ID L5L2T7_PTEAL Unreviewed; 296 AA.
AC L5L2T7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Thioredoxin-related transmembrane protein 2 {ECO:0000256|ARBA:ARBA00016033};
DE AltName: Full=Thioredoxin domain-containing protein 14 {ECO:0000256|ARBA:ARBA00032391};
GN ORFNames=PAL_GLEAN10001701 {ECO:0000313|EMBL:ELK17750.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK17750.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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:0000256|ARBA:ARBA00023427}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004583}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004583}.
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DR EMBL; KB030399; ELK17750.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L2T7; -.
DR STRING; 9402.L5L2T7; -.
DR eggNOG; KOG0914; Eukaryota.
DR InParanoid; L5L2T7; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..269
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 268..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 34004 MW; C03847D665F53C73 CRC64;
MAVLAPLIAL VYSVPRLSRW LARPYYLLSA LLSAAFLLVR KLPPLCHTLP TQREDGNPCD
FDWREVEILM FLSAIVMMKN RRSITVEQHI GNIFMFSKVA NVLLFFRLDI RMGLLYITLC
IVFLMTCKPP LYMGPEYIKY FSDKTIDEEL ERDKRVTWIV EFFANWSSDC QSFAPIYADL
SLKYNCTGLN FGKVDVGRYT DVSTRYKVST SPLTKQLPTL ILFQGGKEVM RRPQIDKKGR
AVSWTFSEEN VIREFSLNEL YQRAKKLSKA GDSIPEEQPV APTPTAVPEG ESKKNK
//
