Entry - *602385 - SULFOTRANSFERASE FAMILY 1C, MEMBER 2; SULT1C2 - OMIM
 
* 602385

SULFOTRANSFERASE FAMILY 1C, MEMBER 2; SULT1C2


Alternative titles; symbols

SULFOTRANSFERASE FAMILY 1C, MEMBER 1, FORMERLY; SULT1C1, FORMERLY
SULFOTRANSFERASE 1C1, FORMERLY


HGNC Approved Gene Symbol: SULT1C2

Cytogenetic location: 2q12.3     Genomic coordinates (GRCh38): 2:108,288,895-108,309,915 (from NCBI)


TEXT

Description

Cytosolic sulfotransferase (ST) enzymes catalyze the sulfate conjugation of many drugs, xenobiotic compounds, hormones, and neurotransmitters.


Cloning and Expression

Her et al. (1997) identified a cDNA containing a region highly conserved among STs. They stated that the predicted 296-amino acid protein appears to be related to the phenol sulfotransferases (PSTs; see 171150). Her et al. (1997) designated it SULT1C1 on the basis of its homology (62% identity) to a rat liver ST, ST1C1. SULT1C1 was expressed as a 1.4-kb mRNA in adult human stomach, kidney, and thyroid, and in fetal kidney and liver.

By RT-PCR, Sakakibara et al. (1998) amplified SULT1C1 from liver, lung, and intestine. Recombinant SULT1C1 expressed in E. coli showed an apparent molecular mass of 34 kD by SDS-PAGE.

Using 3-prime RACE, Freimuth et al. (2000) determined that the SULT1C1 cDNA contains 2 polyadenylation signals. By PCR, they amplified a SULT1C1 splice variant containing an insert that encodes 32 additional in-frame amino acids and no stop codons. Western blot analysis of COS-1 cells transfected with the 296-amino acid SULT1C1 variant resulted in expression of a protein with an apparent molecular mass of about 35 kD. Transfection of COS-1 cells with the variant containing the 32-amino acid insert resulted in no protein, possibly due to mRNA or protein instability.


Gene Function

By functional characterization of recombinant protein, Sakakibara et al. (1998) determined that SULT1C1 catalyzed the sulfonation of p-nitrophenol and N-hydroxy-2-acetylaminofluorene, but not dopamine.

Freimuth et al. (2000) found that recombinant SULT1C1 catalyzed the sulfate conjugation of 4-nitrophenol, but not dopamine, 17-beta-estradiol, or dehydroepiandrosterone. The optimal pH was 7.4.


Gene Structure

Freimuth et al. (2000) determined that the SULT1C1 gene contains 8 exons and spans about 21.2 kb. Exon 1 is untranslated. A SULT1C1 splice variant utilizes cryptic splice sites within an Alu repetitive element within intron 3; the additional exon was designated exon 3b. The 5-prime flanking region of the SULT1C1 gene contains no TATA or CAAT motifs.


Mapping

Her et al. (1997) used PCR of somatic cell hybrid mapping panels to map the SULT1C1 gene (SULT1C2) to 2q11.1-q11.2. By genomic sequence analysis and FISH, Freimuth et al. (2000) mapped the SULT1C1 gene to chromosome 2q11.2, close to the SULT1C2 gene (SULT1C4; 608357).


REFERENCES

  1. Freimuth, R. R., Raftogianis, R. B., Wood, T. C., Moon, E., Kim, U.-J., Xu, J., Siciliano, M. J., Weinshilboum, R. M. Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization, gene cloning, and chromosomal localization. Genomics 65: 157-165, 2000. [PubMed: 10783263, related citations] [Full Text]

  2. Her, C., Kaur, G. P., Athwal, R. S., Weinshilboum, R. M. Human sulfotransferase SULT1C1: cDNA cloning, tissue-specific expression, and chromosomal localization. Genomics 41: 467-470, 1997. [PubMed: 9169148, related citations] [Full Text]

  3. Sakakibara, Y., Yanagisawa, K., Katafuchi, J., Ringer, D. P., Takami, Y., Nakayama, T., Suiko, M., Liu, M.-C. Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene. J. Biol. Chem. 273: 33929-33935, 1998. [PubMed: 9852044, related citations] [Full Text]


Contributors:
Patricia A. Hartz - updated : 12/19/2003
Creation Date:
Rebekah S. Rasooly : 2/24/1998
alopez : 06/19/2018
mgross : 12/19/2003
terry : 12/19/2003
terry : 12/19/2003
alopez : 6/14/1999
alopez : 4/23/1998
alopez : 2/24/1998

* 602385

SULFOTRANSFERASE FAMILY 1C, MEMBER 2; SULT1C2


Alternative titles; symbols

SULFOTRANSFERASE FAMILY 1C, MEMBER 1, FORMERLY; SULT1C1, FORMERLY
SULFOTRANSFERASE 1C1, FORMERLY


HGNC Approved Gene Symbol: SULT1C2

Cytogenetic location: 2q12.3     Genomic coordinates (GRCh38): 2:108,288,895-108,309,915 (from NCBI)


TEXT

Description

Cytosolic sulfotransferase (ST) enzymes catalyze the sulfate conjugation of many drugs, xenobiotic compounds, hormones, and neurotransmitters.


Cloning and Expression

Her et al. (1997) identified a cDNA containing a region highly conserved among STs. They stated that the predicted 296-amino acid protein appears to be related to the phenol sulfotransferases (PSTs; see 171150). Her et al. (1997) designated it SULT1C1 on the basis of its homology (62% identity) to a rat liver ST, ST1C1. SULT1C1 was expressed as a 1.4-kb mRNA in adult human stomach, kidney, and thyroid, and in fetal kidney and liver.

By RT-PCR, Sakakibara et al. (1998) amplified SULT1C1 from liver, lung, and intestine. Recombinant SULT1C1 expressed in E. coli showed an apparent molecular mass of 34 kD by SDS-PAGE.

Using 3-prime RACE, Freimuth et al. (2000) determined that the SULT1C1 cDNA contains 2 polyadenylation signals. By PCR, they amplified a SULT1C1 splice variant containing an insert that encodes 32 additional in-frame amino acids and no stop codons. Western blot analysis of COS-1 cells transfected with the 296-amino acid SULT1C1 variant resulted in expression of a protein with an apparent molecular mass of about 35 kD. Transfection of COS-1 cells with the variant containing the 32-amino acid insert resulted in no protein, possibly due to mRNA or protein instability.


Gene Function

By functional characterization of recombinant protein, Sakakibara et al. (1998) determined that SULT1C1 catalyzed the sulfonation of p-nitrophenol and N-hydroxy-2-acetylaminofluorene, but not dopamine.

Freimuth et al. (2000) found that recombinant SULT1C1 catalyzed the sulfate conjugation of 4-nitrophenol, but not dopamine, 17-beta-estradiol, or dehydroepiandrosterone. The optimal pH was 7.4.


Gene Structure

Freimuth et al. (2000) determined that the SULT1C1 gene contains 8 exons and spans about 21.2 kb. Exon 1 is untranslated. A SULT1C1 splice variant utilizes cryptic splice sites within an Alu repetitive element within intron 3; the additional exon was designated exon 3b. The 5-prime flanking region of the SULT1C1 gene contains no TATA or CAAT motifs.


Mapping

Her et al. (1997) used PCR of somatic cell hybrid mapping panels to map the SULT1C1 gene (SULT1C2) to 2q11.1-q11.2. By genomic sequence analysis and FISH, Freimuth et al. (2000) mapped the SULT1C1 gene to chromosome 2q11.2, close to the SULT1C2 gene (SULT1C4; 608357).


REFERENCES

  1. Freimuth, R. R., Raftogianis, R. B., Wood, T. C., Moon, E., Kim, U.-J., Xu, J., Siciliano, M. J., Weinshilboum, R. M. Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization, gene cloning, and chromosomal localization. Genomics 65: 157-165, 2000. [PubMed: 10783263] [Full Text: https://doi.org/10.1006/geno.2000.6150]

  2. Her, C., Kaur, G. P., Athwal, R. S., Weinshilboum, R. M. Human sulfotransferase SULT1C1: cDNA cloning, tissue-specific expression, and chromosomal localization. Genomics 41: 467-470, 1997. [PubMed: 9169148] [Full Text: https://doi.org/10.1006/geno.1997.4683]

  3. Sakakibara, Y., Yanagisawa, K., Katafuchi, J., Ringer, D. P., Takami, Y., Nakayama, T., Suiko, M., Liu, M.-C. Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene. J. Biol. Chem. 273: 33929-33935, 1998. [PubMed: 9852044] [Full Text: https://doi.org/10.1074/jbc.273.51.33929]


Contributors:
Patricia A. Hartz - updated : 12/19/2003

Creation Date:
Rebekah S. Rasooly : 2/24/1998

Edit History:
alopez : 06/19/2018
mgross : 12/19/2003
terry : 12/19/2003
terry : 12/19/2003
alopez : 6/14/1999
alopez : 4/23/1998
alopez : 2/24/1998