Entry - *610133 - ST6 ALPHA-N-ACETYL-NEURAMINYL-2,3-BETA-GALACTOSYL-1,3-N-ACETYLGALACTOSAMINIDE ALPHA-2,6-SIALYLTRANSFERASE 3; ST6GALNAC3 - OMIM

 
 
* 610133

ST6 ALPHA-N-ACETYL-NEURAMINYL-2,3-BETA-GALACTOSYL-1,3-N-ACETYLGALACTOSAMINIDE ALPHA-2,6-SIALYLTRANSFERASE 3; ST6GALNAC3


Alternative titles; symbols

ST6GALNAC III
SIALYLTRANSFERASE 7C; SIAT7C


HGNC Approved Gene Symbol: ST6GALNAC3

Cytogenetic location: 1p31.1     Genomic coordinates (GRCh38): 1:76,074,746-76,637,339 (from NCBI)


TEXT

▼ Description

ST6GALNAC3 belongs to a family of sialyltransferases that transfer sialic acids from CMP-sialic acid to terminal positions of carbohydrate groups in glycoproteins and glycolipids (Lee et al., 1999).


▼ Cloning and Expression

By searching an EST database for the human homolog of mouse St6GalNAc III, followed by PCR of a brain cDNA library, Tsuchida et al. (2005) cloned 2 splice variants of human ST6GalNAc III. The longer deduced protein contains 305 amino acids and has a short N-terminal tail, followed by a transmembrane region, a sialyl motif L, and a sialyl motif S. The truncated human ST6GalNAc III contains 240 amino acids and lacks the transmembrane domain. Northern blot analysis detected a 3.2-kb transcript in kidney and brain only.

Lee et al. (1999) cloned 2 splice variants of mouse St6GalNAc III from a brain cDNA library.


▼ Gene Function

Lee et al. (1999) assayed the ability of a soluble form of mouse St6GalNAc III to transfer radiolabeled N-acetylneuraminic acid (NeuAc) from CMP-NeuAc to several glycolipid, glycoprotein, and free oligosaccharide substrates. Only fetuin (AHSG; 138680) and the glycolipid GM1b were good acceptor substrates. The unconjugated NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc residue found in fetuin and GM1b was a poor substrate. The incorporated sialic acids contained an alpha-2,6 linkage, confirming that the enzyme belongs to the ST6GalNAc family. The truncated St6GalNAc III isoform showed very low enzymatic activity.

Using CMP-NeuAc as donor, Tsuchida et al. (2005) found that GM1b was a good acceptor substrate for human ST6GalNAc III. No other gangliosides were significant acceptors. ST6GalNAc III also used sialyl-lactotetraosyl-ceramide and fetuin as acceptor substrates. Digestion of the sialylated fetuin product with glycopeptidase indicated that ST6GalNAc III sialylated O-glycans but not N-glycans.


▼ Gene Structure

Tsuchida et al. (2005) determined the ST6GALNAC3 gene contains 5 coding exons.


▼ Mapping

The International Radiation Hybrid Mapping Consortium mapped the ST6GALNAC3 gene to chromosome 1 (SHGC-75038).

▼ REFERENCES

  1. Lee, Y.-C., Kaufmann, M., Kitazume-Kawaguchi, S., Kono, M., Takashima, S., Kurosawa, N., Liu, H., Pircher, H., Tsuji, S. Molecular cloning and functional expression of two members of mouse NeuAc-alpha-2,3Gal-beta-1,3GalNAc GalNAc-alpha-2,6-sialyltransferase family, ST6GalNAc III and IV. J. Biol. Chem. 274: 11958-11967, 1999. [PubMed: 10207017, related citations] [Full Text]

  2. Tsuchida, A., Ogiso, M., Nakamura, Y., Kiso, M., Furukawa, K., Furukawa, K. Molecular cloning and expression of human ST6GalNAc III: restricted tissue distribution and substrate specificity. J. Biochem. 138: 237-243, 2005. [PubMed: 16169874, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 5/19/2006
Edit History:
terry : 06/14/2006
mgross : 5/19/2006

* 610133

ST6 ALPHA-N-ACETYL-NEURAMINYL-2,3-BETA-GALACTOSYL-1,3-N-ACETYLGALACTOSAMINIDE ALPHA-2,6-SIALYLTRANSFERASE 3; ST6GALNAC3


Alternative titles; symbols

ST6GALNAC III
SIALYLTRANSFERASE 7C; SIAT7C


HGNC Approved Gene Symbol: ST6GALNAC3

Cytogenetic location: 1p31.1     Genomic coordinates (GRCh38): 1:76,074,746-76,637,339 (from NCBI)


TEXT

Description

ST6GALNAC3 belongs to a family of sialyltransferases that transfer sialic acids from CMP-sialic acid to terminal positions of carbohydrate groups in glycoproteins and glycolipids (Lee et al., 1999).


Cloning and Expression

By searching an EST database for the human homolog of mouse St6GalNAc III, followed by PCR of a brain cDNA library, Tsuchida et al. (2005) cloned 2 splice variants of human ST6GalNAc III. The longer deduced protein contains 305 amino acids and has a short N-terminal tail, followed by a transmembrane region, a sialyl motif L, and a sialyl motif S. The truncated human ST6GalNAc III contains 240 amino acids and lacks the transmembrane domain. Northern blot analysis detected a 3.2-kb transcript in kidney and brain only.

Lee et al. (1999) cloned 2 splice variants of mouse St6GalNAc III from a brain cDNA library.


Gene Function

Lee et al. (1999) assayed the ability of a soluble form of mouse St6GalNAc III to transfer radiolabeled N-acetylneuraminic acid (NeuAc) from CMP-NeuAc to several glycolipid, glycoprotein, and free oligosaccharide substrates. Only fetuin (AHSG; 138680) and the glycolipid GM1b were good acceptor substrates. The unconjugated NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc residue found in fetuin and GM1b was a poor substrate. The incorporated sialic acids contained an alpha-2,6 linkage, confirming that the enzyme belongs to the ST6GalNAc family. The truncated St6GalNAc III isoform showed very low enzymatic activity.

Using CMP-NeuAc as donor, Tsuchida et al. (2005) found that GM1b was a good acceptor substrate for human ST6GalNAc III. No other gangliosides were significant acceptors. ST6GalNAc III also used sialyl-lactotetraosyl-ceramide and fetuin as acceptor substrates. Digestion of the sialylated fetuin product with glycopeptidase indicated that ST6GalNAc III sialylated O-glycans but not N-glycans.


Gene Structure

Tsuchida et al. (2005) determined the ST6GALNAC3 gene contains 5 coding exons.


Mapping

The International Radiation Hybrid Mapping Consortium mapped the ST6GALNAC3 gene to chromosome 1 (SHGC-75038).

REFERENCES

  1. Lee, Y.-C., Kaufmann, M., Kitazume-Kawaguchi, S., Kono, M., Takashima, S., Kurosawa, N., Liu, H., Pircher, H., Tsuji, S. Molecular cloning and functional expression of two members of mouse NeuAc-alpha-2,3Gal-beta-1,3GalNAc GalNAc-alpha-2,6-sialyltransferase family, ST6GalNAc III and IV. J. Biol. Chem. 274: 11958-11967, 1999. [PubMed: 10207017] [Full Text: https://doi.org/10.1074/jbc.274.17.11958]

  2. Tsuchida, A., Ogiso, M., Nakamura, Y., Kiso, M., Furukawa, K., Furukawa, K. Molecular cloning and expression of human ST6GalNAc III: restricted tissue distribution and substrate specificity. J. Biochem. 138: 237-243, 2005. [PubMed: 16169874] [Full Text: https://doi.org/10.1093/jb/mvi124]


Creation Date:
Patricia A. Hartz : 5/19/2006

Edit History:
terry : 06/14/2006
mgross : 5/19/2006



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OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: May 16, 2024