TMX3_MOUSE
ID TMX3_MOUSE Reviewed; 456 AA.
AC Q8BXZ1; Q3US84; Q6PGA1; Q6ZPH5; Q8BZB8;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein disulfide-isomerase TMX3;
DE EC=5.3.4.1;
DE AltName: Full=Thioredoxin domain-containing protein 10;
DE AltName: Full=Thioredoxin-related transmembrane protein 3;
DE Flags: Precursor;
GN Name=Tmx3; Synonyms=Kiaa1830, Txndc10;
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 TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Corpus striatum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP PROTEIN SEQUENCE OF 132-150 AND 368-375, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: Probable disulfide isomerase, which participates in the
CC folding of proteins containing disulfide bonds. May act as a dithiol
CC oxidase (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BC057139; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK129451; BAC98261.1; ALT_INIT; mRNA.
DR EMBL; AK035946; BAC29254.1; -; mRNA.
DR EMBL; AK042787; BAC31366.2; -; mRNA.
DR EMBL; AK140709; BAE24450.1; -; mRNA.
DR EMBL; BC057139; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS37879.1; -.
DR RefSeq; NP_938037.2; NM_198295.2.
DR AlphaFoldDB; Q8BXZ1; -.
DR SMR; Q8BXZ1; -.
DR BioGRID; 212584; 13.
DR STRING; 10090.ENSMUSP00000025515; -.
DR GlyConnect; 2623; 10 N-Linked glycans (1 site).
DR GlyGen; Q8BXZ1; 3 sites, 10 N-linked glycans (1 site).
DR iPTMnet; Q8BXZ1; -.
DR PhosphoSitePlus; Q8BXZ1; -.
DR SwissPalm; Q8BXZ1; -.
DR EPD; Q8BXZ1; -.
DR jPOST; Q8BXZ1; -.
DR MaxQB; Q8BXZ1; -.
DR PaxDb; Q8BXZ1; -.
DR PeptideAtlas; Q8BXZ1; -.
DR PRIDE; Q8BXZ1; -.
DR ProteomicsDB; 259271; -.
DR Antibodypedia; 2580; 110 antibodies from 21 providers.
DR DNASU; 67988; -.
DR Ensembl; ENSMUST00000025515; ENSMUSP00000025515; ENSMUSG00000024614.
DR GeneID; 67988; -.
DR KEGG; mmu:67988; -.
DR UCSC; uc008fvt.1; mouse.
DR CTD; 54495; -.
DR MGI; MGI:2442418; Tmx3.
DR VEuPathDB; HostDB:ENSMUSG00000024614; -.
DR eggNOG; KOG4277; Eukaryota.
DR GeneTree; ENSGT00930000151022; -.
DR HOGENOM; CLU_040429_1_0_1; -.
DR InParanoid; Q8BXZ1; -.
DR OMA; MWRGNPV; -.
DR OrthoDB; 746938at2759; -.
DR PhylomeDB; Q8BXZ1; -.
DR TreeFam; TF313807; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 67988; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Tmx3; mouse.
DR PRO; PR:Q8BXZ1; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BXZ1; protein.
DR Bgee; ENSMUSG00000024614; Expressed in otolith organ and 220 other tissues.
DR ExpressionAtlas; Q8BXZ1; baseline and differential.
DR Genevisible; Q8BXZ1; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:MGI.
DR GO; GO:0018171; P:peptidyl-cysteine oxidation; 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; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Isomerase; Membrane; Redox-active center; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..456
FT /note="Protein disulfide-isomerase TMX3"
FT /id="PRO_0000034186"
FT TOPO_DOM 30..378
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..131
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 416..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 453..456
FT /note="Di-lysine motif"
FT COMPBIAS 416..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..59
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 456 AA; 51848 MW; 7813FC587B35B88F CRC64;
MANAVGRRSW AALRLCAAVI LLDLAVCKGF VEDLNESFKD NRKDDIWLVD FYAPWCGHCK
KLEPIWNEVG LEMKSIGSPV KVGKMDATSY SSIASEFGVR GYPTIKLLKG DLAYNYRGPR
TKDDIIEFAH RVSGALIRPL PSQQMFDHVR KRHRVFFVYI GGESPLKEKY IDAASELIVY
TYFFSASEDV VPEYVTLKEM PAVLVFKDDT YFVYDEYEDG DLSSWISRER FQNYLTMDGF
LLYELGDTGK LVAIAVIDEK NTSLEHTRLK SIIQEVARDF RDHFHRDFQF GHMDGNDYIN
TLLMDELTVP TIVVLNTSNQ QYFLLDRHIK DASDMVQFIN SILDGTVPAQ GGDSIFQRLK
RIVFDAKSTI VSIFKSSPLM GCFLFGLPLG VISIMCYGIY TADTDGGYIE ERYEVSKSEM
ENQEQIEESK EQESSSGGSL APTVQEPKDV LEKKKD
