TMX2B_DANRE
ID TMX2B_DANRE Reviewed; 307 AA.
AC Q6IQC7; B8A5B2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thioredoxin-related transmembrane protein 2-B;
DE AltName: Full=Thioredoxin domain-containing protein 14;
DE Flags: Precursor;
GN Name=tmx2b; Synonyms=tmx2, txndc14; ORFNames=si:dkey-28b4.1, zgc:86830;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-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. {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; BX511158; CAX14153.1; -; Genomic_DNA.
DR EMBL; BC071481; AAH71481.1; -; mRNA.
DR RefSeq; NP_001002113.1; NM_001002113.1.
DR AlphaFoldDB; Q6IQC7; -.
DR SMR; Q6IQC7; -.
DR STRING; 7955.ENSDARP00000022891; -.
DR PaxDb; Q6IQC7; -.
DR PRIDE; Q6IQC7; -.
DR Ensembl; ENSDART00000009858; ENSDARP00000022891; ENSDARG00000007786.
DR GeneID; 415203; -.
DR KEGG; dre:415203; -.
DR CTD; 415203; -.
DR ZFIN; ZDB-GENE-040625-105; tmx2b.
DR eggNOG; KOG0914; Eukaryota.
DR GeneTree; ENSGT00390000003751; -.
DR HOGENOM; CLU_064868_0_0_1; -.
DR InParanoid; Q6IQC7; -.
DR OMA; IDIGRWK; -.
DR OrthoDB; 1107509at2759; -.
DR PhylomeDB; Q6IQC7; -.
DR TreeFam; TF314606; -.
DR PRO; PR:Q6IQC7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000007786; Expressed in pharyngeal gill and 27 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: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..307
FT /note="Thioredoxin-related transmembrane protein 2-B"
FT /id="PRO_0000315757"
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..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 132..269
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 268..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 304..307
FT /note="Di-lysine motif"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 35723 MW; FC2535458CEAA0E4 CRC64;
MALLTPLFAF LYHLPQVYKW LLKPYYIASL FMSIAFVMIR KMPGVCEHLS TQREDGNSCD
FDWREVEILM FLSAIVMMKN RRAITIEQHV GNIILFCKVA NVILFFRLDI RLGLLYLTLC
IVFLMTCKPP LYMGPEYIKY FSDKTIDEEL EKDHRVTWIV EFFANWSPEC QSFASVYADL
SLKYNCAGLK FGKVDIGRYG EVSKKYRVST SPLSKQLPSL VLFQGGKEVM RRPQVDKKGR
AVSWTFTEEN IIREFNLNEL YQKSKKLGKT KEKLERPSEL VFSTVPEEEE PEAETISAMD
TESKKDK
