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Protein

Thioredoxin domain-containing protein 12

Gene

Txndc12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Possesses significant protein thiol-disulfide oxidase activity.By similarity

Catalytic activityi

2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Txndc12
Synonyms:Tlp19
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1913323. Txndc12.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424By similarityAdd
BLAST
Chaini25 – 170146Thioredoxin domain-containing protein 12PRO_0000034190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi64 ↔ 67Redox-activePROSITE-ProRule annotation
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9CQU0.
PaxDbiQ9CQU0.
PRIDEiQ9CQU0.

2D gel databases

REPRODUCTION-2DPAGEQ9CQU0.

PTM databases

PhosphoSiteiQ9CQU0.

Expressioni

Gene expression databases

BgeeiQ9CQU0.
GenevestigatoriQ9CQU0.

Interactioni

Protein-protein interaction databases

IntActiQ9CQU0. 6 interactions.
MINTiMINT-4137999.
STRINGi10090.ENSMUSP00000030296.

Structurei

3D structure databases

ProteinModelPortaliQ9CQU0.
SMRiQ9CQU0. Positions 28-161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi167 – 1704Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiNOG77442.
GeneTreeiENSGT00530000063273.
HOGENOMiHOG000231100.
HOVERGENiHBG107174.
InParanoidiQ9CQU0.
KOiK05360.
OMAiSYKYFYT.
OrthoDBiEOG7DNNX2.
PhylomeDBiQ9CQU0.
TreeFamiTF321449.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLRFGATCL LSFSFLLLIT SSDGRTGLGK GFGDHIHWRT LEDGKKEAAA
60 70 80 90 100
SGLPLMVIIH KSWCGACKAL KPKFAESTEI SELSHNFVMV NLEDEEEPRD
110 120 130 140 150
EDFSPDGGYI PRILFLDPSG KVRPEIINES GNPSYKYFYV SAEQVVQGMK
160 170
EAQERLTGDA FREKHFQDEL
Length:170
Mass (Da):19,049
Last modified:June 1, 2001 - v1
Checksum:i5B91FC9BE12C5E44
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY548113 mRNA. Translation: AAS55653.1.
AK003481 mRNA. Translation: BAB22811.1.
AK002862 mRNA. Translation: BAB22413.1.
BC006857 mRNA. Translation: AAH06857.1.
CCDSiCCDS18457.1.
RefSeqiNP_079610.1. NM_025334.3.
UniGeneiMm.159965.

Genome annotation databases

EnsembliENSMUST00000030296; ENSMUSP00000030296; ENSMUSG00000028567.
GeneIDi66073.
KEGGimmu:66073.
UCSCiuc008ubs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY548113 mRNA. Translation: AAS55653.1.
AK003481 mRNA. Translation: BAB22811.1.
AK002862 mRNA. Translation: BAB22413.1.
BC006857 mRNA. Translation: AAH06857.1.
CCDSiCCDS18457.1.
RefSeqiNP_079610.1. NM_025334.3.
UniGeneiMm.159965.

3D structure databases

ProteinModelPortaliQ9CQU0.
SMRiQ9CQU0. Positions 28-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CQU0. 6 interactions.
MINTiMINT-4137999.
STRINGi10090.ENSMUSP00000030296.

PTM databases

PhosphoSiteiQ9CQU0.

2D gel databases

REPRODUCTION-2DPAGEQ9CQU0.

Proteomic databases

MaxQBiQ9CQU0.
PaxDbiQ9CQU0.
PRIDEiQ9CQU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030296; ENSMUSP00000030296; ENSMUSG00000028567.
GeneIDi66073.
KEGGimmu:66073.
UCSCiuc008ubs.1. mouse.

Organism-specific databases

CTDi51060.
MGIiMGI:1913323. Txndc12.

Phylogenomic databases

eggNOGiNOG77442.
GeneTreeiENSGT00530000063273.
HOGENOMiHOG000231100.
HOVERGENiHBG107174.
InParanoidiQ9CQU0.
KOiK05360.
OMAiSYKYFYT.
OrthoDBiEOG7DNNX2.
PhylomeDBiQ9CQU0.
TreeFamiTF321449.

Miscellaneous databases

ChiTaRSiTxndc12. mouse.
NextBioi320548.
PROiQ9CQU0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQU0.
GenevestigatoriQ9CQU0.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTXD12_MOUSE
AccessioniPrimary (citable) accession number: Q9CQU0
Secondary accession number(s): Q53YN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.