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   27-MAR-2024, entry version 176.
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;
GN   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.Q9XI01; -.
DR   GlyCosmos; Q9XI01; 2 sites, No reported glycans.
DR   iPTMnet; Q9XI01; -.
DR   SwissPalm; Q9XI01; -.
DR   PaxDb; 3702-AT1G21750-1; -.
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; AT1G21750; PDIL1-1.
DR   eggNOG; KOG0190; Eukaryota.
DR   HOGENOM; CLU_025879_6_1_1; -.
DR   InParanoid; Q9XI01; -.
DR   OMA; FFGMKKD; -.
DR   OrthoDB; 314307at2759; -.
DR   PhylomeDB; Q9XI01; -.
DR   PRO; PR:Q9XI01; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XI01; baseline and differential.
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: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   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; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
DR   SWISS-2DPAGE; Q9XI01; -.
DR   Genevisible; Q9XI01; AT.
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
//