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Q9CQU0 (TXD12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin domain-containing protein 12

EC=1.8.4.2
Alternative name(s):
Endoplasmic reticulum resident protein 19
Short name=ER protein 19
Short name=ERp19
Thioredoxin-like protein p19
Gene names
Name:Txndc12
Synonyms:Tlp19
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length170 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentEndoplasmic reticulum
   DomainRedox-active center
Signal
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein-disulfide reductase (glutathione) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 170146Thioredoxin domain-containing protein 12
PRO_0000034190

Regions

Motif167 – 1704Prevents secretion from ER Potential

Amino acid modifications

Glycosylation1281N-linked (GlcNAc...) Potential
Disulfide bond64 ↔ 67Redox-active Potential

Sequences

Sequence LengthMass (Da)Tools
Q9CQU0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5B91FC9BE12C5E44

FASTA17019,049
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY548113 mRNA. Translation: AAS55653.1.
AK003481 mRNA. Translation: BAB22811.1.
AK002862 mRNA. Translation: BAB22413.1.
BC006857 mRNA. Translation: AAH06857.1.
CCDSCCDS18457.1.
RefSeqNP_079610.1. NM_025334.3.
UniGeneMm.159965.

3D structure databases

ProteinModelPortalQ9CQU0.
SMRQ9CQU0. Positions 28-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9CQU0. 6 interactions.
MINTMINT-4137999.
STRING10090.ENSMUSP00000030296.

PTM databases

PhosphoSiteQ9CQU0.

2D gel databases

REPRODUCTION-2DPAGEQ9CQU0.

Proteomic databases

MaxQBQ9CQU0.
PaxDbQ9CQU0.
PRIDEQ9CQU0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030296; ENSMUSP00000030296; ENSMUSG00000028567.
GeneID66073.
KEGGmmu:66073.
UCSCuc008ubs.1. mouse.

Organism-specific databases

CTD51060.
MGIMGI:1913323. Txndc12.

Phylogenomic databases

eggNOGNOG77442.
GeneTreeENSGT00530000063273.
HOGENOMHOG000231100.
HOVERGENHBG107174.
InParanoidQ9CQU0.
KOK05360.
OMASYKYFYT.
OrthoDBEOG7DNNX2.
PhylomeDBQ9CQU0.
TreeFamTF321449.

Gene expression databases

BgeeQ9CQU0.
GenevestigatorQ9CQU0.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTXNDC12. mouse.
NextBio320548.
PROQ9CQU0.
SOURCESearch...

Entry information

Entry nameTXD12_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot