ID   TMX2_RAT                Reviewed;         295 AA.
AC   Q5XIK2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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       Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to
CC       endoplasmic reticulum mitochondria-associated membrane (MAMs) that
CC       connect the endoplasmic reticulum and the mitochondria.
CC       {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; BC083678; AAH83678.1; -; mRNA.
DR   RefSeq; NP_001007644.1; NM_001007643.1.
DR   AlphaFoldDB; Q5XIK2; -.
DR   BMRB; Q5XIK2; -.
DR   SMR; Q5XIK2; -.
DR   STRING; 10116.ENSRNOP00000007914; -.
DR   PhosphoSitePlus; Q5XIK2; -.
DR   SwissPalm; Q5XIK2; -.
DR   jPOST; Q5XIK2; -.
DR   PaxDb; 10116-ENSRNOP00000007914; -.
DR   Ensembl; ENSRNOT00000007914.5; ENSRNOP00000007914.3; ENSRNOG00000005308.5.
DR   Ensembl; ENSRNOT00055034937; ENSRNOP00055028353; ENSRNOG00055020460.
DR   Ensembl; ENSRNOT00060018211; ENSRNOP00060014174; ENSRNOG00060010748.
DR   Ensembl; ENSRNOT00065037176; ENSRNOP00065029984; ENSRNOG00065021837.
DR   GeneID; 295701; -.
DR   KEGG; rno:295701; -.
DR   UCSC; RGD:1359456; rat.
DR   AGR; RGD:1359456; -.
DR   CTD; 51075; -.
DR   RGD; 1359456; Tmx2.
DR   eggNOG; KOG0914; Eukaryota.
DR   GeneTree; ENSGT00390000003751; -.
DR   HOGENOM; CLU_064868_0_0_1; -.
DR   InParanoid; Q5XIK2; -.
DR   OMA; FYTAWNP; -.
DR   OrthoDB; 7109at2759; -.
DR   PhylomeDB; Q5XIK2; -.
DR   TreeFam; TF314606; -.
DR   PRO; PR:Q5XIK2; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000005308; Expressed in cerebellum and 18 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   CDD; cd02962; TMX2; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; THIOREDOXIN-RELATED; 1.
DR   PANTHER; PTHR15853:SF0; THIOREDOXIN-RELATED TRANSMEMBRANE PROTEIN 2; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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..295
FT                   /note="Thioredoxin-related transmembrane protein 2"
FT                   /id="PRO_0000315756"
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..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          114..269
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          266..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           292..295
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"
SQ   SEQUENCE   295 AA;  33866 MW;  C64BA65CDC600B34 CRC64;
     MAVLAPLIAL VYSVPRLSRW LARPYCLLSA LLSIAFLLVR KLPPICNGLP TQREDGNPCD
     FDWREVEILM FLSAIVMMKN RRSITVEQHV GNIFMFSKVA NAILFFRLDI RMGLLYLTLC
     IVFLMTCKPP LYMGPEYIKY FNDKTIDEEL ERDKRVTWIV EFFANWSNDC QSFAPIYADL
     SLKYNCSGLN FGKVDVGRYT DVSTRYKVST SPLTKQLPTL ILFQGGKEVM RRPQIDKKGR
     AVSWTFSEEN VIREFNLNEL YQRAKKLSKG GDMSEEKPGN PTPTAVPDGE NKKDK
//