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   27-MAR-2024, entry version 154.
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         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: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.
DR   AlphaFoldDB; Q6P1J6; -.
DR   BioGRID; 127341; 63.
DR   IntAct; Q6P1J6; 27.
DR   STRING; 9606.ENSP00000330442; -.
DR   GlyCosmos; Q6P1J6; 13 sites, No reported glycans.
DR   GlyGen; Q6P1J6; 13 sites.
DR   iPTMnet; Q6P1J6; -.
DR   PhosphoSitePlus; Q6P1J6; -.
DR   BioMuta; PLB1; -.
DR   EPD; Q6P1J6; -.
DR   MassIVE; Q6P1J6; -.
DR   PaxDb; 9606-ENSP00000330442; -.
DR   PeptideAtlas; 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; 153 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   AGR; HGNC:30041; -.
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; FCSDPVH; -.
DR   OrthoDB; 6003at2759; -.
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 1141 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 103 other cell types or tissues.
DR   ExpressionAtlas; Q6P1J6; baseline and differential.
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: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: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; 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.
DR   Genevisible; Q6P1J6; HS.
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
//