWF GNSVTFKWWN YYWLNEGFAN YYGYFMTNAL
YPEYQLDQQF VVKELQKIMV TDSQNKTQPM TSPEDSIHTP AEISSKFSNI AYAKGASIVR
MWRNIMGGSK FSEAINGYLH QRHLGNAVPV DLFTHLKEHW PAQSQEVKAD LDEFFYDWTE
QVGYPVMIAN VSEGNRLITL KQQRFLLNPK DGSDTKLRYT VPITFATNTK PTFDTLTPRF
YYLRNLTELR LNSEQPLDWI IFNLKQSNYY RVLYDTPLLR GLRNALFADK HSSIPVENRA
GLIDDLFNFA SAGMIDYAVV FEFMEYLSKE LEYIPFYAAF ENMQHVAKRL TPAQLPDFTR
YLGDITSAAF NKLGVDWDNK DKSTEKPTPD YRETFYCAAA RVGGYERLLE LYAKETFASD
KQLLWRAASC TRDYQKHYKN EVLSKSRDVE LKTIALAQLY QQNPDLITPI FRMIAENVTQ
LAESLNSWEK TAQVLSEMSE YFSSRDQQKM YTDFHEQNHQ LFGSSAQILS KSLDNVKENI
EWAEQRLGRL VNFLQKRNGA AGLKFEVSLL LLLSLLILLL KH
//
