Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00856
Entry Name
UniProt Accession
Theoretical PI
4.91
Molecular Weight
31791.22
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Thioredoxin-related transmembrane protein 1
Protein Synonyms/Alias
Thioredoxin domain-containing protein 1; Transmembrane Trx-related protein;
Gene Name
TMX1
Gene Synonyms/Alias
TMX; TXNDC; TXNDC1; PSEC0085; UNQ235/PRO268;
Created Date
10-MAY-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
106
Canonical
ALPTIYHCKDGEFRR
[1]
S-Palmitoylation
205
Canonical
CMIFVADCLCPSKRR
[1]
S-Palmitoylation
207
Canonical
IFVADCLCPSKRRRP
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions.
Sequence Annotation
Topological domain: 27 180 Extracellular.
Transmembrane: 181 203 Helical.
Topological domain: 204 280 Cytoplasmic.
Domain: 27 132 Thioredoxin.
Modified residue: 247 247 Phosphoserine.
Modified residue: 270 270 Phosphoserine.
Modified residue: 280 280 Phosphoserine.
Protein Length
280 AA.
Protein Sequence
(Canonical)
MAPSGSLAVP LAVLVLLLWG APWTHGRRSN VRVITDENWR ELLEGDWMIE FYAPWCPACQ  60
NLQPEWESFA EWGEDLEVNI AKVDVTEQPG LSGRFIITAL PTIYHCKDGE FRRYQGPRTK  120
KDFINFISDK EWKSIEPVSS WFGPGSVLMS SMSALFQLSM WIRTCHNYFI EDLGLPVWGS  180
YTVFALATLF SGLLLGLCMI FVADCLCPSK RRRPQPYPYP SKKLLSESAQ PLKKVEEEQE  240
ADEEDVSEEE AESKEGTNKD FPQNAIRQRS LGPSLATDKS                        280
FASTA
(Canonical)
>LipidDB-9606-00856|Q9H3N1
MAPSGSLAVPLAVLVLLLWGAPWTHGRRSNVRVITDENWRELLEGDWMIEFYAPWCPACQ
NLQPEWESFAEWGEDLEVNIAKVDVTEQPGLSGRFIITALPTIYHCKDGEFRRYQGPRTK
KDFINFISDKEWKSIEPVSSWFGPGSVLMSSMSALFQLSMWIRTCHNYFIEDLGLPVWGS
YTVFALATLFSGLLLGLCMIFVADCLCPSKRRRPQPYPYPSKKLLSESAQPLKKVEEEQE
ADEEDVSEEEAESKEGTNKDFPQNAIRQRSLGPSLATDKS
Gene Ontology
GO:0005783; C:endoplasmic reticulum; IDA:HPA
GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005730; C:nucleolus; IDA:HPA
GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB
GO:0003756; F:protein disulfide isomerase activity; IBA:RefGenome
GO:0045454; P:cell redox homeostasis; IEA:InterPro
GO:0006457; P:protein folding; IBA:RefGenome
GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB
Interpro
InterPro; IPR012336; Thioredoxin-like_fold
InterPro; IPR017937; Thioredoxin_CS
InterPro; IPR013766; Thioredoxin_domain
Pfam
Pfam; PF00085; Thioredoxin;
SMART
PROSITE
PROSITE; PS00194; THIOREDOXIN_1;
PROSITE; PS51352; THIOREDOXIN_2;
PRINTS