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FLASH GENE

Symbol

TMX4

contributors: mct - updated : 14-11-2019

HGNC name	thioredoxin-related transmembrane protein 4
HGNC id	25237

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

RNA

TRANSCRIPTS	type	messenger

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_021156 8 - 2368 NP_066979 38 349 - 2010 20056998

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 Cardiovascular heart       highly Homo sapiens   vessel       highly Homo sapiens Digestive liver       highly Homo sapiens Reproductive male system testis     highly Homo sapiens Urinary kidney       highly Homo sapiens Visual eye       moderately Homo sapiens

tissue

System Tissue Tissue level 1 Tissue level 2 Level Pubmed Species Stage Rna symbol Nervous peripherous       Homo sapiens

cell lineage

cell lines

fluid/secretion

at STAGE

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains	a single ER-luminal thioredoxin-like domain, which, in contrast with similar domains in other PDIs, is mainly oxidized in living cells
	a Trx-like domain that faced the ER lumen, with N-glycosylation site
	an RQR motif in the TMX4 cytosolic domain was reported to be essential for its ER localization because the deletion of RQR motif caused the transport of TMX4 to the cell surface
	a typical C-terminal di-lysine retrieval signal, in the cytosol
	the cytoplasmic tail has a conserved di-arginine motif of the RXR type

HOMOLOGY

Homologene

FAMILY

thioredoxin family, PDI family

CATEGORY

transport

SUBCELLULAR LOCALIZATION	plasma membrane
	intracellular
	intracellular,cytoplasm,organelle,membrane
	intracellular,cytoplasm,organelle,endoplasmic reticulum
	intracellular,nuclear envelope,int
text	integral to membrane
	type I membrane protein
	N-glycosylated type I membrane protein that localizes to the ER
	localize to the ER
	MFSD10, TMX4, and ARL6IP6 likely residing in the inner nuclear membrane

basic FUNCTION	acting as a redox-active center
	N-glycosylated type I membrane protein that localizes to the ER
	could work as a reductase in the environment of the ER
	role of TMX4 may be to enable protein folding in cooperation with these proteins consisting of folding complex in the ER
	involved in productive folding together with calnexin and PDIA3
	would be a reductase in the ER

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

electron transport

PATHWAY

metabolism

signaling

a component

INTERACTION

DNA

RNA

small molecule

protein

interacts with calnexin, suggesting the possible involvement of TMX4 as a reductase in cooperation with TMX1 or PDIA3 in the calnexin folding complex

cell & other

REGULATION

ASSOCIATED DISORDERS

corresponding disease(s)

Other morbid association(s)

Type Gene Modification Chromosome rearrangement Protein expression Protein Function tumoral     --over   in melanoma cells

Susceptibility

Variant & Polymorphism

Candidate gene

Marker

Therapy target

ANIMAL & CELL MODELS