SAG (gene)

In today's world, SAG (gene) has gained unprecedented relevance, gaining more and more attention and generating all kinds of opinions, debates and research. Since SAG (gene) arrived on the scene, it has deeply impacted various areas of society, influencing everything from popular culture to politics and technology. In this article, we will explore in detail the impact of SAG (gene) on different aspects of everyday life, analyzing its consequences and possible implications for the future. Without a doubt, SAG (gene) has been and will continue to be a topic of great interest and importance for our contemporary society.

SAG
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4ZWJ
Identifiers
Aliases	SAG, RP47, S-AG, S-antigen; retina and pineal gland (arrestin), S-antigen visual arrestin
External IDs	OMIM: 181031; MGI: 98227; HomoloGene: 455; GeneCards: SAG; OMA:SAG - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q37.1 Start 233,307,816 bp[1] End 233,347,055 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 D|1 44.44 cM Start 87,731,402 bp[2] End 87,772,880 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in nucleus accumbens testicle left testis right testis caudate nucleus putamen monocyte granulocyte bone marrow mucosa of transverse colon Top expressed in neural layer of retina retinal pigment epithelium corneal stroma pineal gland epithelium of lens iris conjunctival fornix embryo ciliary body spermatid More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein phosphatase inhibitor activity phosphoprotein binding opsin binding G protein-coupled receptor binding Cellular component cytosol photoreceptor inner segment photoreceptor outer segment membrane cell projection Biological process rhodopsin mediated signaling pathway regulation of rhodopsin mediated signaling pathway signal transduction cell surface receptor signaling pathway negative regulation of phosphoprotein phosphatase activity G protein-coupled receptor internalization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6295 20215 Ensembl ENSG00000281857 ENSG00000130561 ENSMUSG00000056055 UniProt P10523 P20443 RefSeq (mRNA) NM_000541 NM_009118 RefSeq (protein) NP_000532 NP_033144 Location (UCSC) Chr 2: 233.31 – 233.35 Mb Chr 1: 87.73 – 87.77 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

S-arrestin is a protein that in humans is encoded by the SAG gene.^[5][6]

Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G-protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. S-arrestin, also known as S-antigen, is a major soluble protein in photoreceptor cells that is involved in desensitization of the photoactivated transduction cascade. It is expressed in the retina and the pineal gland and inhibits coupling of rhodopsin to transducin in vitro. Additionally, S-arrestin is highly antigenic, and is capable of inducing experimental autoimmune uveoretinitis. Mutations in this gene have been associated with Oguchi disease, a rare autosomal recessive form of night blindness.^[6]

References

1. ^ ^{a b c} ENSG00000130561 GRCh38: Ensembl release 89: ENSG00000281857, ENSG00000130561 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000056055 – 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. ^ Yamaki K, Tsuda M, Kikuchi T, Chen KH, Huang KP, Shinohara T (Jan 1991). "Structural organization of the human S-antigen gene. cDNA, amino acid, intron, exon, promoter, in vitro transcription, retina, and pineal gland". J Biol Chem. 265 (34): 20757–62. doi:10.1016/S0021-9258(17)45280-X. PMID 2249983.
6. ^ ^{a b} "Entrez Gene: SAG S-antigen; retina and pineal gland (arrestin)".

Further reading

• Ghalayini AJ, Anderson RE (1992). "Activation of bovine rod outer segment phospholipase C by arrestin". J. Biol. Chem. 267 (25): 17977–82. doi:10.1016/S0021-9258(19)37139-X. PMID 1325454.
• Huang SK, Klein DC, Korf HW (1992). "Immunocytochemical demonstration of rod-opsin, S-antigen, and neuron-specific proteins in the human pineal gland". Cell Tissue Res. 267 (3): 493–8. doi:10.1007/BF00319371. PMID 1533347. S2CID 22831066.
• Palczewski K, Pulvermüller A, Buczyłko J, Hofmann KP (1991). "Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin". J. Biol. Chem. 266 (28): 18649–54. doi:10.1016/S0021-9258(18)55112-7. PMID 1917988.
• Palczewski K, McDowell JH, Jakes S, et al. (1989). "Regulation of rhodopsin dephosphorylation by arrestin". J. Biol. Chem. 264 (27): 15770–3. doi:10.1016/S0021-9258(18)71543-3. PMID 2550422.
• Yamaki K, Tsuda M, Shinohara T (1988). "The sequence of human retinal S-antigen reveals similarities with alpha-transducin". FEBS Lett. 234 (1): 39–43. Bibcode:1988FEBSL.234...39Y. doi:10.1016/0014-5793(88)81298-5. PMID 3164688. S2CID 83543675.
• Adams MD, Kerlavage AR, Fleischmann RD, et al. (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
• Fuchs S, Nakazawa M, Maw M, et al. (1995). "A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese". Nat. Genet. 10 (3): 360–2. doi:10.1038/ng0795-360. PMID 7670478. S2CID 8836948.
• Calabrese G, Sallese M, Stornaiuolo A, et al. (1995). "Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes". Genomics. 23 (1): 286–8. doi:10.1006/geno.1994.1497. PMID 7695743.
• Diviani D, Lattion AL, Larbi N, et al. (1996). "Effect of different G protein-coupled receptor kinases on phosphorylation and desensitization of the alpha1B-adrenergic receptor". J. Biol. Chem. 271 (9): 5049–58. doi:10.1074/jbc.271.9.5049. PMID 8617782.
• Yamamoto S, Sippel KC, Berson EL, Dryja TP (1997). "Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness". Nat. Genet. 15 (2): 175–8. doi:10.1038/ng0297-175. PMID 9020843. S2CID 9317102.
• Sippel KC, DeStefano JD, Berson EL, Dryja TP (1998). "Evaluation of the human arrestin gene in patients with retinitis pigmentosa and stationary night blindness". Invest. Ophthalmol. Vis. Sci. 39 (3): 665–70. PMID 9501883.
• Andersen PS, Lavoie PM, Sékaly RP, et al. (1999). "Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-MHC class II complexes". Immunity. 10 (4): 473–83. doi:10.1016/S1074-7613(00)80047-3. PMID 10229190.
• Lee KB, Ptasienski JA, Bunemann M, Hosey MM (2000). "Acidic amino acids flanking phosphorylation sites in the M2 muscarinic receptor regulate receptor phosphorylation, internalization, and interaction with arrestins". J. Biol. Chem. 275 (46): 35767–77. doi:10.1074/jbc.M002225200. PMID 10952973.
• Wistow G, Bernstein SL, Wyatt MK, et al. (2002). "Expressed sequence tag analysis of human retina for the NEIBank Project: retbindin, an abundant, novel retinal cDNA and alternative splicing of other retina-preferred gene transcripts". Mol. Vis. 8: 196–204. PMID 12107411.
• Zhu X, Li A, Brown B, et al. (2002). "Mouse cone arrestin expression pattern: light induced translocation in cone photoreceptors". Mol. Vis. 8: 462–71. PMID 12486395.
• Zhang H, Cuenca N, Ivanova T, et al. (2003). "Identification and light-dependent translocation of a cone-specific antigen, cone arrestin, recognized by monoclonal antibody 7G6". Invest. Ophthalmol. Vis. Sci. 44 (7): 2858–67. doi:10.1167/iovs.03-0072. hdl:10045/13046. PMID 12824223.
• Chuang JZ, Vega C, Jun W, Sung CH (2004). "Structural and functional impairment of endocytic pathways by retinitis pigmentosa mutant rhodopsin-arrestin complexes". J. Clin. Invest. 114 (1): 131–40. doi:10.1172/jci21136. PMC 437971. PMID 15232620.
• Nakamura M, Yamamoto S, Okada M, et al. (2004). "Novel mutations in the arrestin gene and associated clinical features in Japanese patients with Oguchi's disease". Ophthalmology. 111 (7): 1410–4. doi:10.1016/j.ophtha.2003.11.006. PMID 15234147.
• Saga M, Mashima Y, Kudoh J, et al. (2004). "Gene analysis and evaluation of the single founder effect in Japanese patients with Oguchi disease". Jpn. J. Ophthalmol. 48 (4): 350–2. doi:10.1007/s10384-004-0070-2. PMID 15295660. S2CID 23424425.

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