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 27-MAR-2024, entry version 99.
DE RecName: Full=Protein disulfide-isomerase TMX3;
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:Q96JJ7};
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. May act as a dithiol
CC oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria
CC contact sites via its ability to regulate redox signals.
CC {ECO:0000250|UniProtKB:Q96JJ7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:Q96JJ7};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96JJ7}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96JJ7}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250|UniProtKB:Q9Y320}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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 EMBL; BC073549; AAH73549.1; -; mRNA.
DR RefSeq; NP_001085926.1; NM_001092457.1.
DR AlphaFoldDB; Q6GNG3; -.
DR SMR; Q6GNG3; -.
DR GlyCosmos; Q6GNG3; 2 sites, No reported glycans.
DR DNASU; 444355; -.
DR GeneID; 444355; -.
DR KEGG; xla:444355; -.
DR AGR; Xenbase:XB-GENE-946771; -.
DR CTD; 444355; -.
DR Xenbase; XB-GENE-946771; tmx3.S.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 444355; Expressed in egg cell and 19 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd03000; PDI_a_TMX3; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR46426; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR PANTHER; PTHR46426:SF1; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 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 /evidence="ECO:0000255"
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 ACT_SITE 53
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9H3N1"
FT ACT_SITE 56
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9H3N1"
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
//
