ID M3VWT0_FELCA Unreviewed; 469 AA. AC M3VWT0; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 03-MAY-2023, entry version 66. 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:ENSFCAP00000001407.3}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000001407.3, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000001407.3, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001407.3, 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., Schaffer A.A., RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A., RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G., RA 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:ENSFCAP00000001407.3, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001407.3, RC ECO:0000313|Proteomes:UP000011712}; 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:ENSFCAP00000001407.3} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001407.3}; RG Ensembl; RL Submitted (JAN-2023) to UniProtKB. 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:0000256|RuleBase:RU362046}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613, CC ECO:0000256|RuleBase:RU362046}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family. CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}. 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; AANG04000273; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003994490.1; XM_003994441.3. DR AlphaFoldDB; M3VWT0; -. DR STRING; 9685.ENSFCAP00000001407; -. DR ESTHER; felca-m3vwt0; Pancreatic_lipase. DR Ensembl; ENSFCAT00000001516.6; ENSFCAP00000001407.3; ENSFCAG00000001515.6. DR GeneID; 101083714; -. DR KEGG; fca:101083714; -. DR eggNOG; ENOG502QUK7; Eukaryota. DR GeneTree; ENSGT00940000162375; -. DR HOGENOM; CLU_027171_0_2_1; -. DR InParanoid; M3VWT0; -. DR OrthoDB; 3428256at2759; -. DR Proteomes; UP000011712; Chromosome D2. DR Bgee; ENSFCAG00000001515; Expressed in zone of skin and 9 other tissues. 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 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; PS50095; PLAT; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000865-3, ECO:0000256|PROSITE- KW ProRule:PRU00152}; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, KW ECO:0000256|RuleBase:RU362046}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, KW ECO:0000256|RuleBase:RU362046}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362046}; KW Signal {ECO:0000256|RuleBase:RU362046}. FT SIGNAL 1..17 FT /evidence="ECO:0000256|RuleBase:RU362046" FT CHAIN 18..469 FT /note="Triacylglycerol lipase" FT /evidence="ECO:0000256|RuleBase:RU362046" FT /id="PRO_5005140382" FT DOMAIN 357..469 FT /note="PLAT" FT /evidence="ECO:0000259|PROSITE:PS50095" FT ACT_SITE 171 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 195 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT ACT_SITE 282 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1" FT BINDING 206 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT BINDING 209 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT BINDING 211 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT BINDING 214 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2" FT DISULFID 21..27 FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3" FT DISULFID 109..120 FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3" FT DISULFID 256..280 FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3" FT DISULFID 304..315 FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3" FT DISULFID 318..323 FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3" FT DISULFID 453..469 FT /evidence="ECO:0000256|PIRSR:PIRSR000865-3, FT ECO:0000256|PROSITE-ProRule:PRU00152" 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 //