(data stored in ACNUC5340 zone)

SWISSPROT: 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   08-MAY-2019, entry version 136.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   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
RT   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;
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
CC       the presence of NADPH and glutathione reductase. Reduces low
CC       molecular weight disulfides and proteins.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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   SMR; P12309; -.
DR   STRING; 9823.ENSSSCP00000015066; -.
DR   PaxDb; P12309; -.
DR   PeptideAtlas; P12309; -.
DR   PRIDE; P12309; -.
DR   Ensembl; ENSSSCT00000048927; ENSSSCP00000046535; ENSSSCG00000039731.
DR   Ensembl; ENSSSCT00000051052; ENSSSCP00000059302; ENSSSCG00000039731.
DR   GeneID; 397463; -.
DR   KEGG; ssc:397463; -.
DR   CTD; 2745; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   eggNOG; COG0695; LUCA.
DR   GeneTree; ENSGT00900000141068; -.
DR   HOGENOM; HOG000095204; -.
DR   InParanoid; P12309; -.
DR   KO; K03676; -.
DR   OMA; PNIFIGQ; -.
DR   OrthoDB; 1535999at2759; -.
DR   TreeFam; TF326994; -.
DR   EvolutionaryTrace; P12309; -.
DR   Proteomes; UP000008227; Chromosome 2.
DR   Bgee; ENSSSCG00000014167; Expressed in 6 organ(s), highest expression level in lung.
DR   ExpressionAtlas; P12309; differential.
DR   Genevisible; P12309; SS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; 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;
DR   PRODOM; P12309.
DR   SWISS-2DPAGE; P12309.
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Electron transport;
KW   Redox-active center; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P10575}.
FT   CHAIN         2    106       Glutaredoxin-1.
FT                                /FTId=PRO_0000141602.
FT   DOMAIN        3    106       Glutaredoxin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00686}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:P10575}.
FT   MOD_RES       9      9       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9QUH0}.
FT   DISULFID     23     26       Redox-active.
FT   DISULFID     79     83       {ECO:0000269|PubMed:3571278}.
FT   CONFLICT      2      3       AQ -> QA (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   HELIX         3      9       {ECO:0000244|PDB:1KTE}.
FT   STRAND       15     19       {ECO:0000244|PDB:1KTE}.
FT   HELIX        24     35       {ECO:0000244|PDB:1KTE}.
FT   STRAND       42     47       {ECO:0000244|PDB:1KTE}.
FT   HELIX        48     50       {ECO:0000244|PDB:1KTE}.
FT   HELIX        54     65       {ECO:0000244|PDB:1KTE}.
FT   STRAND       72     75       {ECO:0000244|PDB:1KTE}.
FT   STRAND       78     82       {ECO:0000244|PDB:1KTE}.
FT   HELIX        83     91       {ECO:0000244|PDB:1KTE}.
FT   HELIX        94    102       {ECO:0000244|PDB:1KTE}.
SQ   SEQUENCE   106 AA;  11828 MW;  FEA9B18376E1D5B0 CRC64;
     MAQAFVNSKI QPGKVVVFIK PTCPFCRKTQ ELLSQLPFKE GLLEFVDITA TSDTNEIQDY
     LQQLTGARTV PRVFIGKECI GGCTDLESMH KRGELLTRLQ QIGALK
//

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