TMX2_BOVIN
ID TMX2_BOVIN Reviewed; 296 AA.
AC Q2TBU2; Q5E937;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2TBU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2TBU2-2; Sequence=VSP_030695;
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; BT021083; AAX09100.1; -; mRNA.
DR EMBL; BC109664; AAI09665.1; -; mRNA.
DR RefSeq; NP_001015558.1; NM_001015558.1. [Q2TBU2-2]
DR RefSeq; XP_005201014.1; XM_005200957.1. [Q2TBU2-1]
DR AlphaFoldDB; Q2TBU2; -.
DR BMRB; Q2TBU2; -.
DR SMR; Q2TBU2; -.
DR STRING; 9913.ENSBTAP00000041352; -.
DR PaxDb; Q2TBU2; -.
DR PRIDE; Q2TBU2; -.
DR Ensembl; ENSBTAT00000043809; ENSBTAP00000041352; ENSBTAG00000002404. [Q2TBU2-1]
DR GeneID; 509244; -.
DR KEGG; bta:509244; -.
DR CTD; 51075; -.
DR VEuPathDB; HostDB:ENSBTAG00000002404; -.
DR eggNOG; KOG0914; Eukaryota.
DR GeneTree; ENSGT00390000003751; -.
DR HOGENOM; CLU_064868_0_0_1; -.
DR InParanoid; Q2TBU2; -.
DR OMA; IDIGRWK; -.
DR OrthoDB; 1107509at2759; -.
DR TreeFam; TF314606; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000002404; Expressed in retina and 105 other tissues.
DR ExpressionAtlas; Q2TBU2; baseline.
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:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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 Alternative splicing; Disulfide bond; Endoplasmic reticulum; Membrane;
KW Mitochondrion; 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_0000315751"
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 132..269
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 272..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 VAR_SEQ 208..248
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_030695"
SQ SEQUENCE 296 AA; 34029 MW; A8E85D20FEFF9042 CRC64;
MAVLAPLIAL VYSVPRLSRW LARPYYFLSA LLSAAFLLVR KLPPVCESLP TQREDGNPCD
FDWREVEILM FLSAIVMMKN RRSITVEQHV GNIFMFSKVA NAILFFRLDI RMGLLYITLC
IVFLMTCKPP LYMGPEYIKY FSDKTIDEEL ERDKRVTWIV EFFANWSSDC QSFAPIYADL
SLKYNCTGLN FGKVDVGRYT DVSTRYKVST SPLTKQLPTL ILFQGGKEVM RRPQIDKKGR
AVSWTFSEEN VIREFNLNEL YQRAKKLSKA GDKIPEEQPV AAVPAAVPDE ESKKDK
