Tag | Content |
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CPLM ID | CPLM-001798 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Pancreatic triacylglycerol lipase |
Protein Synonyms/Alias | PL; PTL; Pancreatic lipase |
Gene Name | PNLIP |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Sus scrofa (Pig) |
NCBI Taxa ID | 9823 |
Lysine Modification | Position | Peptide | Type | References |
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374 | SRQYEIYKGTLQPDN | acetylation | [1] |
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Reference | [1] Acetylation of Lys-373 in porcine pancreatic lipase after reaction of the enzyme or its C-terminal fragment [corrected] with p-nitrophenyl acetate. De Caro JD, Chautan MP, Rouimi P, Rovery M. Biochimie. 1988 Dec;70(12):1785-90. [ PMID: 3150684] |
Functional Description | |
Sequence Annotation | DOMAIN 339 450 PLAT. ACT_SITE 153 153 Nucleophile. ACT_SITE 177 177 Charge relay system. ACT_SITE 264 264 Charge relay system. METAL 188 188 Calcium; via carbonyl oxygen. METAL 191 191 Calcium; via carbonyl oxygen. METAL 193 193 Calcium. METAL 196 196 Calcium. CARBOHYD 167 167 N-linked (GlcNAc...). DISULFID 4 10 DISULFID 91 104 Alternate. DISULFID 91 102 Alternate. DISULFID 238 262 DISULFID 286 297 DISULFID 300 305 DISULFID 434 450 |
Keyword | 3D-structure; Calcium; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Reference proteome; Secreted. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 450 AA |
Protein Sequence | SEVCFPRLGC FSDDAPWAGI VQRPLKILPW SPKDVDTRFL LYTNQNQNNY QELVADPSTI 60 TNSNFRMDRK TRFIIHGFID KGEEDWLSNI CKNLFKVESV NCICVDWKGG SRTGYTQASQ 120 NIRIVGAEVA YFVEVLKSSL GYSPSNVHVI GHSLGSHAAG EAGRRTNGTI ERITGLDPAE 180 PCFQGTPELV RLDPSDAKFV DVIHTDAAPI IPNLGFGMSQ TVGHLDFFPN GGKQMPGCQK 240 NILSQIVDID GIWEGTRDFV ACNHLRSYKY YADSILNPDG FAGFPCDSYN VFTANKCFPC 300 PSEGCPQMGH YADRFPGKTN GVSQVFYLNT GDASNFARWR YKVSVTLSGK KVTGHILVSL 360 FGNEGNSRQY EIYKGTLQPD NTHSDEFDSD VEVGDLQKVK FIWYNNNVIN PTLPRVGASK 420 ITVERNDGKV YDFCSQETVR EEVLLTLNPC 450 |
Gene Ontology | GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0050253; F:retinyl-palmitate esterase activity; IEA:EC. GO:0004806; F:triglyceride lipase activity; IEA:EC. GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |