Q6AX23 (QSOX2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfhydryl oxidase 2
EC=1.8.3.2

Alternative name(s):
Quiescin Q6-like protein 1

Gene names

Name:	qsox2
Synonyms:	qscn6l1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	661 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	2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2.
Cofactor	Binds 1 FAD per subunit Potential.
Subcellular location	Membrane; Single-pass membrane protein Potential.
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	Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	thiol oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 661	632	Sulfhydryl oxidase 2		PRO_0000249540
Regions
	Transmembrane	625 – 645	21	Helical; Potential
	Domain	30 – 155	126	Thioredoxin
	Domain	400 – 509	110	ERV/ALR sulfhydryl oxidase
	Nucleotide binding	484 – 491	8	FAD By similarity
	Compositional bias	642 – 647	6	Poly-Phe
Sites
	Active site	67	1	Nucleophile By similarity
	Active site	70	1	Nucleophile By similarity
	Binding site	405	1	FAD By similarity
	Binding site	412	1	FAD By similarity
	Binding site	416	1	FAD By similarity
	Binding site	457	1	FAD By similarity
	Binding site	461	1	FAD By similarity
	Binding site	506	1	FAD By similarity
	Binding site	509	1	FAD By similarity
Amino acid modifications
	Glycosylation	53	1	N-linked (GlcNAc...) Potential
	Glycosylation	390	1	N-linked (GlcNAc...) Potential
	Disulfide bond	67 ↔ 70		Redox-active By similarity
	Disulfide bond	397 ↔ 409		By similarity
	Disulfide bond	455 ↔ 458		By similarity
	Disulfide bond	515 ↔ 518		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6AX23 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 6D2CF79098B20188	FASTA	661	75,121
	10 20 30 40 50 60 MAAFVGLPLR SVPMLLLLLL LVVAGTARGE TLYGPEDSVT ILNKESVARA VFNSSSAWLL 70 80 90 100 110 120 EFYSSWCGHC INYAPTWKAL ARDVRDWEPA IKIGVLDCAE EDNYGACKDF GVTLYPTFRF 130 140 150 160 170 180 FKAFTKEFTQ GENYKAVGDR EIQTVRQVII DFLQTSPAES KPQAWPSLEP ISSSEISSLL 190 200 210 220 230 240 TPKQSHYTAI IFESEESYEG REVILDLIQY SNIVVRRALP SDKPILEKLG IGSVPSCYLI 250 260 270 280 290 300 QPNGLHGLIN DVKSIRSQLS LHLKALSNVR KLLPSETAHS GLSKGVQQED TTMNQFDRSK 310 320 330 340 350 360 LYMTDLESGL HYILRAELAN HHTLEGEKLK TFKDFVTILY KLFPGRPHVM KLLETLQEWL 370 380 390 400 410 420 VSMPLDTIPY DAILDLVNNK MRISGIFLTN HTQWVGCRGS KSNLRGYPCS LWKLFHSLTV 430 440 450 460 470 480 QAAVKPDALA NTAFEAEPRA VLQTMRRYIR EFFGCRECAK HFEAMAKETV DSVKTPDQAI 490 500 510 520 530 540 LWLWRKHNVV NNRLSGAPSE DPKFPKVQWP TSDLCSACHS QTGGVHSWNE DEVLAFLKRY 550 560 570 580 590 600 YGNQEISLEF ADPRKDLSEA ATDNGNKEPH FTKKPQERDY VKKQNPQFLD KLVQKKPEKS 610 620 630 640 650 660 LDSEAAESSQ SVSFLGIGFS NIDMSLCVIL YVTSSLFLMI MFFFFRFRSK RWKVRYNRPF V

References

[1]	NIH - Xenopus Gene Collection (XGC) project Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC079798 mRNA. Translation: AAH79798.1.
RefSeq	NP_001087446.1. NM_001093977.1.
UniGene	Xl.77047.
3D structure databases
HSSP	HSSP built from PDB template 1MEK based on UniProtKB P07237.
ProteinModelPortal	Q6AX23.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	447270.
KEGG	xla:447270.
Organism-specific databases
CTD	169714.
Xenbase	XB-GENE-986401. qsox2.
Phylogenomic databases
HOVERGEN	HBG080360.
Family and domain databases
InterPro	IPR017905. ERV/ALR_sulphydryl_oxidase. IPR006863. Evr1_Alr. IPR012336. Thioredoxin-like_fold. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:1.20.120.310. Evr1_Alr. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K10758.
Pfam	PF04777. Evr1_Alr. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view]
SUPFAM	SSF69000. Evr1_Alr. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS51324. ERV_ALR. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

QSOX2_XENLA

Accession

Primary (citable) accession number: Q6AX23

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	September 13, 2004
Last modified:	November 16, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program