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Database: UniProt
Entry: A0A026X5V0_OOCBI
LinkDB: A0A026X5V0_OOCBI
Original site: A0A026X5V0_OOCBI 
ID   A0A026X5V0_OOCBI        Unreviewed;       584 AA.
AC   A0A026X5V0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:EZA62864.1};
DE   Flags: Fragment;
GN   ORFNames=X777_16438 {ECO:0000313|EMBL:EZA62864.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA62864.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA62864.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
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; KK107015; EZA62864.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026X5V0; -.
DR   OMA; ITHEHNE; -.
DR   Proteomes; UP000053097; 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; 1.25.50.20; -; 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; 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; 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:0000313|EMBL:EZA62864.1};
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:UP000053097};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          2..73
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          141..323
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          420..580
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EZA62864.1"
SQ   SEQUENCE   584 AA;  69538 MW;  82B153E38D274859 CRC64;
     NVLLATNIHS IGARHLFPCW DEPELKATFQ FRFTHLQKYK IWPISVSERS AREDYKRNWL
     CTNSFIEDKI STYQLMFILT NFEFSIKTKF LAYNALGIYH TVIKLSIASR SRVENSMQVL
     YDVSNKILHS TWYHKIPLRR NITLLAIPAM KEDVMANWGL IVYEESLVTY DKQLDSYTRQ
     REVVNTVARG IAYQLVEENI VTLPWWSHLW FNKGLAALLH VQILDEVFWE WGFMDLFVVQ
     VHQDCLHLDT NFIMKPLLYE VQTSSEIKSL FSFPIYVKAP VILRMVRHIM GKMFEESIKK
     SIIYSTYSWD LIQVHTLCGS MDVIDNQELC NYTMKDIMET WITTNNYPIA HVHRNESTLF
     ICQSEEEFYN DNGSKALRHW LPITFTTSEQ LDFNNTTPRD WITPENSNRI SVRLTHKNEW
     IILNLQQTGY YRVKYDTNSL KFVTNYLLHE NYEKIHVLNR AQIIDDTYYF LMRGEVTYNT
     FMRLMNYLAR DRDYIAWYPM LQIFIDLSYF LPFAESAVIK QDMRYILKKL LSTLSYNEEV
     DDNDLTMRLR QEAIKWACIF GYTECQHTAT DKLKEHLEDP TNRK
//
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