ID I1LD87_SOYBN Unreviewed; 433 AA.
AC I1LD87;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=PDIL7 {ECO:0000313|EMBL:BAV14037.1};
GN Name=100791778 {ECO:0000313|EnsemblPlants:KRH34995};
GN Synonyms=pdil7 {ECO:0000313|EMBL:BAV14037.1};
GN ORFNames=GLYMA_10G217600 {ECO:0000313|EMBL:KRH34995.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH34995};
RN [1] {ECO:0000313|EMBL:KRH34995.1, ECO:0000313|EnsemblPlants:KRH34995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH34995};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH34995.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EMBL:BAV14037.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:BAV14037.1};
RX PubMed=27960051;
RA Okuda A., Matsusaki M., Masuda T., Urade R.;
RT "Identification and characterization of GmPDIL7, a soybean ER membrane-
RT bound protein disulfide isomerase family protein.";
RL FEBS J. 284:414-428(2017).
RN [3] {ECO:0000313|EnsemblPlants:KRH34995}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH34995};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KRH34995.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH34995.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
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DR EMBL; LC158001; BAV14037.1; -; mRNA.
DR EMBL; CM000843; KRH34995.1; -; Genomic_DNA.
DR RefSeq; XP_003536390.1; XM_003536342.3.
DR AlphaFoldDB; I1LD87; -.
DR SMR; I1LD87; -.
DR STRING; 3847.I1LD87; -.
DR PaxDb; 3847-GLYMA10G36170-1; -.
DR EnsemblPlants; KRH34995; KRH34995; GLYMA_10G217600.
DR GeneID; 100791778; -.
DR Gramene; KRH34995; KRH34995; GLYMA_10G217600.
DR KEGG; gmx:100791778; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_054116_0_0_1; -.
DR InParanoid; I1LD87; -.
DR OMA; NSTTQHH; -.
DR OrthoDB; 1053050at2759; -.
DR Proteomes; UP000008827; Chromosome 10.
DR ExpressionAtlas; I1LD87; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR CDD; cd02961; PDI_a_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..433
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014578269"
FT TRANSMEM 378..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..138
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 410..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 49240 MW; 5522F17A045413D6 CRC64;
MRMKRVFVVY SVLLLLVQFW LGEAETFSVD GKVLVLDESN FDSAIASFDH ILVDFYAPWC
GHCKRLSPEL DAAAPVLATL KEPIIIAKVD ADKHTRLAKK YDVDAYPTIL LFNHGVPTEY
RGPRKADLLV RYLKKFSASD VSILDSDSAV NMFVEEAGTF FPIYIGFGLN SSVLEKFGIK
YKKNAWFSVA KDFSEDLMVL HDFDKIPALV SLNPQYNERN TFYGPFEEDF LEDFVRQNLI
PLAVPVSYET LKLMKADGRK IVLTIVEDED EETTRELIKL LKAAASANRD LIFGYVGVKQ
MEEFAENFDI DTKLPKMVIW DKSDDYLSVV DSETIEGEDQ GTQITKFLEG YREGRTIKKT
FSGPSLMRFI HRSFDIRMVY IIVFVVAVLM LIQTFSKGGD EYQSVPNQVQ TDHAISSVSE
AENNEYKPGD KED
//
