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TMX2_XENLA
ID   TMX2_XENLA              Reviewed;         287 AA.
AC   Q58E26;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Thioredoxin-related transmembrane protein 2;
DE   AltName: Full=Thioredoxin domain-containing protein 14;
DE   Flags: Precursor;
GN   Name=tmx2; Synonyms=txndc14;
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2005) 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; BC092100; AAH92100.1; -; mRNA.
DR   RefSeq; NP_001089331.1; NM_001095862.1.
DR   AlphaFoldDB; Q58E26; -.
DR   SMR; Q58E26; -.
DR   MaxQB; Q58E26; -.
DR   DNASU; 734381; -.
DR   GeneID; 734381; -.
DR   KEGG; xla:734381; -.
DR   CTD; 734381; -.
DR   Xenbase; XB-GENE-865871; tmx2.S.
DR   OrthoDB; 1107509at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 734381; Expressed in brain 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: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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Membrane; Mitochondrion;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..287
FT                   /note="Thioredoxin-related transmembrane protein 2"
FT                   /id="PRO_0000315758"
FT   TOPO_DOM        14..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          137..209
FT                   /note="Thioredoxin"
FT   MOTIF           284..287
FT                   /note="Di-lysine motif"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   287 AA;  33125 MW;  EE94BFDFAE7E03F5 CRC64;
     MAVLAPLLAV LYAAPGLLRW VSQPYYLISA LLSASFLLVR KVPPACSVLP TQREDGNPCD
     FDWREVEILM FLSAIVMMKN RRSITVEQHI GNIFMFSKVA NTILFFRLDL RMGLLYITLC
     IVFLMTCKPP LYLGPEHIKY FSDKTLEEEM QSDGRVSWIV EFFANWSSEC QSFAPIYAEL
     SLKYNCAGLK FGKVDIGRYP EVSCRYSISP SPLSKQLPTL ILFQGGREVF RRPQVDKKGR
     AVSWSFTQEN VIREFNLNEL YLKAKKIRKH QEESIHENEW NDGKKDQ
 
 
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