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 24-JAN-2024, entry version 177. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P54317; 2 sites, No reported glycans. DR GlyGen; P54317; 2 sites. DR iPTMnet; P54317; -. DR PhosphoSitePlus; P54317; -. DR BioMuta; PNLIPRP2; -. DR DMDM; 1708840; -. DR MassIVE; P54317; -. DR PeptideAtlas; P54317; -. DR ProteomicsDB; 56684; -. DR Antibodypedia; 73327; 118 antibodies from 16 providers. DR DNASU; 5408; -. DR GeneID; 5408; -. DR KEGG; hsa:5408; -. DR AGR; HGNC:9157; -. DR CTD; 5408; -. DR DisGeNET; 5408; -. DR GeneCards; PNLIPRP2; -. DR HGNC; HGNC:9157; PNLIPRP2. DR MIM; 604423; gene. DR neXtProt; NX_P54317; -. DR PharmGKB; PA33480; -. DR VEuPathDB; HostDB:ENSG00000266200; -. DR InParanoid; P54317; -. DR OMA; CFSNEKP; -. DR OrthoDB; 3428256at2759; -. 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 311 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 95 other cell types or tissues. DR ExpressionAtlas; P54317; baseline and differential. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB. DR GO; GO:0042589; C:zymogen granule membrane; IEA:UniProtKB-SubCell. 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: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: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 CDD; cd01759; PLAT_PL; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 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; LIPASE; 1. DR PANTHER; PTHR11610:SF165; PANCREATIC LIPASE-RELATED PROTEIN 2; 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; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 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 (common variant; more frequent in FT populations that rely primarily on cereals as the main FT dietary component; expected to result in near complete FT absence of the protein and loss of function; if expressed FT is weakly secreted, mostly intracellularly retained and FT degraded; 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 //