Stanniocalcin 2, also known as STC2, is a human gene.[1]
This gene encodes a secreted, homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The encoded protein has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. Its C-terminus contains a cluster of histidine residues which may interact with metal ions.[1]
The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Constitutive overexpression of human stanniocalcin 2 in mice resulted in pre- and postnatal growth restriction, reduced bone and skeletal muscle growth, and organomegaly. Expression of this gene is induced by estrogen and altered in some breast cancers.[1] Stanniocalcin 2 may suppress Pi cotransport.[2]
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Jellinek DA, Chang AC, Larsen MR; et al. (2001). "Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells". Biochem. J. 350 Pt 2: 453–61. PMID10947959.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
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Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
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Gagliardi AD, Kuo EY, Raulic S; et al. (2005). "Human stanniocalcin-2 exhibits potent growth-suppressive properties in transgenic mice independently of growth hormone and IGFs". Am. J. Physiol. Endocrinol. Metab. 288 (1): E92–105. doi:10.1152/ajpendo.00268.2004. PMID15367391.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
Luo CW, Pisarska MD, Hsueh AJ (2005). "Identification of a stanniocalcin paralog, stanniocalcin-2, in fish and the paracrine actions of stanniocalcin-2 in the mammalian ovary". Endocrinology. 146 (1): 469–76. doi:10.1210/en.2004-1197. PMID15486227.CS1 maint: Multiple names: authors list (link)
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. PMID15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
Stelzl U, Worm U, Lalowski M; et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID16169070.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
Otsuki T, Ota T, Nishikawa T; et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID16303743.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
Esseghir S, Kennedy A, Seedhar P; et al. (2007). "Identification of NTN4, TRA1, and STC2 as prognostic markers in breast cancer in a screen for signal sequence encoding proteins". Clin. Cancer Res. 13 (11): 3164–73. doi:10.1158/1078-0432.CCR-07-0224. PMID17545519.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
Ichikawa T, Horie-Inoue K, Ikeda K; et al. (2007). "Vitamin K2 induces phosphorylation of protein kinase A and expression of novel target genes in osteoblastic cells". J. Mol. Endocrinol. 39 (4): 239–47. doi:10.1677/JME-07-0048. PMID17909264.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)