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FLASH GENE

Symbol

TXNDC17

contributors: mct - updated : 11-06-2021

HGNC name	thioredoxin domain containing 17
HGNC id	28218

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

DNA

TYPE	functioning gene
STRUCTURE	3.48 kb     4 Exon(s)

MAPPING

cloned

Y

linked

N

status

provisional

RNA

TRANSCRIPTS	type	messenger

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_032731 4 - 1917 NP_116120 13 123 - 2014 24778250

EXPRESSION

Type	ubiquitous

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Reproductive male system prostate     highly Respiratory respiratory tract larynx       Skin/Tegument skin         Urinary kidney

cell lineage

cell lines

fluid/secretion

at STAGE

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains

two active site Cys residues in its WCPDC motif, which is comparable to the WCGPC motif of thioredoxin (Trx)

HOMOLOGY

Homologene

FAMILY

thioredoxin family

CATEGORY

enzyme , signaling

SUBCELLULAR LOCALIZATION	extracellular
	intracellular
	intracellular,cytoplasm,cytosolic
	intracellular,cytoplasm,cytoskeleton

basic FUNCTION	disulfide reductase modulating TNF-alpha signaling pathways
	oxidoreductase activities of TXNDC17 complement those of TXN and must therefore be considered for the full understanding of enzymatic control of cellular thiols and nitrosothiols
	TXNDC17 is likely a member of the thioredoxin system dedicated to the control of cellular redox signalling pathways

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component

INTERACTION

DNA

RNA

small molecule

protein	interacting with TXN
	DYNLL1 binds IkappaBalpha in a redox-dependent manner and thereby prevents its phosphorylation by IKK, and TXNDC17contributes to this inhibitory activity by maintaining DYNLL1 in a reduced state
	inhibits the TNF-induced NFKB1 activation to a greater extent than TXN
	DYNLL1 was identified as a new target of disulfide reductase activity of TXNDC17, and DYNLL1 was shown to bind IkappaBalpha in a redox-dependent manner, thereby preventing its phosphorylation by IKBKB

cell & other

REGULATION

ASSOCIATED DISORDERS

ANIMAL & CELL MODELS