ID   TMX2_PONAB              Reviewed;         296 AA.
AC   Q5RF53;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 77.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-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. Indirectly regulates neuronal
CC       proliferation, migration, and organization in the developing brain.
CC       {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). Interacts with CANX (By similarity). Interacts with ATP2A2
CC       (By 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; CR857308; CAH89604.1; -; mRNA.
DR   RefSeq; NP_001127174.1; NM_001133702.2.
DR   AlphaFoldDB; Q5RF53; -.
DR   BMRB; Q5RF53; -.
DR   SMR; Q5RF53; -.
DR   PRIDE; Q5RF53; -.
DR   GeneID; 100174226; -.
DR   KEGG; pon:100174226; -.
DR   CTD; 51075; -.
DR   InParanoid; Q5RF53; -.
DR   OrthoDB; 1107509at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Membrane; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..48
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..296
FT                   /note="Thioredoxin-related transmembrane protein 2"
FT                   /id="PRO_0000315755"
FT   TOPO_DOM        49..102
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..296
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          114..270
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          266..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           293..296
FT                   /note="Di-lysine motif"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y320"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y320"
FT   MOD_RES         288
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y320"
SQ   SEQUENCE   296 AA;  33966 MW;  298AF38AF08141D5 CRC64;
     MAVLAPLIAL VYSVPRLSRW LAQPYYLLSA LLSAAFLLVR KLPPLCHGLP TQREDGNPCD
     FDWREVEILM FLSAIVMMKN RRSITVEQHI GNIFMFSKVA NAILFFRLDI RMGLLYITLC
     IVFLMTCEPP LYMGPEYIKY FNDKTIDEEL ERDKKVTWIV EFFANWSNDC QSFAPIYADL
     SLKYNCTGLN FGKVDVGRYT DVSMRYKVST SPLTKQLPTL ILFQGGKEVM RRPQIDKKGR
     AVSWTFSEEN VIREFNLNEL YQRAKKPSKA GDSIPEEQPV ASAPTTVSDG ENKKDK