ID I2H2Q2_TETBL Unreviewed; 366 AA.
AC I2H2Q2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=TBLA0D01470 {ECO:0000313|EMBL:CCH60654.1};
GN ORFNames=TBLA_0D01470 {ECO:0000313|EMBL:CCH60654.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60654.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH60654.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the OST3/OST6 family.
CC {ECO:0000256|ARBA:ARBA00009561}.
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DR EMBL; HE806319; CCH60654.1; -; Genomic_DNA.
DR RefSeq; XP_004180173.1; XM_004180125.1.
DR AlphaFoldDB; I2H2Q2; -.
DR STRING; 1071380.I2H2Q2; -.
DR GeneID; 14495690; -.
DR KEGG; tbl:TBLA_0D01470; -.
DR eggNOG; KOG2603; Eukaryota.
DR HOGENOM; CLU_052855_2_1_1; -.
DR InParanoid; I2H2Q2; -.
DR OMA; WQFGIEI; -.
DR OrthoDB; 2021955at2759; -.
DR Proteomes; UP000002866; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12692:SF3; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT OST6; 1.
DR PANTHER; PTHR12692; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE-RELATED; 1.
DR Pfam; PF04756; OST3_OST6; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..366
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003660433"
FT TRANSMEM 191..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 366 AA; 42197 MW; 60875A1E6AD7B57A CRC64;
MLTILRVFLL IFYVCQSIVL GEYLTPEQLL NLRDEDGLIR ITPENYNQLN QRFEEWHQVL
YLTMGPDPNT GEPICPVCGP FEETVRRAAK FIMENSPDTK VLFYVSEVEK NADIIREFNL
TAVPHLLAYP PIDIYSSPGT PINWAFSQFY EYKLPENAIS DVFRLMDFLN QIMGTRINVP
LDINDNIGFD YQVFILYFII FTSIFVILKK ITLKFLKSSE SDSESSESEN NTISKETRGR
LNSIYMQIVC ICISFGILLT SITGLKFTQM NQIVFIARNG EGQIMYFSGG TGWQFGIEVL
TVSLMYVSMA LLVVGLVYLY KAEKLSLLQR NIIGIILSAM LYYGFHYYLL CYEIKNNGYP
FTYKLF
//
