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Protein disulfide-isomerase TMX3 (EC 5.3.4.1) (Thioredoxin domain-containing protein 10) (Thioredoxin-related transmembrane protein 3)

 TMX3_HUMAN              Reviewed;         454 AA.
Q96JJ7; B3KV75; Q52LT7; Q8N5J0; Q9NWJ9;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 2.
27-SEP-2017, entry version 156.
RecName: Full=Protein disulfide-isomerase TMX3;
EC=5.3.4.1;
AltName: Full=Thioredoxin domain-containing protein 10;
AltName: Full=Thioredoxin-related transmembrane protein 3;
Flags: Precursor;
Name=TMX3; Synonyms=KIAA1830, TXNDC10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
SER-61.
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, INDUCTION, AND GLYCOSYLATION.
PubMed=15623505; DOI=10.1074/jbc.M413924200;
Haugstetter J., Blicher T., Ellgaard L.;
"Identification and characterization of a novel thioredoxin-related
transmembrane protein of the endoplasmic reticulum.";
J. Biol. Chem. 280:8371-8380(2005).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-258.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Probable disulfide isomerase, which participates in the
folding of proteins containing disulfide bonds. May act as a
dithiol oxidase. {ECO:0000269|PubMed:15623505}.
-!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
proteins. {ECO:0000269|PubMed:15623505}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Redox potential:
E(0) is -157 mV. {ECO:0000269|PubMed:15623505};
-!- INTERACTION:
Q13643:FHL3; NbExp=3; IntAct=EBI-2514069, EBI-741101;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15623505}; Single-pass membrane protein
{ECO:0000269|PubMed:15623505}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96JJ7-1; Sequence=Displayed;
Name=2;
IsoId=Q96JJ7-2; Sequence=VSP_013748, VSP_013749;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, testis,
lung, skin, kidney, uterus, bone, stomach, liver, prostate,
placenta, eye and muscle. {ECO:0000269|PubMed:15623505}.
-!- INDUCTION: Not up-regulated by unfolded protein response (UPR).
{ECO:0000269|PubMed:15623505}.
-!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
localization for type I membrane proteins. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15623505,
ECO:0000269|PubMed:19159218}.
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91381.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB47459.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB058733; BAB47459.1; ALT_INIT; mRNA.
EMBL; AK000800; BAA91381.1; ALT_INIT; mRNA.
EMBL; AK122715; BAG53687.1; -; mRNA.
EMBL; BX647846; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC032325; AAH32325.1; -; mRNA.
EMBL; BC093792; AAH93792.1; -; mRNA.
EMBL; BC093794; AAH93794.1; -; mRNA.
CCDS; CCDS32840.1; -. [Q96JJ7-1]
RefSeq; NP_061895.3; NM_019022.3. [Q96JJ7-1]
UniGene; Hs.440534; -.
ProteinModelPortal; Q96JJ7; -.
SMR; Q96JJ7; -.
BioGrid; 119991; 13.
IntAct; Q96JJ7; 22.
MINT; MINT-3054729; -.
STRING; 9606.ENSP00000299608; -.
iPTMnet; Q96JJ7; -.
PhosphoSitePlus; Q96JJ7; -.
SwissPalm; Q96JJ7; -.
BioMuta; TMX3; -.
DMDM; 78103208; -.
EPD; Q96JJ7; -.
MaxQB; Q96JJ7; -.
PaxDb; Q96JJ7; -.
PeptideAtlas; Q96JJ7; -.
PRIDE; Q96JJ7; -.
TopDownProteomics; Q96JJ7-1; -. [Q96JJ7-1]
DNASU; 54495; -.
Ensembl; ENST00000299608; ENSP00000299608; ENSG00000166479. [Q96JJ7-1]
Ensembl; ENST00000562706; ENSP00000457262; ENSG00000166479. [Q96JJ7-2]
GeneID; 54495; -.
KEGG; hsa:54495; -.
UCSC; uc002lkf.4; human. [Q96JJ7-1]
CTD; 54495; -.
DisGeNET; 54495; -.
EuPathDB; HostDB:ENSG00000166479.9; -.
GeneCards; TMX3; -.
HGNC; HGNC:24718; TMX3.
HPA; HPA014157; -.
MIM; 616102; gene.
neXtProt; NX_Q96JJ7; -.
OpenTargets; ENSG00000166479; -.
PharmGKB; PA164726632; -.
eggNOG; KOG4277; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00860000133691; -.
HOGENOM; HOG000154655; -.
InParanoid; Q96JJ7; -.
KO; K09585; -.
OMA; MQKRHRV; -.
OrthoDB; EOG091G0MS9; -.
PhylomeDB; Q96JJ7; -.
TreeFam; TF313807; -.
Reactome; R-HSA-114608; Platelet degranulation.
GeneWiki; TMX3; -.
GenomeRNAi; 54495; -.
PRO; PR:Q96JJ7; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000166479; -.
CleanEx; HS_TXNDC10; -.
ExpressionAtlas; Q96JJ7; baseline and differential.
Genevisible; Q96JJ7; HS.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:WormBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
GO; GO:0016972; F:thiol oxidase activity; IDA:WormBase.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0018171; P:peptidyl-cysteine oxidation; IDA:WormBase.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0006457; P:protein folding; IBA:GO_Central.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
InterPro; IPR012336; Thioredoxin-like_fold.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 2.
PROSITE; PS00194; THIOREDOXIN_1; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Isomerase; Membrane;
Polymorphism; Redox-active center; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 454 Protein disulfide-isomerase TMX3.
/FTId=PRO_0000034185.
TOPO_DOM 25 375 Lumenal. {ECO:0000255}.
TRANSMEM 376 396 Helical. {ECO:0000255}.
TOPO_DOM 397 454 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 128 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 451 454 Di-lysine motif.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 313 313 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 53 56 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VAR_SEQ 191 195 YVTLK -> VIFKI (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013748.
VAR_SEQ 196 454 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013749.
VARIANT 61 61 P -> S (in dbSNP:rs11557684).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_022451.
SEQUENCE 454 AA; 51872 MW; 37EBA0C70ED84A9B CRC64;
MAAWKSWTAL RLCATVVVLD MVVCKGFVED LDESFKENRN DDIWLVDFYA PWCGHCKKLE
PIWNEVGLEM KSIGSPVKVG KMDATSYSSI ASEFGVRGYP TIKLLKGDLA YNYRGPRTKD
DIIEFAHRVS GALIRPLPSQ QMFEHMQKRH RVFFVYVGGE SPLKEKYIDA ASELIVYTYF
FSASEEVVPE YVTLKEMPAV LVFKDETYFV YDEYEDGDLS SWINRERFQN YLAMDGFLLY
ELGDTGKLVA LAVIDEKNTS VEHTRLKSII QEVARDYRDL FHRDFQFGHM DGNDYINTLL
MDELTVPTVV VLNTSNQQYF LLDRQIKNVE DMVQFINNIL DGTVEAQGGD SILQRLKRIV
FDAKSTIVSI FKSSPLMGCF LFGLPLGVIS IMCYGIYTAD TDGGYIEERY EVSKSENENQ
EQIEESKEQQ EPSSGGSVVP TVQEPKDVLE KKKD


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