Reviewed, UniProtKB/Swiss-Prot Q8BND5 (QSOX1_MOUSE)

Names and origin

Protein names

Recommended name:
    Sulfhydryl oxidase 1
      Short name=mSOx
    EC=1.8.3.2
Alternative name(s):
    Quiescin Q6
    Skin sulfhydryl oxidase

Gene names

Name:	Qsox1
Synonyms:	Qscn6, Sox

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	748 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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 By similarity.
Catalytic activity	4 R'C(R)SH + O2 = 2 R'C(R)S-S(R)CR' + 2 H2O.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Isoform 1: Golgi apparatus membrane; Single-pass membrane protein By similarity. Isoform 2: Secreted. Note: Found in the extracellular medium of quiescent cells but not in proliferating cells. Ref.1 Isoform 3: Secreted. Note: Found in the extracellular medium of quiescent cells but not in proliferating cells. Ref.1 Isoform 4: Secreted. Note: Found in the extracellular medium of quiescent cells but not in proliferating cells. Ref.1
Tissue specificity	Expressed in the seminal vesicles and skin. Ref.1
Sequence similarities	Belongs to the quiescin-sulfhydryl oxidase (QSOX) family. Contains 1 ERV/ALR sulfhydryl oxidase domain. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein thiol-disulfide exchange Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB integral to Golgi membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	flavin-linked sulfhydryl oxidase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BND5-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BND5-2) The sequence of this isoform differs from the canonical sequence as follows:      660-661: VN → LL      662-748: Missing.
Note: Found in the extracellular medium of quiescent cells but not in proliferating cells. Ref.1 No experimental confirmation available.
Isoform 3 (identifier: Q8BND5-3) The sequence of this isoform differs from the canonical sequence as follows:      567-568: VM → LL      569-748: Missing.
Note: Found in the extracellular medium of quiescent cells but not in proliferating cells. Ref.1 No experimental confirmation available.
Isoform 4 (identifier: Q8BND5-4) The sequence of this isoform differs from the canonical sequence as follows:      126-154: FFQAFTKNGSGATLPGAGANVQTLRMRLI → VCEGGATVEWFWPSTQSSVPHFPGTFLGC      155-748: Missing.
Note: Found in the extracellular medium of quiescent cells but not in proliferating cells. Ref.1 No experimental confirmation available.
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Sequence conflict	127	1	C → Y in BAE37202. Ref.2

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	Potential
	Chain	33 – 748	716	Sulfhydryl oxidase 1		PRO_0000249534
Regions
	Transmembrane	711 – 731	21	Potential
	Domain	33 – 159	127	Thioredoxin
	Domain	399 – 506	108	ERV/ALR sulfhydryl oxidase
Amino acid modifications
	Glycosylation	133	1	N-linked (GlcNAc...) Potential
	Glycosylation	246	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	126 – 154	29	FFQAF…RMRLI → VCEGGATVEWFWPSTQSSVP HFPGTFLGC in isoform 4.		VSP_020491
	Alternative sequence	155 – 748	594	Missing in isoform 4.		VSP_020492
	Alternative sequence	567 – 568	2	VM → LL in isoform 3.		VSP_020493
	Alternative sequence	569 – 748	180	Missing in isoform 3.		VSP_020494
	Alternative sequence	660 – 661	2	VN → LL in isoform 2.		VSP_020495
	Alternative sequence	662 – 748	87	Missing in isoform 2.		VSP_020496
Experimental info
	Sequence conflict	637	1	M → I in BAE41429. Ref.2
	Sequence conflict	656	1	F → L in BAE41429. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 0499F6B8DAB5A8D1	FASTA	748	82,785
	10 20 30 40 50 60 MRRCGRLSGP PSLLLLLLLL SPLLFSGPGA YAARLSVLYS SSDPLTLLDA DSVRPTVLGS 70 80 90 100 110 120 SSAWAVEFFA SWCGHCIAFA PTWKELANDV KDWRPALNLA VLDCAEETNS AVCREFNIAG 130 140 150 160 170 180 FPTVRFFQAF TKNGSGATLP GAGANVQTLR MRLIDALESH RDTWPPACPP LEPAKLNDID 190 200 210 220 230 240 GFFTRNKADY LALVFEREDS YLGREVTLDL SQYHAVAVRR VLNTESDLVN KFGVTDFPSC 250 260 270 280 290 300 YLLLRNGSVS RVPVLVESRS FYTSYLRGLP GLTRDAPPTT ATPVTADKIA PTVWKFADRS 310 320 330 340 350 360 KIYMADLESA LHYILRVEVG KFSVLEGQRL VALKKFVAVL AKYFPGQPLV QNFLHSINDW 370 380 390 400 410 420 LQKQQKKRIP YSFFKAALDS RKEDAVLTEK VNWVGCQGSE PHFRGFPCSL WVLFHFLTVQ 430 440 450 460 470 480 ANRYSEAHPQ EPADGQEVLQ AMRSYVQFFF GCRDCADHFE QMAAASMHQV RSPSNAILWL 490 500 510 520 530 540 WTSHNRVNAR LSGALSEDPH FPKVQWPPRE LCSACHNELN GQVPLWDLGA TLNFLKAHFS 550 560 570 580 590 600 PANIVIDSSA SRHTGRRGSP EATPELVMDT LKLESRNSVL GHEQAASAES PGATALDVPA 610 620 630 640 650 660 EKPEASGPQE LYTGLRMGGA SPGQGPPERM EDHQRDMQEN APGQQHLSKR DTEALFLPEV 670 680 690 700 710 720 NHLQGPLELR RGGRSPKQLA PILEEEPEAL AIQGQGQWLQ VLGGGISHLD ISLCVGLYSV 730 740 SFMGLLAMYT YFRARLRTPK GHASYPTA
	Isoform 2. Checksum: AFC4B43576BEE56B	FASTA	661	73,297
	10 20 30 40 50 60 MRRCGRLSGP PSLLLLLLLL SPLLFSGPGA YAARLSVLYS SSDPLTLLDA DSVRPTVLGS 70 80 90 100 110 120 SSAWAVEFFA SWCGHCIAFA PTWKELANDV KDWRPALNLA VLDCAEETNS AVCREFNIAG 130 140 150 160 170 180 FPTVRFFQAF TKNGSGATLP GAGANVQTLR MRLIDALESH RDTWPPACPP LEPAKLNDID 190 200 210 220 230 240 GFFTRNKADY LALVFEREDS YLGREVTLDL SQYHAVAVRR VLNTESDLVN KFGVTDFPSC 250 260 270 280 290 300 YLLLRNGSVS RVPVLVESRS FYTSYLRGLP GLTRDAPPTT ATPVTADKIA PTVWKFADRS 310 320 330 340 350 360 KIYMADLESA LHYILRVEVG KFSVLEGQRL VALKKFVAVL AKYFPGQPLV QNFLHSINDW 370 380 390 400 410 420 LQKQQKKRIP YSFFKAALDS RKEDAVLTEK VNWVGCQGSE PHFRGFPCSL WVLFHFLTVQ 430 440 450 460 470 480 ANRYSEAHPQ EPADGQEVLQ AMRSYVQFFF GCRDCADHFE QMAAASMHQV RSPSNAILWL 490 500 510 520 530 540 WTSHNRVNAR LSGALSEDPH FPKVQWPPRE LCSACHNELN GQVPLWDLGA TLNFLKAHFS 550 560 570 580 590 600 PANIVIDSSA SRHTGRRGSP EATPELVMDT LKLESRNSVL GHEQAASAES PGATALDVPA 610 620 630 640 650 660 EKPEASGPQE LYTGLRMGGA SPGQGPPERM EDHQRDMQEN APGQQHLSKR DTEALFLPEL L
	Isoform 3. Checksum: 761F44799536DBBB	FASTA	568	63,336
	10 20 30 40 50 60 MRRCGRLSGP PSLLLLLLLL SPLLFSGPGA YAARLSVLYS SSDPLTLLDA DSVRPTVLGS 70 80 90 100 110 120 SSAWAVEFFA SWCGHCIAFA PTWKELANDV KDWRPALNLA VLDCAEETNS AVCREFNIAG 130 140 150 160 170 180 FPTVRFFQAF TKNGSGATLP GAGANVQTLR MRLIDALESH RDTWPPACPP LEPAKLNDID 190 200 210 220 230 240 GFFTRNKADY LALVFEREDS YLGREVTLDL SQYHAVAVRR VLNTESDLVN KFGVTDFPSC 250 260 270 280 290 300 YLLLRNGSVS RVPVLVESRS FYTSYLRGLP GLTRDAPPTT ATPVTADKIA PTVWKFADRS 310 320 330 340 350 360 KIYMADLESA LHYILRVEVG KFSVLEGQRL VALKKFVAVL AKYFPGQPLV QNFLHSINDW 370 380 390 400 410 420 LQKQQKKRIP YSFFKAALDS RKEDAVLTEK VNWVGCQGSE PHFRGFPCSL WVLFHFLTVQ 430 440 450 460 470 480 ANRYSEAHPQ EPADGQEVLQ AMRSYVQFFF GCRDCADHFE QMAAASMHQV RSPSNAILWL 490 500 510 520 530 540 WTSHNRVNAR LSGALSEDPH FPKVQWPPRE LCSACHNELN GQVPLWDLGA TLNFLKAHFS 550 560 PANIVIDSSA SRHTGRRGSP EATPELLL
	Isoform 4. Checksum: F13FDA0BC3335587	FASTA	154	16,624
	10 20 30 40 50 60 MRRCGRLSGP PSLLLLLLLL SPLLFSGPGA YAARLSVLYS SSDPLTLLDA DSVRPTVLGS 70 80 90 100 110 120 SSAWAVEFFA SWCGHCIAFA PTWKELANDV KDWRPALNLA VLDCAEETNS AVCREFNIAG 130 140 150 FPTVRVCEGG ATVEWFWPST QSSVPHFPGT FLGC

References

[1]	"Sulfhydryl oxidase (SOx) from mouse epidermis: molecular cloning, nucleotide sequence, and expression of recombinant protein in the cultured cells." Matsuba S., Suga Y., Ishidoh K., Hashimoto Y., Takamori K., Kominami E., Wilhelm B., Seitz J., Ogawa H. J. Dermatol. Sci. 30:50-62(2002) [PubMed: 12354420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). Strain: C57BL/6J and NOD. Tissue: Cerebellum, Liver and Spinal ganglion.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-538 (ISOFORM 3). Strain: C57BL/6 and FVB/N. Tissue: Eye and Salivary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB044284 mRNA. Translation: BAB21936.1. AK004880 mRNA. Translation: BAB23638.1. AK083938 mRNA. Translation: BAC39073.1. AK149465 mRNA. Translation: BAE28897.1. AK163119 mRNA. Translation: BAE37202.1. AK166839 mRNA. Translation: BAE39061.1. AK169877 mRNA. Translation: BAE41429.1. AK169920 mRNA. Translation: BAE41459.1. AK170449 mRNA. Translation: BAE41807.1. BC034131 mRNA. Translation: AAH34131.1. BC076590 mRNA. Translation: AAH76590.1.
IPI	IPI00223231. IPI00469211. IPI00788412. IPI00788476.
RefSeq	NP_001020116.1. NP_075757.1.
UniGene	Mm.27035
3D structure databases
HSSP	HSSP built from PDB template 2TRX based on UniProtKB P00274.
ModBase	Search...
PTM databases
PhosphoSite	Q8BND5.
Proteomic databases
PRIDE	Q8BND5.
Genome annotation databases
Ensembl	ENSMUSG00000033684. Mus musculus. [Contig view]
GeneID	104009.
KEGG	mmu:104009.
Organism-specific databases
MGI	MGI:1330818. Qsox1.
Phylogenomic databases
HOVERGEN	Q8BND5.
OMA	Q8BND5. CAEETNS.
Enzyme and pathway databases
BRENDA	1.8.3.2. 244.
Gene expression databases
ArrayExpress	Q8BND5.
Bgee	Q8BND5.
CleanEx	MM_QSOX1.
GermOnline	ENSMUSG00000033684. Mus musculus.
Family and domain databases
InterPro	IPR017905. ERV/ALR_sulphydryl_oxidase. IPR006863. Evr1_Alr. IPR017936. Thioredoxin-like. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:1.20.120.310. Evr1_Alr. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF04777. Evr1_Alr. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view]
PROSITE	PS51324. ERV_ALR. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	356343.
SOURCE	Search...

Entry information

Entry name

QSOX1_MOUSE

Accession

Primary (citable) accession number: Q8BND5
Secondary accession number(s): Q3TDY9 , Q3TE19, Q3TR29, Q3UEL4, Q8K041, Q9DBL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)