TXD17_MOUSE
ID TXD17_MOUSE Reviewed; 123 AA.
AC Q9CQM5; Q3TE14; Q921A9; Q9D0Y4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Thioredoxin domain-containing protein 17;
DE AltName: Full=14 kDa thioredoxin-related protein;
DE Short=TRP14;
DE AltName: Full=Protein 42-9-9;
DE AltName: Full=Thioredoxin-like protein 5;
GN Name=Txndc17; Synonyms=Txnl5;
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 [MRNA].
RC TISSUE=Embryo;
RA Schmidt T.;
RL Thesis (2001), University of Goettingen, Germany.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Dendritic cell, Embryo, Head, and Pancreas;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 [5]
RP IDENTIFICATION BY 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).
RN [6]
RP STRUCTURE BY NMR.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of mouse putative 42-9-9 protein.";
RL Submitted (AUG-2004) to the PDB data bank.
CC -!- FUNCTION: Disulfide reductase. May participate in various redox
CC reactions through the reversible oxidation of its active center dithiol
CC to a disulfide and catalyze dithiol-disulfide exchange reactions.
CC Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase
CC activity and may contribute to the elimination of cellular hydrogen
CC peroxide (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TRXR1 and DYNLL1/DNCL1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: The oxidized protein is reduced by TRXR1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ344103; CAC51438.1; -; mRNA.
DR EMBL; AK004219; BAB23225.1; -; mRNA.
DR EMBL; AK007595; BAB25126.1; -; mRNA.
DR EMBL; AK013103; BAB28648.1; -; mRNA.
DR EMBL; AK076425; BAC36336.1; -; mRNA.
DR EMBL; AK169882; BAE41434.1; -; mRNA.
DR EMBL; BX119911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030344; AAH30344.1; -; mRNA.
DR CCDS; CCDS24980.1; -.
DR RefSeq; NP_080835.1; NM_026559.3.
DR PDB; 1V9W; NMR; -; A=1-123.
DR PDBsum; 1V9W; -.
DR AlphaFoldDB; Q9CQM5; -.
DR BMRB; Q9CQM5; -.
DR SMR; Q9CQM5; -.
DR BioGRID; 206741; 4.
DR STRING; 10090.ENSMUSP00000021158; -.
DR iPTMnet; Q9CQM5; -.
DR PhosphoSitePlus; Q9CQM5; -.
DR CPTAC; non-CPTAC-3677; -.
DR EPD; Q9CQM5; -.
DR jPOST; Q9CQM5; -.
DR MaxQB; Q9CQM5; -.
DR PaxDb; Q9CQM5; -.
DR PeptideAtlas; Q9CQM5; -.
DR PRIDE; Q9CQM5; -.
DR ProteomicsDB; 298342; -.
DR Antibodypedia; 11673; 88 antibodies from 24 providers.
DR DNASU; 52700; -.
DR Ensembl; ENSMUST00000021158; ENSMUSP00000021158; ENSMUSG00000020803.
DR GeneID; 52700; -.
DR KEGG; mmu:52700; -.
DR UCSC; uc007jyj.1; mouse.
DR CTD; 84817; -.
DR MGI; MGI:1289248; Txndc17.
DR VEuPathDB; HostDB:ENSMUSG00000020803; -.
DR eggNOG; KOG3425; Eukaryota.
DR GeneTree; ENSGT00390000012195; -.
DR HOGENOM; CLU_120161_0_1_1; -.
DR InParanoid; Q9CQM5; -.
DR OMA; IMVVTHN; -.
DR OrthoDB; 1624076at2759; -.
DR PhylomeDB; Q9CQM5; -.
DR TreeFam; TF313854; -.
DR BioGRID-ORCS; 52700; 19 hits in 72 CRISPR screens.
DR ChiTaRS; Txndc17; mouse.
DR EvolutionaryTrace; Q9CQM5; -.
DR PRO; PR:Q9CQM5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQM5; protein.
DR Bgee; ENSMUSG00000020803; Expressed in seminal vesicle and 254 other tissues.
DR Genevisible; Q9CQM5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004601; F:peroxidase activity; ISO:MGI.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; ISO:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR045108; TXNDC17-like.
DR InterPro; IPR010357; TXNDC17_dom.
DR PANTHER; PTHR12452; PTHR12452; 1.
DR Pfam; PF06110; DUF953; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Disulfide bond; Redox-active center;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT CHAIN 2..123
FT /note="Thioredoxin domain-containing protein 17"
FT /id="PRO_0000120023"
FT DOMAIN 41..123
FT /note="Thioredoxin"
FT /evidence="ECO:0000255"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT SITE 44
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT SITE 45
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT DISULFID 43..46
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT CONFLICT 22
FT /note="H -> R (in Ref. 2; BAE41434)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="G -> S (in Ref. 2; BAB23225)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="K -> Q (in Ref. 1; CAC51438)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Y -> H (in Ref. 2; BAE41434)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1V9W"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:1V9W"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:1V9W"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1V9W"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:1V9W"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1V9W"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1V9W"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1V9W"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1V9W"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1V9W"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:1V9W"
SQ SEQUENCE 123 AA; 14015 MW; 763689BCCAABD8ED CRC64;
MATFEEVSVL GFEEFDKAVK EHEGKTIFAY FSGSKDTEGK SWCPDCVEAE PVIREGLKHV
TEDCVFIYCQ VGDKPYWKDP NNDFRQKLKI TAVPTLLKYG TPQKLVESEC CQSSLVEMIF
SED
