PLB1_CAVPO
ID PLB1_CAVPO Reviewed; 1463 AA.
AC O70320;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phospholipase B1, membrane-associated;
DE Short=Phospholipase B;
DE AltName: Full=Lysophospholipase;
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:O54728};
DE AltName: Full=Phospholipase A2;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:O54728};
DE AltName: Full=Phospholipase B/lipase;
DE Short=PLB/LIP;
DE AltName: Full=Triacylglycerol lipase;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:O54728};
DE Flags: Precursor;
GN Name=PLB1; Synonyms=PLB;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 396-402; 463-470 AND
RP 895-904, FUNCTION, CATALYTIC ACTIVITY, PROTEOLYTIC PROCESSING, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Crl:(BFA)BR; TISSUE=Intestine;
RX PubMed=9593672; DOI=10.1074/jbc.273.22.13407;
RA Delagebeaudeuf C., Gassama-Diagne A., Nauze M., Ragab A., Li R.Y.,
RA Capdevielle J., Ferrara P., Fauvel J., Chap H.;
RT "Ectopic epididymal expression of guinea pig intestinal phospholipase B.
RT Possible role in sperm maturation and activation by limited proteolytic
RT digestion.";
RL J. Biol. Chem. 273:13407-13414(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=2722844; DOI=10.1016/s0021-9258(18)60555-1;
RA Gassama-Diagne A., Fauvel J., Chap H.;
RT "Purification of a new, calcium-independent, high molecular weight
RT phospholipase A2/lysophospholipase (phospholipase B) from guinea pig
RT intestinal brush-border membrane.";
RL J. Biol. Chem. 264:9470-9475(1989).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=1716922; DOI=10.1139/o91-054;
RA Pind S., Kuksis A.;
RT "Further characterization of a novel phospholipase B (phospholipase A2-
RT lysophospholipase) from intestinal brush-border membranes.";
RL Biochem. Cell Biol. 69:346-357(1991).
CC -!- FUNCTION: Calcium-independent membrane-associated phospholipase that
CC catalyzes complete diacylation of phospholipids by hydrolyzing both sn-
CC 1 and sn-2 fatty acyl chains attached to the glycerol backbone
CC (phospholipase B activity) (PubMed:2722844). Has dual phospholipase and
CC lysophospholipase activities toward diacylphospholipids. Preferentially
CC cleaves sn-2 ester bonds over sn-1 bonds (PubMed:2722844,
CC PubMed:9593672). Acts as a lipase toward glycerolipid substrates (By
CC similarity). Hydrolyzes fatty acyl chains of diacylglycerols with
CC preference for the sn-2 position and of triacylglycerols with not
CC positional selectivity (By similarity). May also hydrolyze long chain
CC retinyl esters such as retinyl palmitate (By similarity). May
CC contribute to digestion of dietary phospholipids, glycerolipids and
CC retinoids, facilitating lipid absorption at the brush border (By
CC similarity). {ECO:0000250|UniProtKB:O54728,
CC ECO:0000250|UniProtKB:Q05017, ECO:0000269|PubMed:2722844,
CC ECO:0000269|PubMed:9593672}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine
CC + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:40643, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:60000; Evidence={ECO:0000269|PubMed:2722844,
CC ECO:0000269|PubMed:9593672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40644;
CC Evidence={ECO:0000305|PubMed:2722844, ECO:0000305|PubMed:9593672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:73002, ChEBI:CHEBI:76084;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-
CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40639,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75069;
CC Evidence={ECO:0000269|PubMed:2722844};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40640;
CC Evidence={ECO:0000305|PubMed:2722844};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2
CC H(+) + 2 hexadecanoate + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40975, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:2722844};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976;
CC Evidence={ECO:0000305|PubMed:2722844};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:40915, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:34112,
CC ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:41111, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75466,
CC ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-
CC octadecenoate + 1,3-dihexadecanoylglycerol + H(+);
CC Xref=Rhea:RHEA:40983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75688, ChEBI:CHEBI:77619;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)glycerol + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40979, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:75585, ChEBI:CHEBI:75688;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-
CC glycerol + H(+); Xref=Rhea:RHEA:41103, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77623,
CC ChEBI:CHEBI:77624; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:41107, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75558,
CC ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O =
CC (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:40927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75550, ChEBI:CHEBI:77097;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 1-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:41219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:75757;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41220;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:42604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75824, ChEBI:CHEBI:75938;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75735, ChEBI:CHEBI:75937;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:O54728}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Present in the intestinal brush border membranes.
CC {ECO:0000269|PubMed:9593672}.
CC -!- TISSUE SPECIFICITY: Expressed in the epididymis, jejunum and ileon (at
CC protein level). {ECO:0000269|PubMed:1716922,
CC ECO:0000269|PubMed:2722844, ECO:0000269|PubMed:9593672}.
CC -!- DOMAIN: Repeat 2 contains the catalytic domain.
CC {ECO:0000250|UniProtKB:O54728}.
CC -!- PTM: Undergoes proteolytic cleavage in the ileum.
CC {ECO:0000269|PubMed:9593672}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC Phospholipase B1 subfamily. {ECO:0000305}.
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DR EMBL; AF045454; AAC40129.1; -; mRNA.
DR RefSeq; NP_001166499.1; NM_001173028.1.
DR AlphaFoldDB; O70320; -.
DR STRING; 10141.ENSCPOP00000009712; -.
DR PRIDE; O70320; -.
DR GeneID; 100135633; -.
DR KEGG; cpoc:100135633; -.
DR CTD; 151056; -.
DR eggNOG; KOG3670; Eukaryota.
DR InParanoid; O70320; -.
DR OrthoDB; 1232962at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01824; Phospholipase_B_like; 4.
DR Gene3D; 3.40.50.1110; -; 3.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR008265; Lipase_GDSL_AS.
DR InterPro; IPR035547; Phospholipase_B.
DR InterPro; IPR038885; PLB1.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR21325; PTHR21325; 3.
DR Pfam; PF00657; Lipase_GDSL; 3.
DR PROSITE; PS01098; LIPASE_GDSL_SER; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Phospholipid metabolism; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1463
FT /note="Phospholipase B1, membrane-associated"
FT /id="PRO_0000324382"
FT TOPO_DOM 25..1419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1420..1440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1441..1463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 38..346
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 361..706
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 707..1053
FT /note="3"
FT /evidence="ECO:0000255"
FT REPEAT 1063..1403
FT /note="4"
FT /evidence="ECO:0000255"
FT REGION 38..1403
FT /note="4 X 308-326 AA approximate repeats"
FT /evidence="ECO:0000255"
FT REGION 356..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1450
FT /note="Necessary for membrane localization"
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT COMPBIAS 356..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT ACT_SITE 513
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT ACT_SITE 654
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1463 AA; 162176 MW; 101C4969815F24B1 CRC64;
MGLQPGVLLV GLLLLGQGIT QIHTSSGKST LEGQLWPETK KNFPFSCSPK KLGLNMPSES
VHTLTPADIK LIAAIGDMET PPDSGAVNLD TSERTEKEPW RGCMGMMTVL SDIISHFNPS
VLLPTCPPWR SAAVRGGVEE LRTQAEELVS SLKKNPQLDF QQDWKLINVF FSNASLCYLC
PSAHENGPLM SNMDKLAGIL HYLHQEVPRA FVNLVDLFEV VAMPRWHQGT MLSRPSPEAC
GCSGETSKLD TVVMQWSYQE TWDSLLASSS FNDQESFAVV FQPFFYEVSS PVEEPPSQDP
TTLALSLWNN MMKPVGQKDE PFSTIERRPM KCPSQESPYL FTYRNSNYQS RLLKRQRQHK
EREGTEIRCP DKDPSDSTPT SVHRLKPADI KVIGALGDSL TAGNGAGSRP GNILDVLTEY
RGLSWSIGAD HNISSVTTLP NILREFNPSL KGFSTGTGKA NSVGAFFNQA VAGARAGDLI
PQARTLVDLM KNHTSINFEE DWKIITVFIG GNDLCDFCSD PVTNSPENFT DNIRQALDIL
HAEVPRAFVN MVKVLQIVNL RELYKDSRVS CPRLILRNLC RCVLLPDDNS TELESLIDIN
KKYQERTHQL IESGRYDTRE DFTVVLQPFF EKVDIPKTSE GLPDNTSFAP DCFHFSSKTH
ARAASALWKN MLEPVGQKTT QNNFENSIDI ICPNQAFPYL STYKNGIEGH GTWLTCRERT
PSASPPTSVH ALRPADVRVV AALGDSLTAG SGIGSKPGDL ADVITQYRGL SYSSGGDGSL
MNVTTLPNIL REFNSNLTGY AVGTGDASNT NAFLNQAVPG AKAEELMSQV KTLVQKMKDD
PRINFHEDWK VITVLIGTND LCNHCTDLDL YSSANFFNHL LNALDILHRE VPRALVNLVD
FMNPSIMRQV FLGNPDKCPV QQASILCNCV LSLRENSYEL ARMDALTRAY QSSMRELVES
GRYDTREDFS VVLQPFFLNI RLPILEDGRP DTSFFAPDCI NPGQKFHSQL SRALWVNMLE
PVGSKTDTLD LTADISLPCP TQEEPFLRTP QNSDYTYPTK PAIENWGSDF LCTEWKPSNS
VPTSVHKLQP ADIKVVAALG DSLTTAVGAR ASNSSDLLMS WRGLSWSIGG DGALETHTTL
PNILKKFNPS IFGFSTGTLE ETAGFNVAVE EARARDMPAQ ARDLVERMKA STEINLEMDW
KLITLFIGSN DLCHYCDNPE NHSAEEYVQH IRQALDILYE ELPRAFINVV DIIMELAGLH
QGQGGHCTAL LPAQSTCSCL RHFPSSPVIQ ELKKVTWNLQ SDMSRLSYQE KYTQREDFAV
VVQPFFQNTL IPLDKLGSTD PTFFSEDCLH FSERGHAEMA IALWNNMLEP VGHKTTFNNF
TYNRTKLKCP STESPYLYTL QNSLSLPVQT EKASGVAPGI VSAAAAGGLL VGLIVGILAV
SLWSSFRRRQ KKSPPESVPV ANF
