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Database: UniProt
Entry: A0A1B0BQL8_9MUSC
LinkDB: A0A1B0BQL8_9MUSC
Original site: A0A1B0BQL8_9MUSC 
ID   A0A1B0BQL8_9MUSC        Unreviewed;      1075 AA.
AC   A0A1B0BQL8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EnsemblMetazoa:GPPI037525-PA};
OS   Glossina palpalis gambiensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=67801 {ECO:0000313|EnsemblMetazoa:GPPI037525-PA, ECO:0000313|Proteomes:UP000092460};
RN   [1] {ECO:0000313|Proteomes:UP000092460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092460};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPPI037525-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPPI037525-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
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}.
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DR   EMBL; JXJN01018681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A1B0BQL8; -.
DR   STRING; 67801.A0A1B0BQL8; -.
DR   EnsemblMetazoa; GPPI037525-RA; GPPI037525-PA; GPPI037525.
DR   VEuPathDB; VectorBase:GPPI037525; -.
DR   Proteomes; UP000092460; 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: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; 1.25.50.20; -; 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:SF291; AMINOPEPTIDASE-RELATED; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   TRANSMEM        64..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          167..363
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          401..629
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          712..1030
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        477
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         476
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         480
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         499
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            562
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1075 AA;  124001 MW;  1EB8E2763864883E CRC64;
     MSCISISELD DIFKDNCGPR DSLNIRFPSK QFLLIFERGQ LKTKNGQKYV FNGRPSGIFV
     SRTCAIFTAI ITILILIFTI LITYFVTVNT VPSGCTNGHY VPNTQIAAPF NVSPVTTASM
     LGMPMPKNKY QTISSPVGDI PPDNDVFGEN KGKFIDRKLQ LYEGWTPLHY KLVIEPTLRT
     STNNGSLAIR IQRNANITTF EPIVLDVNNI SISNVRVIRS KNNPDEEEAE LEFDSDYGLN
     NQTFVVVLNK ELAKEKNLTL ILSMDFISQI TDTLQGVYKT SYANVQTGRE EWMISTQFSP
     IDARRAFPCF DRPDMKANFT ISIIRSTRTS MALSNMPVYH SSIHRPGFTK DDFMTTPKMP
     TYLVAFIVSN LVKSHYSDRD TSAIPRVEIW TRPENKDMTK YAYYLVRKYL DYFEGYFGIE
     NRLPKIDLVS IPDFGFGAME NWGLITFRDA ALLVPDDLEK ASSSEHMEYV AKIIAHELAH
     QWFGNLVTPK WWDDLWLKEG FACYMSYMAL NFVHPEYEIL DNLAIFEFKY SMQHDSDNSS
     HAIAFEVKST NDIRRIFDPI TYSKGTILVR MLSSIVGYDA FRNATQDFLS SLAYANADRN
     DLWEFMTKHG HLEKTLPDDM TVKTIMDTWI SKPGYPVITV ERRDADLIVT QERFMLPSRN
     ISDSSKWIVP ITYETDELHK GDNIPTHWLM DNGHELVIND IFTSDNNSEN VVYLNLDRRS
     YYRVNYDMPS WLALKKKFTS LPRVTRAQLM DDALHLAQAE YLTYDIPLTF LLELFTSTDD
     ELLWSAAQKG LEYLIFMLSR EPAYETFRAF MKFIVRPAFD RYGLQEPDNE SHIQLQHRAL
     VSRLACKFKY DRCFNAAHNK YREWMANPKA NFITPNMKPT IYCTALAEGS FQEWYFAYKQ
     YKRTTSASEK EQILSSLGCT TKPWLLSKYL NMTLSSTSGI LKQDGTQAFR AVAENPIGFE
     IAFDFLQTNI KEIAEYYGDG FSTLTSMIKS VTTYMNKDYH KEQLERFKER AQKLGLKSVT
     TAIQLAVEQV KNNIYWRNRS YYSLKGFLEA IYSGFLSYSC KVFKLNHNLL FNIFV
//
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