GLRX1_PIG
ID GLRX1_PIG Reviewed; 106 AA.
AC P12309;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Glutaredoxin-1;
DE AltName: Full=Thioltransferase-1;
DE Short=TTase-1;
GN Name=GLRX; Synonyms=GRX;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2583530; DOI=10.1016/0378-1119(89)90120-0;
RA Yang Y., Gan Z.-R., Wells W.W.;
RT "Cloning and sequencing the cDNA encoding pig liver thioltransferase.";
RL Gene 83:339-346(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Yang Y., Wells W.W.;
RT "Cloning and sequencing of the cDNA for pig liver thioltransferase
RT (glutaredoxin).";
RL J. Cell Biol. 107:747A-747A(1988).
RN [3]
RP PROTEIN SEQUENCE OF 2-106.
RC TISSUE=Liver;
RX PubMed=3571278; DOI=10.1016/s0021-9258(18)48298-1;
RA Gan Z.-R., Wells W.W.;
RT "The primary structure of pig liver thioltransferase.";
RL J. Biol. Chem. 262:6699-6703(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=8535236; DOI=10.1002/pro.5560041005;
RA Katti S.K., Robbins A.R., Yang Y., Wells W.W.;
RT "Crystal structure of thioltransferase at 2.2-A resolution.";
RL Protein Sci. 4:1998-2005(1995).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; M31453; AAA31132.1; -; mRNA.
DR PIR; JQ0117; GDPG.
DR RefSeq; NP_999398.1; NM_214233.1.
DR RefSeq; XP_005655046.1; XM_005654989.2.
DR PDB; 1KTE; X-ray; 2.20 A; A=2-106.
DR PDBsum; 1KTE; -.
DR AlphaFoldDB; P12309; -.
DR SMR; P12309; -.
DR STRING; 9823.ENSSSCP00000015066; -.
DR PaxDb; P12309; -.
DR PeptideAtlas; P12309; -.
DR PRIDE; P12309; -.
DR Ensembl; ENSSSCT00000051052; ENSSSCP00000059302; ENSSSCG00000039731.
DR Ensembl; ENSSSCT00015042086; ENSSSCP00015016629; ENSSSCG00015031581.
DR Ensembl; ENSSSCT00025011805; ENSSSCP00025004706; ENSSSCG00025008850.
DR Ensembl; ENSSSCT00030011918; ENSSSCP00030005351; ENSSSCG00030008733.
DR Ensembl; ENSSSCT00035063938; ENSSSCP00035025886; ENSSSCG00035048008.
DR Ensembl; ENSSSCT00040014777; ENSSSCP00040005769; ENSSSCG00040011271.
DR Ensembl; ENSSSCT00050100287; ENSSSCP00050043495; ENSSSCG00050073370.
DR Ensembl; ENSSSCT00055017383; ENSSSCP00055013744; ENSSSCG00055008895.
DR Ensembl; ENSSSCT00060034428; ENSSSCP00060014750; ENSSSCG00060025386.
DR Ensembl; ENSSSCT00065016810; ENSSSCP00065006872; ENSSSCG00065012614.
DR Ensembl; ENSSSCT00065016819; ENSSSCP00065006878; ENSSSCG00065012614.
DR Ensembl; ENSSSCT00070018496; ENSSSCP00070015369; ENSSSCG00070009533.
DR GeneID; 397463; -.
DR KEGG; ssc:397463; -.
DR CTD; 2745; -.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00900000141068; -.
DR HOGENOM; CLU_026126_7_2_1; -.
DR InParanoid; P12309; -.
DR OMA; KPGHLEC; -.
DR OrthoDB; 1535999at2759; -.
DR TreeFam; TF326994; -.
DR Reactome; R-SSC-499943; Interconversion of nucleotide di- and triphosphates.
DR EvolutionaryTrace; P12309; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Chromosome 2.
DR Bgee; ENSSSCG00000039731; Expressed in epididymis and 46 other tissues.
DR ExpressionAtlas; P12309; baseline and differential.
DR Genevisible; P12309; SS.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P10575"
FT CHAIN 2..106
FT /note="Glutaredoxin-1"
FT /id="PRO_0000141602"
FT DOMAIN 3..106
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P10575"
FT MOD_RES 9
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QUH0"
FT DISULFID 23..26
FT /note="Redox-active"
FT DISULFID 79..83
FT /evidence="ECO:0000269|PubMed:3571278"
FT CONFLICT 2..3
FT /note="AQ -> QA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1KTE"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:1KTE"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:1KTE"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1KTE"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1KTE"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:1KTE"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1KTE"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1KTE"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1KTE"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:1KTE"
SQ SEQUENCE 106 AA; 11828 MW; FEA9B18376E1D5B0 CRC64;
MAQAFVNSKI QPGKVVVFIK PTCPFCRKTQ ELLSQLPFKE GLLEFVDITA TSDTNEIQDY
LQQLTGARTV PRVFIGKECI GGCTDLESMH KRGELLTRLQ QIGALK
