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TMX1_MOUSE
ID   TMX1_MOUSE              Reviewed;         278 AA.
AC   Q8VBT0; Q3UCI8; Q9CSD5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Thioredoxin-related transmembrane protein 1;
DE   AltName: Full=Thioredoxin domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Tmx1; Synonyms=Txndc, Txndc1;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Embryo, Pancreatic islet, and Pituitary;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland, and Retina;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP   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: May participate in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide and
CC       catalyze dithiol-disulfide exchange reactions.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC       {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC       Note=Predominantly found in the endoplasmic reticulum. {ECO:0000250}.
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DR   EMBL; AK013150; BAB28680.3; -; mRNA.
DR   EMBL; AK030429; BAC26960.1; -; mRNA.
DR   EMBL; AK050567; BAC34326.1; -; mRNA.
DR   EMBL; AK137059; BAE23223.1; -; mRNA.
DR   EMBL; AK150511; BAE29624.1; -; mRNA.
DR   EMBL; AK153027; BAE31660.1; -; mRNA.
DR   EMBL; AK170468; BAE41816.1; -; mRNA.
DR   EMBL; BC017603; AAH17603.1; -; mRNA.
DR   EMBL; BC021533; AAH21533.1; -; mRNA.
DR   CCDS; CCDS25958.1; -.
DR   RefSeq; NP_082615.1; NM_028339.1.
DR   AlphaFoldDB; Q8VBT0; -.
DR   SMR; Q8VBT0; -.
DR   BioGRID; 215541; 3.
DR   IntAct; Q8VBT0; 4.
DR   MINT; Q8VBT0; -.
DR   STRING; 10090.ENSMUSP00000021471; -.
DR   iPTMnet; Q8VBT0; -.
DR   PhosphoSitePlus; Q8VBT0; -.
DR   SwissPalm; Q8VBT0; -.
DR   EPD; Q8VBT0; -.
DR   jPOST; Q8VBT0; -.
DR   MaxQB; Q8VBT0; -.
DR   PaxDb; Q8VBT0; -.
DR   PeptideAtlas; Q8VBT0; -.
DR   PRIDE; Q8VBT0; -.
DR   ProteomicsDB; 259443; -.
DR   Antibodypedia; 163; 299 antibodies from 33 providers.
DR   DNASU; 72736; -.
DR   Ensembl; ENSMUST00000021471; ENSMUSP00000021471; ENSMUSG00000021072.
DR   GeneID; 72736; -.
DR   KEGG; mmu:72736; -.
DR   UCSC; uc007ntu.1; mouse.
DR   CTD; 81542; -.
DR   MGI; MGI:1919986; Tmx1.
DR   VEuPathDB; HostDB:ENSMUSG00000021072; -.
DR   eggNOG; KOG0913; Eukaryota.
DR   GeneTree; ENSGT00940000155959; -.
DR   HOGENOM; CLU_069292_2_1_1; -.
DR   InParanoid; Q8VBT0; -.
DR   OMA; WMIEFHA; -.
DR   OrthoDB; 1481386at2759; -.
DR   PhylomeDB; Q8VBT0; -.
DR   TreeFam; TF106376; -.
DR   BioGRID-ORCS; 72736; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Tmx1; mouse.
DR   PRO; PR:Q8VBT0; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8VBT0; protein.
DR   Bgee; ENSMUSG00000021072; Expressed in pigmented layer of retina and 257 other tissues.
DR   ExpressionAtlas; Q8VBT0; baseline and differential.
DR   Genevisible; Q8VBT0; MM.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; ISO:MGI.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Electron transport; Endoplasmic reticulum; Membrane;
KW   Phosphoprotein; Redox-active center; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..278
FT                   /note="Thioredoxin-related transmembrane protein 1"
FT                   /id="PRO_0000034154"
FT   TOPO_DOM        27..181
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        203..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..132
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          217..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17208939,
FT                   ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3N1"
FT   DISULFID        56..59
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   278 AA;  31396 MW;  EB682243008E3333 CRC64;
     MAHLGRLMVP LAALVLLLWA VPGAHGRRNN VRVLTDENWT SLLEGEWMIE FYAPWCPACQ
     NLQPEWESFA EWGEDLEVKV AKVDVTEQTG LSGRFIITAL PSIYHCKDGE FRRYVGPRTK
     KDFINFVSDK EWKNIEPISS WFGPSSVLMT MMSALFQLSV YIRTSHSYFV HDLGIPAWGS
     YLVFAFATVL SGLLLGLCMI FVADCLCPSK RRKPQQQYAK KTSPEFSQPL KKVEEEQEAD
     EEDVSEEEAE DREGASKATS QSSIRQRCVG LPSATDTS
 
 
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