ID F4WC23_ACREC Unreviewed; 930 AA.
AC F4WC23;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=G5I_03095 {ECO:0000313|EMBL:EGI68003.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI68003.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL888070; EGI68003.1; -; Genomic_DNA.
DR RefSeq; XP_011050058.1; XM_011051756.1.
DR AlphaFoldDB; F4WC23; -.
DR MEROPS; M01.A24; -.
DR EnsemblMetazoa; XM_011051756.1; XP_011050058.1; LOC105143429.
DR GeneID; 105143429; -.
DR KEGG; aec:105143429; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; F4WC23; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000007755; 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; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 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|ARBA:ARBA00022438,
KW 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 Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 80..263
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 298..515
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 596..909
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 456
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 930 AA; 105478 MW; F31526FD3A0F8BA4 CRC64;
MFSRIVARVS VRCRFVSQQK EKGVDDNLLL RLLRACTVRN GGIQDARYCV KTCQVAVSEP
CGAMSGDEKP FRRLPLCVRP YHYDISLTPH ITTFTFSGTE KVHLNVETST DTIVLNCLEI
NIKHASFYGN DGKIIVPVQI VLSGSEETAT LVFPEALPSG KSGYLNIEFM GEINDKMKGF
YRSKYTGEDG TVEYAAVTQF EPTDARRCFP CWDEPALKAT FDITLKVPIG LTALSNMPVK
SKVTNGNCET LTFERTPIMS TYLVAVVIGD FDYIENMSSD GVLVRVYVPK SKKEQGQFAL
EVATKVLPYY KTYFGIAYPL PKIDLIAIAD FSSGAMENWG LVTYRETCLL VDPQNTSAVR
KQWIALIVAH ELAHQWFGNL VTMEWWTHLW LNEGYASFVE FLCVAHLFPE YDIWTQFVTD
TYIRALELDA LKNSHPIEVP VGHPSEIDEI FDDISYHKGA SVIRMLHAYI GDDDFRKGMN
LYLKRHSYAN AETEDLWAAL EEVSNKAVRK VMSSWTKRQG FPVVKVDYHQ EGNNRILSLS
QERFLADGSV DNNADNAWLI PISVSSSQDP KKTIFDGILD AKTKEFVIQN VPEGTWLKIN
PGTIGFYRTR YSQSALSLLL PAIKDHTLPP LDRLGLLDDL FAMVQAGYAS TVEVLELMQA
FLHEDNYTVW STIVNILSKI GILISHLDFE DSLKAFGRNL FREVNVRLGW NPKPNESHLN
TLLRSLVLGR MAALNDQDTI EEAKRRFELH VNGTTTLAAD LRSPVYRAVL SVGDANTYDT
MLKLYKEADL QEEKERILRA LGAIKDETLL RKVLDFSMSE EVRAQDTVFA IMSVSLSYKG
RLMAWNFFKE KWKTLLDRYE GGFLLARLIK FTTENFVTEE QAKDVESFFE GHPTPGTERT
VQQCVESIRL NAAWLNREKD SIRKYLTTQV
//
