ID   TMX3_XENLA              Reviewed;         452 AA.
AC   Q6GNG3;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Protein disulfide-isomerase TMX3;
DE            EC=5.3.4.1;
DE   AltName: Full=Thioredoxin domain-containing protein 10;
DE   AltName: Full=Thioredoxin-related transmembrane protein 3;
DE   Flags: Precursor;
GN   Name=tmx3; Synonyms=txndc10;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable disulfide isomerase, which participates in the
CC       folding of proteins containing disulfide bonds. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC       for type I membrane proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BC073549; AAH73549.1; -; mRNA.
DR   RefSeq; NP_001085926.1; NM_001092457.1.
DR   AlphaFoldDB; Q6GNG3; -.
DR   SMR; Q6GNG3; -.
DR   PRIDE; Q6GNG3; -.
DR   DNASU; 444355; -.
DR   GeneID; 444355; -.
DR   KEGG; xla:444355; -.
DR   CTD; 444355; -.
DR   Xenbase; XB-GENE-946771; tmx3.S.
DR   OrthoDB; 746938at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 444355; Expressed in egg cell and 19 other tissues.
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:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
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; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase; Membrane;
KW   Redox-active center; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..452
FT                   /note="Protein disulfide-isomerase TMX3"
FT                   /id="PRO_0000034188"
FT   TOPO_DOM        27..375
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        397..452
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..128
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          405..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           449..452
FT                   /note="Di-lysine motif"
FT   COMPBIAS        419..433
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..56
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   452 AA;  50861 MW;  DE4CB700D2255945 CRC64;
     MAAAGLCFIL AIVSSTSLLA SVPVSALVED LDDSFKENRK DDIWLVDFYA PWCGHCKKLE
     PVWNEVGIEI RTSGSPIRVG KIDATVYSSI ASEFGVRGFP TIKALKGDMA YNYRGPRTKE
     DIVEFANRVA GPLIRPLPSQ QMFDHVKKRH PVLFVYVGVE STLKEKFIEV ASELIVYTYF
     FSASEDVLPK YVTLNEVPAV LVFKDSTYFV YDEYEDGDLS SWVNKERFEG YLHIDGFTLY
     ELGDTGKLVA VAVIDEKNNS IEHTRIKSIA QDVAKNNRNN FHRDFQFGHM DGNDYINSLL
     MDELSIPTFV VLNTSNQQYF LPSKHIENPE EMIQFINSIL DGTAEAQGGD GILQRIKRVF
     YDAKSTVVSV FKSSPLLGCF LFGLPLGVIS IMCYGICTAD TEDGSEEMTR KDVIDQNASD
     EGSDEEEEKG REITDVSDED QQEKDFMEKK ID