TXD12_MOUSE
ID TXD12_MOUSE Reviewed; 170 AA.
AC Q9CQU0; Q53YN1;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Thioredoxin domain-containing protein 12 {ECO:0000250|UniProtKB:O95881};
DE EC=1.8.4.2 {ECO:0000250|UniProtKB:O95881};
DE AltName: Full=Endoplasmic reticulum resident protein 19;
DE Short=ER protein 19 {ECO:0000303|PubMed:12930873};
DE Short=ERp19 {ECO:0000303|PubMed:12930873};
DE AltName: Full=Thioredoxin-like protein p19;
DE Flags: Precursor;
GN Name=Txndc12 {ECO:0000312|MGI:MGI:1913323}; Synonyms=Tlp19;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=12930873; DOI=10.1074/mcp.m300053-mcp200;
RA Knoblach B., Keller B.O., Groenendyk J., Aldred S., Zheng J., Lemire B.D.,
RA Li L., Michalak M.;
RT "ERp19 and ERp46, new members of the thioredoxin family of endoplasmic
RT reticulum proteins.";
RL Mol. Cell. Proteomics 2:1104-1119(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protein-disulfide reductase of the endoplasmic reticulum that
CC promotes disulfide bond formation in client proteins through its thiol-
CC disulfide oxidase activity. {ECO:0000250|UniProtKB:O95881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + 2 glutathione = [protein]-dithiol +
CC glutathione disulfide; Xref=Rhea:RHEA:21064, Rhea:RHEA-COMP:10593,
CC Rhea:RHEA-COMP:10594, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.8.4.2;
CC Evidence={ECO:0000250|UniProtKB:O95881};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21066;
CC Evidence={ECO:0000250|UniProtKB:O95881};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:12930873}.
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DR EMBL; AY548113; AAS55653.1; -; mRNA.
DR EMBL; AK003481; BAB22811.1; -; mRNA.
DR EMBL; AK002862; BAB22413.1; -; mRNA.
DR EMBL; BC006857; AAH06857.1; -; mRNA.
DR CCDS; CCDS18457.1; -.
DR RefSeq; NP_079610.1; NM_025334.3.
DR AlphaFoldDB; Q9CQU0; -.
DR SMR; Q9CQU0; -.
DR BioGRID; 211195; 6.
DR IntAct; Q9CQU0; 2.
DR STRING; 10090.ENSMUSP00000030296; -.
DR GlyConnect; 2763; 1 N-Linked glycan (1 site).
DR GlyGen; Q9CQU0; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9CQU0; -.
DR PhosphoSitePlus; Q9CQU0; -.
DR SwissPalm; Q9CQU0; -.
DR REPRODUCTION-2DPAGE; Q9CQU0; -.
DR EPD; Q9CQU0; -.
DR jPOST; Q9CQU0; -.
DR MaxQB; Q9CQU0; -.
DR PaxDb; Q9CQU0; -.
DR PeptideAtlas; Q9CQU0; -.
DR PRIDE; Q9CQU0; -.
DR ProteomicsDB; 298038; -.
DR Antibodypedia; 46886; 142 antibodies from 20 providers.
DR DNASU; 66073; -.
DR Ensembl; ENSMUST00000030296; ENSMUSP00000030296; ENSMUSG00000028567.
DR GeneID; 66073; -.
DR KEGG; mmu:66073; -.
DR UCSC; uc008ubs.1; mouse.
DR CTD; 51060; -.
DR MGI; MGI:1913323; Txndc12.
DR VEuPathDB; HostDB:ENSMUSG00000028567; -.
DR eggNOG; ENOG502RXP1; Eukaryota.
DR GeneTree; ENSGT00530000063273; -.
DR HOGENOM; CLU_088048_2_0_1; -.
DR InParanoid; Q9CQU0; -.
DR OMA; DIAWVKW; -.
DR OrthoDB; 1382017at2759; -.
DR PhylomeDB; Q9CQU0; -.
DR TreeFam; TF321449; -.
DR BioGRID-ORCS; 66073; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Txndc12; mouse.
DR PRO; PR:Q9CQU0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9CQU0; protein.
DR Bgee; ENSMUSG00000028567; Expressed in placenta labyrinth and 257 other tissues.
DR Genevisible; Q9CQU0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; ISS:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR CDD; cd02959; ERp19; 1.
DR InterPro; IPR037462; ERp19.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Oxidoreductase;
KW Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:O95881"
FT CHAIN 25..170
FT /note="Thioredoxin domain-containing protein 12"
FT /id="PRO_0000034190"
FT MOTIF 167..170
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..67
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 170 AA; 19049 MW; 5B91FC9BE12C5E44 CRC64;
MSLRFGATCL LSFSFLLLIT SSDGRTGLGK GFGDHIHWRT LEDGKKEAAA SGLPLMVIIH
KSWCGACKAL KPKFAESTEI SELSHNFVMV NLEDEEEPRD EDFSPDGGYI PRILFLDPSG
KVRPEIINES GNPSYKYFYV SAEQVVQGMK EAQERLTGDA FREKHFQDEL
