ID A0A0J7L330_LASNI Unreviewed; 170 AA.
AC A0A0J7L330;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=phospholipase A1 {ECO:0000256|ARBA:ARBA00013179};
DE EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
GN ORFNames=RF55_2429 {ECO:0000313|EMBL:KMQ97242.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ97242.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ97242.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ97242.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMQ97242.1}.
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DR EMBL; LBMM01000904; KMQ97242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7L330; -.
DR STRING; 67767.A0A0J7L330; -.
DR PaxDb; 67767-A0A0J7L330; -.
DR OrthoDB; 3125528at2759; -.
DR Proteomes; UP000036403; 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 Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; LIPASE; 1.
DR PANTHER; PTHR11610:SF172; LIPASE MEMBER H-A-LIKE PROTEIN; 1.
DR Pfam; PF00151; Lipase; 1.
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:UP000036403};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 2..78
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
SQ SEQUENCE 170 AA; 19165 MW; 58E19623BAB1592A CRC64;
MNRLDAGDAD FVEVIHTNAG YYGEVGRVGH VDFCVNGGKL QPFCRDREMF HLCSHVWSVC
FMAQSIDDDG ASMMAESCSR RCPSGPRIAA RAGEYVTMGQ HTPANARGSF CFSEVNPPFC
PKYWNGRGDE RCCVPELTND EEIDENNVKY DNTTKRLTTE LDLRRPRRVN
//
