TMX1_HUMAN
ID TMX1_HUMAN Reviewed; 280 AA.
AC Q9H3N1; B2R7A4; Q8N487; Q8NBN5; Q9Y4T6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Thioredoxin-related transmembrane protein 1;
DE AltName: Full=Thioredoxin domain-containing protein 1;
DE AltName: Full=Transmembrane Trx-related protein;
DE Flags: Precursor;
GN Name=TMX1; Synonyms=TMX, TXNDC, TXNDC1; ORFNames=PSEC0085, UNQ235/PRO268;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DISULFIDE BOND, AND
RP MUTAGENESIS OF CYS-56 AND CYS-59.
RX PubMed=11152479; DOI=10.1074/jbc.m011037200;
RA Matsuo Y., Akiyama N., Nakamura H., Yodoi J., Noda M., Kizaka-Kondoh S.;
RT "Identification of a novel thioredoxin-related transmembrane protein.";
RL J. Biol. Chem. 276:10032-10038(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, and Hippocampus;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-270 AND SER-280, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-270 AND SER-280, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; SER-247; SER-270;
RP SER-274 AND SER-280, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP STRUCTURE BY NMR OF 30-142.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the thioredoxin-like domain of human
RT thioredoxin-related transmembrane protein.";
RL Submitted (NOV-2005) to the PDB data bank.
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 -!- INTERACTION:
CC Q9H3N1; Q92843: BCL2L2; NbExp=3; IntAct=EBI-1051115, EBI-707714;
CC Q9H3N1; P32246: CCR1; NbExp=3; IntAct=EBI-1051115, EBI-608322;
CC Q9H3N1; Q14318: FKBP8; NbExp=3; IntAct=EBI-1051115, EBI-724839;
CC Q9H3N1; O43681: GET3; NbExp=3; IntAct=EBI-1051115, EBI-2515857;
CC Q9H3N1; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-1051115, EBI-11991950;
CC Q9H3N1; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-1051115, EBI-6166686;
CC Q9H3N1; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-1051115, EBI-2820517;
CC Q9H3N1; Q01453: PMP22; NbExp=3; IntAct=EBI-1051115, EBI-2845982;
CC Q9H3N1; P00441: SOD1; NbExp=3; IntAct=EBI-1051115, EBI-990792;
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.
CC {ECO:0000269|PubMed:11152479}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in kidney, liver,
CC placenta and lung.
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DR EMBL; AB048246; BAB20629.1; -; mRNA.
DR EMBL; AY358640; AAQ89003.1; -; mRNA.
DR EMBL; AK075395; BAC11593.1; -; mRNA.
DR EMBL; AK312905; BAG35751.1; -; mRNA.
DR EMBL; AL080080; CAB45700.2; -; mRNA.
DR EMBL; AL591807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65678.1; -; Genomic_DNA.
DR EMBL; BC036460; AAH36460.1; -; mRNA.
DR EMBL; BC056874; AAH56874.2; -; mRNA.
DR CCDS; CCDS41953.1; -.
DR PIR; T12471; T12471.
DR RefSeq; NP_110382.3; NM_030755.4.
DR PDB; 1X5E; NMR; -; A=30-142.
DR PDBsum; 1X5E; -.
DR AlphaFoldDB; Q9H3N1; -.
DR SMR; Q9H3N1; -.
DR BioGRID; 123510; 208.
DR IntAct; Q9H3N1; 70.
DR MINT; Q9H3N1; -.
DR STRING; 9606.ENSP00000393316; -.
DR ChEMBL; CHEMBL4295941; -.
DR TCDB; 8.A.88.2.5; the calciquestrin (casq) family.
DR iPTMnet; Q9H3N1; -.
DR PhosphoSitePlus; Q9H3N1; -.
DR SwissPalm; Q9H3N1; -.
DR BioMuta; TMX1; -.
DR DMDM; 47117631; -.
DR EPD; Q9H3N1; -.
DR jPOST; Q9H3N1; -.
DR MassIVE; Q9H3N1; -.
DR MaxQB; Q9H3N1; -.
DR PaxDb; Q9H3N1; -.
DR PeptideAtlas; Q9H3N1; -.
DR PRIDE; Q9H3N1; -.
DR ProteomicsDB; 80733; -.
DR TopDownProteomics; Q9H3N1; -.
DR Antibodypedia; 163; 299 antibodies from 33 providers.
DR DNASU; 81542; -.
DR Ensembl; ENST00000457354.7; ENSP00000393316.2; ENSG00000139921.13.
DR GeneID; 81542; -.
DR KEGG; hsa:81542; -.
DR MANE-Select; ENST00000457354.7; ENSP00000393316.2; NM_030755.5; NP_110382.3.
DR UCSC; uc001wza.5; human.
DR CTD; 81542; -.
DR DisGeNET; 81542; -.
DR GeneCards; TMX1; -.
DR HGNC; HGNC:15487; TMX1.
DR HPA; ENSG00000139921; Low tissue specificity.
DR MIM; 610527; gene.
DR neXtProt; NX_Q9H3N1; -.
DR OpenTargets; ENSG00000139921; -.
DR PharmGKB; PA37968; -.
DR VEuPathDB; HostDB:ENSG00000139921; -.
DR eggNOG; KOG0913; Eukaryota.
DR GeneTree; ENSGT00940000155959; -.
DR HOGENOM; CLU_069292_2_1_1; -.
DR InParanoid; Q9H3N1; -.
DR OMA; WMIEFHA; -.
DR OrthoDB; 1481386at2759; -.
DR PhylomeDB; Q9H3N1; -.
DR TreeFam; TF106376; -.
DR PathwayCommons; Q9H3N1; -.
DR SignaLink; Q9H3N1; -.
DR BioGRID-ORCS; 81542; 16 hits in 1074 CRISPR screens.
DR ChiTaRS; TMX1; human.
DR EvolutionaryTrace; Q9H3N1; -.
DR GeneWiki; TMX1; -.
DR GenomeRNAi; 81542; -.
DR Pharos; Q9H3N1; Tbio.
DR PRO; PR:Q9H3N1; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9H3N1; protein.
DR Bgee; ENSG00000139921; Expressed in tibia and 216 other tissues.
DR ExpressionAtlas; Q9H3N1; baseline and differential.
DR Genevisible; Q9H3N1; HS.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
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 3D-structure; Disulfide bond; Electron transport; Endoplasmic reticulum;
KW Membrane; Phosphoprotein; Redox-active center; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..280
FT /note="Thioredoxin-related transmembrane protein 1"
FT /id="PRO_0000034153"
FT TOPO_DOM 27..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..132
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 218..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT DISULFID 56..59
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:11152479"
FT MUTAGEN 56
FT /note="C->S: Loss of reductase activity; when associated
FT with S-59."
FT /evidence="ECO:0000269|PubMed:11152479"
FT MUTAGEN 59
FT /note="C->S: Loss of reductase activity; when associated
FT with S-56."
FT /evidence="ECO:0000269|PubMed:11152479"
FT CONFLICT 14..16
FT /note="LVL -> MVP (in Ref. 8; AAH36460)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="T -> N (in Ref. 8; AAH36460)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="V -> A (in Ref. 4; BAC11593)"
FT /evidence="ECO:0000305"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1X5E"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1X5E"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1X5E"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:1X5E"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:1X5E"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1X5E"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1X5E"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1X5E"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:1X5E"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:1X5E"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1X5E"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:1X5E"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:1X5E"
SQ SEQUENCE 280 AA; 31791 MW; A57E222481A997DE CRC64;
MAPSGSLAVP LAVLVLLLWG APWTHGRRSN VRVITDENWR ELLEGDWMIE FYAPWCPACQ
NLQPEWESFA EWGEDLEVNI AKVDVTEQPG LSGRFIITAL PTIYHCKDGE FRRYQGPRTK
KDFINFISDK EWKSIEPVSS WFGPGSVLMS SMSALFQLSM WIRTCHNYFI EDLGLPVWGS
YTVFALATLF SGLLLGLCMI FVADCLCPSK RRRPQPYPYP SKKLLSESAQ PLKKVEEEQE
ADEEDVSEEE AESKEGTNKD FPQNAIRQRS LGPSLATDKS
