8ERC

Human Membrane-bound O-acyltransferase 7

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003841	molecular_function	1-acylglycerol-3-phosphate O-acyltransferase activity
A	0005515	molecular_function	protein binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006629	biological_process	lipid metabolic process
A	0006644	biological_process	phospholipid metabolic process
A	0006661	biological_process	phosphatidylinositol biosynthetic process
A	0008374	molecular_function	O-acyltransferase activity
A	0008654	biological_process	phospholipid biosynthetic process
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0021591	biological_process	ventricular system development
A	0021819	biological_process	layer formation in cerebral cortex
A	0030258	biological_process	lipid modification
A	0036149	biological_process	phosphatidylinositol acyl-chain remodeling
A	0036151	biological_process	phosphatidylcholine acyl-chain remodeling
A	0044233	cellular_component	mitochondria-associated endoplasmic reticulum membrane contact site
A	0046488	biological_process	phosphatidylinositol metabolic process
A	0047144	molecular_function	2-acylglycerol-3-phosphate O-acyltransferase activity
A	0071617	molecular_function	lysophospholipid acyltransferase activity
A	0090207	biological_process	regulation of triglyceride metabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	37
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"30959108","evidenceCode":"ECO:0000305"}]}

Chain

Residue

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site_id	SWS_FT_FI2
Number of Residues	104
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30959108","evidenceCode":"ECO:0000305"}]}

Chain

Residue

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site_id	SWS_FT_FI3
Number of Residues	274
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"30959108","evidenceCode":"ECO:0000305"}]}

Chain

Residue

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

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