ID D7MTW1_ARALL Unreviewed; 597 AA.
AC D7MTW1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
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=ARALYDRAFT_496212 {ECO:0000313|EMBL:EFH42646.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348720; EFH42646.1; -; Genomic_DNA.
DR RefSeq; XP_002866387.1; XM_002866341.1.
DR AlphaFoldDB; D7MTW1; -.
DR STRING; 81972.D7MTW1; -.
DR EnsemblPlants; fgenesh2_kg.8__2028__AT5G60640.1; fgenesh2_kg.8__2028__AT5G60640.1; fgenesh2_kg.8__2028__AT5G60640.1.
DR GeneID; 9302461; -.
DR Gramene; fgenesh2_kg.8__2028__AT5G60640.1; fgenesh2_kg.8__2028__AT5G60640.1; fgenesh2_kg.8__2028__AT5G60640.1.
DR KEGG; aly:9302461; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_7_0_1; -.
DR OrthoDB; 314307at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
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:SF246; 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 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:UP000008694};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 26..597
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005127025"
FT DOMAIN 85..208
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 420..550
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 24..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 132..135
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 471..474
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 597 AA; 66183 MW; 4F3FB03D881056E0 CRC64;
MAFRVLLLFS LTALLIFSAV SPSFATSSSD DVDDEDLSFL EDLKEDDVPG ADSLSSSTGL
DEFEGGEDED PDMYNDDDDE DGDFSDLGNP DSDPLPTPEI DEKDVVVIKE RNFTDVIENN
QYVLVEFYAP WCGHCQSLVP EYAAAATELK DDGVVLAKID ATEENELAQE YSVQGFPTIL
FFVDGEHKPY TGGRTKETIV TWVKKKIGPG VYNLTTLDDA EKVLTSGNKV VLGYLNSLVG
VEHDQLAATS KVEDDVNFYQ TVNPDVAKMF HIDPESKRPA LVLVKREEEK ISHYDGEFVK
SALVSFVSAN KLALVSVFTR ETAPEIFESA IKKQLLLFAT QNDSEKVLPE FQEAAKSFKG
KLIFVSVDLD NEDYGKPVAE YFGVSGNGPK LIAYTGNEDP KKYFFDGEIK SDKIKTFGED
FLNDKLKPFY KSDPIPEKND GDVKIVVGDN FDEIVLDDSK DVLLEVYAPW CGHCQALEPM
YNKLAKHLRS IDSLVIAKMD GTTNEHPKAK AEGFPTILFF PAGNKTSEPI TVDTDRTVVA
FYKFLRKHAT IPFKLEKPAS TESPKTAEST PKVETTETKE SPDSTTKSSQ SDSKDEL
//
