SULF2

Extracellular sulfatase Sulf-2 is an enzyme that in humans is encoded by the SULF2 gene.[5][6]

SULF2
Identifiers
Aliases	SULF2, HSULF-2, sulfatase 2
External IDs	OMIM: 610013 MGI: 1919293 HomoloGene: 10313 GeneCards: SULF2
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20q13.12 Start 47,656,348 bp[1] End 47,786,616 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 H3 Start 166,073,089 bp[2] End 166,155,663 bp[2]
Gene ontology Molecular function • calcium ion binding • arylsulfatase activity • metal ion binding • catalytic activity • sulfuric ester hydrolase activity • hydrolase activity • N-acetylglucosamine-6-sulfatase activity • glycosaminoglycan binding Cellular component • Golgi apparatus • cell membrane • cell surface • endoplasmic reticulum • Golgi stack • extracellular Biological process • glomerular basement membrane development • kidney development • positive regulation of canonical Wnt signaling pathway • chondrocyte development • embryonic skeletal system development • positive regulation of Wnt signaling pathway • negative regulation of fibroblast growth factor receptor signaling pathway • liver regeneration • cartilage development • glomerular filtration • response to wounding • regulation of hepatocyte proliferation • glial cell-derived neurotrophic factor receptor signaling pathway • positive regulation of vascular endothelial growth factor production • metabolism • esophagus smooth muscle contraction • innervation • bone development • heparan sulfate proteoglycan metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	55959	72043
Ensembl	ENSG00000196562	ENSMUSG00000006800
UniProt	Q8IWU5	Q8CFG0
RefSeq (mRNA)	NM_001161841 NM_018837 NM_198596	NM_001252578 NM_001252579 NM_028072 NM_001355619
RefSeq (protein)	NP_001155313 NP_061325 NP_940998	NP_001239507 NP_001239508 NP_082348 NP_001342548
Location (UCSC)	Chr 20: 47.66 – 47.79 Mb	Chr 2: 166.07 – 166.16 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Heparan sulfate proteoglycans (HSPGs) act as coreceptors for numerous heparin-binding growth factors and cytokines and are involved in cell signaling. Heparan sulfate 6-O-endosulfatases, such as SULF2, selectively remove 6-O-sulfate groups from heparan sulfate. This activity modulates the effects of heparan sulfate by altering binding sites for signaling molecules (Dai et al., 2005).[supplied by OMIM][6]

References

1. GRCh38: Ensembl release 89: ENSG00000196562 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000006800 - 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. Morimoto-Tomita M, Uchimura K, Werb Z, Hemmerich S, Rosen SD (December 2002). "Cloning and characterization of two extracellular heparin-degrading endosulfatases in mice and humans". The Journal of Biological Chemistry. 277 (51): 49175–49185. doi:10.1074/jbc.M205131200. PMC 2779716. PMID 12368295.
6. "Entrez Gene: SULF2 sulfatase 2".

Further reading

• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (June 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research. 9 (3): 99–106. CiteSeerX 10.1.1.500.923. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O (October 1999). "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 6 (5): 337–345. doi:10.1093/dnares/6.5.337. PMID 10574462.
• Fossey SC, Mychaleckyj JC, Pendleton JK, Snyder JR, Bensen JT, Hirakawa S, Rich SS, Freedman BI, Bowden DW (August 2001). "A high-resolution 6.0-megabase transcript map of the type 2 diabetes susceptibility region on human chromosome 20". Genomics. 76 (1–3): 45–57. doi:10.1006/geno.2001.6584. PMID 11549316.
• Dai Y, Yang Y, MacLeod V, Yue X, Rapraeger AC, Shriver Z, Venkataraman G, Sasisekharan R, Sanderson RD (December 2005). "HSulf-1 and HSulf-2 are potent inhibitors of myeloma tumor growth in vivo". The Journal of Biological Chemistry. 280 (48): 40066–40073. doi:10.1074/jbc.M508136200. PMID 16192265.
• Morimoto-Tomita M, Uchimura K, Bistrup A, Lum DH, Egeblad M, Boudreau N, Werb Z, Rosen SD (November 2005). "Sulf-2, a proangiogenic heparan sulfate endosulfatase, is upregulated in breast cancer". Neoplasia. 7 (11): 1001–1010. doi:10.1593/neo.05496. PMC 1502017. PMID 16331886.
• Uchimura K, Morimoto-Tomita M, Bistrup A, Li J, Lyon M, Gallagher J, Werb Z, Rosen SD (2006). "HSulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparin-bound growth factors and chemokines: effects on VEGF, FGF-1, and SDF-1". BMC Biochemistry. 7: 2. doi:10.1186/1471-2091-7-2. PMC 1386684. PMID 16417632.