TMX1_BOVIN
ID TMX1_BOVIN Reviewed; 278 AA.
AC Q0Z7W6; A3KN45; A5D9C0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Thioredoxin-related transmembrane protein 1;
DE AltName: Full=Thioredoxin domain-containing protein 1;
DE Flags: Precursor;
GN Name=TMX1; Synonyms=TXNDC1;
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 [GENOMIC DNA].
RA Heaton M.P., Clawson M.L., Snelling W.M., Keele J.W., Harhay G.P.,
RA Wiedmann R.T., Bennett G.L., Smith T.P.L., Freking B.A., Van Tassell C.P.,
RA Sonstegard T.S., Gasbarre L.C., Moore S.S., Murdoch B., McKay S.D.,
RA Kalbfleisch T., Laegreid W.W.;
RT "Estimating probability of parentage in U.S. beef and dairy cattle with
RT single nucleotide polymorphisms.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May participate in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyze dithiol-disulfide exchange reactions. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC Note=Predominantly found in the endoplasmic reticulum. {ECO:0000250}.
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DR EMBL; DQ786761; ABG45803.1; -; Genomic_DNA.
DR EMBL; BT030539; ABQ12979.1; -; mRNA.
DR EMBL; BC133591; AAI33592.1; -; mRNA.
DR RefSeq; NP_001068853.1; NM_001075385.2.
DR AlphaFoldDB; Q0Z7W6; -.
DR SMR; Q0Z7W6; -.
DR STRING; 9913.ENSBTAP00000014908; -.
DR PaxDb; Q0Z7W6; -.
DR PRIDE; Q0Z7W6; -.
DR Ensembl; ENSBTAT00000014908; ENSBTAP00000014908; ENSBTAG00000011225.
DR GeneID; 509037; -.
DR KEGG; bta:509037; -.
DR CTD; 81542; -.
DR VEuPathDB; HostDB:ENSBTAG00000011225; -.
DR VGNC; VGNC:50016; TMX1.
DR eggNOG; KOG0913; Eukaryota.
DR GeneTree; ENSGT00940000155959; -.
DR HOGENOM; CLU_069292_2_1_1; -.
DR InParanoid; Q0Z7W6; -.
DR OMA; WMIEFHA; -.
DR OrthoDB; 1481386at2759; -.
DR TreeFam; TF106376; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000011225; Expressed in spermatid and 107 other tissues.
DR ExpressionAtlas; Q0Z7W6; baseline.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
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; Electron transport; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Redox-active center; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..278
FT /note="Thioredoxin-related transmembrane protein 1"
FT /id="PRO_0000273551"
FT TOPO_DOM 27..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..132
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 213..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3N1"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3N1"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3N1"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3N1"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3N1"
FT DISULFID 56..59
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 278 AA; 31581 MW; A95E65CF18F008A5 CRC64;
MAPSGSLRIP VAVLLLLLWG APWAHGKRSD VRIITDENWR ELLEGEWMIE FYAPWCPACQ
NLQPEWESFA EWGEDLEVNV AKVDVTEQPG LSGRFIITAL PTIYHCKDGE FRRYQGPRTK
KDFINFISDK EWKSIEPVSS WFGPGSILMS SMSALFQLSM WIRTCHNYFI EDLGLPIWGS
YTVFALATLL SGLLLGLFMI FVADCLCPSK RRRPQPYPSR KLLPESSQPL KKVEEEQEAD
VEDVSEEESE SKEGANKDFA QNAVRQRSVG PSLATDKS
