ID I3M789_ICTTR Unreviewed; 172 AA.
AC I3M789;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Thioredoxin domain-containing protein 12 {ECO:0000256|ARBA:ARBA00016955};
DE EC=1.8.4.2 {ECO:0000256|ARBA:ARBA00013094};
GN Name=TXNDC12 {ECO:0000313|Ensembl:ENSSTOP00000005447.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000005447.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000005447.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + 2 glutathione = [protein]-dithiol +
CC glutathione disulfide; Xref=Rhea:RHEA:21064, Rhea:RHEA-COMP:10593,
CC Rhea:RHEA-COMP:10594, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.8.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00033687};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21066;
CC Evidence={ECO:0000256|ARBA:ARBA00033687};
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DR EMBL; AGTP01043098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01043099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005326132.1; XM_005326075.2.
DR AlphaFoldDB; I3M789; -.
DR STRING; 43179.ENSSTOP00000005447; -.
DR Ensembl; ENSSTOT00000006088.3; ENSSTOP00000005447.3; ENSSTOG00000006093.3.
DR GeneID; 101971496; -.
DR CTD; 51060; -.
DR eggNOG; ENOG502RXP1; Eukaryota.
DR GeneTree; ENSGT00530000063273; -.
DR HOGENOM; CLU_088048_2_0_1; -.
DR InParanoid; I3M789; -.
DR OrthoDB; 101767at2759; -.
DR TreeFam; TF321449; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IEA:UniProtKB-EC.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR CDD; cd02959; ERp19; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR037462; ERp19.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR15337; ANTERIOR GRADIENT PROTEIN-RELATED; 1.
DR PANTHER; PTHR15337:SF10; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 12; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..172
FT /note="Thioredoxin domain-containing protein 12"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011757692"
FT DOMAIN 6..156
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 172 AA; 19351 MW; 7833AF1B74BF584C CRC64;
MEMWPRLGAT CLLGFSFLLL ITSSDGHIGL GKGFGDHIHW RTLEDGKREA AASGLPIMVI
IHKSWCGACK ALKPKFAEST EISELSHNFI MVNLEDEEEP KDEDFSPDGG YIPRILFLDP
SGKVHPEIIN ENGNPSYKYF YINAEQVVQG MKEAQERLTG DAFREKHLED EL
//
