ID   A0A2K6KNE0_RHIBE        Unreviewed;       390 AA.
AC   A0A2K6KNE0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Phospholipase A1 {ECO:0000256|ARBA:ARBA00031180};
GN   Name=LIPG {ECO:0000313|Ensembl:ENSRBIP00000012758.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000012758.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000012758.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000012758.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC         octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC         Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC         Evidence={ECO:0000256|ARBA:ARBA00000652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000256|ARBA:ARBA00000652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC         dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC         ChEBI:CHEBI:76478; Evidence={ECO:0000256|ARBA:ARBA00001601};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC         Evidence={ECO:0000256|ARBA:ARBA00001601};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
CC         Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000256|ARBA:ARBA00000879};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC         Evidence={ECO:0000256|ARBA:ARBA00000879};
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   AlphaFoldDB; A0A2K6KNE0; -.
DR   ESTHER; rhibe-a0a2k6kn93; Lipoprotein_Lipase.
DR   Ensembl; ENSRBIT00000036490.1; ENSRBIP00000012758.1; ENSRBIG00000030348.1.
DR   GeneTree; ENSGT00940000159394; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004465; F:lipoprotein lipase activity; IEA:InterPro.
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; IPR002330; Lipo_Lipase.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610:SF13; ENDOTHELIAL LIPASE; 1.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PRINTS; PR00822; LIPOLIPASE.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          79..380
FT                   /note="Lipase"
FT                   /evidence="ECO:0000259|Pfam:PF00151"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  42704 MW;  E90903FD240CA3C4 CRC64;
     VLSFSRDGVP SGRRVSGKCP PPPLGVAGAR GGSGGPGEGS GRKLGLLESH LPAERAGEEA
     GPSVRRPRDE LHKPKAIQTE VKPSVRFNFR TSKDPEHEGC YLSLGHSQPL EDCGFNMTAK
     TFFIIHGWTM SGIFENWLHK LVSALHTREK DANVVVVDWL PLAHQLYTDA VNNTRVVGHS
     IARMLDWLQE KDDFSLGNVH LIGYSLGAHV AGYAGNFVKG TVGRITGLDP AGPMFEGADI
     HKRLSPDDAD FVDVLHTYTR SFGLSIGIQM PVGHIDIYPN GGDFQPGCGL NDVLGSIAYG
     TITEVVKCEH ERAVHLFVDS LVNQDKPSFA FQCTDSNRFK KGICLSCRKN RCNSIGYNAK
     KMRNKRNSKM YLKTRAGMPF KGNLQSLKHP
//