TXD12_RAT
ID TXD12_RAT Reviewed; 170 AA.
AC Q498E0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thioredoxin domain-containing protein 12 {ECO:0000250|UniProtKB:O95881};
DE EC=1.8.4.2 {ECO:0000250|UniProtKB:O95881};
DE Flags: Precursor;
GN Name=Txndc12 {ECO:0000312|RGD:1305960};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=12930873; DOI=10.1074/mcp.m300053-mcp200;
RA Knoblach B., Keller B.O., Groenendyk J., Aldred S., Zheng J., Lemire B.D.,
RA Li L., Michalak M.;
RT "ERp19 and ERp46, new members of the thioredoxin family of endoplasmic
RT reticulum proteins.";
RL Mol. Cell. Proteomics 2:1104-1119(2003).
CC -!- FUNCTION: Protein-disulfide reductase of the endoplasmic reticulum that
CC promotes disulfide bond formation in client proteins through its thiol-
CC disulfide oxidase activity. {ECO:0000250|UniProtKB:O95881}.
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:0000250|UniProtKB:O95881};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21066;
CC Evidence={ECO:0000250|UniProtKB:O95881};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:12930873}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00256.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC100255; AAI00256.1; ALT_INIT; mRNA.
DR RefSeq; NP_001094310.1; NM_001100840.1.
DR AlphaFoldDB; Q498E0; -.
DR SMR; Q498E0; -.
DR IntAct; Q498E0; 2.
DR STRING; 10116.ENSRNOP00000010700; -.
DR GlyGen; Q498E0; 1 site.
DR iPTMnet; Q498E0; -.
DR PhosphoSitePlus; Q498E0; -.
DR jPOST; Q498E0; -.
DR PaxDb; Q498E0; -.
DR PRIDE; Q498E0; -.
DR Ensembl; ENSRNOT00000100650; ENSRNOP00000094562; ENSRNOG00000008090.
DR GeneID; 298370; -.
DR KEGG; rno:298370; -.
DR UCSC; RGD:1305960; rat.
DR CTD; 51060; -.
DR RGD; 1305960; Txndc12.
DR eggNOG; ENOG502RXP1; Eukaryota.
DR GeneTree; ENSGT00530000063273; -.
DR HOGENOM; CLU_088048_2_0_1; -.
DR InParanoid; Q498E0; -.
DR OMA; DIAWVKW; -.
DR OrthoDB; 1382017at2759; -.
DR TreeFam; TF321449; -.
DR PRO; PR:Q498E0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008090; Expressed in ovary and 20 other tissues.
DR Genevisible; Q498E0; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; ISS:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR CDD; cd02959; ERp19; 1.
DR InterPro; IPR037462; ERp19.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Oxidoreductase;
KW Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:O95881"
FT CHAIN 25..170
FT /note="Thioredoxin domain-containing protein 12"
FT /id="PRO_0000233975"
FT MOTIF 167..170
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..67
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 170 AA; 19019 MW; 444B6C9BE12C5E44 CRC64;
MSLRFGATCL LSFSFLLLIT SSDGRTGLGK GFGDHIHWRT LEDGKKEAAA SGLPLMVIIH
KSWCGACKAL KPKFAESTEI SELSHNFVMV NLEDEEEPRD EDFSPDGGYI PRILFLDPSG
KVRPEIINES GNPSYKYFYV SAEQVVQGMK EAQVRLTGDA FREKHFQDEL
