PLB1_HUMAN
ID PLB1_HUMAN Reviewed; 1458 AA.
AC Q6P1J6; A8KAX2; Q53S03; Q8IUP7; Q96DP9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phospholipase B1, membrane-associated;
DE Short=Phospholipase B;
DE Short=hPLB;
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 3-1458 (ISOFORM 3).
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 426-1458 (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12150957; DOI=10.1016/s0006-291x(02)00657-5;
RA Maury E., Prevost M.-C., Nauze M., Redoules D., Tarroux R., Charveron M.,
RA Salles J.-P., Perret B., Chap H., Gassama-Diagne A.;
RT "Human epidermis is a novel site of phospholipase B expression.";
RL Biochem. Biophys. Res. Commun. 295:362-369(2002).
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) (By similarity). 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 (By similarity). Hydrolyzes fatty acyl chains
CC of diacylglycerols with preference for the sn-2 position and of
CC triacylglycerols with not positional selectivity (By similarity). May
CC also hydrolyze long chain retinyl esters such as retinyl palmitate (By
CC similarity). May contribute to digestion of dietary phospholipids,
CC glycerolipids and retinoids, facilitating lipid absorption at the brush
CC border (By similarity). {ECO:0000250|UniProtKB:O54728,
CC ECO:0000250|UniProtKB:Q05017}.
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-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-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:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
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 -!- INTERACTION:
CC Q6P1J6-2; O43559: FRS3; NbExp=3; IntAct=EBI-10694821, EBI-725515;
CC Q6P1J6-2; P14136: GFAP; NbExp=3; IntAct=EBI-10694821, EBI-744302;
CC Q6P1J6-2; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-10694821, EBI-8561769;
CC Q6P1J6-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-10694821, EBI-7116203;
CC Q6P1J6-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-10694821, EBI-1055254;
CC Q6P1J6-2; Q92993: KAT5; NbExp=3; IntAct=EBI-10694821, EBI-399080;
CC Q6P1J6-2; O14901: KLF11; NbExp=3; IntAct=EBI-10694821, EBI-948266;
CC Q6P1J6-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-10694821, EBI-11742507;
CC Q6P1J6-2; Q13449: LSAMP; NbExp=3; IntAct=EBI-10694821, EBI-4314821;
CC Q6P1J6-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-10694821, EBI-713665;
CC Q6P1J6-2; P17252: PRKCA; NbExp=3; IntAct=EBI-10694821, EBI-1383528;
CC Q6P1J6-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-10694821, EBI-9090795;
CC Q6P1J6-2; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-10694821, EBI-372432;
CC Q6P1J6-2; P61981: YWHAG; NbExp=3; IntAct=EBI-10694821, EBI-359832;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6P1J6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1J6-2; Sequence=VSP_032226, VSP_032231, VSP_032232;
CC Name=3;
CC IsoId=Q6P1J6-3; Sequence=VSP_032227, VSP_032228;
CC Name=4;
CC IsoId=Q6P1J6-4; Sequence=VSP_032229, VSP_032230;
CC Name=5;
CC IsoId=Q6P1J6-5; Sequence=VSP_032225;
CC -!- TISSUE SPECIFICITY: Expressed in the epidermis (at protein level).
CC {ECO:0000269|PubMed:12150957}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB70920.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC074011; AAY24081.1; -; Genomic_DNA.
DR EMBL; AC074011; AAY24082.1; -; Genomic_DNA.
DR EMBL; AC093164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00532.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00533.1; -; Genomic_DNA.
DR EMBL; BC042674; AAH42674.1; -; mRNA.
DR EMBL; BC065041; AAH65041.1; -; mRNA.
DR EMBL; BC153864; AAI53865.1; -; mRNA.
DR EMBL; AK055428; BAB70920.1; ALT_INIT; mRNA.
DR CCDS; CCDS33168.1; -. [Q6P1J6-1]
DR CCDS; CCDS54340.1; -. [Q6P1J6-3]
DR RefSeq; NP_001164056.1; NM_001170585.1. [Q6P1J6-3]
DR RefSeq; NP_694566.4; NM_153021.4. [Q6P1J6-1]
DR RefSeq; XP_016858922.1; XM_017003433.1. [Q6P1J6-1]
DR AlphaFoldDB; Q6P1J6; -.
DR BioGRID; 127341; 62.
DR IntAct; Q6P1J6; 27.
DR STRING; 9606.ENSP00000330442; -.
DR GlyGen; Q6P1J6; 13 sites.
DR iPTMnet; Q6P1J6; -.
DR PhosphoSitePlus; Q6P1J6; -.
DR BioMuta; PLB1; -.
DR EPD; Q6P1J6; -.
DR MassIVE; Q6P1J6; -.
DR PaxDb; Q6P1J6; -.
DR PeptideAtlas; Q6P1J6; -.
DR PRIDE; Q6P1J6; -.
DR ProteomicsDB; 66829; -. [Q6P1J6-1]
DR ProteomicsDB; 66830; -. [Q6P1J6-2]
DR ProteomicsDB; 66831; -. [Q6P1J6-3]
DR ProteomicsDB; 66832; -. [Q6P1J6-4]
DR ProteomicsDB; 66833; -. [Q6P1J6-5]
DR Antibodypedia; 2675; 131 antibodies from 15 providers.
DR DNASU; 151056; -.
DR Ensembl; ENST00000327757.10; ENSP00000330442.5; ENSG00000163803.13. [Q6P1J6-1]
DR Ensembl; ENST00000422425.6; ENSP00000416440.2; ENSG00000163803.13. [Q6P1J6-3]
DR GeneID; 151056; -.
DR KEGG; hsa:151056; -.
DR MANE-Select; ENST00000327757.10; ENSP00000330442.5; NM_153021.5; NP_694566.4.
DR UCSC; uc002rmb.3; human. [Q6P1J6-1]
DR CTD; 151056; -.
DR DisGeNET; 151056; -.
DR GeneCards; PLB1; -.
DR HGNC; HGNC:30041; PLB1.
DR HPA; ENSG00000163803; Tissue enriched (intestine).
DR MIM; 610179; gene.
DR neXtProt; NX_Q6P1J6; -.
DR OpenTargets; ENSG00000163803; -.
DR PharmGKB; PA134891309; -.
DR VEuPathDB; HostDB:ENSG00000163803; -.
DR eggNOG; KOG3670; Eukaryota.
DR GeneTree; ENSGT00530000063883; -.
DR HOGENOM; CLU_006677_0_0_1; -.
DR InParanoid; Q6P1J6; -.
DR OMA; VDFMNPS; -.
DR OrthoDB; 1232962at2759; -.
DR PhylomeDB; Q6P1J6; -.
DR TreeFam; TF314942; -.
DR PathwayCommons; Q6P1J6; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; Q6P1J6; -.
DR BioGRID-ORCS; 151056; 12 hits in 1065 CRISPR screens.
DR ChiTaRS; PLB1; human.
DR GenomeRNAi; 151056; -.
DR Pharos; Q6P1J6; Tbio.
DR PRO; PR:Q6P1J6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6P1J6; protein.
DR Bgee; ENSG00000163803; Expressed in adrenal tissue and 101 other tissues.
DR ExpressionAtlas; Q6P1J6; baseline and differential.
DR Genevisible; Q6P1J6; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0046340; P:diacylglycerol catabolic process; IEA:Ensembl.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:Ensembl.
DR GO; GO:0046338; P:phosphatidylethanolamine catabolic process; IEA:Ensembl.
DR GO; GO:0034478; P:phosphatidylglycerol catabolic process; IEA:Ensembl.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:Ensembl.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
DR GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl.
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 Alternative splicing; Cell membrane; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Phospholipid metabolism; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1458
FT /note="Phospholipase B1, membrane-associated"
FT /id="PRO_0000324383"
FT TOPO_DOM 22..1417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1418..1438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1439..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..1402
FT /note="4"
FT /evidence="ECO:0000255"
FT REGION 39..1402
FT /note="4 X 308-326 AA approximate repeats"
FT /evidence="ECO:0000255"
FT REGION 1403..1445
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 240
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 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1055
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 1275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..1035
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032225"
FT VAR_SEQ 1..312
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032226"
FT VAR_SEQ 184
FT /note="Q -> QQAPSLSTVLLS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032227"
FT VAR_SEQ 523..544
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032228"
FT VAR_SEQ 750..760
FT /note="AGNGIGSKPDD -> VRTLGPQVVWG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032229"
FT VAR_SEQ 761..1458
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032230"
FT VAR_SEQ 774..800
FT /note="SAGGDGSLENVTTLPNILREFNRNLTG -> RESKPGFLSDSWVSKSNRKCT
FT RKAPNP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032231"
FT VAR_SEQ 801..1458
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032232"
FT VARIANT 212
FT /note="V -> L (in dbSNP:rs6753929)"
FT /id="VAR_039793"
FT VARIANT 708
FT /note="M -> V (in dbSNP:rs11681826)"
FT /id="VAR_039794"
FT VARIANT 821
FT /note="G -> R (in dbSNP:rs10201128)"
FT /id="VAR_039795"
FT VARIANT 879
FT /note="H -> D (in dbSNP:rs7601771)"
FT /id="VAR_039796"
FT VARIANT 987
FT /note="A -> V (in dbSNP:rs34289907)"
FT /id="VAR_061358"
FT VARIANT 1318
FT /note="A -> V (in dbSNP:rs2199619)"
FT /id="VAR_039797"
FT CONFLICT 426
FT /note="W -> Y (in Ref. 4; BAB70920)"
FT /evidence="ECO:0000305"
FT CONFLICT 1186
FT /note="V -> L (in Ref. 3; AAH42674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1458 AA; 163081 MW; 0B260E1489D8137B CRC64;
MGLRPGIFLL ELLLLLGQGT PQIHTSPRKS TLEGQLWPET LKNSPFPCNP NKLGVNMPSK
SVHSLKPSDI KFVAAIGNLE IPPDPGTGDL EKQDWTERPQ QVCMGVMTVL SDIIRYFSPS
VPMPVCHTGK RVIPHDGAED LWIQAQELVR NMKENLQLDF QFDWKLINVF FSNASQCYLC
PSAQQNGLAA GGVDELMGVL DYLQQEVPRA FVNLVDLSEV AEVSRQYHGT WLSPAPEPCN
CSEETTRLAK VVMQWSYQEA WNSLLASSRY SEQESFTVVF QPFFYETTPS LHSEDPRLQD
STTLAWHLWN RMMEPAGEKD EPLSVKHGRP MKCPSQESPY LFSYRNSNYL TRLQKPQDKL
EVREGAEIRC PDKDPSDTVP TSVHRLKPAD INVIGALGDS LTAGNGAGST PGNVLDVLTQ
YRGLSWSVGG DENIGTVTTL ANILREFNPS LKGFSVGTGK ETSPNAFLNQ AVAGGRAEDL
PVQARRLVDL MKNDTRIHFQ EDWKIITLFI GGNDLCDFCN DLVHYSPQNF TDNIGKALDI
LHAEVPRAFV NLVTVLEIVN LRELYQEKKV YCPRMILRSL CPCVLKFDDN STELATLIEF
NKKFQEKTHQ LIESGRYDTR EDFTVVVQPF FENVDMPKTS EGLPDNSFFA PDCFHFSSKS
HSRAASALWN NMLEPVGQKT TRHKFENKIN ITCPNQVQPF LRTYKNSMQG HGTWLPCRDR
APSALHPTSV HALRPADIQV VAALGDSLTA GNGIGSKPDD LPDVTTQYRG LSYSAGGDGS
LENVTTLPNI LREFNRNLTG YAVGTGDAND TNAFLNQAVP GAKAEDLMSQ VQTLMQKMKD
DHRVNFHEDW KVITVLIGGS DLCDYCTDSN LYSAANFVHH LRNALDVLHR EVPRVLVNLV
DFLNPTIMRQ VFLGNPDKCP VQQASVLCNC VLTLRENSQE LARLEAFSRA YRSSMRELVG
SGRYDTQEDF SVVLQPFFQN IQLPVLADGL PDTSFFAPDC IHPNQKFHSQ LARALWTNML
EPLGSKTETL DLRAEMPITC PTQNEPFLRT PRNSNYTYPI KPAIENWGSD FLCTEWKASN
SVPTSVHQLR PADIKVVAAL GDSLTTAVGA RPNNSSDLPT SWRGLSWSIG GDGNLETHTT
LPNILKKFNP YLLGFSTSTW EGTAGLNVAA EGARARDMPA QAWDLVERMK NSPDINLEKD
WKLVTLFIGV NDLCHYCENP EAHLATEYVQ HIQQALDILS EELPRAFVNV VEVMELASLY
QGQGGKCAML AAQNNCTCLR HSQSSLEKQE LKKVNWNLQH GISSFSYWHQ YTQREDFAVV
VQPFFQNTLT PLNERGDTDL TFFSEDCFHF SDRGHAEMAI ALWNNMLEPV GRKTTSNNFT
HSRAKLKCPS PESPYLYTLR NSRLLPDQAE EAPEVLYWAV PVAAGVGLVV GIIGTVVWRC
RRGGRREDPP MSLRTVAL
