ID E2AIM4_CAMFO Unreviewed; 311 AA.
AC E2AIM4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=phospholipase A1 {ECO:0000256|ARBA:ARBA00013179};
DE EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
GN ORFNames=EAG_00703 {ECO:0000313|EMBL:EFN66713.1};
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:EFN66713.1, 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; GL439840; EFN66713.1; -; Genomic_DNA.
DR RefSeq; XP_011258702.1; XM_011260400.2.
DR AlphaFoldDB; E2AIM4; -.
DR STRING; 104421.E2AIM4; -.
DR GeneID; 105252815; -.
DR KEGG; cfo:105252815; -.
DR InParanoid; E2AIM4; -.
DR OMA; QPGCPLN; -.
DR OrthoDB; 3466854at2759; -.
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: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:SF37; GH01208P; 1.
DR PANTHER; PTHR11610; LIPASE; 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:UP000000311};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..311
FT /note="phospholipase A1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003157236"
FT DOMAIN 56..302
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
SQ SEQUENCE 311 AA; 34611 MW; 5944DFFE540E2E1C CRC64;
MMIHTSQLFV ITITIYAAII DGAPSANLES IFLRIYVGTT MDEYVDYSLK NTDALLSRIN
SSKPTVLYIH GYMEHIGKDS IRTIVQAYLK RNDHNIIAMD YGKLVSDSYM TAVKNAFHVA
AALTVTLDKM VGSGFNSEKL HIVAHSLGSQ VAGYLGRSVN FQIPRITGLD PAGPLFNYLE
PHLTSSDARF VDIIHTDLGF YGIMKIIGTV DFYPNGGRRV QPGCPLNATI YSKEDFCSHH
RSWRFYAESL IDETAFLGVE CPSLYHFYSG KCNNNTQIIM GYGTPSNAQR NIYLVTADQS
PFGLHEKGTH L
//
