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Pancreatic lipase-related protein 2 (PL-RP2) (EC 3.1.1.26) (EC 3.1.1.3) (Galactolipase)

 LIPR2_HUMAN             Reviewed;         469 AA.
P54317; A0A075B781; A8K627; Q6IB55;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 2.
20-JUN-2018, entry version 146.
RecName: Full=Pancreatic lipase-related protein 2 {ECO:0000312|HGNC:HGNC:9157};
Short=PL-RP2 {ECO:0000305|PubMed:1379598};
EC=3.1.1.26;
EC=3.1.1.3;
AltName: Full=Galactolipase;
Flags: Precursor;
Name=PNLIPRP2 {ECO:0000312|HGNC:HGNC:9157};
Synonyms=PLRP2 {ECO:0000303|PubMed:1379598};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-361.
TISSUE=Pancreas;
PubMed=1379598;
Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.;
"Two novel human pancreatic lipase related proteins, hPLRP1 and
hPLRP2. Differences in colipase dependence and in lipase activity.";
J. Biol. Chem. 267:16509-16516(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-361.
TISSUE=Pancreas;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-361.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-361.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-361.
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19824014; DOI=10.1002/mnfr.200800563;
Berton A., Sebban-Kreuzer C., Rouvellac S., Lopez C., Crenon I.;
"Individual and combined action of pancreatic lipase and pancreatic
lipase-related proteins 1 and 2 on native versus homogenized milk fat
globules.";
Mol. Nutr. Food Res. 53:1592-1602(2009).
[8]
FUNCTION.
PubMed=20083229; DOI=10.1016/j.bbalip.2010.01.003;
Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P.,
De Caro A., Carriere F.;
"Lipolysis of natural long chain and synthetic medium chain
galactolipids by pancreatic lipase-related protein 2.";
Biochim. Biophys. Acta 1801:508-516(2010).
[9]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH
CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353,
MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
SPECTROMETRY, ACTIVE SITE, AND DISULFIDE BONDS.
PubMed=18702514; DOI=10.1021/bi8005576;
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A.,
Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.;
"Structure of human pancreatic lipase-related protein 2 with the lid
in an open conformation.";
Biochemistry 47:9553-9564(2008).
-!- FUNCTION: Lipase with broad substrate specificity. Can hydrolyze
both phospholipids and galactolipids. Acts preferentially on
monoglycerides, phospholipids and galactolipids. Contributes to
milk fat hydrolysis. {ECO:0000269|PubMed:18702514,
ECO:0000269|PubMed:19824014, ECO:0000269|PubMed:20083229}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate. {ECO:0000269|PubMed:18702514}.
-!- CATALYTIC ACTIVITY: 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2
H(2)O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates.
{ECO:0000269|PubMed:18702514}.
-!- ENZYME REGULATION: CLPS stimulates triacylglycerol lipase
activity. Triacylglycerol lipase activity is not inhibited by
increasing bile salt concentration.
{ECO:0000250|UniProtKB:P17892}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18702514,
ECO:0000269|PubMed:19824014}.
-!- TISSUE SPECIFICITY: Pancreas.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
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EMBL; M93284; AAA59533.1; -; mRNA.
EMBL; AK291492; BAF84181.1; -; mRNA.
EMBL; CR456949; CAG33230.1; -; mRNA.
EMBL; AC016825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; FO082044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49448.1; -; Genomic_DNA.
EMBL; BC005989; AAH05989.1; -; mRNA.
PIR; B43357; B43357.
RefSeq; NP_005387.2; NM_005396.4.
UniGene; Hs.423598; -.
PDB; 2OXE; X-ray; 2.80 A; A/B=18-469.
PDB; 2PVS; X-ray; 3.00 A; A/B=18-469.
PDBsum; 2OXE; -.
PDBsum; 2PVS; -.
ProteinModelPortal; P54317; -.
SMR; P54317; -.
BioGrid; 111409; 9.
ChEMBL; CHEMBL2169728; -.
SwissLipids; SLP:000001434; -.
ESTHER; human-PNLIPRP2; Pancreatic_lipase.
iPTMnet; P54317; -.
PhosphoSitePlus; P54317; -.
BioMuta; PNLIPRP2; -.
DMDM; 1708840; -.
PeptideAtlas; P54317; -.
PRIDE; P54317; -.
ProteomicsDB; 56684; -.
DNASU; 5408; -.
Ensembl; ENST00000591655; ENSP00000468117; ENSG00000266200.
GeneID; 5408; -.
KEGG; hsa:5408; -.
CTD; 5408; -.
DisGeNET; 5408; -.
EuPathDB; HostDB:ENSG00000266200.6; -.
GeneCards; PNLIPRP2; -.
H-InvDB; HIX0009237; -.
HGNC; HGNC:9157; PNLIPRP2.
MIM; 604423; gene.
neXtProt; NX_P54317; -.
OpenTargets; ENSG00000266200; -.
PharmGKB; PA33480; -.
GeneTree; ENSGT00760000119069; -.
HOVERGEN; HBG003243; -.
InParanoid; P54317; -.
KO; K14075; -.
PhylomeDB; P54317; -.
BRENDA; 3.1.1.26; 2681.
Reactome; R-HSA-192456; Digestion of dietary lipid.
ChiTaRS; PNLIPRP2; human.
EvolutionaryTrace; P54317; -.
GenomeRNAi; 5408; -.
PRO; PR:P54317; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000266200; -.
CleanEx; HS_PNLIPRP2; -.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0102549; F:1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity; IEA:UniProtKB-EC.
GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0047714; F:galactolipase activity; IDA:UniProtKB.
GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
GO; GO:0019376; P:galactolipid catabolic process; IDA:UniProtKB.
GO; GO:0044241; P:lipid digestion; TAS:Reactome.
GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
GO; GO:0006641; P:triglyceride metabolic process; TAS:ProtInc.
CDD; cd00707; Pancreat_lipase_like; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013818; Lipase/vitellogenin.
InterPro; IPR016272; Lipase_LIPH.
InterPro; IPR033906; Lipase_N.
InterPro; IPR002331; Lipase_panc.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
InterPro; IPR000734; TAG_lipase.
PANTHER; PTHR11610; PTHR11610; 1.
Pfam; PF00151; Lipase; 1.
Pfam; PF01477; PLAT; 1.
PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
PRINTS; PR00823; PANCLIPASE.
PRINTS; PR00821; TAGLIPASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF49723; SSF49723; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00120; LIPASE_SER; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
Metal-binding; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 469 Pancreatic lipase-related protein 2.
/FTId=PRO_0000017793.
DOMAIN 357 469 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
ACT_SITE 171 171 Nucleophile.
{ECO:0000269|PubMed:18702514}.
ACT_SITE 195 195 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10037,
ECO:0000269|PubMed:18702514}.
ACT_SITE 282 282 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10037,
ECO:0000269|PubMed:18702514}.
METAL 206 206 Calcium; via carbonyl oxygen.
METAL 209 209 Calcium; via carbonyl oxygen.
METAL 211 211 Calcium.
METAL 214 214 Calcium.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18702514}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 21 27 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:18702514}.
DISULFID 109 120 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:18702514}.
DISULFID 256 280 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:18702514}.
DISULFID 304 315 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:18702514}.
DISULFID 318 323 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:18702514}.
DISULFID 453 469 {ECO:0000255|PROSITE-ProRule:PRU00152,
ECO:0000269|PubMed:18702514}.
VARIANT 361 361 I -> V (in dbSNP:rs4751996).
{ECO:0000269|PubMed:1379598}.
/FTId=VAR_080185.
MUTAGEN 353 353 N->Q: Loss of N-glycosylation.
{ECO:0000269|PubMed:18702514}.
CONFLICT 239 239 K -> R (in Ref. 2; BAF84181).
{ECO:0000305}.
CONFLICT 352 352 G -> V (in Ref. 2; BAF84181).
{ECO:0000305}.
STRAND 19 21 {ECO:0000244|PDB:2OXE}.
HELIX 23 25 {ECO:0000244|PDB:2OXE}.
STRAND 27 29 {ECO:0000244|PDB:2OXE}.
TURN 32 34 {ECO:0000244|PDB:2OXE}.
STRAND 35 37 {ECO:0000244|PDB:2OXE}.
HELIX 49 52 {ECO:0000244|PDB:2OXE}.
STRAND 55 59 {ECO:0000244|PDB:2OXE}.
STRAND 61 66 {ECO:0000244|PDB:2OXE}.
STRAND 68 70 {ECO:0000244|PDB:2OXE}.
STRAND 72 74 {ECO:0000244|PDB:2OXE}.
HELIX 76 80 {ECO:0000244|PDB:2OXE}.
STRAND 87 93 {ECO:0000244|PDB:2OXE}.
HELIX 104 112 {ECO:0000244|PDB:2OXE}.
TURN 113 115 {ECO:0000244|PDB:2OXE}.
STRAND 118 124 {ECO:0000244|PDB:2OXE}.
HELIX 126 129 {ECO:0000244|PDB:2OXE}.
HELIX 133 158 {ECO:0000244|PDB:2OXE}.
HELIX 162 164 {ECO:0000244|PDB:2OXE}.
STRAND 165 170 {ECO:0000244|PDB:2OXE}.
HELIX 173 183 {ECO:0000244|PDB:2OXE}.
TURN 184 186 {ECO:0000244|PDB:2OXE}.
STRAND 188 195 {ECO:0000244|PDB:2OXE}.
TURN 199 203 {ECO:0000244|PDB:2OXE}.
TURN 206 208 {ECO:0000244|PDB:2OXE}.
HELIX 212 214 {ECO:0000244|PDB:2OXE}.
STRAND 215 221 {ECO:0000244|PDB:2OXE}.
STRAND 223 226 {ECO:0000244|PDB:2OXE}.
STRAND 228 230 {ECO:0000244|PDB:2OXE}.
STRAND 234 236 {ECO:0000244|PDB:2OXE}.
STRAND 241 247 {ECO:0000244|PDB:2OXE}.
TURN 248 251 {ECO:0000244|PDB:2OXE}.
HELIX 276 278 {ECO:0000244|PDB:2OXE}.
HELIX 280 294 {ECO:0000244|PDB:2OXE}.
STRAND 298 300 {ECO:0000244|PDB:2OXE}.
HELIX 307 311 {ECO:0000244|PDB:2OXE}.
TURN 312 315 {ECO:0000244|PDB:2PVS}.
STRAND 325 327 {ECO:0000244|PDB:2PVS}.
HELIX 330 332 {ECO:0000244|PDB:2OXE}.
TURN 334 337 {ECO:0000244|PDB:2OXE}.
STRAND 338 346 {ECO:0000244|PDB:2OXE}.
STRAND 357 369 {ECO:0000244|PDB:2OXE}.
STRAND 371 380 {ECO:0000244|PDB:2OXE}.
STRAND 385 396 {ECO:0000244|PDB:2OXE}.
STRAND 401 410 {ECO:0000244|PDB:2OXE}.
STRAND 417 423 {ECO:0000244|PDB:2OXE}.
STRAND 434 443 {ECO:0000244|PDB:2OXE}.
TURN 444 446 {ECO:0000244|PDB:2OXE}.
STRAND 449 453 {ECO:0000244|PDB:2OXE}.
STRAND 464 468 {ECO:0000244|PDB:2OXE}.
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


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