ID A0A026VTD4_OOCBI Unreviewed; 1076 AA.
AC A0A026VTD4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:EZA46940.1};
GN ORFNames=X777_00542 {ECO:0000313|EMBL:EZA46940.1};
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:EZA46940.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA46940.1, 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; KK108073; EZA46940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026VTD4; -.
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; 1.10.3480.20; -; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 2.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 2.
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; 2.
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; 2.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:EZA46940.1};
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 6..135
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 206..407
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 487..668
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 767..885
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 965..1065
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 1076 AA; 128735 MW; CE3210572028C994 CRC64;
MNGTTYKPIN KTHSEEENVL DLYFEDQLSP GRYSLTIHYS KDVGDDKKEG DFFKIIFKPA
TRNRWLATNI NSVEARKWFL CWDEPEFKTT FNFTFYHHRR FKIWPALPNA TSIGHVHKKE
WCLTKFFIAV TISTYQLMFV VTEIPLFSHT EYTSYSASCE LHKVNEDNTI LSRAPVENSI
KFSDVVIEKI LDSEWYCKIL LTDFNINQLA LPAVPEDVIA KWRLILCKEP LITYDKEIDS
SVHEREVAST IVRGIVYQVI DNAISPSWWS HLWLNKGLAT LIHVEILDEV LLYYFSKWRL
LDLFMVQVQQ DCLHLDTQFT MKPLSYEVQT SSEIKSLFSF PIYVKAPVIL RMVQHIIGHE
FQEIIKNYLK SYYYRSLSPD YLWNMMQVHK KNPKLGNYTM KDIMETWITR NNHPIVYVYR
KGSILFIRQS KKVFYIDDKG NAQVLRHWLP ITFTTWEQLD FNDTTPRDWI TPDSSEIIVE
LSNNTGWIIV NLQQTGYYRV RYDDTSLDEI AKYLTTNEYE KIHVLNRAQI IDDTYYFVKR
GVIPYVTVFK SLIRYLHQER DYVAWYPMFQ IFRDVSSFLP FEEIETLKID MRYILEGLLE
NLTYDEKSDE DDLTKWLRQE AVRWACIFGD TNCHKIAKLK LKEHLKDPLH HKLSPEWREW
TYCKGAMVAK KRVLMQLEKL SRRNDHKVFN YISCVEKPRR AFDIFFNSAL KWKDRYPNFF
HYAIFVDYTV EHRDEIRNFI KFIDIMAPAS VKTKLVFIII KHIFSEATLQ RIFPKWRFLD
LFVVQVQQDC LRLDTNFIMK PLSYEVQTSS EIKSLFSFPI YVKAPVILRM VQHIIGHEFQ
EIIKNYLKSY SYHSLSLDYL WNMMQVHKKN PKLGNYTMKD IMETWITRNN HPIVHVHRSD
FMLSIYQCQE GYVDDDGEYC QLPHNWLPIT FTTWEQLDFN DTTPRDWITP DSSEIIVELS
NNTGWIIVNL QQTGYYRVRY DDTSLDEIAK YLWSNDYEKI HVLNRAQIID DTYYFVKRGV
VPYNKFRRLI RYLGQERDCV AWYPMFQIFR DISRFLPFEE IATLKRKVSH TCSEKL
//
