(data stored in ACNUC5340 zone)

HOGENOM: PIG2_95_PE3

ID   PIG2_95_PE3                          STANDARD;      PRT;   106 AA.
AC   PIG2_95_PE3; P12309;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Glutaredoxin-1;AltName: Full=Thioltransferase-1;
DE   Short=TTase-1; (PIG2_95.PE3).
GN   Name=GLRX; Synonyms=GRX;
OS   SUS SCROFA.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PIG2_95.PE3.
CC       Sus scrofa chromosome 2 Sscrofa9 partial sequence 91022235..92000905
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:GLRX1_PIG
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.
CC   -!- SIMILARITY: Contains 1 glutaredoxin domain.
CC   -!- GENE_FAMILY: HOG000095204 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Sus_scrofa;ENSSSCG00000014167;ENSSSCT00000015476;ENSSSCP00000015066.
DR   EMBL; AY550049; - ;
DR   EMBL; M31453; - ;
DR   UniProtKB/Swiss-Prot; P12309; -.
DR   EMBL; M31453; AAA31132.1; -; mRNA.
DR   PIR; JQ0117; GDPG.
DR   RefSeq; NP_999398.1; NM_214233.1.
DR   UniGene; Ssc.54096; -.
DR   PDB; 1KTE; X-ray; 2.20 A; A=2-104.
DR   PDBsum; 1KTE; -.
DR   ProteinModelPortal; P12309; -.
DR   SMR; P12309; 2-106.
DR   STRING; P12309; -.
DR   Ensembl; ENSSSCT00000015476; ENSSSCP00000015066; ENSSSCG00000014167.
DR   GeneID; 397463; -.
DR   KEGG; ssc:397463; -.
DR   CTD; 2745; -.
DR   OMA; TNAIQDY; -.
DR   OrthoDB; EOG4N8R6D; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier 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   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR011899; Glutaredoxin_euk/vir.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   TIGRFAMs; TIGR02180; GRX_euk; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   HOGENOMDNA; PIG2_95.PE3; -.
KW   ENSSSCG00000014167820036002503210000011;
KW   GLRX1_PIG; Q6QAS1_PIG; AY550049; M31453;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Electron transport;
KW   Redox-active center; Transport.
SQ   SEQUENCE   106 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAQAFVNSKI QPGKVVVFIK PTCPFCRKTQ ELLSQLPFKE GLLEFVDITA TSDTNEIQDY
     LQQLTGARTV PRVFIGKECI GGCTDLESMH KRGELLTRLQ QIGALK
//

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