ID   TXD12_BOVIN             Reviewed;         172 AA.
AC   Q5E936;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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:0000250|UniProtKB:O95881};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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
CC       {ECO:0000250|UniProtKB:O95881, ECO:0000255|PROSITE-ProRule:PRU10138}.
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DR   EMBL; BT021084; AAX09101.1; -; mRNA.
DR   EMBL; BC102314; AAI02315.1; -; mRNA.
DR   RefSeq; NP_001015536.1; NM_001015536.1.
DR   RefSeq; XP_015320857.1; XM_015465371.1.
DR   AlphaFoldDB; Q5E936; -.
DR   SMR; Q5E936; -.
DR   STRING; 9913.ENSBTAP00000014645; -.
DR   PaxDb; Q5E936; -.
DR   PeptideAtlas; Q5E936; -.
DR   PRIDE; Q5E936; -.
DR   Ensembl; ENSBTAT00000014645; ENSBTAP00000014645; ENSBTAG00000011024.
DR   GeneID; 506991; -.
DR   KEGG; bta:506991; -.
DR   CTD; 51060; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011024; -.
DR   VGNC; VGNC:36535; TXNDC12.
DR   eggNOG; ENOG502RXP1; Eukaryota.
DR   GeneTree; ENSGT00530000063273; -.
DR   HOGENOM; CLU_088048_2_0_1; -.
DR   InParanoid; Q5E936; -.
DR   OMA; DIAWVKW; -.
DR   OrthoDB; 1382017at2759; -.
DR   TreeFam; TF321449; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000011024; Expressed in spermatocyte and 104 other tissues.
DR   ExpressionAtlas; Q5E936; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; ISS:UniProtKB.
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; IEA:Ensembl.
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; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Oxidoreductase; Redox-active center;
KW   Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250|UniProtKB:O95881"
FT   CHAIN           27..172
FT                   /note="Thioredoxin domain-containing protein 12"
FT                   /id="PRO_0000233974"
FT   MOTIF           169..172
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   DISULFID        66..69
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   172 AA;  19222 MW;  BE0614789E51D437 CRC64;
     MELRPRLGAT CLLGFSFLLL VTSSHGPNGL GKGFGDHIHW RTLEDGKKEA AASGLPLMVI
     IHKSWCGACK ALKPKFAEST EISELSHNFV MVNLEDEEEP KDEDFSPDGG YIPRILFLDP
     SGKVRPEIIN ENGNPSYKYF YISAEQVVQG MKEAQERLTG DAFREKHLED EL