Q8BXZ1 (TMX3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase TMX3
EC=5.3.4.1

Alternative name(s):
Thioredoxin domain-containing protein 10
Thioredoxin-related transmembrane protein 3

Gene names

Name:	Tmx3
Synonyms:	Kiaa1830, Txndc10

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase By similarity.
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.
Domain	The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins By similarity.
Post-translational modification	N-glycosylated By similarity.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 1 thioredoxin domain.
Sequence caution	The sequence BAC98261.1 differs from that shown. Reason: Erroneous initiation. The sequence BC057139 differs from that shown. Reason: Frameshift at position 176.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Redox-active center Signal Transmembrane Transmembrane helix
Molecular function	Isomerase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from electronic annotation. Source: EC protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 456	427	Protein disulfide-isomerase TMX3		PRO_0000034186
Regions
	Topological domain	30 – 378	349	Lumenal Potential
	Transmembrane	379 – 399	21	Helical; Potential
	Topological domain	400 – 456	57	Cytoplasmic Potential
	Domain	30 – 131	102	Thioredoxin
	Motif	453 – 456	4	Di-lysine motif
Amino acid modifications
	Modified residue	271	1	Phosphoserine By similarity
	Glycosylation	35	1	N-linked (GlcNAc...) Potential
	Glycosylation	261	1	N-linked (GlcNAc...) Potential
	Glycosylation	316	1	N-linked (GlcNAc...) Potential
	Disulfide bond	56 ↔ 59		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8BXZ1 [UniParc]. Last modified May 24, 2005. Version 2. Checksum: 7813FC587B35B88F	FASTA	456	51,848
	10 20 30 40 50 60 MANAVGRRSW AALRLCAAVI LLDLAVCKGF VEDLNESFKD NRKDDIWLVD FYAPWCGHCK 70 80 90 100 110 120 KLEPIWNEVG LEMKSIGSPV KVGKMDATSY SSIASEFGVR GYPTIKLLKG DLAYNYRGPR 130 140 150 160 170 180 TKDDIIEFAH RVSGALIRPL PSQQMFDHVR KRHRVFFVYI GGESPLKEKY IDAASELIVY 190 200 210 220 230 240 TYFFSASEDV VPEYVTLKEM PAVLVFKDDT YFVYDEYEDG DLSSWISRER FQNYLTMDGF 250 260 270 280 290 300 LLYELGDTGK LVAIAVIDEK NTSLEHTRLK SIIQEVARDF RDHFHRDFQF GHMDGNDYIN 310 320 330 340 350 360 TLLMDELTVP TIVVLNTSNQ QYFLLDRHIK DASDMVQFIN SILDGTVPAQ GGDSIFQRLK 370 380 390 400 410 420 RIVFDAKSTI VSIFKSSPLM GCFLFGLPLG VISIMCYGIY TADTDGGYIE ERYEVSKSEM 430 440 450 ENQEQIEESK EQESSSGGSL APTVQEPKDV LEKKKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed: 14621295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryonic tail.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum and Corpus striatum.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[4]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 132-150 AND 368-375, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK129451 mRNA. Translation: BAC98261.1. Different initiation. AK035946 mRNA. Translation: BAC29254.1. AK042787 mRNA. Translation: BAC31366.2. AK140709 mRNA. Translation: BAE24450.1. BC057139 mRNA. No translation available.
IPI	IPI00453798.
RefSeq	NP_938037.2. NM_198295.2.
UniGene	Mm.268041.
3D structure databases
ProteinModelPortal	Q8BXZ1.
SMR	Q8BXZ1. Positions 28-230.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BXZ1.
PTM databases
PhosphoSite	Q8BXZ1.
Proteomic databases
PRIDE	Q8BXZ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025515; ENSMUSP00000025515; ENSMUSG00000024614.
GeneID	67988.
KEGG	mmu:67988.
UCSC	uc008fvt.1. mouse.
Organism-specific databases
CTD	54495.
MGI	MGI:2442418. Tmx3.
Rouge	Search...
Phylogenomic databases
eggNOG	roNOG10254.
GeneTree	ENSGT00590000082864.
InParanoid	Q8BXZ1.
OMA	CYGICTA.
OrthoDB	EOG444KKF.
Gene expression databases
ArrayExpress	Q8BXZ1.
Bgee	Q8BXZ1.
CleanEx	MM_TXNDC10.
Genevestigator	Q8BXZ1.
GermOnline	ENSMUSG00000024614. Mus musculus.
Family and domain databases
InterPro	IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K09585.
Pfam	PF00085. Thioredoxin. 1 hit. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 2 hits.
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	326146.
SOURCE	Search...

Entry information

Entry name

TMX3_MOUSE

Accession

Primary (citable) accession number: Q8BXZ1
Secondary accession number(s): Q3US84 , Q6PGA1, Q6ZPH5, Q8BZB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2005
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program