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Database: UniProt
Entry: F4WI35_ACREC
LinkDB: F4WI35_ACREC
Original site: F4WI35_ACREC 
ID   F4WI35_ACREC            Unreviewed;       309 AA.
AC   F4WI35;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 33.
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_05357 {ECO:0000313|EMBL:EGI66128.1};
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:EGI66128.1}
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; GL888172; EGI66128.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4WI35; -.
DR   STRING; 103372.F4WI35; -.
DR   eggNOG; ENOG502RZTK; Eukaryota.
DR   InParanoid; F4WI35; -.
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; IPR013818; Lipase.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610:SF184; LD47264P; 1.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   Pfam; PF00151; Lipase; 1.
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}.
FT   DOMAIN          46..278
FT                   /note="Lipase"
FT                   /evidence="ECO:0000259|Pfam:PF00151"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGI66128.1"
SQ   SEQUENCE   309 AA;  33799 MW;  4A897F6C183C1B56 CRC64;
     LSAVYPTLLA SLASHSNYTL FANEHGMLYM IDISEPTVLT QTEYKEISYI TFQIQFLLYT
     RNNRKVGEPL IINDNDSVEK SSWNPTHPTR IITHGWRGDI EDKSACALIR DAYLSIGHYN
     VILIDWSKAA GYLWYWKVAR SVPLVAERVT QLIDFLQSQA GLDPSKTKVI GHSLGGHVVG
     IAARNANGDI AEAVALDPAK PLFDSKGPGE RVDRSDAARV QVIHTSILGL EEPIGNADFY
     PNGGKSQPGC GIIALTCAHA RSYEYYAESI LNPTGFRAGN VFMGGPSLDP NARGEYILET
     AEKSPFGLG
//
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