Reviewed, UniProtKB/Swiss-Prot Q9CQU0 (TXD12_MOUSE)

Names and origin

Protein names

Recommended name:
    Thioredoxin domain-containing protein 12
    EC=1.8.4.2
Alternative name(s):
    Thioredoxin-like protein p19
    Endoplasmic reticulum protein ERp19

Gene names

Name:	Txndc12
Synonyms:	Tlp19

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

Protein attributes

Sequence length	170 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Possesses significant protein thiol-disulfide oxidase activity By similarity.
Catalytic activity	2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol.
Subcellular location	Endoplasmic reticulum lumen. Ref.1
Sequence similarities	Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Redox-active center Signal
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein-disulfide reductase (glutathione) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	By similarity
	Chain	25 – 170	146	Thioredoxin domain-containing protein 12		PRO_0000034190
Regions
	Motif	167 – 170	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	128	1	N-linked (GlcNAc...) Potential
	Disulfide bond	64 ↔ 67		Redox-active Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9CQU0-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 5B91FC9BE12C5E44	FASTA	170	19,049
	10 20 30 40 50 60 MSLRFGATCL LSFSFLLLIT SSDGRTGLGK GFGDHIHWRT LEDGKKEAAA SGLPLMVIIH 70 80 90 100 110 120 KSWCGACKAL KPKFAESTEI SELSHNFVMV NLEDEEEPRD EDFSPDGGYI PRILFLDPSG 130 140 150 160 170 KVRPEIINES GNPSYKYFYV SAEQVVQGMK EAQERLTGDA FREKHFQDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins." Knoblach B., Keller B.O., Groenendyk J., Aldred S., Zheng J., Lemire B.D., Li L., Michalak M. Mol. Cell. Proteomics 2:1104-1119(2003) [PubMed: 12930873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Tissue: Embryo.
[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: Embryo and Kidney.
[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]. Tissue: Mammary gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY548113 mRNA. Translation: AAS55653.1. AK003481 mRNA. Translation: BAB22811.1. AK002862 mRNA. Translation: BAB22413.1. BC006857 mRNA. Translation: AAH06857.1.
IPI	IPI00133110.
RefSeq	NP_079610.1.
UniGene	Mm.159965
3D structure databases
SMR	Q9CQU0. Positions 28-161.
ModBase	Search...
2-D gel databases
REPRODUCTION-2DPAGE	Q9CQU0.
Proteomic databases
PRIDE	Q9CQU0.
Genome annotation databases
Ensembl	ENSMUSG00000028567. Mus musculus. [Contig view]
GeneID	66073.
KEGG	mmu:66073.
Organism-specific databases
MGI	MGI:1913323. Txndc12.
Phylogenomic databases
HOGENOM	Q9CQU0.
HOVERGEN	Q9CQU0.
OMA	Q9CQU0. CHACKAL.
Enzyme and pathway databases
BRENDA	1.8.4.2. 244.
Gene expression databases
ArrayExpress	Q9CQU0.
Bgee	Q9CQU0.
Family and domain databases
InterPro	IPR000886. ER_targeting_sequence. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	320548.
SOURCE	Search...

Entry information

Entry name

TXD12_MOUSE

Accession

Primary (citable) accession number: Q9CQU0
Secondary accession number(s): Q53YN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)