ID A0A2Y9NAM0_DELLE Unreviewed; 311 AA.
AC A0A2Y9NAM0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Thioredoxin-related transmembrane protein 1 {ECO:0000313|RefSeq:XP_022426283.1};
GN Name=TMX1 {ECO:0000313|RefSeq:XP_022426283.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022426283.1};
RN [1] {ECO:0000313|RefSeq:XP_022426283.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022426283.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_022426283.1; XM_022570575.1.
DR AlphaFoldDB; A0A2Y9NAM0; -.
DR STRING; 9749.A0A2Y9NAM0; -.
DR Ensembl; ENSDLET00000011530; ENSDLEP00000010431; ENSDLEG00000007582.
DR KEGG; dle:111173164; -.
DR InParanoid; A0A2Y9NAM0; -.
DR OrthoDB; 2909094at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:Ensembl.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:Ensembl.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
DR GO; GO:0010868; P:negative regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; IEA:Ensembl.
DR GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR CDD; cd02994; PDI_a_TMX; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR46107; DUMPY: SHORTER THAN WILD-TYPE; 1.
DR PANTHER; PTHR46107:SF2; THIOREDOXIN-RELATED TRANSMEMBRANE PROTEIN 1; 1.
DR Pfam; PF00085; Thioredoxin; 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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 173..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 253..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 34962 MW; E81FE6E226B8FA66 CRC64;
MRTSRSARVG GSAEPLREVR AAALVVGGRA ADMAPSGSLR IPVAVLLLLL WGASWTHGRR
SDVRIITDEN WRELLEGEWM IEFYAPWCPA CQNLQPEWES FAEWGEDLEV NVAKVDVTEQ
PGLSGRFIIS ALPTVYHCKN GEFRRYQGPR TKKDFINFIS EKEWKSIEPV SSWVGPGSVL
MSSMSALFQL SMWIRTYHNY FIEDLGLPVW GSYTVFALAT LLSGLLLGLC MIFVADCLCP
SKRRRPQPYP SKKLLLESSQ PLKKVEEEQE ADEEDVSEEE PESKEGINTD FAQNAIRQRS
VAPSLATDKS S
//
