TMX2_RAT
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 03-AUG-2022, entry version 108.
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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 jPOST; Q5XIK2; -.
DR PaxDb; Q5XIK2; -.
DR PRIDE; Q5XIK2; -.
DR Ensembl; ENSRNOT00000007914; ENSRNOP00000007914; ENSRNOG00000005308.
DR GeneID; 295701; -.
DR KEGG; rno:295701; -.
DR UCSC; RGD:1359456; rat.
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; 1107509at2759; -.
DR PhylomeDB; Q5XIK2; -.
DR TreeFam; TF314606; -.
DR PRO; PR:Q5XIK2; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000005308; Expressed in cerebellum and 18 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
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:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:RGD.
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 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..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
