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QSOX1

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QSOX1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesQSOX1, Q6, QSCN6, quiescin sulfhydryl oxidase 1
External IDsOMIM: 603120; MGI: 1330818; HomoloGene: 37690; GeneCards: QSOX1; OMA:QSOX1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002826
NM_001004128

NM_001024945
NM_023268

RefSeq (protein)

NP_001004128
NP_002817

NP_001020116
NP_075757

Location (UCSC)Chr 1: 180.15 – 180.2 MbChr 1: 155.65 – 155.69 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Quiescin sulfhydryl oxidase 1 is an enzyme that in humans is encoded by the QSOX1 gene.[5][6][7]

This gene encodes an enzyme that is localized primarily to the Golgi apparatus and secreted fluids.[8] QSOX1 is a multi-domain disulfide catalyst. Unlike other disulfide catalysts, QSOX1 can both generate disulfides de novo and catalyze dithiol/disulfide exchange. The de novo disulfide bond formation is catalyzed by the ERV1 domain that contains a FAD co-factor that allows depositions of electrons onto the terminal electron acceptor, typically molecular oxygen. The dithiol/disulfide exchange is catalyzed by the thioredoxin domain. The two domains are linked together by a flexible linker that allows the thioredoxin domain to first interact with the substrate protein and then regenerate by ERV1 domain.[9]

QSOX1 gene expression is induced as fibroblasts begin to exit the proliferative cycle and enter quiescence,[10][11] suggesting that this gene plays an important role in growth regulation. In fibroblasts QSOX1 is required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration.[12]

Two transcript variants encoding two different isoforms have been found for this gene.[13][7] The two isoforms have different tissue distribution and in addition isoform 1 has a transmembrane helix in the carboxy terminal while isoform 2 is a secreted soluble protein.

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000116260Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033684Ensembl, 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. ^ Coppock DL, Cina-Poppe D, Gilleran S (December 1998). "The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1". Genomics. 54 (3): 460–468. doi:10.1006/geno.1998.5605. PMID 9878249.
  6. ^ Coppock DL, Kopman C, Scandalis S, Gilleran S (June 1993). "Preferential gene expression in quiescent human lung fibroblasts". Cell Growth & Differentiation. 4 (6): 483–493. PMID 8396966.
  7. ^ a b "Entrez Gene: QSCN6 quiescin Q6".
  8. ^ Kodali VK, Thorpe C (October 2010). "Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins". Antioxidants & Redox Signaling. 13 (8): 1217–1230. doi:10.1089/ars.2010.3098. PMC 2959182. PMID 20136510.
  9. ^ Alon A, Grossman I, Gat Y, Kodali VK, DiMaio F, Mehlman T, et al. (August 2012). "The dynamic disulphide relay of quiescin sulphydryl oxidase". Nature. 488 (7411): 414–418. doi:10.1038/nature11267. PMC 3521037. PMID 22801504.
  10. ^ Coppock DL, Cina-Poppe D, Gilleran S (December 1998). "The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1". Genomics. 54 (3): 460–468. doi:10.1006/geno.1998.5605. PMID 9878249.
  11. ^ Coppock DL, Kopman C, Scandalis S, Gilleran S (June 1993). "Preferential gene expression in quiescent human lung fibroblasts". Cell Growth & Differentiation. 4 (6): 483–493. PMID 8396966.
  12. ^ Ilani T, Alon A, Grossman I, Horowitz B, Kartvelishvily E, Cohen SR, et al. (July 2013). "A secreted disulfide catalyst controls extracellular matrix composition and function". Science. 341 (6141): 74–76. doi:10.1126/science.1238279. PMID 23704371.
  13. ^ * Radom J, Colin D, Thiebault F, Dognin-Bergeret M, Mairet-Coello G, Esnard-Feve A, et al. (May 2006). "Identification and expression of a new splicing variant of FAD-sulfhydryl oxidase in adult rat brain". Biochimica et Biophysica Acta. 1759 (5): 225–233. doi:10.1016/j.bbaexp.2006.04.008. PMID 16806532.

Further reading

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]* Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–12135. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.