ID A0A3B6IQT3_WHEAT Unreviewed; 488 AA.
AC A0A3B6IQT3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN ORFNames=CFC21_056954 {ECO:0000313|EMBL:KAF7048142.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS4B02G101800.1};
RN [1] {ECO:0000313|EMBL:KAF7048142.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7048142.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS4B02G101800.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4B02G101800.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS4B02G101800.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7048142.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7048142.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182,
CC ECO:0000256|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; CM022221; KAF7048142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6IQT3; -.
DR EnsemblPlants; TraesCS4B02G101800.1; TraesCS4B02G101800.1; TraesCS4B02G101800.
DR Gramene; TraesCAD_scaffold_013001_01G000100.1; TraesCAD_scaffold_013001_01G000100.1; TraesCAD_scaffold_013001_01G000100.
DR Gramene; TraesCLE_scaffold_007916_01G000100.1; TraesCLE_scaffold_007916_01G000100.1; TraesCLE_scaffold_007916_01G000100.
DR Gramene; TraesCS4B02G101800.1; TraesCS4B02G101800.1; TraesCS4B02G101800.
DR Gramene; TraesCS4B03G0231600.1; TraesCS4B03G0231600.1.CDS; TraesCS4B03G0231600.
DR Gramene; TraesPAR_scaffold_038320_01G000300.1; TraesPAR_scaffold_038320_01G000300.1; TraesPAR_scaffold_038320_01G000300.
DR Gramene; TraesROB_scaffold_033393_01G000300.1; TraesROB_scaffold_033393_01G000300.1; TraesROB_scaffold_033393_01G000300.
DR Gramene; TraesWEE_scaffold_002921_01G000100.1; TraesWEE_scaffold_002921_01G000100.1; TraesWEE_scaffold_002921_01G000100.
DR Proteomes; UP000019116; Chromosome 4B.
DR Proteomes; UP000815260; Chromosome 4B.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR NCBIfam; TIGR01126; pdi_dom; 2.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF254; PROTEIN DISULFIDE ISOMERASE-LIKE 1-1; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 23..488
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5040519587"
FT DOMAIN 9..126
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 322..465
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 467..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 44..47
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 388..391
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 488 AA; 54194 MW; 22B4B8ACAD8BC3AA CRC64;
MAICKVWISL LLALAAVLTL HADNFDDAIA KHPFILVEFY APWCGHCKSL APEYEKAAQL
LSKHDPAIVL AKVDANDEKN KPLAGKYEVQ GFPTLKIFRN GGKNIQEYKG PREAEGIVEY
LKKQVGPASK EIKAPEDATY LEDGKIHIVG VFTEFSGTEF TNFLEVAEKL RSDYDFGHTV
HANHLPRGDA AVERPLVRLF KPFDELVVDS KDFDVSALEK FIEASSTPKV VTFDKNPDNH
PYLLKFFQSN APKAMLFLNF STGPFESFKK AYYGAVEEFS GKDVKFLIGD IEASQGAFQY
FGLKEDQAPL ILIQDSDSKK FLKEQVEAGQ IVAWLKDYFD GKLTPFRKSE PIPEANNEPV
KVVVADNVHD VVFKSGKNVL IEFYAPWCGH CKKLAPILDE AAATLQSEED VVIAKMDATA
NDVPSEFDVQ GYPTLYFVTP SGKKVSYEGG RTADEIVDYI KKNKETAGQA ATEKAAEPAA
TEPLKDEL
//
