ID A0A0N0U310_9HYME Unreviewed; 570 AA.
AC A0A0N0U310;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phospholipase A1 {ECO:0000256|ARBA:ARBA00013179};
DE EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
GN ORFNames=WN51_08230 {ECO:0000313|EMBL:KOX67324.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX67324.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX67324.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX67324.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX67324.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR EMBL; KQ436240; KOX67324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0U310; -.
DR STRING; 166423.A0A0N0U310; -.
DR OrthoDB; 3428256at2759; -.
DR Proteomes; UP000053105; 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 Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610:SF184; LD47264P; 1.
DR PANTHER; PTHR11610; LIPASE; 1.
DR Pfam; PF00151; Lipase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS50095; PLAT; 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:UP000053105};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 455..570
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
SQ SEQUENCE 570 AA; 64778 MW; D9ADCAC2C6E8E42C CRC64;
MKFCTVSKKR RYLWVSLMVR KLINTIKVPN IPHQFLKLGL SPLYATLPRG RAKRETKQAI
FRHIMIVSWT HIDQKWYMWR CYEPYGCFYI GSPWSGENRP VSTFPARPDS INPRFSLYTR
DTAEQPHDLK IDKFVTIRKS PLKKDGNFYL IIHGFLDNGD KTWVMIVWNF RLTLYIRIFK
ALNYHKRKLP SFCSTLRILL SSRRIPLPQR LMKELLIREH CNVLIVNWIG GAGPPYTQAV
ANTRLVGAMT ARLAYQLVEI GGIDSTRIHC IGHSLGAHTC GYIGYTLRHT YYLKLGRITG
LDPAEPHFSN TSTMVRLDPT DATFVTAVHT DCNPFISGGF GITQPVGHID FYPNGGRSQP
GCNEGVLSSI TLEHGRIRRF VSCNHIRSYE YFIESINTDC PFLTVPCVSW DKFLEGGCFD
CTNQYCPKFG LDAQPGNYHA SVYLMTGSTK PFCRGHYKIV INVSKTNESL DHGGEVGTFA
VKAIGQNGKK SERMPLSSQS MYYEPGSTHA VVLPGDVVGK LEAVEISWEY RASVFNPLTW
RLLHTPRVYI DSLSIESLEA AHGLHYSNKI
//
