ID A0A087WX88_HUMAN Unreviewed; 468 AA. AC A0A087WX88; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 13-FEB-2019, entry version 34. DE RecName: Full=Triacylglycerol lipase {ECO:0000256|RuleBase:RU362046}; DE EC=3.1.1.3 {ECO:0000256|RuleBase:RU362046}; DE AltName: Full=Pancreatic lipase {ECO:0000256|RuleBase:RU362046}; GN Name=PNLIPRP2 {ECO:0000313|Ensembl:ENSP00000480815}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000480815, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000480815, ECO:0000313|Proteomes:UP000005640} 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., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R., Hubbard T., RA 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 [2] {ECO:0000313|Ensembl:ENSP00000480815} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid CC + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, CC ChEBI:CHEBI:28868; EC=3.1.1.3; CC Evidence={ECO:0000256|RuleBase:RU362046}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362046, CC ECO:0000256|SAAS:SAAS00553472}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase CC family. {ECO:0000256|RuleBase:RU004262, CC ECO:0000256|SAAS:SAAS00591292}. 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; AC016825; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; FO082044; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A087WX88; -. DR PeptideAtlas; A0A087WX88; -. DR Ensembl; ENST00000611850; ENSP00000480815; ENSG00000266200. DR UCSC; uc057wer.1; human. DR EuPathDB; HostDB:ENSG00000266200.6; -. DR HGNC; HGNC:9157; PNLIPRP2. DR OpenTargets; ENSG00000266200; -. DR GeneTree; ENSGT00940000155139; -. DR ChiTaRS; PNLIPRP2; human. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000266200; Expressed in 90 organ(s), highest expression level in body of pancreas. DR ExpressionAtlas; A0A087WX88; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR CDD; cd00707; Pancreat_lipase_like; 1. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR013818; Lipase/vitellogenin. 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; PS50095; PLAT; 1. PE 1: Evidence at protein level; KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000865-3, KW ECO:0000256|RuleBase:RU362046, ECO:0000256|SAAS:SAAS00709807}; KW Lipid degradation {ECO:0000256|RuleBase:RU362046}; KW Lipid metabolism {ECO:0000256|RuleBase:RU362046}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2}; KW Proteomics identification {ECO:0000213|MaxQB:A0A087WX88, KW ECO:0000213|PeptideAtlas:A0A087WX88}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Secreted {ECO:0000256|RuleBase:RU362046, KW ECO:0000256|SAAS:SAAS00439306}; KW Signal {ECO:0000256|RuleBase:RU362046}. FT SIGNAL 1 17 {ECO:0000256|RuleBase:RU362046}. FT CHAIN 18 468 Triacylglycerol lipase. FT {ECO:0000256|RuleBase:RU362046}. FT /FTId=PRO_5005106657. FT DOMAIN 356 468 PLAT. {ECO:0000259|PROSITE:PS50095}. FT ACT_SITE 171 171 Nucleophile. FT {ECO:0000256|PIRSR:PIRSR000865-1}. FT ACT_SITE 195 195 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR000865-1}. FT ACT_SITE 282 282 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR000865-1}. FT METAL 206 206 Calcium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000865-2}. FT METAL 209 209 Calcium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000865-2}. FT METAL 211 211 Calcium. {ECO:0000256|PIRSR:PIRSR000865- FT 2}. FT METAL 214 214 Calcium. {ECO:0000256|PIRSR:PIRSR000865- FT 2}. FT DISULFID 21 27 {ECO:0000256|PIRSR:PIRSR000865-3}. FT DISULFID 109 120 {ECO:0000256|PIRSR:PIRSR000865-3}. FT DISULFID 256 280 {ECO:0000256|PIRSR:PIRSR000865-3}. FT DISULFID 304 315 {ECO:0000256|PIRSR:PIRSR000865-3}. FT DISULFID 318 323 {ECO:0000256|PIRSR:PIRSR000865-3}. FT DISULFID 452 468 {ECO:0000256|PIRSR:PIRSR000865-3}. SQ SEQUENCE 468 AA; 51774 MW; 34E6D120E962E4C6 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 SGNFTSRYKI SVTLSGKEKV NGYIRIALYG SNENSKQYEI FKGSLKPDAS HTCAIDVDFN VGKIQKVKFL WNKRGINLSE PKLGASQITV QSGEDGTEYN FCSSDTVEEN VLQSLYPC //