SULF2

SULF2
Identifiers
Aliases	SULF2 , HSULF-2, sulfatase 2
External IDs	OMIM: 610013; MGI: 1919293; HomoloGene: 10313; GeneCards: SULF2; OMA:SULF2 - orthologs
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 165,915,009 bp [2] End 165,997,583 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in decidua body of uterus myometrium left ovary right ovary ectocervix left uterine tube monocyte tendon of biceps brachii smooth muscle tissue Top expressed in tail of embryo calvaria genital tubercle fossa umbilical cord condyle abdominal wall decidua endothelial cell of lymphatic vessel transitional epithelium of urinary bladder More reference expression data BioGPS n/a
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 plasma membrane cell surface endoplasmic reticulum Golgi stack extracellular space 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: 165.92 – 166 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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.