Full text data of TMX1
TMX1
(TMX, TXNDC, TXNDC1)
[Confidence: high (present in two of the MS resources)]
Thioredoxin-related transmembrane protein 1 (Thioredoxin domain-containing protein 1; Transmembrane Trx-related protein; Flags: Precursor)
Thioredoxin-related transmembrane protein 1 (Thioredoxin domain-containing protein 1; Transmembrane Trx-related protein; Flags: Precursor)
hRBCD
IPI00395887
IPI00395887 Thioredoxin domain containing protein 1 precursor Protein disulfide-isomerase A6 precursor Thioredoxin domain containing protein 1 precursor Protein disulfide-isomerase A6 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a 2 n/a ER lumen n/a found at its expected molecular weight found at molecular weight
IPI00395887 Thioredoxin domain containing protein 1 precursor Protein disulfide-isomerase A6 precursor Thioredoxin domain containing protein 1 precursor Protein disulfide-isomerase A6 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a 2 n/a ER lumen n/a found at its expected molecular weight found at molecular weight
UniProt
Q9H3N1
ID TMX1_HUMAN Reviewed; 280 AA.
AC Q9H3N1; B2R7A4; Q8N487; Q8NBN5; Q9Y4T6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 123.
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;
GN ORFNames=PSEC0085, UNQ235/PRO268;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Kizaka-Kondoh S.;
RT "Identification of a novel thioredoxin-related transmembrane
RT 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA 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.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASS
RP SPECTROMETRY.
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
RP SER-280, AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange 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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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
RP SER-280, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
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
CC and catalyze dithiol-disulfide exchange reactions.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein (Potential). Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein (Potential). Note=Predominantly found in
CC the endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in kidney, liver,
CC placenta and lung.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
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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 PIR; T12471; T12471.
DR RefSeq; NP_110382.3; NM_030755.4.
DR UniGene; Hs.125221; -.
DR PDB; 1X5E; NMR; -; A=30-142.
DR PDBsum; 1X5E; -.
DR ProteinModelPortal; Q9H3N1; -.
DR SMR; Q9H3N1; 24-146.
DR IntAct; Q9H3N1; 12.
DR MINT; MINT-3067322; -.
DR STRING; 9606.ENSP00000393316; -.
DR PhosphoSite; Q9H3N1; -.
DR DMDM; 47117631; -.
DR PaxDb; Q9H3N1; -.
DR PeptideAtlas; Q9H3N1; -.
DR PRIDE; Q9H3N1; -.
DR DNASU; 81542; -.
DR Ensembl; ENST00000457354; ENSP00000393316; ENSG00000139921.
DR GeneID; 81542; -.
DR KEGG; hsa:81542; -.
DR UCSC; uc001wza.4; human.
DR CTD; 81542; -.
DR GeneCards; GC14P051706; -.
DR HGNC; HGNC:15487; TMX1.
DR HPA; HPA003085; -.
DR MIM; 610527; gene.
DR neXtProt; NX_Q9H3N1; -.
DR PharmGKB; PA37968; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000045750; -.
DR InParanoid; Q9H3N1; -.
DR OMA; CHNYFIE; -.
DR OrthoDB; EOG7KM5VC; -.
DR PhylomeDB; Q9H3N1; -.
DR EvolutionaryTrace; Q9H3N1; -.
DR GeneWiki; TMX1; -.
DR GenomeRNAi; 81542; -.
DR NextBio; 71773; -.
DR PRO; PR:Q9H3N1; -.
DR ArrayExpress; Q9H3N1; -.
DR Bgee; Q9H3N1; -.
DR CleanEx; HS_TXNDC1; -.
DR Genevestigator; Q9H3N1; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; NAS:UniProtKB.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:UniProtKB.
DR GO; GO:0045321; P:leukocyte activation; NAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0045927; P:positive regulation of growth; NAS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
DR GO; GO:0006950; P:response to stress; NAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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; Complete proteome; Disulfide bond; Electron transport;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Redox-active center;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1 26 Potential.
FT CHAIN 27 280 Thioredoxin-related transmembrane protein
FT 1.
FT /FTId=PRO_0000034153.
FT TOPO_DOM 27 180 Extracellular (Potential).
FT TRANSMEM 181 203 Helical; (Potential).
FT TOPO_DOM 204 280 Cytoplasmic (Potential).
FT DOMAIN 27 132 Thioredoxin.
FT MOD_RES 247 247 Phosphoserine.
FT MOD_RES 270 270 Phosphoserine.
FT MOD_RES 280 280 Phosphoserine.
FT DISULFID 56 59 Redox-active.
FT MUTAGEN 56 56 C->S: Loss of reductase activity; when
FT associated with S-59.
FT MUTAGEN 59 59 C->S: Loss of reductase activity; when
FT associated with S-56.
FT CONFLICT 14 16 LVL -> MVP (in Ref. 8; AAH36460).
FT CONFLICT 98 98 T -> N (in Ref. 8; AAH36460).
FT CONFLICT 177 177 V -> A (in Ref. 4; BAC11593).
FT STRAND 30 33
FT TURN 36 38
FT HELIX 39 42
FT STRAND 44 52
FT HELIX 57 73
FT HELIX 74 76
FT STRAND 79 84
FT TURN 85 87
FT HELIX 89 94
FT STRAND 99 107
FT STRAND 110 113
FT HELIX 120 128
FT HELIX 131 134
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
//
ID TMX1_HUMAN Reviewed; 280 AA.
AC Q9H3N1; B2R7A4; Q8N487; Q8NBN5; Q9Y4T6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 123.
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;
GN ORFNames=PSEC0085, UNQ235/PRO268;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Kizaka-Kondoh S.;
RT "Identification of a novel thioredoxin-related transmembrane
RT 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA 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.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASS
RP SPECTROMETRY.
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
RP SER-280, AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange 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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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
RP SER-280, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
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
CC and catalyze dithiol-disulfide exchange reactions.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein (Potential). Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein (Potential). Note=Predominantly found in
CC the endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in kidney, liver,
CC placenta and lung.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
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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 PIR; T12471; T12471.
DR RefSeq; NP_110382.3; NM_030755.4.
DR UniGene; Hs.125221; -.
DR PDB; 1X5E; NMR; -; A=30-142.
DR PDBsum; 1X5E; -.
DR ProteinModelPortal; Q9H3N1; -.
DR SMR; Q9H3N1; 24-146.
DR IntAct; Q9H3N1; 12.
DR MINT; MINT-3067322; -.
DR STRING; 9606.ENSP00000393316; -.
DR PhosphoSite; Q9H3N1; -.
DR DMDM; 47117631; -.
DR PaxDb; Q9H3N1; -.
DR PeptideAtlas; Q9H3N1; -.
DR PRIDE; Q9H3N1; -.
DR DNASU; 81542; -.
DR Ensembl; ENST00000457354; ENSP00000393316; ENSG00000139921.
DR GeneID; 81542; -.
DR KEGG; hsa:81542; -.
DR UCSC; uc001wza.4; human.
DR CTD; 81542; -.
DR GeneCards; GC14P051706; -.
DR HGNC; HGNC:15487; TMX1.
DR HPA; HPA003085; -.
DR MIM; 610527; gene.
DR neXtProt; NX_Q9H3N1; -.
DR PharmGKB; PA37968; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000045750; -.
DR InParanoid; Q9H3N1; -.
DR OMA; CHNYFIE; -.
DR OrthoDB; EOG7KM5VC; -.
DR PhylomeDB; Q9H3N1; -.
DR EvolutionaryTrace; Q9H3N1; -.
DR GeneWiki; TMX1; -.
DR GenomeRNAi; 81542; -.
DR NextBio; 71773; -.
DR PRO; PR:Q9H3N1; -.
DR ArrayExpress; Q9H3N1; -.
DR Bgee; Q9H3N1; -.
DR CleanEx; HS_TXNDC1; -.
DR Genevestigator; Q9H3N1; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; NAS:UniProtKB.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:UniProtKB.
DR GO; GO:0045321; P:leukocyte activation; NAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0045927; P:positive regulation of growth; NAS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
DR GO; GO:0006950; P:response to stress; NAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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; Complete proteome; Disulfide bond; Electron transport;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Redox-active center;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1 26 Potential.
FT CHAIN 27 280 Thioredoxin-related transmembrane protein
FT 1.
FT /FTId=PRO_0000034153.
FT TOPO_DOM 27 180 Extracellular (Potential).
FT TRANSMEM 181 203 Helical; (Potential).
FT TOPO_DOM 204 280 Cytoplasmic (Potential).
FT DOMAIN 27 132 Thioredoxin.
FT MOD_RES 247 247 Phosphoserine.
FT MOD_RES 270 270 Phosphoserine.
FT MOD_RES 280 280 Phosphoserine.
FT DISULFID 56 59 Redox-active.
FT MUTAGEN 56 56 C->S: Loss of reductase activity; when
FT associated with S-59.
FT MUTAGEN 59 59 C->S: Loss of reductase activity; when
FT associated with S-56.
FT CONFLICT 14 16 LVL -> MVP (in Ref. 8; AAH36460).
FT CONFLICT 98 98 T -> N (in Ref. 8; AAH36460).
FT CONFLICT 177 177 V -> A (in Ref. 4; BAC11593).
FT STRAND 30 33
FT TURN 36 38
FT HELIX 39 42
FT STRAND 44 52
FT HELIX 57 73
FT HELIX 74 76
FT STRAND 79 84
FT TURN 85 87
FT HELIX 89 94
FT STRAND 99 107
FT STRAND 110 113
FT HELIX 120 128
FT HELIX 131 134
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
//
MIM
610527
*RECORD*
*FIELD* NO
610527
*FIELD* TI
*610527 THIOREDOXIN DOMAIN-CONTAINING PROTEIN 1; TXNDC1
;;TRANSMEMBRANE TRX-RELATED PROTEIN; TMX
read more*FIELD* TX
DESCRIPTION
TXNDC1 is a thioredoxin (TXN; see 187700)-related protein with disulfide
reductase activity (Matsuo et al., 2001).
CLONING
Using gene trap screening of cDNA from a TGF-beta (TGFB; 190180)-treated
human lung adenocarcinoma cell line, followed by 5-prime RACE, Akiyama
et al. (2000) isolated a partial TXNDC1 cDNA. Using this fragment for
further screening of the cDNA library, Matsuo et al. (2001) isolated
full-length TXNDC1. The deduced 280-amino acid protein has a predicted
molecular mass of 31.8 kD and contains an N-terminal signal sequence, a
TRX-like domain with an active site sequence CPAC, and a transmembrane
domain. Northern blot analysis detected a 2.5-kb transcript in all
tissues examined, with highest expression in kidney, liver, placenta,
and lung. Confocal microscopy of intact HEK293 cells expressing TXNDC1
and Western analysis of subcellular fractions localized TXNDC1 primarily
in the microsomal fraction in an endoplasmic reticulum (ER)-like
staining pattern characterized by a diffuse network-like labeling of the
cytoplasm and nuclear rim.
GENE FUNCTION
Using recombinant TXNDC1 catalytic domain expressed in E. coli, Matsuo
et al. (2001) showed that TXNDC1 had dose-dependent insulin (INS;
176730) disulfide reducing activity. Using doxycycline-regulated TXNDC1
expression in HEK293 cells treated with reagents known to induce ER
stress, namely, thapsigargin, calcium ionophore A23187, or brefeldin A
(BFA), Matsuo et al. (2001) showed that TXNDC1 expression suppressed
BFA-induced apoptosis. Mutation of the two TXNDC1 active site cysteine
residues abolished both disulfide-reducing activity and suppression of
BFA-induced apoptosis.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TXNDC1
gene to chromosome 14 (TMAP RH94716).
*FIELD* RF
1. Akiyama, N.; Matsuo, Y.; Sai, H.; Noda, M.; Kizaka-Kondoh, S.:
Identification of a series of transforming growth factor beta-responsive
genes by retrovirus-mediated gene trap screening. Molec. Cell. Biol. 20:
3266-3273, 2000.
2. Matsuo, Y.; Akiyama, N.; Nakamura, H.; Yokoi, J.; Noda, M.; Kizaka-Kondoh,
S.: Identification of a novel thioredoxin-related transmembrane protein. J.
Biol. Chem. 276: 10032-10038, 2001.
*FIELD* CD
Dorothy S. Reilly: 10/26/2006
*FIELD* ED
carol: 06/20/2007
carol: 10/26/2006
*RECORD*
*FIELD* NO
610527
*FIELD* TI
*610527 THIOREDOXIN DOMAIN-CONTAINING PROTEIN 1; TXNDC1
;;TRANSMEMBRANE TRX-RELATED PROTEIN; TMX
read more*FIELD* TX
DESCRIPTION
TXNDC1 is a thioredoxin (TXN; see 187700)-related protein with disulfide
reductase activity (Matsuo et al., 2001).
CLONING
Using gene trap screening of cDNA from a TGF-beta (TGFB; 190180)-treated
human lung adenocarcinoma cell line, followed by 5-prime RACE, Akiyama
et al. (2000) isolated a partial TXNDC1 cDNA. Using this fragment for
further screening of the cDNA library, Matsuo et al. (2001) isolated
full-length TXNDC1. The deduced 280-amino acid protein has a predicted
molecular mass of 31.8 kD and contains an N-terminal signal sequence, a
TRX-like domain with an active site sequence CPAC, and a transmembrane
domain. Northern blot analysis detected a 2.5-kb transcript in all
tissues examined, with highest expression in kidney, liver, placenta,
and lung. Confocal microscopy of intact HEK293 cells expressing TXNDC1
and Western analysis of subcellular fractions localized TXNDC1 primarily
in the microsomal fraction in an endoplasmic reticulum (ER)-like
staining pattern characterized by a diffuse network-like labeling of the
cytoplasm and nuclear rim.
GENE FUNCTION
Using recombinant TXNDC1 catalytic domain expressed in E. coli, Matsuo
et al. (2001) showed that TXNDC1 had dose-dependent insulin (INS;
176730) disulfide reducing activity. Using doxycycline-regulated TXNDC1
expression in HEK293 cells treated with reagents known to induce ER
stress, namely, thapsigargin, calcium ionophore A23187, or brefeldin A
(BFA), Matsuo et al. (2001) showed that TXNDC1 expression suppressed
BFA-induced apoptosis. Mutation of the two TXNDC1 active site cysteine
residues abolished both disulfide-reducing activity and suppression of
BFA-induced apoptosis.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TXNDC1
gene to chromosome 14 (TMAP RH94716).
*FIELD* RF
1. Akiyama, N.; Matsuo, Y.; Sai, H.; Noda, M.; Kizaka-Kondoh, S.:
Identification of a series of transforming growth factor beta-responsive
genes by retrovirus-mediated gene trap screening. Molec. Cell. Biol. 20:
3266-3273, 2000.
2. Matsuo, Y.; Akiyama, N.; Nakamura, H.; Yokoi, J.; Noda, M.; Kizaka-Kondoh,
S.: Identification of a novel thioredoxin-related transmembrane protein. J.
Biol. Chem. 276: 10032-10038, 2001.
*FIELD* CD
Dorothy S. Reilly: 10/26/2006
*FIELD* ED
carol: 06/20/2007
carol: 10/26/2006