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UniProtKB/Swiss-Prot entry Q9CQU0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TXD12_MOUSE
Primary accession number Q9CQU0
Secondary accession number Q53YN1
Integrated into Swiss-Prot on April 11, 2003
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 54)
Name and origin of the protein
Protein name Thioredoxin domain-containing protein 12 [Precursor]
Synonyms EC 1.8.4.2
Thioredoxin-like protein p19
Endoplasmic reticulum protein ERp19
Gene name
Name: Txndc12
Synonyms: Tlp19
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Embryo;
DOI=10.1074/mcp.M300053-MCP200; PubMed=12930873 [NCBI, ExPASy, EBI, Israel, Japan]
Knoblach B., Keller B.O., Groenendyk J., Aldred S., Zheng J., Lemire B.D., Li L., Michalak M.;
"ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins.";
Mol. Cell. Proteomics 2:1104-1119(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Embryo, and Kidney;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY548113; AAS55653.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK003481; BAB22811.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002862; BAB22413.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006857; AAH06857.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_079610.1; -.
UniGene Mm.159965
3D structure databases
SMR Q9CQU0; 28-161.
ModBase Q9CQU0.
2D gel databases
REPRODUCTION-2DPAGE Q9CQU0; -.
Organism-specific databases
MGI MGI:1913323; Txndc12.
Gene expression databases
ArrayExpress Q9CQU0; -.
Ontologies
GO
GO:0005788; Cellular component: endoplasmic reticulum lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0019153; Molecular function: protein-disulfide reductase (glutathione) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR000886; ER_targeting_sequence.
IPR006662; Thioredoxin-like.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
PROSITE PS00014; ER_TARGET; 1.
PS00194; THIOREDOXIN_1; 1.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9CQU0.
Genome annotation databases
Ensembl ENSMUSG00000028567; Mus musculus. [Contig view]
GeneID 66073; -.
KEGG mmu:66073; -.
Phylogenomic databases
HOGENOM Q9CQU0; -.
HOVERGEN Q9CQU0; -.
Other
SOURCE Txndc12; Mus musculus.
ProtoNet Q9CQU0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; Glycoprotein; Oxidoreductase; Redox-active center; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    24  24     By similarity. 
CHAIN   25   170  146     Thioredoxin domain-containing protein 12. PRO_0000034190
MOTIF   167   170  4     Prevents secretion from ER (Potential). 
CARBOHYD   128   128        N-linked (GlcNAc...) (Potential). 
DISULFID   64    67        Redox-active (Potential). 
Sequence information
Length: 170 AA [This is the length of the unprocessed precursor] Molecular weight: 19049 Da [This is the MW of the unprocessed precursor] CRC64: 5B91FC9BE12C5E44 [This is a checksum on the sequence]
        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 

Q9CQU0 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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