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2OXE

Structure of the Human Pancreatic Lipase-related Protein 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004465molecular_functionlipoprotein lipase activity
A0004620molecular_functionphospholipase activity
A0004806molecular_functiontriacylglycerol lipase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006629biological_processlipid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006641biological_processtriglyceride metabolic process
A0008970molecular_functionphospholipase A1 activity
A0009395biological_processphospholipid catabolic process
A0016042biological_processlipid catabolic process
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
A0019376biological_processgalactolipid catabolic process
A0019433biological_processtriglyceride catabolic process
A0031410cellular_componentcytoplasmic vesicle
A0034375biological_processhigh-density lipoprotein particle remodeling
A0034638biological_processphosphatidylcholine catabolic process
A0042589cellular_componentzymogen granule membrane
A0042632biological_processcholesterol homeostasis
A0043005cellular_componentneuron projection
A0044241biological_processlipid digestion
A0046872molecular_functionmetal ion binding
A0047372molecular_functionmonoacylglycerol lipase activity
A0047714molecular_functiongalactolipase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
B0004465molecular_functionlipoprotein lipase activity
B0004620molecular_functionphospholipase activity
B0004806molecular_functiontriacylglycerol lipase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006629biological_processlipid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006641biological_processtriglyceride metabolic process
B0008970molecular_functionphospholipase A1 activity
B0009395biological_processphospholipid catabolic process
B0016042biological_processlipid catabolic process
B0016298molecular_functionlipase activity
B0016787molecular_functionhydrolase activity
B0019376biological_processgalactolipid catabolic process
B0019433biological_processtriglyceride catabolic process
B0031410cellular_componentcytoplasmic vesicle
B0034375biological_processhigh-density lipoprotein particle remodeling
B0034638biological_processphosphatidylcholine catabolic process
B0042589cellular_componentzymogen granule membrane
B0042632biological_processcholesterol homeostasis
B0043005cellular_componentneuron projection
B0044241biological_processlipid digestion
B0046872molecular_functionmetal ion binding
B0047372molecular_functionmonoacylglycerol lipase activity
B0047714molecular_functiongalactolipase activity
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VHVIGHSLGA
ChainResidueDetails
AVAL165-ALA174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsRegion: {"description":"Required for galactolipase activity","evidences":[{"source":"PubMed","id":"26494624","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18702514","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10037","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18702514","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18702514","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OXE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PVS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18702514","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OXE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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