GLRX3_BOVIN
ID GLRX3_BOVIN Reviewed; 334 AA.
AC Q58DA7; A3KMZ2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Glutaredoxin-3;
DE AltName: Full=PKC-interacting cousin of thioredoxin;
DE Short=PICOT;
DE AltName: Full=Thioredoxin-like protein 2;
GN Name=GLRX3; Synonyms=TXNL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-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 (By similarity). Acts as a critical
CC negative regulator of cardiac hypertrophy and a positive inotropic
CC regulator (By similarity). Required for hemoglobin maturation. Does not
CC possess any thyoredoxin activity since it lacks the conserved motif
CC that is essential for catalytic activity (By similarity).
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 Interacts (via N-terminus) with PRKCQ/PKC-theta (By similarity).
CC Interacts (via C-terminus) with CSRP3 (By similarity). Interacts with
CC CSRP2 (By similarity). {ECO:0000250|UniProtKB:O76003,
CC ECO:0000250|UniProtKB:Q9CQM9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O76003}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:O76003}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q9CQM9}. Note=Under the plasma membrane (By
CC similarity). After PMA stimulation, GLRX3 and PRKCQ/PKC-theta
CC translocate to a more extended submembrane area (By similarity). In the
CC Z line, found associated with CSRP3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9CQM9}.
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; BT021690; AAX46537.1; -; mRNA.
DR EMBL; BC133428; AAI33429.1; -; mRNA.
DR RefSeq; NP_001030273.1; NM_001035101.1.
DR AlphaFoldDB; Q58DA7; -.
DR SMR; Q58DA7; -.
DR STRING; 9913.ENSBTAP00000006613; -.
DR PaxDb; Q58DA7; -.
DR PeptideAtlas; Q58DA7; -.
DR PRIDE; Q58DA7; -.
DR GeneID; 511528; -.
DR KEGG; bta:511528; -.
DR CTD; 10539; -.
DR eggNOG; KOG0911; Eukaryota.
DR InParanoid; Q58DA7; -.
DR OrthoDB; 1449534at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
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:0010614; P:negative regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
DR GO; GO:0002026; P:regulation of the force of heart contraction; 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; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O76003"
FT CHAIN 2..334
FT /note="Glutaredoxin-3"
FT /id="PRO_0000239988"
FT DOMAIN 2..116
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 145..235
FT /note="Glutaredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DOMAIN 236..334
FT /note="Glutaredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 110..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
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 260
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O76003"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76003"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76003"
FT CONFLICT 3
FT /note="G -> A (in Ref. 2; AAI33429)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="S -> A (in Ref. 2; AAI33429)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="N -> NQ (in Ref. 2; AAI33429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37298 MW; BFC5136B72EB47FB CRC64;
MAGGAAEAAA AVVEVGSSGQ FEELLRLRAK SLLVVHFWAP WAPQCAQMND VMAELAKEHQ
QVSFVKLEAE AVPEVSEKYE ISSVPTFLFF KNSQKIDRLD GAHAPELTKK VQRHASSGSF
SPSGSEHPKE DLSLRLKKLT HAAPCMLFMK GTPQEPRCGF SKQMVEILNK HNIQFSSFDI
FSDEEVRQGL KTYSSWPTYP QLYVSGELIG GLDIIKELEA SKELDTICPK APKLEERLKV
LTNKASVMLF MKGNKQEAKC GFSRQILEIL NSTGIEYETF DILEDEEVRQ GLKAYSNWPT
YPQLYVKGEL VGGLDIVKEL KENGELLPIL KGEN
