ID   TMX2_XENTR              Reviewed;         287 AA.
AC   Q6DFS0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Thioredoxin-related transmembrane protein 2;
DE   AltName: Full=Thioredoxin domain-containing protein 14;
DE   Flags: Precursor;
GN   Name=tmx2; Synonyms=txndc14; ORFNames=TEgg063n24.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoplasmic reticulum and mitochondria-associated protein
CC       that probably functions as a regulator of cellular redox state and
CC       thereby regulates protein post-translational modification, protein
CC       folding and mitochondrial activity. {ECO:0000250|UniProtKB:Q9Y320}.
CC   -!- SUBUNIT: Monomer (By similarity). Homodimer; disulfide-linked (By
CC       similarity). Occurs in both reduced and oxidized monomeric form (By
CC       similarity). Oxidative conditions increase homodimerization (By
CC       similarity). {ECO:0000250|UniProtKB:Q9Y320}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9Y320}; Single-pass type I membrane protein
CC       {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9Y320}.
CC       Note=Localizes to endoplasmic reticulum mitochondria-associated
CC       membrane (MAMs) that connect the endoplasmic reticulum and the
CC       mitochondria. {ECO:0000250|UniProtKB:Q9Y320}.
CC   -!- DOMAIN: The thioredoxin domain lacks the 2 redox-active cysteines,
CC       suggesting that it lacks thioredoxin activity. {ECO:0000305}.
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC       for type I membrane proteins. {ECO:0000305}.
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DR   EMBL; CR761011; CAJ82149.1; -; mRNA.
DR   EMBL; BC076663; AAH76663.1; -; mRNA.
DR   RefSeq; NP_001005010.1; NM_001005010.1.
DR   AlphaFoldDB; Q6DFS0; -.
DR   SMR; Q6DFS0; -.
DR   STRING; 8364.ENSXETP00000055702; -.
DR   PaxDb; Q6DFS0; -.
DR   DNASU; 448502; -.
DR   Ensembl; ENSXETT00000055702; ENSXETP00000055702; ENSXETG00000026417.
DR   GeneID; 448502; -.
DR   KEGG; xtr:448502; -.
DR   CTD; 51075; -.
DR   Xenbase; XB-GENE-489478; tmx2.
DR   eggNOG; KOG0914; Eukaryota.
DR   HOGENOM; CLU_064868_0_0_1; -.
DR   InParanoid; Q6DFS0; -.
DR   OMA; FYTAWNP; -.
DR   OrthoDB; 1107509at2759; -.
DR   PhylomeDB; Q6DFS0; -.
DR   TreeFam; TF314606; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000026417; Expressed in egg cell and 16 other tissues.
DR   ExpressionAtlas; Q6DFS0; differential.
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:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   CDD; cd02962; TMX2; 1.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR039101; TMX2.
DR   InterPro; IPR037463; TMX2_thioredoxin_dom.
DR   PANTHER; PTHR15853; PTHR15853; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Membrane; Mitochondrion;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..287
FT                   /note="Thioredoxin-related transmembrane protein 2"
FT                   /id="PRO_0000315759"
FT   TOPO_DOM        36..112
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          135..269
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           284..287
FT                   /note="Di-lysine motif"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   287 AA;  33250 MW;  164A055686F72A37 CRC64;
     MAVLAPLLAF LYAVPGLLRW VSQPYYLLSA LLSVSFLLVR KVPPVCSVLP TQREDGNPCD
     FDWREVEILM FLSAIVMMKN RRSITVEQHI GNIFMFSKVA NTILFFRLDL RMGLLYITLC
     IVFLMTCKPP LYLGPEHIKY FSDKTLEEEL QSDGRVSWII EFFANWSSEC QSFAPIYAEL
     SLKYNCAGLK FGKVDIGRYP EVSSRYSISP SPLSKQLPTL ILFQGGREIF RRPQVDKKGR
     AVSWSFTQEN VIREFNLNEL YQKAKKIRKH QEDTINENEY NDSKKDQ