EXTL2

Last updated
EXTL2
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases EXTL2 , EXTR2, exostosin-like glycosyltransferase 2, exostosin like glycosyltransferase 2
External IDs OMIM: 602411 MGI: 1889574 HomoloGene: 1102 GeneCards: EXTL2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001033025
NM_001261440
NM_001261441
NM_001261442
NM_001439

Contents

NM_001163514
NM_001163515
NM_021388

RefSeq (protein)

NP_001028197
NP_001248369
NP_001248370
NP_001248371
NP_001430

NP_001156986
NP_001156987
NP_067363

Location (UCSC) Chr 1: 100.87 – 100.9 Mb Chr 3: 116.01 – 116.03 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Exostosin-like 2 is a protein that in humans is encoded by the EXTL2 gene. [5] [6] [7] EXTL2 Glycosyltransferase is required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. (https://www.phosphosite.org/overviewExecuteAction?id=5020882)

Related Research Articles

Glycosaminoglycan Polysaccharides found in animal tissue

Glycosaminoglycans (GAGs) or mucopolysaccharides are long linear polysaccharides consisting of repeating disaccharide units. The repeating two-sugar unit consists of a uronic sugar and an amino sugar, with the exception of keratan, where in the place of the uronic sugar it has galactose. Because GAGs are highly polar and attract water, they are used in the body as a lubricant or shock absorber. Mucopolysaccharidoses are a group of metabolic disorders in which abnormal accumulations of glycosaminoglycans occur because of enzyme deficiencies.

Heparan sulfate Linear polysaccharide in all animal tissues

Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues. It occurs as a proteoglycan in which two or three HS chains are attached in close proximity to cell surface or extracellular matrix proteins. It is in this form that HS binds to a variety of protein ligands, including Wnt, and regulates a wide range of biological activities, including developmental processes, angiogenesis, blood coagulation, abolishing detachment activity by GrB, and tumour metastasis. HS has also been shown to serve as cellular receptor for a number of viruses, including the respiratory syncytial virus. One study suggests that cellular heparan sulfate has a role in SARS-CoV-2 Infection, particularly when the virus attaches with ACE2.

EXT1

Exostosin-1 is a protein that in humans is encoded by the EXT1 gene.

EXT2 (gene)

Exostosin glycosyltransferase-2 is a protein that in humans is encoded by the EXT2 gene.

CHST6

Carbohydrate sulfotransferase 6 is an enzyme that in humans is encoded by the CHST6 gene.

CHST4

Carbohydrate sulfotransferase 4 is an enzyme that in humans is encoded by the CHST4 gene.

B3GAT3

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 is an enzyme that in humans is encoded by the B3GAT3 gene.

NDST1

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 is an enzyme. In humans, it is encoded by the NDST1 gene.

EXTL3

Exostosin-like 3 is a protein that in humans is encoded by the EXTL3 gene.

EXTL1

Exostosin-like 1 is a protein that in humans is encoded by the EXTL1 gene.

HS3ST3A1

Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 is an enzyme that in humans is encoded by the HS3ST3A1 gene.

HGSNAT

Heparan-α-glucosaminide N-acetyltransferase is an enzyme that in humans is encoded by the HGSNAT gene.

NDST2

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2 is an enzyme that in humans is encoded by the NDST2 gene.

HS2ST1

Heparan sulfate 2-O-sulfotransferase 1 is an enzyme that in humans is encoded by the HS2ST1 gene.

HS3ST3B1

Heparan sulfate glucosamine 3-O-sulfotransferase 3B1 is an enzyme that in humans is encoded by the HS3ST3B1 gene. Heparan sulfate biosynthetic enzymes are key components in generating myriad distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It is a type II integral membrane protein and possesses heparan sulfate glucosaminyl 3-O-sulfotransferase activity ( HS3ST3A1). The Sulfotransferase domain of this enzyme is highly similar to the same domain of heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1 and these two enzymes sulfate an identical disaccharide. This gene is widely expressed, with the most abundant expression in liver and placenta.

GLCE

D-glucuronyl C5-epimerase is an enzyme that in humans is encoded by the GLCE gene.

NDST3 Enzyme

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 is an enzyme that in humans is encoded by the NDST3 gene. It catalyses the reaction:

3'-phosphoadenylyl sulfate + α-D-glucosaminyl-[heparan sulfate](n) = adenosine 3',5'-bisphosphate + 2 H+ + N-sulfo-α-D-glucosaminyl-[heparan sulfate](n)

ALG13

UDP-N-acetylglucosamine transferase subunit ALG13 homolog, also known as asparagine-linked glycosylation 13 homolog, is an enzyme that in humans is encoded by the ALG13 gene.

Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan 4IV-alpha-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction

Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase. This enzyme catalyses the following chemical reaction

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000162694 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027963 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Wuyts W, Van Hul W, Hendrickx J, Speleman F, Wauters J, De Boulle K, Van Roy N, Van Agtmael T, Bossuyt P, Willems PJ (Mar 1998). "Identification and characterization of a novel member of the EXT gene family, EXTL2". Eur J Hum Genet. 5 (6): 382–9. doi:10.1159/000484796. PMID   9450183.
  6. Sobhany M, Dong J, Negishi M (Jun 2005). "Two-step mechanism that determines the donor binding specificity of human UDP-N-acetylhexosaminyltransferase". J Biol Chem. 280 (25): 23441–5. doi: 10.1074/jbc.M413379200 . PMID   15831490.
  7. "Entrez Gene: EXTL2 exostoses (multiple)-like 2".

Further reading