ID E2AF33_CAMFO Unreviewed; 594 AA.
AC E2AF33;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=phospholipase A1 {ECO:0000256|ARBA:ARBA00013179};
DE EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
GN ORFNames=EAG_10526 {ECO:0000313|EMBL:EFN67988.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN67988.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL438984; EFN67988.1; -; Genomic_DNA.
DR AlphaFoldDB; E2AF33; -.
DR STRING; 104421.E2AF33; -.
DR InParanoid; E2AF33; -.
DR OMA; CKFIAWP; -.
DR Proteomes; UP000000311; 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:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; cd04301; NAT_SF; 1.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610:SF178; FI22312P1; 1.
DR PANTHER; PTHR11610; LIPASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00151; Lipase; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51186; GNAT; 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:UP000000311};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..594
FT /note="phospholipase A1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003156712"
FT DOMAIN 433..570
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 594 AA; 66757 MW; 532D52C77A8F0E0F CRC64;
MQPVILHHVL FALLIIAVTT SIDGKLHPVK LRTARNRSML RRIAIFREEK SKICYDLLGC
FADQPQHLSI KKPPEHPSII QTRFFLYTHA DRPNPELLQY GDNLRSIVHS RFNVTKHLKV
LIHGFKGSGN DISLILGVNL LLDIEDANIV VLDWTKGAGT TYAAAVANSE LVGRQLALIL
LDTINLGIDP TNIHVIGFSL GAHVAGCASE VLKRKNLLLG RITGLDPASP FFRRHLFREK
SRKLDATDAH LVDVIHTDGS QDFADGFGLL KPIGHIDFFP NGGREQPGCT DVKNSVVVSH
IKEELLDRNI ACSHLRAWQL FVESIRSQNE KCKFIAWPCP QGGLSFTKGM CFPMESSDWN
QEMGYAANRG SLGIYYLSTR AEKPFCGQPL RASVTMSEGM PQVSGILFFK IFLGNSTTLF
KIQCKLYMSN RFSRFWVAEA IQPNLVTQHP KEVHYTILTE QQYCQANMGV SLQAKKIVGT
ICLTKSHTLD KCAWIKRLCV HKQYQRKGIA TCLLNTAVEF AIEAGYSCAN IVASQYTEGG
KELCLKKGFE LKQIYHKSIL GSYVMILMYE LSYQIKPSED DYLPCIGKYY LNHY
//
