HS3ST3A1

HS3ST3A1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1T8T, 1T8U
Identifiers
Aliases	HS3ST3A1 , 30ST3A1, 3OST3A1, 3-OST-3A, heparan sulfate-glucosamine 3-sulfotransferase 3A1
External IDs	OMIM: 604057; MGI: 1333861; HomoloGene: 88735; GeneCards: HS3ST3A1; OMA:HS3ST3A1 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17p12 Start 13,494,032 bp [1] End 13,601,929 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11 B3|11 40.24 cM Start 64,326,158 bp [2] End 64,413,667 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cartilage tissue testicle tibia gingival epithelium oral cavity glomerulus metanephric glomerulus seminal vesicula stromal cell of endometrium germinal epithelium Top expressed in metatarsal bones condyle second metatarsal bone fifth metatarsal bone iris footplate Gonadal ridge third metatarsal bone ciliary body renal corpuscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity sulfotransferase activity [heparan sulfate-glucosamine 3-sulfotransferase 3 activity] [heparan sulfate-glucosamine 3-sulfotransferase 1 activity] heparan sulfate sulfotransferase activity Cellular component integral component of membrane Golgi membrane Golgi apparatus membrane Biological process glycosaminoglycan biosynthetic process heparan sulfate proteoglycan biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9955 15478 Ensembl ENSG00000153976 ENSMUSG00000047759 UniProt Q9Y663 Q8BKN6 RefSeq (mRNA) NM_006042 NM_178870 RefSeq (protein) NP_006033 NP_849201 Location (UCSC) Chr 17: 13.49 – 13.6 Mb Chr 11: 64.33 – 64.41 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 is an enzyme that in humans is encoded by the HS3ST3A1 gene. ^{[5] [6]}

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. 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 the liver and placenta. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000153976 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000047759 – 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. Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD (Mar 1999). "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci". J Biol Chem. 274 (8): 5170–84. doi: 10.1074/jbc.274.8.5170 . PMID   9988767.
6. "Entrez Gene: HS3ST3A1 heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1".

Further reading

• Razi N, Lindahl U (1995). "Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides". J. Biol. Chem. 270 (19): 11267–75. doi: 10.1074/jbc.270.19.11267 . PMID   7744762.
• Liu J, Shworak NW, Sinaÿ P, et al. (1999). "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities". J. Biol. Chem. 274 (8): 5185–92. doi: 10.1074/jbc.274.8.5185 . PMID   9988768.
• Shukla D, Liu J, Blaiklock P, et al. (1999). "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry". Cell. 99 (1): 13–22. doi: 10.1016/S0092-8674(00)80058-6 . PMID   10520990. S2CID   14139940.
• Liu J, Shriver Z, Blaiklock P, et al. (2000). "Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues". J. Biol. Chem. 274 (53): 38155–62. doi: 10.1074/jbc.274.53.38155 . PMID   10608887.
• Salehi LB, Mangino M, De Serio S, et al. (2002). "Assignment of a locus for autosomal dominant idiopathic scoliosis (IS) to human chromosome 17p11". Hum. Genet. 111 (4–5): 401–4. doi:10.1007/s00439-002-0785-4. PMID   12384783. S2CID   29912776.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC   403697 . PMID   12975309.
• Moon AF, Edavettal SC, Krahn JM, et al. (2004). "Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1". J. Biol. Chem. 279 (43): 45185–93. doi: 10.1074/jbc.M405013200 . PMC   4114238 . PMID   15304505.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.