TMX4_HUMAN
ID TMX4_HUMAN Reviewed; 349 AA.
AC Q9H1E5; Q8N4P7; Q8NCC1; Q9UJA1; Q9ULQ8;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Thioredoxin-related transmembrane protein 4;
DE AltName: Full=Thioredoxin domain-containing protein 13;
DE Flags: Precursor;
GN Name=TMX4; Synonyms=KIAA1162, TXNDC13; ORFNames=PSEC0095, UNQ475/PRO938;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-303.
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 88-349.
RA Stavrides G.S., Huckle E.J., Deloukas P.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 235-349.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-259, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-259, 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 [9]
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 [10]
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 [11]
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).
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q8C0L0}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB56344.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY359004; AAQ89363.1; -; mRNA.
DR EMBL; AK074838; BAC11237.1; -; mRNA.
DR EMBL; AK075404; BAC11599.1; -; mRNA.
DR EMBL; AL021396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033787; AAH33787.1; -; mRNA.
DR EMBL; AL118494; CAB56344.1; ALT_INIT; mRNA.
DR EMBL; AB032988; BAA86476.1; -; mRNA.
DR CCDS; CCDS13101.1; -.
DR RefSeq; NP_066979.2; NM_021156.3.
DR AlphaFoldDB; Q9H1E5; -.
DR SMR; Q9H1E5; -.
DR BioGRID; 121120; 79.
DR IntAct; Q9H1E5; 27.
DR MINT; Q9H1E5; -.
DR STRING; 9606.ENSP00000246024; -.
DR GlyConnect; 1802; 1 N-Linked glycan (1 site).
DR GlyGen; Q9H1E5; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9H1E5; -.
DR PhosphoSitePlus; Q9H1E5; -.
DR SwissPalm; Q9H1E5; -.
DR BioMuta; TMX4; -.
DR DMDM; 30173124; -.
DR CPTAC; CPTAC-1512; -.
DR EPD; Q9H1E5; -.
DR jPOST; Q9H1E5; -.
DR MassIVE; Q9H1E5; -.
DR MaxQB; Q9H1E5; -.
DR PaxDb; Q9H1E5; -.
DR PeptideAtlas; Q9H1E5; -.
DR PRIDE; Q9H1E5; -.
DR ProteomicsDB; 80406; -.
DR Antibodypedia; 610; 105 antibodies from 25 providers.
DR DNASU; 56255; -.
DR Ensembl; ENST00000246024.7; ENSP00000246024.2; ENSG00000125827.9.
DR GeneID; 56255; -.
DR KEGG; hsa:56255; -.
DR MANE-Select; ENST00000246024.7; ENSP00000246024.2; NM_021156.4; NP_066979.2.
DR UCSC; uc002wmx.2; human.
DR CTD; 56255; -.
DR GeneCards; TMX4; -.
DR HGNC; HGNC:25237; TMX4.
DR HPA; ENSG00000125827; Low tissue specificity.
DR neXtProt; NX_Q9H1E5; -.
DR OpenTargets; ENSG00000125827; -.
DR PharmGKB; PA164726669; -.
DR VEuPathDB; HostDB:ENSG00000125827; -.
DR eggNOG; KOG0913; Eukaryota.
DR GeneTree; ENSGT00940000160301; -.
DR HOGENOM; CLU_069292_1_0_1; -.
DR InParanoid; Q9H1E5; -.
DR OMA; YIVEKKW; -.
DR OrthoDB; 1481386at2759; -.
DR PhylomeDB; Q9H1E5; -.
DR TreeFam; TF106376; -.
DR PathwayCommons; Q9H1E5; -.
DR SignaLink; Q9H1E5; -.
DR BioGRID-ORCS; 56255; 13 hits in 1083 CRISPR screens.
DR ChiTaRS; TMX4; human.
DR GeneWiki; TMX4; -.
DR GenomeRNAi; 56255; -.
DR Pharos; Q9H1E5; Tdark.
DR PRO; PR:Q9H1E5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H1E5; protein.
DR Bgee; ENSG00000125827; Expressed in germinal epithelium of ovary and 214 other tissues.
DR ExpressionAtlas; Q9H1E5; baseline and differential.
DR Genevisible; Q9H1E5; HS.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IBA:GO_Central.
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; Membrane; Nucleus; Phosphoprotein;
KW Redox-active center; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..349
FT /note="Thioredoxin-related transmembrane protein 4"
FT /id="PRO_0000034191"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 30..137
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 225..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT DISULFID 64..67
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VARIANT 215
FT /note="Y -> C (in dbSNP:rs1135711)"
FT /id="VAR_052578"
FT VARIANT 303
FT /note="G -> R (in dbSNP:rs2076015)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052579"
FT CONFLICT 289
FT /note="V -> E (in Ref. 2; BAC11237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38952 MW; FE944AA2F44131F1 CRC64;
MAGGRCGPQL TALLAAWIAA VAATAGPEEA ALPPEQSRVQ PMTASNWTLV MEGEWMLKFY
APWCPSCQQT DSEWEAFAKN GEILQISVGK VDVIQEPGLS GRFFVTTLPA FFHAKDGIFR
RYRGPGIFED LQNYILEKKW QSVEPLTGWK SPASLTMSGM AGLFSISGKI WHLHNYFTVT
LGIPAWCSYV FFVIATLVFG LFMGLVLVVI SECFYVPLPR HLSERSEQNR RSEEAHRAEQ
LQDAEEEKDD SNEEENKDSL VDDEEEKEDL GDEDEAEEEE EEDNLAAGVD EERSEANDQG
PPGEDGVTRE EVEPEEAEEG ISEQPCPADT EVVEDSLRQR KSQHADKGL
