UniProt ID: Q6PBT5 |
FUNCTION: Probable FAD-dependent oxidoreductase; involved in the cellular oxidative stress response (By similarity). Required for normal sarcomere structure and muscle fiber integrity (PubMed:27745833). {ECO:0000250|UniProtKB:Q8WU10, ECO:0000269|PubMed:27745833}. COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O52582}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O52582}; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27745833}. Cytoplasm {ECO:0000269|PubMed:27745833}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:27745833}. DISRUPTION PHENOTYPE: Morpholino-injected embryos show severe disruption of the musculature with fragmentation of the muscle fibers, altered sarcomeric structure, loss of fiber integrity and accumulation of actin at the myosepta (PubMed:27745833). Disintegration of the myofibrils with mitochondrial infiltration of the resulting space, loss of Z-disk structures, and electron dense, nemaline-like bodies are observed by electron microscopy (PubMed:27745833). {ECO:0000269|PubMed:27745833}. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. PYROXD1 subfamily. {ECO:0000305}. |
UniProt ID: A0A0R4IEM7 |
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974}; SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000256|ARBA:ARBA00004204}. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. PYROXD1 subfamily. {ECO:0000256|ARBA:ARBA00008147}. |
This information was provided by UniProt through a collaboration with ZFIN. (1) |