RNAiDB Tree View

Gene: F53G12.3

F53G12.3	SMap	S_parent	Sequence	F53G12
	Chromosome	I
	Identity (5)
	Gene_info	Allele	snp_F53G12[14]
		GO_term (5)
		Structured_description	Provisional_description	F53G12.3 encodes a large partial homolog of dual oxidase ('Ce-Duox2'), with an N-terminal peroxidase domain, two central calmodulin-binding EF hands, and a C-terminal superoxide-generating NADPH-oxidase domain; F53G12.3 may be required for dityrosine cross-linking of collagen, and thus for cuticular integrity; F53G12.3 may use cytosolic NADPH to generate reactive oxygen, which then may drive the peroxidase ectodomain to cross-link free tyrosine in collagen; F53G12.3 has no visible expression pattern detectable by antibodies, implying very low or rare expression.	Paper_evidence	WBPaper00004841
					Person_evidence	WBPerson567
					Curator_confirmed	WBPerson567
					Date_last_updated	17 Jun 2004 00:00:00
				Joint inactivation of F53G12.3 and its close paralog bli-3 (F56C11.1) caused blistered and dumpy phenotypes reminiscent of those seen for collagen mutations, along with abnormally clear bodies, defective egg-laying, and strong paralysis; in electron micrographs of [bli-3 + F53G12.3](RNAi) animals, the fine structure of the cuticle is grossly defective.
				Moroever, dityrosine and trityrosine are absent from hydrolysates of [bli-3 + F53G12.3](RNAi) animals, implying a requirement for bli-3 and perhaps F53G12.3 for dityrosine and trityrosine cross-linkages of collagen.
				F53G12.3 is homologous to human DUOX1 (OMIM:606758) and DUOX2 (OMIM:606759), and to Drosophila CG3131; F53G12.3 is 91% identical to its paralog bli-3; F53G12.3 has an N-terminal signal peptide sequence, implying that its N-terminal peroxidase domain is extracellular or in a cellular compartment.
			Concise_description	F53G12.3 encodes a large partial homolog of dual oxidase ('Ce-Duox2'), with an N-terminal peroxidase domain, two central calmodulin-binding EF hands, and a C-terminal superoxide-generating NADPH-oxidase domain; F53G12.3 may be required for dityrosine cross-linking of collagen, and thus for cuticular integrity; F53G12.3 may use cytosolic NADPH to generate reactive oxygen, which then may drive the peroxidase ectodomain to cross-link free tyrosine in collagen; F53G12.3 has no visible expression pattern detectable by antibodies, implying very low or rare expression.
	Molecular_info (5)
	Experimental_info	RNAi_result	Cenix:244-d7
			JA:F53G12.3
			Simmer:F53G12.3:Screen_A
			Simmer:F53G12.3:Screen_B
		WB_RNAi_result (9)
	Method	Gene