ID E2C143_HARSA Unreviewed; 846 AA.
AC E2C143;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:EFN78364.1};
GN ORFNames=EAI_07553 {ECO:0000313|EMBL:EFN78364.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN78364.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN78364.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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; GL451853; EFN78364.1; -; Genomic_DNA.
DR AlphaFoldDB; E2C143; -.
DR STRING; 610380.E2C143; -.
DR EnsemblMetazoa; XM_011150459.3; XP_011148761.1; LOC105188811.
DR EnsemblMetazoa; XM_025299864.1; XP_025155649.1; LOC105188837.
DR InParanoid; E2C143; -.
DR OMA; TEIDIHY; -.
DR Proteomes; UP000008237; 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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3480.20; -; 1.
DR Gene3D; 1.25.50.20; -; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF276; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 2.
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:0000313|EMBL:EFN78364.1};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008237};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 9..268
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 267..338
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 370..548
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 578..843
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 846 AA; 101274 MW; E0E3A546B0D2A763 CRC64;
MEHWIFVSAI GYYRVNYEYN NWVKIWKYLK EDHRKIHVLN RAQIIDDTYH FVMENEIGYE
TFENVISYLR KERDFIVWNS MMNILHYMSP FFNYPESKRF KEKMLKIMRH VLDKIEYDEQ
PEDDEMVRAM RLLLLDWSCK HGLAECRNNA RYKLVAHFTD PKEHKILPKW KDWTYCAGFM
SISDHEEILN VLYKPNKEIL KYLICVDEDH LLQKLVELAT FNPRDTWTEF KVAQLRKLYH
GIVKKHAKKQ KVLDFILSNF DKIVQGLSYV TTFEPRKGAQ YLFPCWDEPR LKATFNISIE
HSAIYKVFSN MEEEKIVKIG KDTKRTILKS TPVMSTYLLT IVLTKLKYSY YPEEEIWFSY
TPNNETLELV KVINFLTDYF FVQYTQKYSD NSKLKKLNMK NSTIVAVPGL PLKAMGAWQN
IFLRKSDLLY DKSVDFPGRV LDIWKTISYG KTRQYIQSFV SPNHWSHMWF SRALALYLSY
NVLGKGFNKE QMMQLFVVQV QLPAMHNDIV LKVPPILSTD DPIYSTLIYK KDKWPVPVTY
TTQGKHRFNQ PASIQWLNNH YTGWNSFLEL TLDNVTEWVI LNLQQIGYYR VQYDNRNWLR
IARFLKKDKQ KTIHVLSRVQ LIDDAYYFLI QGTIDYKVYC ELIDFLRNEI DFIVWHSMMN
VLHYISPFFK FPESTDFKDL IMDIMDDVLM QIEYNEKTAD DNMIKATRLL LLNWMCNHGH
NKCRQAASNK LRPYIKNAVE SPISPGWKNW VYCAGLMNAD YELRMLAKDE ILNKKDKNML
QYMTCYDNDV WIQELLTWIM FKPRDEKLSL DDRQEMDLYR TIVKKHARKS NVLDFILKNM
TQILPG
//
