ID   TMX2A_DANRE             Reviewed;         301 AA.
AC   A8WG88;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Thioredoxin-related transmembrane protein 2-A {ECO:0000312|ZFIN:ZDB-GENE-050208-95};
DE   Flags: Precursor;
GN   Name=tmx2a {ECO:0000312|ZFIN:ZDB-GENE-050208-95}; ORFNames=zgc:172264;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:AAI54621.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=WIK {ECO:0000312|EMBL:AAI54621.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2007) 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. Homodimer; disulfide-linked. Occurs in both reduced
CC       and oxidized monomeric form. Oxidative conditions increase
CC       homodimerization. {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; BC154620; AAI54621.1; -; mRNA.
DR   RefSeq; NP_001103857.1; NM_001110387.1.
DR   AlphaFoldDB; A8WG88; -.
DR   SMR; A8WG88; -.
DR   STRING; 7955.ENSDARP00000098029; -.
DR   PaxDb; A8WG88; -.
DR   GeneID; 561718; -.
DR   KEGG; dre:561718; -.
DR   CTD; 561718; -.
DR   ZFIN; ZDB-GENE-050208-95; tmx2a.
DR   eggNOG; KOG0914; Eukaryota.
DR   HOGENOM; CLU_064868_0_0_1; -.
DR   InParanoid; A8WG88; -.
DR   OrthoDB; 1107509at2759; -.
DR   PhylomeDB; A8WG88; -.
DR   TreeFam; TF314606; -.
DR   PRO; PR:A8WG88; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IBA:GO_Central.
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   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..301
FT                   /note="Thioredoxin-related transmembrane protein 2-A"
FT                   /id="PRO_0000401126"
FT   TOPO_DOM        20..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..301
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          122..269
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          268..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           298..301
FT                   /note="Di-lysine motif"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  35172 MW;  7632C362B4B50E3A CRC64;
     MSLIRGLIST IYYLPKIYKW FYRPYYFLSL LMTLAFVIVR CCPGLCEHLP SQREDGDSCA
     FDWREVEIFM FLGAIVMMKN RRAVTVEQHI GNIFLFSKVA NVVLFFRVDL RFGLLYLTLC
     VVFLITCKPP AYMGPENIKY FRDSTIDEEL QRDSRVTWIV EFYANWSPEC QSFAPIFADL
     SLKYTCLGLK FGKVDIGHYG AVAERYKVNP SPLCKQLPSL LMLQAGRELM RRPLVDKKGR
     AVSWNFTEDN IIRDFNLNEI FQKYKKFSKG EKPEEPQPVL EEESESPLEE EEEDSESKKD
     K