6vz1 - Revision history

OCA at 14:40, 6 March 2024

OCA — Wed, 06 Mar 2024 14:40:51 GMT

←Older revision		Revision as of 14:40, 6 March 2024
Line 3:		Line 3:
	<StructureSection load='6vz1' size='340' side='right'caption='[[6vz1]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='6vz1' size='340' side='right'caption='[[6vz1]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6vz1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VZ1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6vz1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VZ1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3VV:S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]-3,5,9-TRIHYDROXY-8,8-DIMETHYL-3,5-DIOXIDO-10,14-DIOXO-2,4,6-TRIOXA-11,15-DIAZA-3LAMBDA~5~,5LAMBDA~5~-DIPHOSPHAHEPTADECAN-17-YL}+(9Z)-OCTADEC-9-ENETHIOATE+(NON-PREFERRED+NAME)'>3VV</scene>, <scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene>~~</td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 3.2Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DGAT1, AGRP1, DGAT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3VV:S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]-3,5,9-TRIHYDROXY-8,8-DIMETHYL-3,5-DIOXIDO-10,14-DIOXO-2,4,6-TRIOXA-11,15-DIAZA-3LAMBDA~5~,5LAMBDA~5~-DIPHOSPHAHEPTADECAN-17-YL}+(9Z)-OCTADEC-9-ENETHIOATE+(NON-PREFERRED+NAME)'>3VV</scene>, <scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vz1 OCA], [https://pdbe.org/6vz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vz1 RCSB], [https://www.ebi.ac.uk/pdbsum/6vz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vz1 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vz1 OCA], [https://pdbe.org/6vz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vz1 RCSB], [https://www.ebi.ac.uk/pdbsum/6vz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vz1 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN]] Congenital chronic diarrhea with protein-losing enteropathy. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN] Congenital chronic diarrhea with protein-losing enteropathy. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN]] Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders.<ref>PMID:16214399</ref> <ref>PMID:9756920</ref>	+	[https://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN] Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders.<ref>PMID:16214399</ref> <ref>PMID:9756920</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Triacylglycerols store metabolic energy in organisms and have industrial uses as foods and fuels. Excessive accumulation of triacylglycerols in humans causes obesity and is associated with metabolic diseases(1). Triacylglycerol synthesis is catalysed by acyl-CoA diacylglycerol acyltransferase (DGAT) enzymes(2-4), the structures and catalytic mechanisms of which remain unknown. Here we determined the structure of dimeric human DGAT1, a member of the membrane-bound O-acyltransferase (MBOAT) family, by cryo-electron microscopy at approximately 3.0 A resolution. DGAT1 forms a homodimer through N-terminal segments and a hydrophobic interface, with putative active sites within the membrane region. A structure obtained with oleoyl-CoA substrate resolved at approximately 3.2 A shows that the CoA moiety binds DGAT1 on the cytosolic side and the acyl group lies deep within a hydrophobic channel, positioning the acyl-CoA thioester bond near an invariant catalytic histidine residue. The reaction centre is located inside a large cavity, which opens laterally to the membrane bilayer, providing lipid access to the active site. A lipid-like density-possibly representing an acyl-acceptor molecule-is located within the reaction centre, orthogonal to acyl-CoA. Insights provided by the DGAT1 structures, together with mutagenesis and functional studies, provide the basis for a model of the catalysis of triacylglycerol synthesis by DGAT.	+
-		+
-	Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme.,Sui X, Wang K, Gluchowski NL, Elliott SD, Liao M, Walther TC, Farese RV Jr Nature. 2020 May;581(7808):323-328. doi: 10.1038/s41586-020-2289-6. Epub 2020 May, 13. PMID:32433611<ref>PMID:32433611</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6vz1" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Farese~~, V R~~]]	+	[[Category: Farese Jr VR]]
-	[[Category: Gluchowski, N]]	+	[[Category: Gluchowski N]]
-	[[Category: Liao, M]]	+	[[Category: Liao M]]
-	[[Category: Sui, X]]	+	[[Category: Sui X]]
-	[[Category: Walther~~, C T~~]]	+	[[Category: Walther CT]]
-	[[Category: Wang, K]]	+	[[Category: Wang K]]
-	~~[[Category: Lipid metabolism]]~~	+
-	~~[[Category: Lipid storage]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Triglyceride biosynthesis~~]]	+

OCA at 15:26, 8 June 2021

OCA — Tue, 08 Jun 2021 15:26:56 GMT

OCA at 06:40, 3 June 2020

OCA — Wed, 03 Jun 2020 06:40:25 GMT

←Older revision		Revision as of 06:40, 3 June 2020
Line 1:		Line 1:

	==Cryo-EM structure of human diacylglycerol O-acyltransferase 1 complexed with acyl-CoA substrate==		==Cryo-EM structure of human diacylglycerol O-acyltransferase 1 complexed with acyl-CoA substrate==
-	<StructureSection load='6vz1' size='340' side='right'caption='[[6vz1]]' scene=''>	+	<StructureSection load='6vz1' size='340' side='right'caption='[[6vz1]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VZ1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6vz1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VZ1 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vz1 OCA], [http://pdbe.org/6vz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vz1 RCSB], [http://www.ebi.ac.uk/pdbsum/6vz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vz1 ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3VV:S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]-3,5,9-TRIHYDROXY-8,8-DIMETHYL-3,5-DIOXIDO-10,14-DIOXO-2,4,6-TRIOXA-11,15-DIAZA-3LAMBDA~5~,5LAMBDA~5~-DIPHOSPHAHEPTADECAN-17-YL}+(9Z)-OCTADEC-9-ENETHIOATE+(NON-PREFERRED+NAME)'>3VV</scene>, <scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DGAT1, AGRP1, DGAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vz1 OCA], [http://pdbe.org/6vz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vz1 RCSB], [http://www.ebi.ac.uk/pdbsum/6vz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vz1 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN]] Congenital chronic diarrhea with protein-losing enteropathy. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN]] Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders.<ref>PMID:16214399</ref> <ref>PMID:9756920</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Triacylglycerols store metabolic energy in organisms and have industrial uses as foods and fuels. Excessive accumulation of triacylglycerols in humans causes obesity and is associated with metabolic diseases(1). Triacylglycerol synthesis is catalysed by acyl-CoA diacylglycerol acyltransferase (DGAT) enzymes(2-4), the structures and catalytic mechanisms of which remain unknown. Here we determined the structure of dimeric human DGAT1, a member of the membrane-bound O-acyltransferase (MBOAT) family, by cryo-electron microscopy at approximately 3.0 A resolution. DGAT1 forms a homodimer through N-terminal segments and a hydrophobic interface, with putative active sites within the membrane region. A structure obtained with oleoyl-CoA substrate resolved at approximately 3.2 A shows that the CoA moiety binds DGAT1 on the cytosolic side and the acyl group lies deep within a hydrophobic channel, positioning the acyl-CoA thioester bond near an invariant catalytic histidine residue. The reaction centre is located inside a large cavity, which opens laterally to the membrane bilayer, providing lipid access to the active site. A lipid-like density-possibly representing an acyl-acceptor molecule-is located within the reaction centre, orthogonal to acyl-CoA. Insights provided by the DGAT1 structures, together with mutagenesis and functional studies, provide the basis for a model of the catalysis of triacylglycerol synthesis by DGAT.
		+
		+	Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme.,Sui X, Wang K, Gluchowski NL, Elliott SD, Liao M, Walther TC, Farese RV Jr Nature. 2020 May;581(7808):323-328. doi: 10.1038/s41586-020-2289-6. Epub 2020 May, 13. PMID:32433611<ref>PMID:32433611</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6vz1" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Farese ~~Jr VR~~]]	+	[[Category: Farese, V R]]
-	[[Category: Gluchowski N]]	+	[[Category: Gluchowski, N]]
-	[[Category: Liao M]]	+	[[Category: Liao, M]]
-	[[Category: Sui X]]	+	[[Category: Sui, X]]
-	[[Category: Walther CT]]	+	[[Category: Walther, C T]]
-	[[Category: Wang K]]	+	[[Category: Wang, K]]
		+	[[Category: Lipid metabolism]]
		+	[[Category: Lipid storage]]
		+	[[Category: Transferase]]
		+	[[Category: Triglyceride biosynthesis]]

OCA at 05:35, 13 May 2020

OCA — Wed, 13 May 2020 05:35:11 GMT

←Older revision		Revision as of 05:35, 13 May 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6vz1 is ~~ON HOLD until Paper Publication~~	+	==Cryo-EM structure of human diacylglycerol O-acyltransferase 1 complexed with acyl-CoA substrate==
-		+	<StructureSection load='6vz1' size='340' side='right'caption='[[6vz1]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VZ1 FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vz1 OCA], [http://pdbe.org/6vz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vz1 RCSB], [http://www.ebi.ac.uk/pdbsum/6vz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vz1 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Farese Jr VR]]
		+	[[Category: Gluchowski N]]
		+	[[Category: Liao M]]
		+	[[Category: Sui X]]
		+	[[Category: Walther CT]]
		+	[[Category: Wang K]]

OCA at 07:24, 1 April 2020

OCA — Wed, 01 Apr 2020 07:24:35 GMT

←Older revision		Revision as of 07:24, 1 April 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6vz1 is ON HOLD	+	The entry 6vz1 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6vz1" [edit=sysop:move=sysop]

OCA — Wed, 04 Mar 2020 05:41:14 GMT

Protected "6vz1" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:41, 4 March 2020

OCA: New page: '''Unreleased structure''' The entry 6vz1 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 04 Mar 2020 05:41:13 GMT

New page: '''Unreleased structure''' The entry 6vz1 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6vz1 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]

←Older revision		Revision as of 15:26, 8 June 2021
Line 3:		Line 3:
	<StructureSection load='6vz1' size='340' side='right'caption='[[6vz1]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='6vz1' size='340' side='right'caption='[[6vz1]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6vz1]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VZ1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6VZ1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6vz1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VZ1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3VV:S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]-3,5,9-TRIHYDROXY-8,8-DIMETHYL-3,5-DIOXIDO-10,14-DIOXO-2,4,6-TRIOXA-11,15-DIAZA-3LAMBDA~5~,5LAMBDA~5~-DIPHOSPHAHEPTADECAN-17-YL}+(9Z)-OCTADEC-9-ENETHIOATE+(NON-PREFERRED+NAME)'>3VV</scene>, <scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3VV:S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]-3,5,9-TRIHYDROXY-8,8-DIMETHYL-3,5-DIOXIDO-10,14-DIOXO-2,4,6-TRIOXA-11,15-DIAZA-3LAMBDA~5~,5LAMBDA~5~-DIPHOSPHAHEPTADECAN-17-YL}+(9Z)-OCTADEC-9-ENETHIOATE+(NON-PREFERRED+NAME)'>3VV</scene>, <scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DGAT1, AGRP1, DGAT ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DGAT1, AGRP1, DGAT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vz1 OCA], [~~http~~://pdbe.org/6vz1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6vz1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6vz1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6vz1 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vz1 OCA], [https://pdbe.org/6vz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vz1 RCSB], [https://www.ebi.ac.uk/pdbsum/6vz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vz1 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN]] Congenital chronic diarrhea with protein-losing enteropathy. The disease is caused by mutations affecting the gene represented in this entry.	+	[[https://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN]] Congenital chronic diarrhea with protein-losing enteropathy. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN]] Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders.<ref>PMID:16214399</ref> <ref>PMID:9756920</ref>	+	[[https://www.uniprot.org/uniprot/DGAT1_HUMAN DGAT1_HUMAN]] Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders.<ref>PMID:16214399</ref> <ref>PMID:9756920</ref>
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	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==