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Database: UniProt
Entry: A0A026WXN2_OOCBI
LinkDB: A0A026WXN2_OOCBI
Original site: A0A026WXN2_OOCBI 
ID   A0A026WXN2_OOCBI        Unreviewed;       353 AA.
AC   A0A026WXN2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=phospholipase A1 {ECO:0000256|ARBA:ARBA00013179};
DE            EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
GN   ORFNames=DMN91_000433 {ECO:0000313|EMBL:RLU26637.1}, X777_16107
GN   {ECO:0000313|EMBL:EZA59904.1};
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:EZA59904.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA59904.1, 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).
RN   [2] {ECO:0000313|EMBL:RLU26637.1, ECO:0000313|Proteomes:UP000279307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU26637.1};
RX   PubMed=30249741; DOI=10.1101/gr.237123.118;
RA   McKenzie S.K., Kronauer D.J.C.;
RT   "The genomic architecture and molecular evolution of ant odorant
RT   receptors.";
RL   Genome Res. 28:1757-1765(2018).
RN   [3] {ECO:0000313|EMBL:RLU26637.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU26637.1};
RA   Mckenzie S.K., Kronauer D.J.C.;
RL   Submitted (JUL-2018) 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; KK107087; EZA59904.1; -; Genomic_DNA.
DR   EMBL; QOIP01000001; RLU26637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026WXN2; -.
DR   STRING; 2015173.A0A026WXN2; -.
DR   EnsemblMetazoa; XM_011331428.3; XP_011329730.1; LOC105274935.
DR   OMA; KEHTSIM; -.
DR   OrthoDB; 5398733at2759; -.
DR   Proteomes; UP000053097; Unassembled WGS sequence.
DR   Proteomes; UP000279307; Chromosome 1.
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:SF150; FI01825P-RELATED; 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:UP000053097};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..353
FT                   /note="phospholipase A1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033208081"
FT   DOMAIN          70..344
FT                   /note="Lipase"
FT                   /evidence="ECO:0000259|Pfam:PF00151"
SQ   SEQUENCE   353 AA;  39315 MW;  31EDAA2FE45D1AA4 CRC64;
     MQILVLIGLL FACVATGLPA EKETSNDIFT QLDYEKFENS VAYVYDDNEN LVRLTFEDDE
     DDESFDETKK DLANRVFFFL YTKDNPTDPK PLYLDDENAL KNSFFDPKKP TRFITHGWMN
     SRNSAACTLI RDAYVKHDDY NVIVIDWSKI SIRPYIWAST RVKMVGMFVS SMIDFLVKHG
     LDLSQTTLIG HSLGAHVSGL AARFAKGDVN YVVGLDPALP GFYLAGPGSR ISSGDATYVE
     IIHTNGGLLG FLAAIGDVDF FPNGGSKQLG CLIDIGGSCS HARSYRFYAE SILSDVGFHG
     RKCNSFLRWQ LGLCKKEHTS IMGGHKLFNG HGNYFLMTRS AFPFAKGLLA RDP
//
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