Quiescin-sulfhydryl Oxidase-like

Contact: Norma Houston
Organization: North Carolina State University
Website: http://www.ncsu.edu/
Source: Norma L. Houston, Chuanzhu Fan, Qiu-Yun Xiang, Jan-Michael Schulze, Rudolf Jung, and Rebecca S. Boston (2005) Phylogenetic Analyses Identify 10 Classes of the Protein Disulfide Isomerase Family in Plants, Including Single-Domain Protein Disulfide Isomerase-Related Proteins. Plant Physiology 137: 762-778
Criteria: Thioredoxin domains from PDIL amino acid alignments formed a distinct, well-supported clade within the thioredoxin gene family. The QSOXL subfamily designation was given to members based on amino acid sequence homology to proteins with quiescin-sulfhydryl oxidase activity in other species (Thorpe et al., 2002). Members of the QSOXL subfamily, in addition to a TRX domain, possess an Erv1-like domain that has been independently implicated in cellular redox processes (Lange et al., 2001).


Gene Name: OsQSOXL1
Gene Description: Oryza sativa quiescin-sulfhydryl oxidase-like (OsQSOXL1)
MSU Annotation: OsQSOXL1 quiescin-sulfhydryl oxidase-like OsQSOXL1, expressed
GenBank Protein Acc: AAT85195
Comment: AK121660
Predicted Localization1: S'
Domain Composition2: thioredoxin
Domain Composition2:Evr1_Alr
Structural Annotation:  


1 S, Secretory pathway assignment by TargetP; (Emanuelsson et al., 2000) reliability value 0.6; S', secretory pathway assignment reliability value <0.6; O, other localization predicted.

2 Domains predicted by CDD (Conserved Domain Database) followed by number of each domain

Lange H, Lisowsky T, Gerber J, Muhlenhoff U, Kispal G, Lill R (2001) An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO J 2: 715-720

Thorpe C, Hoober KL, Raje S, Glynn NM , Burnside J, Turi GK, Coppock DL (2002) Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Arch Biochem Biophys 405: 1-12

NSF Logo This work is supported by grants (DBI-0321538/DBI-0834043) from the National Science Foundation.