TMX2_MOUSE
ID TMX2_MOUSE Reviewed; 295 AA.
AC Q9D710; Q8BW13;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Thioredoxin-related transmembrane protein 2;
DE AltName: Full=Thioredoxin domain-containing protein 14;
DE Flags: Precursor;
GN Name=Tmx2; Synonyms=Txndc14;
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 STRAIN=C57BL/6J, and NOD; TISSUE=Mammary gland, Testis, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and NMRI; TISSUE=Kidney, and 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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: Endoplasmic reticulum and mitochondria-associated protein
CC that probably functions as a regulator of cellular redox state and
CC thereby regulates protein post-translational modification, protein
CC folding and mitochondrial activity. Indirectly regulates neuronal
CC proliferation, migration, and organization in the developing brain.
CC {ECO:0000250|UniProtKB:Q9Y320}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer; disulfide-linked (By
CC similarity). Occurs in both reduced and oxidized monomeric form (By
CC similarity). Oxidative conditions increase homodimerization (By
CC similarity). Interacts with CANX (By similarity). Interacts with ATP2A2
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y320}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y320}; Single-pass type I membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9Y320}.
CC Note=Localizes to endoplasmic reticulum mitochondria-associated
CC membrane (MAMs) that connect the endoplasmic reticulum and the
CC mitochondria. {ECO:0000250|UniProtKB:Q9Y320}.
CC -!- DOMAIN: The thioredoxin domain lacks the 2 redox-active cysteines,
CC suggesting that it lacks thioredoxin activity. {ECO:0000305}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000305}.
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DR EMBL; AK009759; BAB26483.1; -; mRNA.
DR EMBL; AK075750; BAC35930.1; -; mRNA.
DR EMBL; AK145245; BAE26323.1; -; mRNA.
DR EMBL; AK170587; BAE41896.1; -; mRNA.
DR EMBL; BC013544; AAH13544.1; -; mRNA.
DR EMBL; BC110994; AAI10995.1; -; mRNA.
DR CCDS; CCDS16188.1; -.
DR RefSeq; NP_001277680.1; NM_001290751.1.
DR RefSeq; NP_080144.1; NM_025868.4.
DR AlphaFoldDB; Q9D710; -.
DR SMR; Q9D710; -.
DR BioGRID; 211835; 8.
DR STRING; 10090.ENSMUSP00000107294; -.
DR iPTMnet; Q9D710; -.
DR PhosphoSitePlus; Q9D710; -.
DR SwissPalm; Q9D710; -.
DR EPD; Q9D710; -.
DR jPOST; Q9D710; -.
DR MaxQB; Q9D710; -.
DR PaxDb; Q9D710; -.
DR PRIDE; Q9D710; -.
DR ProteomicsDB; 259270; -.
DR DNASU; 66958; -.
DR Ensembl; ENSMUST00000053664; ENSMUSP00000059582; ENSMUSG00000050043.
DR Ensembl; ENSMUST00000111665; ENSMUSP00000107294; ENSMUSG00000050043.
DR GeneID; 66958; -.
DR KEGG; mmu:66958; -.
DR UCSC; uc008kix.2; mouse.
DR CTD; 51075; -.
DR MGI; MGI:1914208; Tmx2.
DR VEuPathDB; HostDB:ENSMUSG00000050043; -.
DR eggNOG; KOG0914; Eukaryota.
DR GeneTree; ENSGT00390000003751; -.
DR HOGENOM; CLU_064868_0_0_1; -.
DR InParanoid; Q9D710; -.
DR OMA; FYTAWNP; -.
DR OrthoDB; 1107509at2759; -.
DR PhylomeDB; Q9D710; -.
DR TreeFam; TF314606; -.
DR BioGRID-ORCS; 66958; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Tmx2; mouse.
DR PRO; PR:Q9D710; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D710; protein.
DR Bgee; ENSMUSG00000050043; Expressed in cerebellum and 82 other tissues.
DR ExpressionAtlas; Q9D710; baseline and differential.
DR Genevisible; Q9D710; MM.
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:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR CDD; cd02962; TMX2; 1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR039101; TMX2.
DR InterPro; IPR037463; TMX2_thioredoxin_dom.
DR PANTHER; PTHR15853; PTHR15853; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..48
FT /evidence="ECO:0000255"
FT CHAIN 49..295
FT /note="Thioredoxin-related transmembrane protein 2"
FT /id="PRO_0000315754"
FT TOPO_DOM 49..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 114..269
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 266..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 292..295
FT /note="Di-lysine motif"
FT /evidence="ECO:0000305"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y320"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 247
FT /note="S -> F (in Ref. 1; BAC35930)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="D -> V (in Ref. 1; BAC35930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 33943 MW; 25E4477F7BB17E3C CRC64;
MAVLAPLIAL VYSVPRLSRW LARPYCLLSA LLSIAFLLVR KLPPICNGLP TQREDGNPCD
FDWREVEILM FLSAIVMMKN RRSITVEQHV GNIFMFSKVA NAILFFRLDI RMGLLYLTLC
IVFLMTCKPP LYMGPEYIKY FNDKTIDEEL ERDKRVTWIV EFFANWSNDC QSFAPIYADL
SLKYNCSGLN FGKVDVGRYT DVSTRYKVST SPLTRQLPTL ILFQGGKEVI RRPQIDKKGR
AVSWTFSEEN VIREFNLNEL YQRAKKHSKG GDMSEEKPVD PAPTTVPDGE NKKDK
