Hmdb loader
Identification
HMDB Protein ID HMDBP08287
Secondary Accession Numbers
  • 13999
Name Sulfhydryl oxidase 1
Synonyms
  1. Quiescin Q6
  2. hQSOX
Gene Name QSOX1
Protein Type Unknown
Biological Properties
General Function Involved in thiol oxidase activity
Specific Function Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. In fibroblasts, it may have tumor-suppressing capabilities being involved in growth regulation.
Pathways Not Available
Reactions
R'C(R)SH + Oxygen → R'C(R)S-S(R)CR' + Hydrogen peroxide details
GO Classification
Biological Process
cell redox homeostasis
Cellular Component
integral to Golgi membrane
extracellular space
Function
catalytic activity
oxidoreductase activity, acting on a sulfur group of donors
oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor
thiol oxidase activity
oxidoreductase activity
Molecular Function
flavin-linked sulfhydryl oxidase activity
protein disulfide isomerase activity
Process
metabolic process
cellular process
oxidation reduction
cellular homeostasis
cell redox homeostasis
Cellular Location
  1. extracellular space
  2. Isoform 2:Secreted
Gene Properties
Chromosome Location 1
Locus 1q24
SNPs QSOX1
Gene Sequence
>2244 bp
ATGAGGAGGTGCAACAGCGGCTCCGGGCCGCCGCCGTCGCTGCTGCTGCTGCTGCTGTGG
CTGCTCGCGGTTCCCGGCGCTAACGCGGCCCCGCGGTCGGCGCTCTATTCGCCTTCCGAC
CCGCTGACGCTGCTGCAGGCGGACACGGTGCGCGGCGCGGTGCTGGGCTCCCGCAGCGCC
TGGGCCGTGGAGTTCTTCGCCTCCTGGTGCGGCCACTGCATCGCCTTCGCCCCGACGTGG
AAGGCGCTGGCCGAAGACGTCAAAGCCTGGAGGCCGGCCCTGTATCTCGCCGCCCTGGAC
TGTGCTGAGGAGACCAACAGTGCAGTCTGCAGAGACTTCAACATCCCTGGCTTCCCGACT
GTGAGGTTCTTCAAGGCCTTTACCAAGAACGGCTCGGGAGCAGTATTTCCAGTGGCTGGT
GCTGACGTGCAGACACTGCGGGAGAGGCTCATTGACGCCCTGGAGTCCCATCATGACACG
TGGCCCCCAGCCTGTCCCCCACTGGAGCCTGCCAAGCTGGAGGAGATTGATGGATTCTTT
GCGAGAAATAACGAAGAGTACCTGGCTCTGATCTTTGAAAAGGGAGGCTCCTACCTGGGT
AGAGAGGTGGCTCTGGACCTGTCCCAGCACAAAGGCGTGGCGGTGCGCAGGGTGCTGAAC
ACAGAGGCCAATGTGGTGAGAAAGTTTGGTGTCACCGACTTCCCCTCTTGCTACCTGCTG
TTCCGGAATGGCTCTGTCTCCCGAGTCCCCGTGCTCATGGAATCCAGGTCCTTCTATACC
GCTTACCTGCAGAGACTCTCTGGGCTCACCAGGGAGGCTGCCCAGACCACAGTTGCACCA
ACCACTGCTAACAAGATAGCTCCCACTGTTTGGAAATTGGCAGATCGCTCCAAGATCTAC
ATGGCTGACCTGGAATCTGCACTGCACTACATCCTGCGGATAGAAGTGGGCAGGTTCCCG
GTCCTGGAAGGGCAGCGCCTGGTGGCCCTGAAAAAGTTTGTGGCAGTGCTGGCCAAGTAT
TTCCCTGGCCGGCCCTTAGTCCAGAACTTCCTGCACTCCGTGAATGAATGGCTCAAGAGG
CAGAAGAGAAATAAAATTCCCTACAGTTTCTTTAAAACTGCCCTGGACGACAGGAAAGAG
GGTGCCGTTCTTGCCAAGAAGGTGAACTGGATTGGCTGCCAGGGGAGTGAGCCGCATTTC
CGGGGCTTTCCCTGCTCCCTGTGGGTCCTCTTCCACTTCTTGACTGTGCAGGCAGCTCGG
CAAAATGTAGACCACTCACAGGAAGCAGCCAAGGCCAAGGAGGTCCTCCCAGCCATCCGA
GGCTACGTGCACTACTTCTTCGGCTGCCGAGACTGCGCTAGCCACTTCGAGCAGATGGCT
GCTGCCTCCATGCACCGGGTGGGGAGTCCCAACGCCGCTGTCCTCTGGCTCTGGTCTAGC
CACAACAGGGTCAATGCTCGCCTTGCAGGTGCCCCCAGCGAGGACCCCCAGTTCCCCAAG
GTGCAGTGGCCACCCCGTGAACTTTGTTCTGCCTGCCACAATGAACGCCTGGATGTGCCC
GTGTGGGACGTGGAAGCCACCCTCAACTTCCTCAAGGCCCACTTCTCCCCAAGCAACATC
ATCCTGGACTTCCCTGCAGCTGGGTCAGCTGCCCGGAGGGATGTGCAGAATGTGGCAGCC
GCCCCAGAGCTGGCGATGGGAGCCCTGGAGCTGGAAAGCCGGAATTCAACTCTGGACCCT
GGGAAGCCTGAGATGATGAAGTCCCCCACAAACACCACCCCACATGTGCCGGCTGAGGGA
CCTGAGGCAAGTCGACCCCCGAAGCTGCACCCTGGCCTCAGAGCTGCACCAGGCCAGGAG
CCTCCTGAGCACATGGCAGAGCTTCAGAGGAATGAGCAGGAGCAGCCGCTTGGGCAGTGG
CACTTGAGCAAGCGAGACACAGGGGCTGCATTGCTGGCTGAGTCCAGGGCTGAGAAGAAC
CGCCTCTGGGGCCCTTTGGAGGTCAGGCGCGTGGGCCGCAGCTCCAAGCAGCTGGTCGAC
ATCCCTGAGGGCCAGCTGGAGGCCCGAGCTGGACGGGGCCGAGGCCAGTGGCTGCAGGTG
CTGGGAGGGGGCTTCTCTTACCTGGACATCAGCCTCTGTGTGGGGCTCTATTCCCTGTCC
TTCATGGGCCTGCTGGCCATGTACACCTACTTCCAGGCCAAGATAAGGGCCCTGAAGGGC
CATGCTGGCCACCCTGCAGCCTGA
Protein Properties
Number of Residues 747
Molecular Weight 66860.075
Theoretical pI 8.559
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Sulfhydryl oxidase 1
MRRCNSGSGPPPSLLLLLLWLLAVPGANAAPRSALYSPSDPLTLLQADTVRGAVLGSRSA
WAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPT
VRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFF
ARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLL
FRNGSVSRVPVLMESRSFYTAYLQRLSGLTREAAQTTVAPTTANKIAPTVWKLADRSKIY
MADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKR
QKRNKIPYSFFKTALDDRKEGAVLAKKVNWIGCQGSEPHFRGFPCSLWVLFHFLTVQAAR
QNVDHSQEAAKAKEVLPAIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSS
HNRVNARLAGAPSEDPQFPKVQWPPRELCSACHNERLDVPVWDVEATLNFLKAHFSPSNI
ILDFPAAGSAARRDVQNVAAAPELAMGALELESRNSTLDPGKPEMMKSPTNTTPHVPAEG
PEASRPPKLHPGLRAAPGQEPPEHMAELQRNEQEQPLGQWHLSKRDTGAALLAESRAEKN
RLWGPLEVRRVGRSSKQLVDIPEGQLEARAGRGRGQWLQVLGGGFSYLDISLCVGLYSLS
FMGLLAMYTYFQAKIRALKGHAGHPAA
GenBank ID Protein 13325075
UniProtKB/Swiss-Prot ID O00391
UniProtKB/Swiss-Prot Entry Name QSOX1_HUMAN
PDB IDs
GenBank Gene ID NM_002826.4
GeneCard ID QSOX1
GenAtlas ID QSOX1
HGNC ID HGNC:9756
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed:12975309 ]
  4. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed:16335952 ]
  5. Coppock DL, Cina-Poppe D, Gilleran S: The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1. Genomics. 1998 Dec 15;54(3):460-8. [PubMed:9878249 ]
  6. Radom J, Colin D, Thiebault F, Dognin-Bergeret M, Mairet-Coello G, Esnard-Feve A, Fellmann D, Jouvenot M: Identification and expression of a new splicing variant of FAD-sulfhydryl oxidase in adult rat brain. Biochim Biophys Acta. 2006 May;1759(5):225-33. Epub 2006 May 9. [PubMed:16806532 ]
  7. Hoober KL, Glynn NM, Burnside J, Coppock DL, Thorpe C: Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases. J Biol Chem. 1999 Nov 5;274(45):31759-62. [PubMed:10542195 ]
  8. Coppock D, Kopman C, Gudas J, Cina-Poppe DA: Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29. Biochem Biophys Res Commun. 2000 Mar 16;269(2):604-10. [PubMed:10708601 ]
  9. Thorpe C, Hoober KL, Raje S, Glynn NM, Burnside J, Turi GK, Coppock DL: Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Arch Biochem Biophys. 2002 Sep 1;405(1):1-12. [PubMed:12176051 ]
  10. Chakravarthi S, Jessop CE, Willer M, Stirling CJ, Bulleid NJ: Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1. Biochem J. 2007 Jun 15;404(3):403-11. [PubMed:17331072 ]