ID E9PRT6_HUMAN Unreviewed; 467 AA. AC E9PRT6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 13-FEB-2019, entry version 59. 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=PNLIPRP1 {ECO:0000313|Ensembl:ENSP00000434159}; 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:ENSP00000434159, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000434159, 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:ENSP00000434159} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) 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 ProteinModelPortal; E9PRT6; -. DR PeptideAtlas; E9PRT6; -. DR PRIDE; E9PRT6; -. DR Ensembl; ENST00000534537; ENSP00000434159; ENSG00000187021. DR UCSC; uc057wel.1; human. DR EuPathDB; HostDB:ENSG00000187021.14; -. DR HGNC; HGNC:9156; PNLIPRP1. DR OpenTargets; ENSG00000187021; -. DR eggNOG; ENOG410IHRX; Eukaryota. DR eggNOG; ENOG410Y92X; LUCA. DR GeneTree; ENSGT00940000162375; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000187021; Expressed in 80 organ(s), highest expression level in body of pancreas. DR ExpressionAtlas; E9PRT6; 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|PeptideAtlas:E9PRT6}; 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 18 467 Triacylglycerol lipase. FT {ECO:0000256|RuleBase:RU362046}. FT /FTId=PRO_5005128615. FT DOMAIN 356 467 PLAT. {ECO:0000259|PROSITE:PS50095}. FT ACT_SITE 171 171 Nucleophile. FT {ECO:0000256|PIRSR:PIRSR000865-1}. FT ACT_SITE 194 194 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR000865-1}. FT ACT_SITE 281 281 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR000865-1}. FT METAL 205 205 Calcium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000865-2}. FT METAL 208 208 Calcium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000865-2}. FT METAL 210 210 Calcium. {ECO:0000256|PIRSR:PIRSR000865- FT 2}. FT METAL 213 213 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 255 279 {ECO:0000256|PIRSR:PIRSR000865-3}. FT DISULFID 303 314 {ECO:0000256|PIRSR:PIRSR000865-3}. FT DISULFID 317 322 {ECO:0000256|PIRSR:PIRSR000865-3}. FT DISULFID 451 467 {ECO:0000256|PIRSR:PIRSR000865-3}. SQ SEQUENCE 467 AA; 51845 MW; C1085905E985BBB1 CRC64; MLIFWTITLF LLGAAKGKEV CYEDLGCFSD TEPWGGTAIR PLKILPWSPE KIGTRFLLYT NENPNNFQIL LLSDPSTIEA SNFQMDRKTR FIIHGFIDKG DESWVTDMCK KLFEVEEVNC ICVDWKKGSQ ATYTQAANNV RVVGAQVAQM LDILLVKYSY PPSKVHLIGH SLGAHVAGEA GSKTPGLSRI TGLDPVEASF ESTPEEVRLD PSDADFVDVI HTDAAPLIPF LGFGTNQQMG HLDFFPNGGE SMPGCKKNAL SQIVDLDGIW AGTRDFVACN HLRSYKYYLE SILNPDGFAA YPCTSYKSFE SDKCFPCPDQ GCPQMGHYAD KFAGRTSEEQ QKFFLNTGEA SNFARWRYGV SITLSGRTAT GQIKVALFGN KGNTHQYSIF RGILKPGSTH SYEFDAKLDV GTIEKVKFLW NNNVINPTLP KVGATKITVQ KGEEKTVYNF CSEDTVREDT LLTLTPC //