TRXR1_CAEEL
ID TRXR1_CAEEL Reviewed; 667 AA.
AC Q17745; Q9N2K1; Q9NJH3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Thioredoxin reductase 1;
DE Short=TR-Se;
DE Short=TRR;
DE EC=1.8.1.9 {ECO:0000269|PubMed:21199936};
GN Name=trxr-1; ORFNames=C06G3.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROBABLE SELENOCYSTEINE.
RX PubMed=10362494; DOI=10.1006/bbrc.1999.0765;
RA Gladyshev V.N., Krause M., Xu X.-M., Korotkov K.V., Kryukov G.V.,
RA Sun Q.-A., Lee B.J., Wootton J.C., Hatfield D.L.;
RT "Selenocysteine-containing thioredoxin reductase in C. elegans.";
RL Biochem. Biophys. Res. Commun. 259:244-249(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 143-667, AND PROBABLE SELENOCYSTEINE AT
RP SEC-666.
RC STRAIN=Bristol N2;
RX PubMed=10419466; DOI=10.1074/jbc.274.31.21598;
RA Buettner C., Harney J.W., Berry M.J.;
RT "The Caenorhabditis elegans homologue of thioredoxin reductase contains a
RT selenocysteine insertion sequence (SECIS) element that differs from
RT mammalian SECIS elements but directs selenocysteine incorporation.";
RL J. Biol. Chem. 274:21598-21602(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF SEC-666.
RX PubMed=21199936; DOI=10.1073/pnas.1006328108;
RA Stenvall J., Fierro-Gonzalez J.C., Swoboda P., Saamarthy K., Cheng Q.,
RA Cacho-Valadez B., Arner E.S., Persson O.P., Miranda-Vizuete A., Tuck S.;
RT "Selenoprotein TRXR-1 and GSR-1 are essential for removal of old cuticle
RT during molting in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1064-1069(2011).
CC -!- FUNCTION: Together with glutathione reductase gsr-1, required for the
CC reduction of disulfide groups in the cuticle during molting.
CC {ECO:0000269|PubMed:21199936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000269|PubMed:21199936};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, pharynx, seam cells,
CC hypodermis, rectal epithelial cells, neurons in the nerve ring and
CC amphid sheath cells. {ECO:0000269|PubMed:21199936}.
CC -!- PTM: Contains a selenide-sulfide bond between Cys-665 and Sec-666. This
CC bond is speculated to serve as redox-active pair (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype. RNAi-mediated knockdown of
CC gsr-1 in mutants lacking trxr-1 causes an arrest during larval molting
CC characterized by a partial detachment of the old cuticle and an
CC impaired ability to reduce cuticle components. Also results in growth
CC arrest during the postdauer molt. {ECO:0000269|PubMed:21199936}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF148217; AAD41826.1; -; mRNA.
DR EMBL; FO080396; CCD83555.1; -; Genomic_DNA.
DR EMBL; AF162693; AAD46625.1; -; mRNA.
DR PIR; T30091; T30091.
DR RefSeq; NP_001294239.1; NM_001307310.1.
DR STRING; 6239.C06G3.7; -.
DR iPTMnet; Q17745; -.
DR EPD; Q17745; -.
DR PaxDb; Q17745; -.
DR PeptideAtlas; Q17745; -.
DR EnsemblMetazoa; C06G3.7a.1; C06G3.7a.1; WBGene00015553.
DR GeneID; 177466; -.
DR KEGG; cel:CELE_C06G3.7; -.
DR UCSC; C06G3.7; c. elegans.
DR CTD; 31760; -.
DR WormBase; C06G3.7a; CE34250; WBGene00015553; trxr-1.
DR eggNOG; KOG4716; Eukaryota.
DR InParanoid; Q17745; -.
DR OMA; HPTCGEI; -.
DR OrthoDB; 581771at2759; -.
DR PhylomeDB; Q17745; -.
DR PRO; PR:Q17745; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00015553; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; Q17745; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; ISS:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0042395; P:ecdysis, collagen and cuticulin-based cuticle; IGI:WormBase.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01438; TGR; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome; Selenocysteine.
FT CHAIN 1..667
FT /note="Thioredoxin reductase 1"
FT /id="PRO_0000067980"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 639
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 202..219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT NON_STD 666
FT /note="Selenocysteine"
FT /evidence="ECO:0000269|PubMed:21199936"
FT DISULFID 219..224
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CROSSLNK 665..666
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000250"
FT MUTAGEN 666
FT /note="U->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21199936"
SQ SEQUENCE 667 AA; 74263 MW; 58B86D4274E4FA77 CRC64;
MKSLTELFGC FKRQPRQQEA SSPANPHVSD TLSMGVAASG MPPPKRPAPA ESPTLPGETL
VDAPGIPLKE ALKEAANSKI VIFYNSSDEE KQLVEFETYL NSLKEPADAE KPLEIPEIKK
LQVSRASQKV IQYLTLHTSW PLMYIKGNAV GGLKELKALK QDYLKEWLRD HTYDLIVIGG
GSGGLAAAKE ASRLGKKVAC LDFVKPSPQG TSWGLGGTCV NVGCIPKKLM HQASLLGHSI
HDAKKYGWKL PEGKVEHQWN HLRDSVQDHI ASLNWGYRVQ LREKTVTYIN SYGEFTGPFE
ISATNKKKKV EKLTADRFLI STGLRPKYPE IPGVKEYTIT SDDLFQLPYS PGKTLCVGAS
YVSLECAGFL HGFGFDVTVM VRSILLRGFD QDMAERIRKH MIAYGMKFEA GVPTRIEQID
EKTDEKAGKY RVFWPKKNEE TGEMQEVSEE YNTILMAIGR EAVTDDVGLT TIGVERAKSK
KVLGRREQST TIPWVYAIGD VLEGTPELTP VAIQAGRVLM RRIFDGANEL TEYDQIPTTV
FTPLEYGCCG LSEEDAMMKY GKDNIIIYHN VFNPLEYTIS ERMDKDHCYL KMICLRNEEE
KVVGFHILTP NAGEVTQGFG IALKLAAKKA DFDRLIGIHP TVAENFTTLT LEKKEGDEEL
QASGCUG
