PDI11_ARATH
ID PDI11_ARATH Reviewed; 501 AA.
AC Q9XI01;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=Protein disulfide isomerase-like 1-1;
DE Short=AtPDIL1-1;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide-isomerase 1;
DE Short=PDI 1;
DE AltName: Full=Protein disulfide-isomerase 5;
DE Short=AtPDI5;
DE Flags: Precursor;
GN Name=PDIL1-1; Synonyms=PDI5; OrderedLocusNames=At1g21750; ORFNames=F8K7.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15684019; DOI=10.1104/pp.104.056507;
RA Houston N.L., Fan C., Xiang J.Q., Schulze J.M., Jung R., Boston R.S.;
RT "Phylogenetic analyses identify 10 classes of the protein disulfide
RT isomerase family in plants, including single-domain protein disulfide
RT isomerase-related proteins.";
RL Plant Physiol. 137:762-778(2005).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18574595; DOI=10.1007/s00438-008-0356-z;
RA Lu D.-P., Christopher D.A.;
RT "Endoplasmic reticulum stress activates the expression of a sub-group of
RT protein disulfide isomerase genes and AtbZIP60 modulates the response in
RT Arabidopsis thaliana.";
RL Mol. Genet. Genomics 280:199-210(2008).
RN [6]
RP FUNCTION, INTERACTION WITH RD21A; AT3G19390 AND AT5G43060, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18676877; DOI=10.1105/tpc.108.058339;
RA Andeme Ondzighi C., Christopher D.A., Cho E.J., Chang S.C., Staehelin L.A.;
RT "Arabidopsis protein disulfide isomerase-5 inhibits cysteine proteases
RT during trafficking to vacuoles before programmed cell death of the
RT endothelium in developing seeds.";
RL Plant Cell 20:2205-2220(2008).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20525253; DOI=10.1186/1471-2229-10-101;
RA d'Aloisio E., Paolacci A.R., Dhanapal A.P., Tanzarella O.A., Porceddu E.,
RA Ciaffi M.;
RT "The protein disulfide isomerase gene family in bread wheat (T. aestivum
RT L.).";
RL BMC Plant Biol. 10:101-101(2010).
CC -!- FUNCTION: Protein disulfide isomerase that associates with RD21A
CC protease for trafficking from the ER through the Golgi to lytic and
CC protein storage vacuoles of endothelial cells in developing seeds.
CC Regulates the timing of programmed cell death (PCD) of the endothelial
CC cells by chaperoning and inhibiting cysteine proteases during their
CC trafficking to vacuoles. {ECO:0000269|PubMed:18676877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBUNIT: Interacts with RD21A, At3g19390, At5g43060.
CC {ECO:0000269|PubMed:18676877}.
CC -!- INTERACTION:
CC Q9XI01; P43297: RD21A; NbExp=4; IntAct=EBI-449394, EBI-1993101;
CC Q9XI01; Q9FMH8: RD21B; NbExp=3; IntAct=EBI-449394, EBI-1993115;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:18676877}. Vacuole
CC {ECO:0000269|PubMed:18676877}. Note=Found in protein storage vacuoles
CC and lytic vacuoles in endothelial cells of developing seeds.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9XI01-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers, stems and immature
CC seeds, and at lower levels in leaves and siliques (at protein level).
CC {ECO:0000269|PubMed:18574595, ECO:0000269|PubMed:18676877}.
CC -!- DEVELOPMENTAL STAGE: During embryo development, expressed exclusively
CC in endothelial cells from the pre-embryo up to the heart stage.
CC Expression disappears when the endothelial cells undergo PCD in the
CC early-bent cotyledon stage (at protein level).
CC -!- INDUCTION: By chemically-induced ER stress response.
CC {ECO:0000269|PubMed:18574595}.
CC -!- DISRUPTION PHENOTYPE: Reduced seed set. {ECO:0000269|PubMed:18676877}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AC007727; AAD41430.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30151.1; -; Genomic_DNA.
DR EMBL; AY035096; AAK59601.1; -; mRNA.
DR EMBL; AY063059; AAL34233.1; -; mRNA.
DR PIR; B86351; B86351.
DR RefSeq; NP_173594.1; NM_102024.4. [Q9XI01-1]
DR AlphaFoldDB; Q9XI01; -.
DR SMR; Q9XI01; -.
DR BioGRID; 24018; 14.
DR IntAct; Q9XI01; 5.
DR STRING; 3702.AT1G21750.1; -.
DR iPTMnet; Q9XI01; -.
DR SwissPalm; Q9XI01; -.
DR SWISS-2DPAGE; Q9XI01; -.
DR PaxDb; Q9XI01; -.
DR PRIDE; Q9XI01; -.
DR ProteomicsDB; 236717; -. [Q9XI01-1]
DR EnsemblPlants; AT1G21750.1; AT1G21750.1; AT1G21750. [Q9XI01-1]
DR GeneID; 838779; -.
DR Gramene; AT1G21750.1; AT1G21750.1; AT1G21750. [Q9XI01-1]
DR KEGG; ath:AT1G21750; -.
DR Araport; AT1G21750; -.
DR TAIR; locus:2036906; AT1G21750.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_6_1_1; -.
DR InParanoid; Q9XI01; -.
DR OMA; YMEYTSE; -.
DR PhylomeDB; Q9XI01; -.
DR PRO; PR:Q9XI01; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI01; baseline and differential.
DR Genevisible; Q9XI01; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0000327; C:lytic vacuole within protein storage vacuole; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0000326; C:protein storage vacuole; IDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0043067; P:regulation of programmed cell death; IMP:TAIR.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:TAIR.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Isomerase; Redox-active center; Reference proteome; Repeat; Signal;
KW Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..501
FT /note="Protein disulfide isomerase-like 1-1"
FT /id="PRO_0000034205"
FT DOMAIN 24..141
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 354..482
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 498..501
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 404
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 407
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 61
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 405
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 406
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 468
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..62
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 404..407
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 501 AA; 55602 MW; C27C564D38ECA6E8 CRC64;
MAMRGFTLFS ILVLSLCASS IRSEETETKE FVLTLDHTNF TDTINKHDFI VVEFYAPWCG
HCKQLAPEYE KAASALSSNV PPVVLAKIDA SEETNREFAT QYEVQGFPTI KIFRNGGKAV
QEYNGPREAE GIVTYLKKQS GPASAEIKSA DDASEVVSDK KVVVVGIFPK LSGSEFDSFM
AIAEKLRSEL DFAHTSDAKL LPRGESSVTG PVVRLFKPFD EQFVDSKDFD GEALEKFVKE
SSIPLITVFD KDPNNHPYVI KFFESTNTKA MLFINFTGEG AESLKSKYRE VATSNKGQGL
SFLLGDAENS QGAFQYFGLE ESQVPLIIIQ TADDKKYLKT NVEVDQIESW VKDFKDGKIA
PHKKSQPIPA ENNEPVKVVV SDSLDDIVLN SGKNVLLEFY APWCGHCQKL APILDEVAVS
YQSDSSVVIA KLDATANDFP KDTFDVKGFP TIYFKSASGN VVVYEGDRTK EDFISFVDKN
KDTVGEPKKE EETTEEVKDE L
