ID   A0A3B0K3C5_DROGU        Unreviewed;      1112 AA.
AC   A0A3B0K3C5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Blast:Endoplasmic reticulum aminopeptidase 2 {ECO:0000313|EMBL:SPP80126.1};
GN   ORFNames=DGUA_6G004981 {ECO:0000313|EMBL:SPP80126.1};
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:SPP80126.1, 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   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; OUUW01000005; SPP80126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0K3C5; -.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF302; AMINOPEPTIDASE N-LIKE PROTEIN; 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   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:0000313|EMBL:SPP80126.1};
KW   Hydrolase {ECO:0000313|EMBL:SPP80126.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:SPP80126.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        73..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          128..296
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          449..661
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          769..1066
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   REGION          26..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1112 AA;  125096 MW;  DAC158093AB69ACA CRC64;
     MLCCGFCCGN MSKRDYKVAT TDGIELEPLG GEKSDKEKDK DKEKQTNGVT FGGESSGGRQ
     TRTGVAVCSQ RRALLVAGIV LGSLLLTAII IAYAGPSNEN NTQPFNPIAT NGEPFPWLEK
     MLPTSARPLR YMVTIHPNLT TLDVKGQVTI DLHIEKETNF LVLHIQDLNV TEKAIVTPGP
     KGYALKIVKV LEFPQRQQLY IEVKERLKKK SNYTLNLRWY SKLNPEPEGF YVDQYESSNG
     VERLLAATVF RPNGARRAFP CFDEPHVRAP FRISVFRDRF HIGLSNSIVH TTEDVGFYMG
     TGLLRDDFIE TPALPADAVA WVVSDFQRES LQPSAAYIPT TAAPYSSGAG GKKSAQLNNY
     TQLKSKNPPV RNITALTHSL NVNLTPRQNL SHIAAAATTT TALPVSLNGN GKPTNLTSLS
     QSTSSSIKRA PSYTFYAPRD LLVRSSFILH TSRDVLEYLQ TWLDISYPLT KVDFVALPSL
     DRNMISSLGL VTLKTSFLTD PSSITSEQYQ FSALRIAEAM VRQFFGGITS RKVLKDVWLW
     EGLIQYLGIH ALAPLQQSWP LREMYLLKMA TAALDIDAIQ GWDSIMNGTS HDGKNEDFFV
     QKTAAIFSML HTAIGEDRFR GCLGSFLKVN RFKTAEPTDL WTICTKKANG SKNIKDMMTL
     WTHQPGFPLL TVTKMGNSVS ISQRPFRPAD FLAIHDDSYD GNNYNKTTLN ATDMPSTVAP
     TPQGKHKAAA PHMKWIFPVT YVTDINNVSE TLWMQNVDIN FNVPENVKWI KVNAIQNGYY
     RVVYNDDNWA NLIEELSNNP KRFSSEDRLG LLSDAFTLCH ANLLPCEITM NMIQYLPSET
     HYGPMALALR HLEKWRRILK YSECFLMLSE FIKMKISTVM EKVGWTDEGD VPARLMRPEV
     LLASVLWEDI DSITKAKNML NQYLYYNGSA IAPNLREVVY TGSILSGEYI YWQHCWERFV
     TLQRTSETFV ERMQLLRALG RTKDAWLQNR LLSHVTMLPT EEVVQVLKAI AGTPTGGAMA
     CRFLQAKWFE LEKRLGQGTI SFAKVISAIT QYGATKFDYD ELKSLVHRFG RGQGMSVLNM
     TLSSVASNVE WVARSQTSLY KWVESNLHSH RR
//