ID A0A022RT20_ERYGU Unreviewed; 434 AA.
AC A0A022RT20;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=MIMGU_mgv1a006693mg {ECO:0000313|EMBL:EYU43141.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU43141.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU43141.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; KI630264; EYU43141.1; -; Genomic_DNA.
DR RefSeq; XP_012830114.1; XM_012974660.1.
DR AlphaFoldDB; A0A022RT20; -.
DR STRING; 4155.A0A022RT20; -.
DR GeneID; 105951262; -.
DR KEGG; egt:105951262; -.
DR eggNOG; KOG0191; Eukaryota.
DR OMA; KQKLWGW; -.
DR OrthoDB; 52245at2759; -.
DR PhylomeDB; A0A022RT20; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR CDD; cd02983; P5_C; 1.
DR CDD; cd03001; PDI_a_P5; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01126; pdi_dom; 2.
DR PANTHER; PTHR45815; PROTEIN DISULFIDE-ISOMERASE A6; 1.
DR PANTHER; PTHR45815:SF3; PROTEIN DISULFIDE-ISOMERASE A6; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..434
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001505427"
FT DOMAIN 22..138
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 150..264
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 434 AA; 47165 MW; 010B82AF6F4D8B57 CRC64;
MEKSTLISLI LLSLIGKLGV YALYGPSSPV LQLTADNFKS KVLNSKGVVV VEFFAPWCGH
CQALTPTWEK AATVLKGVAT IAALDADAHQ SLAQEYGIKG FPTIKVFSPG KPPVDYQGAR
DIKPIAEFAL KQVRALVKER LEGKSSGGSS KKSEPSASVE LNSSNFDELV LKSKELWIVE
FFAPWCGHCK KLAPEWKRAA SSLKGQVKLG HVDCDAEKSL MSRFNVQGFP TIMVFGADKD
SPFPYEGARS ASAIESFALE QLETNAPPPE VTELTSPDTL EEKCGSAAIC FVAFLPDILD
SKAEGRNKYL DLLLSVAEKF RKSPFSFLWA AAGKQSDLEK HVGVGGYGYP ALVALNIKKK
VFNPLKSAFQ RAQIIEFVNE ASQGGKGTLP LEGSPEIVKT EAWDGKDGEI FEEDEFSLEE
LMADDDTLAT KDEL
//
