Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

Q92685 · ALG3_HUMAN

  • Protein
    Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
  • Gene
    ALG3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Dol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-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. In the lumen of the endoplasmic reticulum, adds the first dolichyl beta-D-mannosyl phosphate derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-dolichol to produce Man6GlcNAc2-PP-dolichol (PubMed:10581255).
Man6GlcNAc2-PP-dolichol is a substrate for ALG9, the following enzyme in the biosynthetic pathway (PubMed:10581255).

Catalytic activity

Pathway

Protein modification; protein glycosylation.

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular Componentlumenal side of endoplasmic reticulum membrane
Molecular Functionalpha-1,3-mannosyltransferase activity
Molecular Functiondol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity
Biological Processdolichol-linked oligosaccharide biosynthetic process
Biological Processprotein glycosylation
Biological Processprotein N-linked glycosylation

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
  • EC number
  • Alternative names
    • Asparagine-linked glycosylation protein 3 homolog
    • Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
    • Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
    • Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase
    • Not56-like protein

Gene names

    • Name
      ALG3
    • Synonyms
      NOT, NOT56L

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q92685
  • Secondary accessions
    • A8JZZ6
    • Q9BT71

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane41-61Helical
Transmembrane95-115Helical
Transmembrane123-143Helical
Transmembrane149-169Helical
Transmembrane172-192Helical
Transmembrane203-223Helical
Transmembrane231-251Helical
Transmembrane289-309Helical
Transmembrane332-352Helical
Transmembrane356-376Helical
Transmembrane407-427Helical

Keywords

Disease & Variants

Involvement in disease

Congenital disorder of glycosylation 1D (CDG1D)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
  • See also
    MIM:601110
Natural variants in CDG1D
Variant IDPosition(s)ChangeDescription
VAR_010306118G>Din CDG1D; loss of dol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; dbSNP:rs28940588
VAR_037806171R>Qin CDG1D; dbSNP:rs119103236

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_037805107in dbSNP:rs2233463
Natural variantVAR_010306118in CDG1D; loss of dol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; dbSNP:rs28940588
Natural variantVAR_037806171in CDG1D; dbSNP:rs119103236

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 550 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

Type
IDPosition(s)Source
Description
ChainPRO_00000805661-438UniProtDol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase
Modified residue (large scale data)11PRIDEPhosphoserine
Modified residue13UniProtPhosphoserine
Modified residue (large scale data)13PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Family & Domains

Sequence similarities

Belongs to the glycosyltransferase 58 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q92685-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    438
  • Mass (Da)
    50,126
  • Last updated
    1997-02-01 v1
  • MD5 Checksum
    E0635E13B7CD13BF88E9961EE77131BB
MAAGLRKRGRSGSAAQAEGLCKQWLQRAWQERRLLLREPRYTLLVAACLCLAEVGITFWVIHRVAYTEIDWKAYMAEVEGVINGTYDYTQLQGDTGPLVYPAGFVYIFMGLYYATSRGTDIRMAQNIFAVLYLATLLLVFLIYHQTCKVPPFVFFFMCCASYRVHSIFVLRLFNDPVAMVLLFLSINLLLAQRWGWGCCFFSLAVSVKMNVLLFAPGLLFLLLTQFGFRGALPKLGICAGLQVVLGLPFLLENPSGYLSRSFDLGRQFLFHWTVNWRFLPEALFLHRAFHLALLTAHLTLLLLFALCRWHRTGESILSLLRDPSKRKVPPQPLTPNQIVSTLFTSNFIGICFSRSLHYQFYVWYFHTLPYLLWAMPARWLTHLLRLLVLGLIELSWNTYPSTSCSSAALHICHAVILLQLWLGPQPFPKSTQHSKKAH

Q92685-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-66: MAAGLRKRGRSGSAAQAEGLCKQWLQRAWQERRLLLREPRYTLLVAACLCLAEVGITFWVIHRVAY → MFPAQAKENAGFSGCGGD

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J7S5C9J7S5_HUMANALG3398
F8WF93F8WF93_HUMANALG365
F8WE30F8WE30_HUMANALG3107
H7BZZ2H7BZZ2_HUMANALG3105
H7C0X4H7C0X4_HUMANALG3323

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0427381-66in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Y09022
EMBL· GenBank· DDBJ
CAA70220.1
EMBL· GenBank· DDBJ
mRNA
AK289361
EMBL· GenBank· DDBJ
BAF82050.1
EMBL· GenBank· DDBJ
mRNA
AC061705
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC002839
EMBL· GenBank· DDBJ
AAH02839.1
EMBL· GenBank· DDBJ
mRNA
BC004313
EMBL· GenBank· DDBJ
AAH04313.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help