ID   GLRX3_XENTR             Reviewed;         326 AA.
AC   Q28ID3; A9JSB2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Glutaredoxin-3;
DE   AltName: Full=Thioredoxin-like protein 2;
GN   Name=glrx3; Synonyms=txnl2; ORFNames=TNeu109g06.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-326.
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Together with bola2, acts as a cytosolic iron-sulfur (Fe-S)
CC       cluster assembly factor that facilitates [2Fe-2S] cluster insertion
CC       into a subset of cytosolic proteins. Required for hemoglobin
CC       maturation. Does not possess any thyoredoxin activity since it lacks
CC       the conserved motif that is essential for catalytic activity.
CC       {ECO:0000250|UniProtKB:O76003, ECO:0000250|UniProtKB:Q9CQM9}.
CC   -!- SUBUNIT: Homodimer; the homodimer is independent of 2Fe-2S clusters.
CC       Heterotrimer; forms a heterotrimeric complex composed by two bola2
CC       molecules and one glrx3 molecule; linked by [2Fe-2S] clusters.
CC       {ECO:0000250|UniProtKB:O76003, ECO:0000250|UniProtKB:Q9CQM9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:O76003}.
CC   -!- DOMAIN: The thioredoxin domain lacks the two redox-active cysteines.
CC       This strongly suggests that it lacks thioredoxin activity.
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DR   EMBL; CR760465; CAJ82722.1; -; mRNA.
DR   EMBL; BC155988; AAI55989.1; -; mRNA.
DR   RefSeq; NP_001017209.1; NM_001017209.2.
DR   AlphaFoldDB; Q28ID3; -.
DR   SMR; Q28ID3; -.
DR   STRING; 8364.ENSXETP00000044832; -.
DR   PaxDb; Q28ID3; -.
DR   GeneID; 549963; -.
DR   KEGG; xtr:549963; -.
DR   CTD; 10539; -.
DR   Xenbase; XB-GENE-492130; glrx3.
DR   eggNOG; KOG0911; Eukaryota.
DR   InParanoid; Q28ID3; -.
DR   OrthoDB; 1449534at2759; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000011308; Expressed in testis and 17 other tissues.
DR   ExpressionAtlas; Q28ID3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; ISS:UniProtKB.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; ISS:UniProtKB.
DR   CDD; cd03028; GRX_PICOT_like; 2.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR033658; GRX_PICOT-like.
DR   InterPro; IPR004480; Monothiol_GRX-rel.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10293; PTHR10293; 1.
DR   Pfam; PF00462; Glutaredoxin; 2.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 3.
DR   TIGRFAMs; TIGR00365; TIGR00365; 2.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome; Repeat.
FT   CHAIN           1..326
FT                   /note="Glutaredoxin-3"
FT                   /id="PRO_0000348928"
FT   DOMAIN          1..108
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          125..227
FT                   /note="Glutaredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DOMAIN          227..326
FT                   /note="Glutaredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   BINDING         150
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:O76003"
FT   BINDING         252
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:O76003"
SQ   SEQUENCE   326 AA;  36424 MW;  C013BFECC6C7AAD1 CRC64;
     MAAVLEAGSA GQFEQLIQNS AKSLTVVHFW APWAPQCTQM NEVMAELAKE QPQVMFVKLE
     AEAVPEVSEK YEVTSVPTFL FFKNSQKIDR LDGAHAPELT KRVQRHASST SFPATPNSAP
     KEDLNGRLKK LINAAPCMLF MKGSPQEPRC GFSRQIVALL NDQKVQFSSF DILSDEEVRQ
     GLKTFSNWPT YPQFYVKGEL VGGLDIVKEM VASGELDQMC PKAQSLEERL KALVNKAPVM
     LFMKGNKEMA KCGFSRQILE IMNNTGVTYE TFDILEDEEV RQGLKAYSNW PTYPQLYVKG
     ELVGGLDIIK ELKESGELVS VLKGDQ