ID A0A1B0DJP5_PHLPP Unreviewed; 824 AA.
AC A0A1B0DJP5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
OS Phlebotomus papatasi (Sandfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Phlebotomus; Phlebotomus.
OX NCBI_TaxID=29031 {ECO:0000313|EnsemblMetazoa:PPAI008469-PA, ECO:0000313|Proteomes:UP000092462};
RN [1] {ECO:0000313|Proteomes:UP000092462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Israel {ECO:0000313|Proteomes:UP000092462};
RA Fulton L., Warren W., Minx P., Wilson R., Clifton S., Abrudan J.,
RA Ramalho-Ortigao M., Lawyer P., Kamhawi S., Rowton E., Lehane M., Bates P.,
RA Valenzeula J., Dillon R., Lobo N., Collins F., McDowell M.A.;
RT "Phlebotomus papatasi, whole genome shotgun sequencing project.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:PPAI008469-PA}
RP IDENTIFICATION.
RC STRAIN=Israel {ECO:0000313|EnsemblMetazoa:PPAI008469-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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; AJVK01065643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0DJP5; -.
DR EnsemblMetazoa; PPAI008469-RA; PPAI008469-PA; PPAI008469.
DR VEuPathDB; VectorBase:PPAI008469; -.
DR OrthoDB; 3264783at2759; -.
DR Proteomes; UP000092462; 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: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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 39..231
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 264..481
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 569..824
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 424
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 824 AA; 95722 MW; 6DF3CFFD48471BA4 CRC64;
MLHPCSGKEN IMGMLWLLFL LLGHCNGFKV VRLNFKVIPS HYEITVTPYI FKGDGGPEWT
FDAVVEITMK AKLLDVRSIT LHAYKLNITG STLTCDDDRK RNLIARHPTY QNETQLLTYE
LLDALEKDVE CFLEIEYSGL ISNDMLGLYR STYWEAGKLK RLAVTQFEHS SARRFMPCFD
EPEFKANFTL VVRRREYMRS WSNMPLERTD KDPYADFFLD TFHTTPQISP YHLAFMVSEY
TNRTGEDSIG MITRPEMQGY TDYGIKVAVN AIKYFSEYFD FPYSKFMPKL DLVALPDFSK
GAMENPGLIT FREALSLYVP NKASLAQKAK IARVISHELA HNWFGNLVTC MFWSHLWLNE
GFATYFEHSP IPGVEETSHL SAQFTINAVH RALLADSTNT TFPLVNKKIE TQNHIERMFG
PISYAKGASV IRMLAHHIGE ENMKSALRMY IKDRQFKTAS DVDLLRMLRK VAVREDNIDG
VFYSFVVEPG YPVVTVRMNE TRDSVTLTQK RYFSHAVSSS CKDHPRACFW VIPITYVSKN
QYSFNDTTTR VVMHDIEVTF NVTPVPNTWI IFNVQHIGYY RVNYDFESWN RIIDGLKAPD
HDGIHELNRA QIIDDLMNLA RSDHIPYCTA FNMLEYLKTE TSYIPWKMAM KNFQFIIYRT
PAYDTKALRK YVLELIENIY KKLQLMPDPS DNQLISSHRS LILKMACKFG LHDCLVKARE
QFNKFKKDDT YDIPVDIRQV VFCVGVREGG KDAFNFLWKR YKLENVETEQ ITILSALACT
NTDATVRDFL DKIFSSDVRE NMKLKTFTML ATQNPANYIR LWDY
//
