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Details on Person UniProt:Q9H553 ALG2

Class:Id	ReferenceGeneProduct:143976
_chainChangeLog	chain:1-416 added on Fri February 6 2015
_displayName	UniProt:Q9H553 ALG2
_timestamp	2024-11-03 19:44:35
chain	chain:1-416
checksum	778DB1FD069E7F29
comment	FUNCTION Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes, on the cytoplasmic face of the endoplasmic reticulum, the addition of the second and third mannose residues to the dolichol-linked oligosaccharide chain, to produce Man3GlcNAc(2)-PP-dolichol core oligosaccharide. Man3GlcNAc(2)-PP-dolichol is a substrate for ALG11, the following enzyme in the biosynthetic pathway (PubMed:12684507, PubMed:35136180). While both alpha 1,3 and alpha 1,6 linkages are possible, the sequential addition of alpha 1,3 followed by alpha 1,6 is probably the preferred route (PubMed:35136180).CATALYTIC ACTIVITY a beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP-alpha-D-mannose = an alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP + H(+)CATALYTIC ACTIVITY an alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP-alpha-D-mannose = an alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP + H(+)CATALYTIC ACTIVITY a beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP-alpha-D-mannose = an alpha-D-Man-(1->6)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP + H(+)CATALYTIC ACTIVITY an alpha-D-Man-(1->6)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP-alpha-D-mannose = an alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP + H(+)BIOPHYSICOCHEMICAL PROPERTIES kcat is 5.4 min(-1) with alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol as substrate. kcat is 63.2 min(-1) with alpha-D-Man-(1->6)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol as substrate.PATHWAY Protein modification; protein glycosylation.INTERACTION Active on cytoplasmic side of endoplasmic reticulum membrane.ALTERNATIVE PRODUCTS The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.
created	[InstanceEdit:143527] Schmidt, EE, 2004-11-12 07:45:10
description	recommendedName: Alpha-1,3/1,6-mannosyltransferase ALG2 ecNumber evidence="2 4"2.4.1.132 ecNumber evidence="2 4"2.4.1.257 alternativeName: Asparagine-linked glycosylation protein 2 homolog alternativeName: GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase alternativeName: GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase alternativeName: GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
geneName	ALG2 UNQ666/PRO1298
identifier	Q9H553
isSequenceChanged	FALSE
keyword	Alternative splicing Congenital disorder of glycosylation Congenital myasthenic syndrome Disease variant Endoplasmic reticulum Glycosyltransferase Membrane Proteomics identification Reference proteome Transferase Transmembrane Transmembrane helix
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03
name	ALG2
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8995269] ENSEMBL:ENSG00000119523 ALG2 [Homo sapiens]
secondaryIdentifier	ALG2_HUMAN A2A2Y0 Q8NBX2 Q8NC39
sequenceLength	416
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:218411] UniProt:Q9H553-2 ALG2 [Homo sapiens] [ReferenceIsoform:414258] UniProt:Q9H553-1 ALG2 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:449336] ALG2 [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:4549361] ALG2 G347Vfs*27 [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5633223] ALG2 72_75delinsSPR [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5633236] ALG2 V68G [endoplasmic reticulum membrane] [Homo sapiens]
(referenceSequence)	[FragmentReplacedModification:4549345] Replacement of residues 347 to 372 by VDPWSPLTTVSQGFCVSLTRCTSQKQ [FragmentReplacedModification:5633224] Replacement of residues 72 to 75 by SPR [ReplacedResidue:5633245] L-valine 68 replaced with glycine
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No pathways have been reviewed or authored by UniProt:Q9H553 ALG2 (143976)