ID D2YZU7_DAUCA Unreviewed; 515 AA.
AC D2YZU7;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 13-SEP-2023, entry version 70.
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 Name=PDI1 {ECO:0000313|EMBL:BAI67717.1};
OS Daucus carota (Wild carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=4039 {ECO:0000313|EMBL:BAI67717.1};
RN [1] {ECO:0000313|EMBL:BAI67717.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Somatic embryo {ECO:0000313|EMBL:BAI67717.1};
RA Kimura Y., Kuroda C., Masuda K.;
RT "Differential nuclear envelope assembly at the end of mitosis in
RT suspension-cultured Apium graveolens cells.";
RL Chromosoma 0:0-0(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB514508; BAI67717.1; -; mRNA.
DR AlphaFoldDB; D2YZU7; -.
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; 1.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF212; PROTEIN DISULFIDE-ISOMERASE; 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 2: Evidence at transcript level;
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 29..515
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005126240"
FT DOMAIN 19..150
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 363..491
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 493..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 67..70
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 413..416
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 515 AA; 56853 MW; 75166E6D1E21943D CRC64;
MAARSRVVIS GFVVLMSLAL LSGSICSAEE ESKESVVDHV LTLDHSNFSE IVGKHESIVV
EFYAPWCGHC KSLAPEYEKA ASVLSSHDPA IVLAKVDANE EANKELAISI SVFKVSPTLK
ILRNGGKLSQ EYKGPREAEG IVSYLKKQVG PASAEIKSAE DASSLIDEKK IPLIGLFPVL
SGEEFENFTA PSEKLRSDYD FGHTVDAKFI PQGDSSISKP TLRLLKPFDE LFVDSQDFHV
DAMEEFIAES GVPTVTLFNQ DPSNHPFLVK FFDSPDAKAM LFLNFSTDKF DDFKKNYNDV
AVLYKGKGLN FLLGDLEASK GAFQYFGLSE DQAPVILVQT SDSQKYLKGN VEADQIAPWL
KEYMDGKLKP YVKSDPIPEV NNEPVKVVVR DSIQDVVFNS GKNALIEFYA PWCGHCKKLA
PILDEVAVSF ENDADVIIAK FDATTNDVPS EVFDVQGFPT LYFRSASGTV VPYEGDRTKD
DFIEFIQKNR DTNAKPVSVK SEESAAKSES PRDEL
//