1BU8

RAT PANCREATIC LIPASE RELATED PROTEIN 2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004465	molecular_function	lipoprotein lipase activity
A	0004620	molecular_function	glycerophospholipase activity
A	0004806	molecular_function	triacylglycerol lipase activity
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region
A	0006629	biological_process	lipid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006644	biological_process	phospholipid metabolic process
A	0008970	molecular_function	glycerophospholipid phospholipase A1 activity
A	0009395	biological_process	phospholipid catabolic process
A	0009791	biological_process	post-embryonic development
A	0016042	biological_process	lipid catabolic process
A	0016298	molecular_function	lipase activity
A	0019376	biological_process	galactolipid catabolic process
A	0019433	biological_process	triglyceride catabolic process
A	0032094	biological_process	response to food
A	0033993	biological_process	response to lipid
A	0034375	biological_process	high-density lipoprotein particle remodeling
A	0034638	biological_process	phosphatidylcholine catabolic process
A	0042589	cellular_component	zymogen granule membrane
A	0042632	biological_process	cholesterol homeostasis
A	0043005	cellular_component	neuron projection
A	0043434	biological_process	response to peptide hormone
A	0047372	molecular_function	monoacylglycerol lipase activity
A	0047714	molecular_function	galactolipase activity
A	0051384	biological_process	response to glucocorticoid
A	0052689	molecular_function	carboxylic ester hydrolase activity
A	0120516	molecular_function	diacylglycerol lipase activity

Functional Information from PROSITE/UniProt

site_id	PS00120
Number of Residues	10
Details	LIPASE_SER Lipases, serine active site. VHLIGHSLGA

Chain	Residue	Details
A	VAL146-ALA155

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	34
Details	Region: {"description":"Required for galactolipase activity","evidences":[{"source":"UniProtKB","id":"P54317","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9822688","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10037","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9822688","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P54317","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9822688","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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