ID F4WY21_ACREC Unreviewed; 357 AA.
AC F4WY21;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=phospholipase A1 {ECO:0000256|ARBA:ARBA00013179};
DE EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
DE Flags: Fragment;
GN ORFNames=G5I_10866 {ECO:0000313|EMBL:EGI60946.1};
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:EGI60946.1}
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000256|ARBA:ARBA00000111};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
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DR EMBL; GL888434; EGI60946.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WY21; -.
DR STRING; 103372.F4WY21; -.
DR EnsemblMetazoa; XM_011063627.1; XP_011061929.1; LOC105150498.
DR eggNOG; ENOG502S0C2; Eukaryota.
DR InParanoid; F4WY21; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002334; Allerg_PlipaseA1.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; LIPASE; 1.
DR PANTHER; PTHR11610:SF173; LIPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00151; Lipase; 1.
DR PRINTS; PR00825; DOLALLERGEN.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..357
FT /note="phospholipase A1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003323931"
FT DOMAIN 70..351
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGI60946.1"
SQ SEQUENCE 357 AA; 39876 MW; 7F932E173932801E CRC64;
KNITMSFIST FLVFLFLNVS FNIAELLRNR PSIQNFQDHH PEEGLLEVFL SPTSIIANDR
ATIGNIIGID FKAEDINYEL YTKNNKEQPV SLRVADATQL KDSPFNPEWP TKVIIHGWAE
SGNAFWLHDI RRNYLNVGNY NVICVDWFAG STKEYLTSVK LIHQVGEYVA AFIEFLESET
QVSFDDIHVV GHSLGAHIAG HIGNYMSKKL GRITGLDPAG PAFETPYLKD TEERLDAADA
NFVDVIHTCA GSLGFLRPIG HADFYPNGGT FRQPGCPVFS SQTCSHGRSH QFFTESIVHP
DGFVAVKCSN WMDFQLGKCD DNNFSTAVMG EFINPNVQGI FYLQTNAQPP FGKGKIK
//
