ID   PLB1_RABIT              Reviewed;        1458 AA.
AC   Q05017;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 113.
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:0000269|PubMed:8509424};
DE   AltName: Full=Phospholipase AdRab-B;
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;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Intestine;
RX   PubMed=8509424; DOI=10.1016/s0021-9258(18)31471-6;
RA   Boll W., Schmid-Chanda T., Semenza G., Mantei N.;
RT   "Messenger RNAs expressed in intestine of adult but not baby rabbits.
RT   Isolation of cognate cDNAs and characterization of a novel brush border
RT   protein with esterase and phospholipase activity.";
RL   J. Biol. Chem. 268:12901-12911(1993).
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:8509424). Has dual phospholipase and
CC       lysophospholipase activities toward diacylphospholipids. Preferentially
CC       cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward
CC       glycerolipid substrates (PubMed:8509424). Hydrolyzes fatty acyl chains
CC       of diacylglycerols with preference for the sn-2 position and of
CC       triacylglycerols with not positional selectivity (PubMed:8509424). May
CC       also hydrolyze long chain retinyl esters such as retinyl palmitate
CC       (Probable). May contribute to digestion of dietary phospholipids,
CC       glycerolipids and retinoids, facilitating lipid absorption at the brush
CC       border (Probable). {ECO:0000269|PubMed:8509424,
CC       ECO:0000305|PubMed:8509424}.
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:0000269|PubMed:8509424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000305|PubMed:8509424};
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-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:0000269|PubMed:8509424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC         Evidence={ECO:0000305|PubMed:8509424};
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:0000269|PubMed:8509424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC         Evidence={ECO:0000305|PubMed:8509424};
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:8509424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976;
CC         Evidence={ECO:0000305|PubMed:8509424};
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)-glycerol + H2O = (9Z)-octadecenoate +
CC         1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:40967,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:52323, ChEBI:CHEBI:75342;
CC         Evidence={ECO:0000269|PubMed:8509424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40968;
CC         Evidence={ECO:0000305|PubMed:8509424};
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         1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:75342, ChEBI:CHEBI:75735;
CC         Evidence={ECO:0000269|PubMed:8509424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940;
CC         Evidence={ECO:0000305|PubMed:8509424};
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:0000269|PubMed:8509424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC         Evidence={ECO:0000305|PubMed:8509424};
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:0000269|PubMed:8509424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC         Evidence={ECO:0000305|PubMed:8509424};
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:0000250|UniProtKB:O54728}.
CC   -!- TISSUE SPECIFICITY: Intestine. {ECO:0000269|PubMed:8509424}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the intestine of adult but not baby
CC       rabbits. {ECO:0000269|PubMed:8509424}.
CC   -!- DOMAIN: Repeat 2 contains the catalytic domain.
CC       {ECO:0000250|UniProtKB:O54728}.
CC   -!- PTM: Undergoes proteolytic cleavage in the ileum.
CC       {ECO:0000250|UniProtKB:O54728}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       Phospholipase B1 subfamily. {ECO:0000305}.
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DR   EMBL; Z12841; CAA78303.1; -; mRNA.
DR   PIR; A45665; A45665.
DR   RefSeq; NP_001095178.1; NM_001101708.1.
DR   AlphaFoldDB; Q05017; -.
DR   STRING; 9986.ENSOCUP00000013064; -.
DR   SwissLipids; SLP:000000630; -.
DR   GlyCosmos; Q05017; 10 sites, No reported glycans.
DR   PaxDb; 9986-ENSOCUP00000013064; -.
DR   GeneID; 100009309; -.
DR   KEGG; ocu:100009309; -.
DR   CTD; 151056; -.
DR   eggNOG; KOG3670; Eukaryota.
DR   InParanoid; Q05017; -.
DR   OrthoDB; 6003at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IDA:UniProtKB.
DR   GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046340; P:diacylglycerol catabolic process; IDA:UniProtKB.
DR   GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:UniProtKB.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR   CDD; cd01824; Phospholipase_B_like; 3.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 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; PHOSPHOLIPASE B, PLB1; 1.
DR   PANTHER; PTHR21325:SF52; PHOSPHOLIPASE B1, MEMBRANE-ASSOCIATED; 1.
DR   Pfam; PF00657; Lipase_GDSL; 3.
DR   SUPFAM; SSF52266; SGNH hydrolase; 3.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Hydrolase; Lipid metabolism; Membrane;
KW   Phospholipid metabolism; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1458
FT                   /note="Phospholipase B1, membrane-associated"
FT                   /id="PRO_0000017854"
FT   TOPO_DOM        20..1415
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1416..1436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1437..1458
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          39..347
FT                   /note="1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          362..707
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          708..1054
FT                   /note="3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1064..1403
FT                   /note="4"
FT                   /evidence="ECO:0000255"
FT   REGION          39..1403
FT                   /note="4 X 308-326 AA approximate repeats"
FT                   /evidence="ECO:0000255"
FT   REGION          1404..1446
FT                   /note="Necessary for membrane localization"
FT                   /evidence="ECO:0000250|UniProtKB:O54728"
FT   ACT_SITE        400
FT                   /evidence="ECO:0000250|UniProtKB:O54728"
FT   ACT_SITE        514
FT                   /evidence="ECO:0000250|UniProtKB:O54728"
FT   ACT_SITE        655
FT                   /evidence="ECO:0000250|UniProtKB:O54728"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        529
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        590
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        690
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        783
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1077
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1114
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"
SQ   SEQUENCE   1458 AA;  161344 MW;  9D1608F47B1062E6 CRC64;
     MALWPSVFLL GLLPLLGRGA DQIQTSSGKN TLEGQLWPES LKTFPFPCDP KTLAESVPSE
     SVHSLRPSDI KFVAAIGNVE TAPDSGADDL EEQDGTEKRP EQACMGVVTV LSDIIGRFSP
     SALMPLCPET RLVPRGGAED LWMQATELVR SMRENPQLDF EHDWKLINVF FSNTSQCFPC
     PSAQQKGLVL GGMDKLTRTL DYLQQEVPKA FVNLVDLSEL AAFSRWRQGA QLSPAAEPCR
     CLRETSQLTK VLTQWSYLEA WDSLLASSKY NTQESFAVVF QPFFYESSLS ALLAEPPLQD
     PTTLALSLWN RMMEPIGRKE EPFSEKERKP LRCPTQESPY LFTYRNSGQL TRVSQPQGKL
     EVREGTEIRC PDKDPSDSVP TSVHRLKPAD IKVIGAMGDS LTAGNGAGSQ PGNILDVLTQ
     YRGLSWSVGG DQNISTVTTL ANILREFNPS LQGFSVGTGR ETTSQAFFNQ AVAGARADGL
     IPQAQRLVAL MKNDTRINFQ EDWKIITVFI GGNDLCDFCN DPVRYSPQNF TDNIGTALDI
     LHAEIPRAFV NLVKVLEISK LRELYQETKV SCPRMILRSL CPCVLKFDDN STEIASLIET
     IKEYQERTQQ LIDSGRYDTR DDFTVVLQPF FEKVNMPKTQ DGLPDNSFFA PDCFHFSSKA
     HAHAASALWN NMLEPVGQKT THNDFEGAVN ITCPNQVWPF LSTYKNSVQG FGTWLPCRDR
     SPSASPPTSV HALRPADIQV VAALGDSLTA GIGIGSKPND LSDGTTQYRG LSYSSGGDGS
     LDNVTTLPNI LRQFNSNLMG FAVGTGDASG TNAFFNQAVP GAKARDLMSQ VQTLVQRMKD
     DHRVNFQEDW KVITVQIGAS DLCDYCTDSN LYSAANFYDH LRDALDALHR EVPRALVNLV
     DFMNPSVTRQ VFLGNPDKCP VQQASALCNC VLSPRENSYE LARLEALAQA YQSSLRELVE
     SGRYDTREDF SVVLQPFFHS IQLPVLQDGR LDTSFFAPDC VHPNQKFHSQ LSRALWRNML
     EPLGGKTDAL DLTAAITLTC PTQNEPFLRT FRNSDYTYPS RPAVENWGSD FLCTAWNASR
     GVPNSVHELQ PGDIKVVAAL GDSLTLAMGA RPSNSSDPPM FWRGLSWSIG GDGALETHTT
     LPNILKKFNP SILGFSTGTL EGTMGLNVAV QGARAQDMPA QARDLVERMR NSPEIDLEKD
     WKLVTLFVGG NDLCHFCENP EGSSEGEYVQ HIQQALDVLY EELPRTFVNV VEVMELAGLH
     QDQGGRCATL LAAQSHCTCF KYSQSSVEMQ ELKKVNWNLQ SGLSRLSYSH QYVQREDFAV
     VVQPFFQNTL VPLNGRGDTD LTFFSDDCFH FSERGHAEMA IALWNNMLEP VGHKTTSNNF
     TYSRTKLKCP SPDSPYLYTL RNSRLLPDQA EADPTVLYWA VPVAAGAGLL IGILAMVAGR
     GMRCRPREDP PLSLSTGL
//