TXNL1_MOUSE
ID TXNL1_MOUSE Reviewed; 289 AA.
AC Q8CDN6; O70379; Q3TI92;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Thioredoxin-like protein 1;
DE AltName: Full=32 kDa thioredoxin-related protein;
GN Name=Txnl1; Synonyms=Trp32, Txnl;
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].
RX PubMed=9668102; DOI=10.1074/jbc.273.30.19160;
RA Lee K.-K., Murakawa M., Takahashi S., Tsubuki S., Kawashima S.,
RA Sakamaki K., Yonehara S.;
RT "Purification, molecular cloning, and characterization of TRP32, a novel
RT thioredoxin-related mammalian protein of 32 kDa.";
RL J. Biol. Chem. 273:19160-19166(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Amnion, Bone marrow, and Testis;
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 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 [4]
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).
CC -!- FUNCTION: Active thioredoxin with a redox potential of about -250 mV.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the 19S regulatory cap of the 26S proteasome.
CC Interacts with PSMD14/RPN11. Interacts with, and reduces EEF1A1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=At least 85% of the cellular TXNL1 is proteasome-associated.
CC {ECO:0000250}.
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DR EMBL; AF052660; AAC40183.1; -; mRNA.
DR EMBL; AK029807; BAC26626.1; -; mRNA.
DR EMBL; AK150326; BAE29469.1; -; mRNA.
DR EMBL; AK167954; BAE39954.1; -; mRNA.
DR EMBL; AK168712; BAE40554.1; -; mRNA.
DR EMBL; BC061123; AAH61123.1; -; mRNA.
DR CCDS; CCDS29297.1; -.
DR RefSeq; NP_058072.2; NM_016792.4.
DR AlphaFoldDB; Q8CDN6; -.
DR BMRB; Q8CDN6; -.
DR SMR; Q8CDN6; -.
DR BioGRID; 207304; 49.
DR IntAct; Q8CDN6; 2.
DR MINT; Q8CDN6; -.
DR STRING; 10090.ENSMUSP00000025476; -.
DR iPTMnet; Q8CDN6; -.
DR PhosphoSitePlus; Q8CDN6; -.
DR SwissPalm; Q8CDN6; -.
DR REPRODUCTION-2DPAGE; Q8CDN6; -.
DR EPD; Q8CDN6; -.
DR jPOST; Q8CDN6; -.
DR MaxQB; Q8CDN6; -.
DR PaxDb; Q8CDN6; -.
DR PRIDE; Q8CDN6; -.
DR ProteomicsDB; 300164; -.
DR Antibodypedia; 1038; 211 antibodies from 28 providers.
DR DNASU; 53382; -.
DR Ensembl; ENSMUST00000237004; ENSMUSP00000158375; ENSMUSG00000024583.
DR GeneID; 53382; -.
DR KEGG; mmu:53382; -.
DR UCSC; uc008fdx.1; mouse.
DR CTD; 9352; -.
DR MGI; MGI:1860078; Txnl1.
DR VEuPathDB; HostDB:ENSMUSG00000024583; -.
DR eggNOG; KOG0908; Eukaryota.
DR GeneTree; ENSGT00940000156170; -.
DR HOGENOM; CLU_072377_0_2_1; -.
DR InParanoid; Q8CDN6; -.
DR OMA; PIFEMFP; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q8CDN6; -.
DR TreeFam; TF314399; -.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 53382; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Txnl1; mouse.
DR PRO; PR:Q8CDN6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8CDN6; protein.
DR Bgee; ENSMUSG00000024583; Expressed in urogenital fold and 259 other tissues.
DR ExpressionAtlas; Q8CDN6; baseline and differential.
DR Genevisible; Q8CDN6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; ISO:MGI.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR Gene3D; 2.60.120.470; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR010400; PITH_dom.
DR InterPro; IPR037047; PITH_dom_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF06201; PITH; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51532; PITH; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Electron transport; Nucleus; Phosphoprotein;
KW Proteasome; Redox-active center; Reference proteome; Transport.
FT CHAIN 1..289
FT /note="Thioredoxin-like protein 1"
FT /id="PRO_0000120017"
FT DOMAIN 2..109
FT /note="Thioredoxin"
FT DOMAIN 115..285
FT /note="PITH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00864"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43396"
FT DISULFID 34..37
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 251
FT /note="N -> K (in Ref. 1; AAC40183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32237 MW; 4BE29C6C1D1DFA0A CRC64;
MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD
VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDADIP
KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDMSFLESD CDEQLLITVA FNQPVKLYSM
KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN
VNSVTLFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH
