ID M3VWT0_FELCA Unreviewed; 469 AA. AC M3VWT0; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 28-FEB-2018, entry version 42. 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:ENSFCAP00000001407}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000001407, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000001407, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001407, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000001407} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001407}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000001407} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001407}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a CC carboxylate. {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:RU362046, CC ECO:0000256|SAAS:SAAS00591292}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSFCAP00000001407}. 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; AANG03004277; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003994490.1; XM_003994441.3. DR STRING; 9685.ENSFCAP00000001407; -. DR Ensembl; ENSFCAT00000001516; ENSFCAP00000001407; ENSFCAG00000001516. DR GeneID; 101083714; -. DR KEGG; fca:101083714; -. DR eggNOG; ENOG410IHRX; Eukaryota. DR eggNOG; ENOG410Y92X; LUCA. DR GeneTree; ENSGT00760000119069; -. DR InParanoid; M3VWT0; -. DR KO; K14075; -. DR OMA; PFKLFPW; -. DR OrthoDB; EOG091G0DJ5; -. DR Proteomes; UP000011712; Chromosome D2. DR Bgee; ENSFCAG00000001516; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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; 2.60.60.20; -; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; 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 Reference proteome {ECO:0000313|Proteomes:UP000011712}; 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 18 469 Triacylglycerol lipase. FT {ECO:0000256|RuleBase:RU362046}. FT /FTId=PRO_5005140382. FT DOMAIN 357 469 PLAT. {ECO:0000259|PROSITE:PS50095}. FT ACT_SITE 171 171 Nucleophile. {ECO:0000256|PIRSR: FT PIRSR000865-1}. FT ACT_SITE 195 195 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR000865-1}. FT ACT_SITE 282 282 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR000865-1}. 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 453 469 {ECO:0000256|PIRSR:PIRSR000865-3}. SQ SEQUENCE 469 AA; 52330 MW; 5BB59993AB3D3230 CRC64; MLPSWTIGLL LLATVRGKEI CYGHLGCFSD GKPWTGILQR PLKLFPWAPK DIDTRFLLYT NENPNNFQLI TATDLETVEA SNFQLERKTR FIIHGFIDKG EESWLLDMCK KMFQVEKVNC ICVDWRRGAK TQYTQAVHNI RVVGAEIAFL IQRLSTELGY GPEDVHLIGH SLGAHAAAEA GRRLGGRVGR ITGLDPAEPC FQGTPEEVRL DASDAMFVDV IHTDSAPMIP FLGFGMSQKV GHLDFYPNGG KQMPGCQKNA LSTIVDINGL WEGTRDFVAC NHLRSYKYYS SSITSPDGFL GYPCASYNDF QEGNCFPCPP EGCPQMGHYA DQFQGKTRAV GQTFFLNTGD SGNFTRWRHR VSVTLAGKRK TSGYFRIALY GSNGNSKQYE IFKGSLQPRA SHMRDIDVDV NVGKIQKVKF LWNNHVINLI RPKLGASQIT VQSGENGTEY NFCSNDAVSE DVLQSLYAC //