ID A0A3B0JYQ7_DROGU Unreviewed; 928 AA.
AC A0A3B0JYQ7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=DGUA_6G004050 {ECO:0000313|EMBL:SPP85572.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP85572.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) 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; OUUW01000010; SPP85572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0JYQ7; -.
DR STRING; 7266.A0A3B0JYQ7; -.
DR OMA; DQNDLWR; -.
DR Proteomes; UP000268350; Unassembled WGS 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; -; 1.
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:SF253; 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 ECO:0000313|EMBL:SPP85572.1}; 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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..928
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017181841"
FT DOMAIN 29..227
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 263..488
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 578..901
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 336
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 299..303
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 855
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT SITE 421
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 928 AA; 107677 MW; 6E432D96BEE9547C CRC64;
MLLLLWFILI ILTLGQASYD HYRLPKALQP QHYNLRVLTH LENVARPCFS GEVEIELRVL
QPTKNITLHA ASRLQLNSNR TNLYYLHEDG TKSKIAVKTV ERNSKYDYYI LMLCKVLERG
HIYLLHMQFF AHFEAGMSGY YASSYKDQNS NKTRYLSVTQ FEPAYARAAF PCFDEPAFKA
TFNITLGHPR KYVALSNMPI TKKFPMSGRR NWLWTIFEQT LPMPSYLVCY SVNDFASITS
RNGLSVAKFT TWARASAIGQ CKYAAEIAPR LLAYYERMFD IDYPLPKVDQ LAVPDFSAGA
MENWGLITYR EAALFYAPEA SSEVDKQRVA NIIAHELAHQ WFGNLVTMKW WNDLWLNEGF
ATYVATLGMQ KLCSKWHAYA EESLDNILVV LNSDAYYSTR AISQSVSRAS QFAEQFDPIT
YRKGAVIIRM MHMFIGDTTF RHGLNCYLKR HAYSNADQND LWRSLSDAAH EFGSLPENLE
VRTIMDTWTL QAGYPLITVQ RDYVRNIISI NQRRFLMQGM DRNNLISKEC WFVPISYTFG
SMANFTATEP QVWLQCDSQG KNMPLEIRSP LCAEENQWLI LNLQLTAPFR VNYDTSNWKL
IIKTLQGADF RRIHTMNRAQ LIIDALALSW NGHLCYKVSL DLIKYIKQEH AYMPWHAALD
HLSAIYRIIK QTSDFALFQR FMNDLLRPIY VYLGGMETES NARHIAHKTL INQWACRLAL
SDCVQRAVQY YQRWLISSDP DLVNPVPQNL RSVVYCAALR QGDEDDWNFL WHRYGNATVA
SERRLILQAL GCTQIVCVAR RYLHMIFDEN SSIRKQDISL AFGAIVRSDI GYTLAKDYFI
NNFSLLTKSF ELNYRDLAAL LLQTTQHISS PQDFGELKMF IDSHKKFQML NTRSVRRAID
VAQVNLLWRQ KQLPELTRVL KARSIYYK
//
