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