LIPR2_HUMAN
ID LIPR2_HUMAN Reviewed; 469 AA.
AC P54317; A0A075B781; A8K627; Q6IB55;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Pancreatic lipase-related protein 2 {ECO:0000312|HGNC:HGNC:9157};
DE Short=PL-RP2 {ECO:0000305|PubMed:1379598};
DE AltName: Full=Cytotoxic T lymphocyte lipase {ECO:0000250|UniProtKB:P17892};
DE AltName: Full=Galactolipase;
DE EC=3.1.1.26 {ECO:0000269|PubMed:15287741, ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:18702514, ECO:0000269|PubMed:20083229};
DE AltName: Full=Triacylglycerol lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:15287741, ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:18702514, ECO:0000269|PubMed:19451396, ECO:0000269|PubMed:21652702, ECO:0000269|PubMed:21865348, ECO:0000269|PubMed:26494624};
DE Flags: Precursor;
GN Name=PNLIPRP2 {ECO:0000312|HGNC:HGNC:9157};
GN Synonyms=PLRP2 {ECO:0000303|PubMed:1379598};
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 [MRNA], AND VARIANT VAL-361.
RC TISSUE=Pancreas;
RX PubMed=1379598; DOI=10.1016/s0021-9258(18)42032-7;
RA Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.;
RT "Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2.
RT Differences in colipase dependence and in lipase activity.";
RL J. Biol. Chem. 267:16509-16516(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-361.
RC TISSUE=Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-361.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-361.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-361.
RC TISSUE=Pancreas;
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 [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10674344; DOI=10.1203/00006450-200002000-00006;
RA Yang Y., Sanchez D., Figarella C., Lowe M.E.;
RT "Discoordinate expression of pancreatic lipase and two related proteins in
RT the human fetal pancreas.";
RL Pediatr. Res. 47:184-188(2000).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=15287741; DOI=10.1021/bi049818d;
RA Sias B., Ferrato F., Grandval P., Lafont D., Boullanger P., De Caro A.,
RA Leboeuf B., Verger R., Carriere F.;
RT "Human pancreatic lipase-related protein 2 is a galactolipase.";
RL Biochemistry 43:10138-10148(2004).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=17401110; DOI=10.1194/jlr.m600486-jlr200;
RA Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R.,
RA Carriere F., De Caro A.;
RT "Further biochemical characterization of human pancreatic lipase-related
RT protein 2 expressed in yeast cells.";
RL J. Lipid Res. 48:1539-1549(2007).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19451396; DOI=10.1189/jlb.1208766;
RA Alves B.N., Leong J., Tamang D.L., Elliott V., Edelnant J., Redelman D.,
RA Singer C.A., Kuhn A.R., Miller R., Lowe M.E., Hudig D.;
RT "Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic
RT T lymphocytes (CTLs) and reevaluation of the negative effects of its gene
RT ablation on cytotoxicity.";
RL J. Leukoc. Biol. 86:701-712(2009).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19824014; DOI=10.1002/mnfr.200800563;
RA Berton A., Sebban-Kreuzer C., Rouvellac S., Lopez C., Crenon I.;
RT "Individual and combined action of pancreatic lipase and pancreatic lipase-
RT related proteins 1 and 2 on native versus homogenized milk fat globules.";
RL Mol. Nutr. Food Res. 53:1592-1602(2009).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RX PubMed=20083229; DOI=10.1016/j.bbalip.2010.01.003;
RA Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P.,
RA De Caro A., Carriere F.;
RT "Lipolysis of natural long chain and synthetic medium chain galactolipids
RT by pancreatic lipase-related protein 2.";
RL Biochim. Biophys. Acta 1801:508-516(2010).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND VARIANT
RP 357-TRP--CYS-469 DEL.
RX PubMed=21652702; DOI=10.1074/jbc.m111.249813;
RA Xiao X., Mukherjee A., Ross L.E., Lowe M.E.;
RT "Pancreatic lipase-related protein-2 (PLRP2) can contribute to dietary fat
RT digestion in human newborns.";
RL J. Biol. Chem. 286:26353-26363(2011).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=21865348; DOI=10.1194/jlr.m015685;
RA Andersson E.L., Hernell O., Blaeckberg L., Faelt H., Lindquist S.;
RT "BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined
RT using the Caco-2 cell line.";
RL J. Lipid Res. 52:1949-1956(2011).
RN [15]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=23732775; DOI=10.1038/pr.2013.90;
RA Johnson K., Ross L., Miller R., Xiao X., Lowe M.E.;
RT "Pancreatic lipase-related protein 2 digests fats in human milk and formula
RT in concert with gastric lipase and carboxyl ester lipase.";
RL Pediatr. Res. 74:127-132(2013).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND REGION.
RX PubMed=26494624; DOI=10.1074/jbc.m115.683375;
RA Xiao X., Lowe M.E.;
RT "The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of
RT Pancreatic Lipase-related Protein 2 (PNLIPRP2).";
RL J. Biol. Chem. 290:28847-28856(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM
RP IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS
RP OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP ACTIVE SITE, AND DISULFIDE BONDS.
RX PubMed=18702514; DOI=10.1021/bi8005576;
RA Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A.,
RA Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.;
RT "Structure of human pancreatic lipase-related protein 2 with the lid in an
RT open conformation.";
RL Biochemistry 47:9553-9564(2008).
RN [18]
RP VARIANT 357-TRP--CYS-469 DEL.
RX PubMed=20445095; DOI=10.1073/pnas.0914625107;
RA Hancock A.M., Witonsky D.B., Ehler E., Alkorta-Aranburu G., Beall C.,
RA Gebremedhin A., Sukernik R., Utermann G., Pritchard J., Coop G.,
RA Di Rienzo A.;
RT "Colloquium paper: human adaptations to diet, subsistence, and ecoregion
RT are due to subtle shifts in allele frequency.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8924-8930(2010).
RN [19]
RP VARIANT 357-TRP--CYS-469 DEL.
RX PubMed=30408063; DOI=10.1371/journal.pone.0206869;
RA Nemeth B.C., Pesei Z.G., Hegyi E., Szuecs A., Szentesi A., Hegyi P.,
RA Lowe M.E., Sahin-Toth M.;
RT "The common truncation variant in pancreatic lipase related protein 2
RT (PNLIPRP2) is expressed poorly and does not alter risk for chronic
RT pancreatitis.";
RL PLoS ONE 13:e0206869-e0206869(2018).
CC -!- FUNCTION: Lipase that primarily hydrolyzes triglycerides and
CC galactosylglycerides (PubMed:15287741, PubMed:17401110,
CC PubMed:19451396, PubMed:21865348, PubMed:20083229, PubMed:26494624,
CC PubMed:18702514). In neonates, may play a major role in pancreatic
CC digestion of dietary fats such as milk fat globules enriched in long-
CC chain triglycerides (PubMed:23732775, PubMed:19824014,
CC PubMed:21652702). Hydrolyzes short-, medium- and long-chain fatty acyls
CC in triglycerides without apparent positional specificity
CC (PubMed:15287741, PubMed:17401110, PubMed:21865348, PubMed:21652702,
CC PubMed:18702514). Can completely deacylate triacylglycerols
CC (PubMed:21865348). When the liver matures and bile salt synthesis
CC increases, likely functions mainly as a galactolipase and
CC monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG)
CC and digalactosyldiacylglycerols (DGDG) present in a plant-based diet,
CC releasing long-chain polyunsaturated fatty acids (PubMed:15287741,
CC PubMed:17401110, PubMed:20083229, PubMed:26494624, PubMed:18702514).
CC Hydrolyzes medium- and long-chain fatty acyls in galactolipids
CC (PubMed:20083229, PubMed:18702514). May act together with LIPF to
CC hydrolyze partially digested triglycerides (PubMed:23732775).
CC Hydrolyzes long-chain monoglycerides with high efficiency
CC (PubMed:17401110, PubMed:21652702, PubMed:23732775). In cytotoxic T
CC cells, contributes to perforin-dependent cell lysis, but is unlikely to
CC mediate direct cytotoxicity (By similarity). Also has low phospholipase
CC activity (PubMed:17401110, PubMed:18702514). In neurons, required for
CC the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to
CC neurite tips through acyl chain remodeling of membrane phospholipids
CC (By similarity). The resulting OPPC-rich lipid membrane domain recruits
CC the t-SNARE protein STX4 by selectively interacting with the STX4
CC transmembrane domain and this promotes surface expression of the
CC dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion
CC of SLC6A3-containing transport vesicles with the plasma membrane (By
CC similarity). {ECO:0000250|UniProtKB:P17892,
CC ECO:0000250|UniProtKB:P54318, ECO:0000269|PubMed:15287741,
CC ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:18702514,
CC ECO:0000269|PubMed:19451396, ECO:0000269|PubMed:19824014,
CC ECO:0000269|PubMed:20083229, ECO:0000269|PubMed:21652702,
CC ECO:0000269|PubMed:21865348, ECO:0000269|PubMed:23732775,
CC ECO:0000269|PubMed:26494624}.
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:0000269|PubMed:15287741, ECO:0000269|PubMed:17401110,
CC ECO:0000269|PubMed:18702514, ECO:0000269|PubMed:19451396,
CC ECO:0000269|PubMed:21652702, ECO:0000269|PubMed:21865348,
CC ECO:0000269|PubMed:26494624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:15287741, ECO:0000305|PubMed:17401110,
CC ECO:0000305|PubMed:18702514, ECO:0000305|PubMed:19451396,
CC ECO:0000305|PubMed:21652702, ECO:0000305|PubMed:21865348,
CC ECO:0000305|PubMed:26494624};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-
CC beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+);
CC Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26;
CC Evidence={ECO:0000269|PubMed:15287741, ECO:0000269|PubMed:17401110,
CC ECO:0000269|PubMed:18702514, ECO:0000269|PubMed:20083229};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190;
CC Evidence={ECO:0000305|PubMed:15287741, ECO:0000305|PubMed:17401110,
CC ECO:0000305|PubMed:18702514, ECO:0000305|PubMed:20083229};
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:0000269|PubMed:18702514, ECO:0000269|PubMed:19451396,
CC ECO:0000269|PubMed:21652702, ECO:0000269|PubMed:21865348,
CC ECO:0000269|PubMed:26494624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:18702514, ECO:0000305|PubMed:19451396,
CC ECO:0000305|PubMed:21652702, ECO:0000305|PubMed:21865348,
CC ECO:0000305|PubMed:26494624};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-(9Z)-octadecenoylglycerol + H2O = (9Z)-octadecenoate + (9Z-
CC octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:47868,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75937, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000269|PubMed:21865348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869;
CC Evidence={ECO:0000305|PubMed:21865348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:39955, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75937; Evidence={ECO:0000269|PubMed:18702514,
CC ECO:0000269|PubMed:21865348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39956;
CC Evidence={ECO:0000305|PubMed:18702514, ECO:0000305|PubMed:21865348};
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:17401110,
CC ECO:0000269|PubMed:18702514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000305|PubMed:17401110, ECO:0000305|PubMed:18702514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tripropanoylglycerol + H2O = dipropanoylglycerol + H(+)
CC + propanoate; Xref=Rhea:RHEA:48024, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:88153,
CC ChEBI:CHEBI:88155; Evidence={ECO:0000269|PubMed:18702514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48025;
CC Evidence={ECO:0000305|PubMed:18702514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:15287741,
CC ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:18702514,
CC ECO:0000269|PubMed:21652702, ECO:0000269|PubMed:26494624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000305|PubMed:15287741, ECO:0000305|PubMed:17401110,
CC ECO:0000305|PubMed:18702514, ECO:0000305|PubMed:21652702,
CC ECO:0000305|PubMed:26494624};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC ChEBI:CHEBI:88066; Evidence={ECO:0000269|PubMed:15287741,
CC ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:18702514,
CC ECO:0000269|PubMed:21652702, ECO:0000269|PubMed:26494624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000305|PubMed:15287741, ECO:0000305|PubMed:17401110,
CC ECO:0000305|PubMed:18702514, ECO:0000305|PubMed:21652702,
CC ECO:0000305|PubMed:26494624};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoylglycerol + H2O = decanoate + decanoylglycerol +
CC H(+); Xref=Rhea:RHEA:48596, ChEBI:CHEBI:11152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:90605;
CC Evidence={ECO:0000269|PubMed:15287741};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48597;
CC Evidence={ECO:0000305|PubMed:15287741};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + long chain 1,2-diacyl-3-O-beta-D-galactosyl-sn-glycerol
CC = a fatty acid + H(+) + long chain acyl-3-O-beta-D-galactosyl-sn-
CC glycerol; Xref=Rhea:RHEA:48700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90477, ChEBI:CHEBI:90770;
CC Evidence={ECO:0000305|PubMed:18702514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48701;
CC Evidence={ECO:0000305|PubMed:18702514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-3-O-beta-D-galactosyl-sn-glycerol + H2O = H(+)
CC + octanoate + octanoyl-3-(beta-D-galactosyl)-sn-glycerol;
CC Xref=Rhea:RHEA:48696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:90453, ChEBI:CHEBI:90769;
CC Evidence={ECO:0000269|PubMed:20083229};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48697;
CC Evidence={ECO:0000305|PubMed:20083229};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didodecanoyl-3-beta-D-galactosyl-sn-glycerol + H2O =
CC dodecanoate + dodecanoyl-3-beta-D-galactosyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:48540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:90340, ChEBI:CHEBI:90515;
CC Evidence={ECO:0000269|PubMed:15287741, ECO:0000269|PubMed:17401110,
CC ECO:0000269|PubMed:18702514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48541;
CC Evidence={ECO:0000305|PubMed:15287741, ECO:0000305|PubMed:17401110,
CC ECO:0000305|PubMed:18702514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-beta-D-galactosyl-2,3-didodecanoyl-sn-glycerol + H2O = 1-
CC beta-D-galactosyl-dodecanoyl-sn-glycerol + dodecanoate + H(+);
CC Xref=Rhea:RHEA:48536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:90342, ChEBI:CHEBI:90514;
CC Evidence={ECO:0000269|PubMed:17401110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48537;
CC Evidence={ECO:0000305|PubMed:17401110};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-
CC sn-glycerol + H2O = a fatty acid + acyl-3-O-[alpha-D-galactosyl-
CC (1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48372,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28396,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90310;
CC Evidence={ECO:0000269|PubMed:26494624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48373;
CC Evidence={ECO:0000305|PubMed:26494624};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + long chain 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-
CC beta-D-galactosyl]-sn-glycerol = a fatty acid + H(+) + long chain
CC acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol;
CC Xref=Rhea:RHEA:48708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90463, ChEBI:CHEBI:90774;
CC Evidence={ECO:0000269|PubMed:20083229};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48709;
CC Evidence={ECO:0000305|PubMed:20083229};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-
CC galactosyl]-sn-glycerol + H2O = H(+) + octanoate + octanoyl-3-O-
CC [alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol;
CC Xref=Rhea:RHEA:48692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:90457, ChEBI:CHEBI:90768;
CC Evidence={ECO:0000269|PubMed:20083229};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48693;
CC Evidence={ECO:0000305|PubMed:20083229};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didodecanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-
CC galactosyl]-sn-glycerol + H2O = dodecanoate + dodecanoyl-3-O-[alpha-
CC D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:48516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:90337, ChEBI:CHEBI:90359;
CC Evidence={ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:18702514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48517;
CC Evidence={ECO:0000305|PubMed:17401110, ECO:0000305|PubMed:18702514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a fatty acid
CC + a monoacyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:44664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:84465;
CC Evidence={ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:18702514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665;
CC Evidence={ECO:0000305|PubMed:17401110, ECO:0000305|PubMed:18702514};
CC -!- ACTIVITY REGULATION: Regulated by CLPS and bile salts levels ranging 1-
CC 5 mM in neonates and 2-30 mM in healthy adults. CLPS stimulates milk
CC fat digestion in the presence of 4 mM bile salts (PubMed:23732775).
CC Triacylglycerol lipase activity toward short- and medium-chain
CC triglycerides is inhibited by increasing concentrations of bile salts
CC and weakly reactivated by CLPS (PubMed:15287741, PubMed:17401110,
CC PubMed:21652702, PubMed:26494624). Optimal triacylglycerol lipase
CC activity is reached at bile salts concentrations ranging from 0.1 to
CC 0.5 mM and then decreases at concentrations higher than 1 mM
CC (PubMed:21652702, PubMed:15287741, PubMed:17401110). Lipase activity
CC toward long-chain glycerolipids is stimulated by CLPS in the presence
CC of 4 mM bile salts (PubMed:21652702). Galactolipase activity is
CC inhibited at high concentrations of bile salts (PubMed:20083229).
CC Triacylglycerol lipase activity is inhibited by anti-obesity drug
CC tetrahydrolipstatin (PubMed:17401110). {ECO:0000269|PubMed:15287741,
CC ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:20083229,
CC ECO:0000269|PubMed:21652702, ECO:0000269|PubMed:23732775,
CC ECO:0000269|PubMed:26494624}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.8 for triacylglycerol lipase activity, 8.5 for
CC phospholipase activity and 8 for galactolipase activity. The enzyme
CC activities decrease in the pH 5-7 range corresponding to the
CC physiological conditions occurring in the small intestine.
CC {ECO:0000269|PubMed:17401110};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC {ECO:0000269|PubMed:21865348}.
CC -!- PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:20083229}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18702514,
CC ECO:0000269|PubMed:19824014}. Zymogen granule membrane
CC {ECO:0000250|UniProtKB:P54318}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite tips in
CC neuronal cells. {ECO:0000250|UniProtKB:P54318}.
CC -!- TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:10674344}.
CC -!- DEVELOPMENTAL STAGE: Expressed by 16 weeks in fetal pancreas.
CC {ECO:0000269|PubMed:10674344}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; M93284; AAA59533.1; -; mRNA.
DR EMBL; AK291492; BAF84181.1; -; mRNA.
DR EMBL; CR456949; CAG33230.1; -; mRNA.
DR EMBL; AC016825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO082044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49448.1; -; Genomic_DNA.
DR EMBL; BC005989; AAH05989.1; -; mRNA.
DR PIR; B43357; B43357.
DR RefSeq; NP_005387.2; NM_005396.4.
DR PDB; 2OXE; X-ray; 2.80 A; A/B=18-469.
DR PDB; 2PVS; X-ray; 3.00 A; A/B=18-469.
DR PDBsum; 2OXE; -.
DR PDBsum; 2PVS; -.
DR AlphaFoldDB; P54317; -.
DR SMR; P54317; -.
DR BioGRID; 111409; 14.
DR IntAct; P54317; 1.
DR ChEMBL; CHEMBL2169728; -.
DR DrugBank; DB02613; Capric dimethyl amine oxide.
DR SwissLipids; SLP:000001434; -.
DR ESTHER; human-PNLIPRP2; Pancreatic_lipase.
DR GlyGen; P54317; 2 sites.
DR iPTMnet; P54317; -.
DR PhosphoSitePlus; P54317; -.
DR BioMuta; PNLIPRP2; -.
DR DMDM; 1708840; -.
DR MassIVE; P54317; -.
DR PeptideAtlas; P54317; -.
DR PRIDE; P54317; -.
DR ProteomicsDB; 56684; -.
DR Antibodypedia; 73327; 77 antibodies from 14 providers.
DR DNASU; 5408; -.
DR Ensembl; ENST00000591655.3; ENSP00000468117.2; ENSG00000266200.7.
DR GeneID; 5408; -.
DR KEGG; hsa:5408; -.
DR CTD; 5408; -.
DR DisGeNET; 5408; -.
DR GeneCards; PNLIPRP2; -.
DR HGNC; HGNC:9157; PNLIPRP2.
DR MIM; 604423; gene.
DR neXtProt; NX_P54317; -.
DR OpenTargets; ENSG00000266200; -.
DR PharmGKB; PA33480; -.
DR VEuPathDB; HostDB:ENSG00000266200; -.
DR GeneTree; ENSGT00940000155139; -.
DR InParanoid; P54317; -.
DR OMA; ELGCFND; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; P54317; -.
DR BRENDA; 3.1.1.26; 2681.
DR PathwayCommons; P54317; -.
DR Reactome; R-HSA-192456; Digestion of dietary lipid.
DR SignaLink; P54317; -.
DR UniPathway; UPA00256; -.
DR BioGRID-ORCS; 5408; 8 hits in 257 CRISPR screens.
DR ChiTaRS; PNLIPRP2; human.
DR EvolutionaryTrace; P54317; -.
DR GenomeRNAi; 5408; -.
DR Pharos; P54317; Tbio.
DR PRO; PR:P54317; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P54317; protein.
DR Bgee; ENSG00000266200; Expressed in body of pancreas and 94 other tissues.
DR ExpressionAtlas; P54317; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0102549; F:1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0047714; F:galactolipase activity; IDA:UniProtKB.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0019376; P:galactolipid catabolic process; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0044241; P:lipid digestion; TAS:Reactome.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB.
DR GO; GO:0006641; P:triglyceride metabolic process; TAS:ProtInc.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR002331; Lipase_panc.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00823; PANCLIPASE.
DR PRINTS; PR00821; TAGLIPASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell projection; Cytoplasmic vesicle;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..469
FT /note="Pancreatic lipase-related protein 2"
FT /id="PRO_0000017793"
FT DOMAIN 357..469
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 93..105
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000269|PubMed:26494624"
FT REGION 257..279
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000269|PubMed:26494624"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:18702514"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037,
FT ECO:0000269|PubMed:18702514"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037,
FT ECO:0000269|PubMed:18702514"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18702514,
FT ECO:0007744|PDB:2OXE, ECO:0007744|PDB:2PVS"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18702514,
FT ECO:0007744|PDB:2OXE, ECO:0007744|PDB:2PVS"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18702514,
FT ECO:0007744|PDB:2OXE, ECO:0007744|PDB:2PVS"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18702514,
FT ECO:0007744|PDB:2OXE, ECO:0007744|PDB:2PVS"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18702514,
FT ECO:0007744|PDB:2OXE"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:18702514"
FT DISULFID 109..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:18702514"
FT DISULFID 256..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:18702514"
FT DISULFID 304..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:18702514"
FT DISULFID 318..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:18702514"
FT DISULFID 453..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:18702514"
FT VARIANT 357..469
FT /note="Missing (associated with adaptation to cereal-based
FT diet and found in different populations with high allele
FT frequencies; expected to result in near complete absence of
FT the protein and loss of function; if expressed is weakly
FT secreted, mostly intracellularly retained and degraded;
FT dbSNP:rs4751995)"
FT /evidence="ECO:0000269|PubMed:20445095,
FT ECO:0000269|PubMed:21652702, ECO:0000269|PubMed:30408063"
FT /id="VAR_083661"
FT VARIANT 361
FT /note="I -> V (in dbSNP:rs4751996)"
FT /evidence="ECO:0000269|PubMed:1379598"
FT /id="VAR_080185"
FT MUTAGEN 353
FT /note="N->Q: Loss of N-glycosylation."
FT /evidence="ECO:0000269|PubMed:18702514"
FT CONFLICT 239
FT /note="K -> R (in Ref. 2; BAF84181)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="G -> V (in Ref. 2; BAF84181)"
FT /evidence="ECO:0000305"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2OXE"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:2OXE"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 133..158
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:2OXE"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:2OXE"
FT TURN 199..203
FT /evidence="ECO:0007829|PDB:2OXE"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:2OXE"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:2OXE"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:2OXE"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:2PVS"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:2PVS"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2OXE"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 357..369
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 371..380
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 385..396
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 401..410
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 434..443
FT /evidence="ECO:0007829|PDB:2OXE"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:2OXE"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:2OXE"
SQ SEQUENCE 469 AA; 51961 MW; 3D57FC5893A52D0D CRC64;
MLPPWTLGLL LLATVRGKEV CYGQLGCFSD EKPWAGTLQR PVKLLPWSPE DIDTRFLLYT
NENPNNFQLI TGTEPDTIEA SNFQLDRKTR FIIHGFLDKA EDSWPSDMCK KMFEVEKVNC
ICVDWRHGSR AMYTQAVQNI RVVGAETAFL IQALSTQLGY SLEDVHVIGH SLGAHTAAEA
GRRLGGRVGR ITGLDPAGPC FQDEPEEVRL DPSDAVFVDV IHTDSSPIVP SLGFGMSQKV
GHLDFFPNGG KEMPGCKKNV LSTITDIDGI WEGIGGFVSC NHLRSFEYYS SSVLNPDGFL
GYPCASYDEF QESKCFPCPA EGCPKMGHYA DQFKGKTSAV EQTFFLNTGE SGNFTSWRYK
ISVTLSGKEK VNGYIRIALY GSNENSKQYE IFKGSLKPDA SHTCAIDVDF NVGKIQKVKF
LWNKRGINLS EPKLGASQIT VQSGEDGTEY NFCSSDTVEE NVLQSLYPC
