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
//