ID   PDI11_ORYSJ             Reviewed;         512 AA.
AC   Q53LQ0; F4MG95; Q52PJ0;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Protein disulfide isomerase-like 1-1;
DE            Short=OsPDIL1-1;
DE            EC=5.3.4.1;
DE   AltName: Full=Endosperm storage protein 2;
DE            Short=Protein ESP2;
DE   Flags: Precursor;
GN   Name=PDIL1-1; OrderedLocusNames=Os11g0199200, LOC_Os11g09280;
GN   ORFNames=OsJ_33281;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=20627947; DOI=10.1093/pcp/pcq098;
RA   Satoh-Cruz M., Crofts A.J., Takemoto-Kuno Y., Sugino A., Washida H.,
RA   Crofts N., Okita T.W., Ogawa M., Satoh H., Kumamaru T.;
RT   "Protein disulfide isomerase like 1-1 participates in the maturation of
RT   proglutelin within the endoplasmic reticulum in rice endosperm.";
RL   Plant Cell Physiol. 51:1581-1593(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wan J.M., Niu H.B., Zhai H.Q., Zhang X., Jiang L., Qin H.D.;
RT   "Cloning and characterization of the protein disulfide isomerase in rice.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [9]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=11950970; DOI=10.1104/pp.010624;
RA   Takemoto Y., Coughlan S.J., Okita T.W., Satoh H., Ogawa M., Kumamaru T.;
RT   "The rice mutant esp2 greatly accumulates the glutelin precursor and
RT   deletes the protein disulfide isomerase.";
RL   Plant Physiol. 128:1212-1222(2002).
RN   [10]
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   [11]
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).
RN   [12]
RP   INDUCTION BY DITHIOTHREITOL.
RX   PubMed=21223397; DOI=10.1111/j.1365-313x.2010.04453.x;
RA   Wakasa Y., Yasuda H., Oono Y., Kawakatsu T., Hirose S., Takahashi H.,
RA   Hayashi S., Yang L., Takaiwa F.;
RT   "Expression of ER quality control-related genes in response to changes in
RT   BiP1 levels in developing rice endosperm.";
RL   Plant J. 65:675-689(2011).
CC   -!- FUNCTION: Probable protein disulfide isomerase that plays an essential
CC       role in the segregation of proglutelin and prolamin polypeptides within
CC       the ER lumen of endosperm. Required to retain proglutelin in the
CC       cisternal ER lumen until ER export and, thereby, indirectly prevents
CC       heterotypic interactions with prolamin polypeptides.
CC       {ECO:0000269|PubMed:11950970, ECO:0000269|PubMed:20627947}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:20627947}. Note=Distributed asymmetrically within
CC       the cortical endoplasmic reticulum (ER) and largely restricted to the
CC       cisternal ER. {ECO:0000269|PubMed:20627947}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 3 to 9 days
CC       after anthesis. {ECO:0000269|PubMed:11950970}.
CC   -!- INDUCTION: By dithiothreitol-induced endoplasmic reticulum (ER) stress
CC       response. {ECO:0000269|PubMed:21223397}.
CC   -!- DISRUPTION PHENOTYPE: Accumulation of large quantities of glutelin
CC       precursor (proglutelin) in the endosperm. {ECO:0000269|PubMed:11950970,
CC       ECO:0000269|PubMed:20627947}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AB373950; BAG50157.1; -; mRNA.
DR   EMBL; AY987391; AAX85991.1; -; mRNA.
DR   EMBL; AC139170; AAX96742.1; -; Genomic_DNA.
DR   EMBL; DP000010; ABA91939.1; -; Genomic_DNA.
DR   EMBL; DP000010; ABA91940.1; -; Genomic_DNA.
DR   EMBL; AP008217; BAF27799.1; -; Genomic_DNA.
DR   EMBL; AP014967; BAT13066.1; -; Genomic_DNA.
DR   EMBL; CM000148; EAZ17736.1; -; Genomic_DNA.
DR   EMBL; AK068268; BAG90833.1; -; mRNA.
DR   RefSeq; XP_015617314.1; XM_015761828.1.
DR   AlphaFoldDB; Q53LQ0; -.
DR   SMR; Q53LQ0; -.
DR   STRING; 39947.Q53LQ0; -.
DR   GlyCosmos; Q53LQ0; 1 site, No reported glycans.
DR   PaxDb; 39947-Q53LQ0; -.
DR   EnsemblPlants; Os11t0199200-01; Os11t0199200-01; Os11g0199200.
DR   GeneID; 4350002; -.
DR   Gramene; Os11t0199200-01; Os11t0199200-01; Os11g0199200.
DR   KEGG; osa:4350002; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   HOGENOM; CLU_025879_6_1_1; -.
DR   InParanoid; Q53LQ0; -.
DR   OMA; FFGMKKD; -.
DR   OrthoDB; 314307at2759; -.
DR   BRENDA; 5.3.4.1; 4460.
DR   PlantReactome; R-OSA-9626305; Regulatory network of nutrient accumulation.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000007752; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
DR   ExpressionAtlas; Q53LQ0; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0009960; P:endosperm development; IMP:CACAO.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; IMP:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
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   Genevisible; Q53LQ0; OS.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW   Redox-active center; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..512
FT                   /note="Protein disulfide isomerase-like 1-1"
FT                   /id="PRO_0000400028"
FT   DOMAIN          32..151
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          372..491
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          492..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           509..512
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        69
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        72
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            70
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            71
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            137
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            415
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            416
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            477
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        69..72
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        414..417
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        435
FT                   /note="K -> E (in Ref. 2; AAX85991)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  56855 MW;  60CA68E115728496 CRC64;
     MAISKAWISL LLALAVVLSA PAARAEEAAA AEEGGDAAAE AVLTLDADGF DEAVAKHPFM
     VVEFYAPWCG HCKKLAPEYE KAAQELSKHD PPIVLAKVDA NDEKNKPLAT KYEIQGFPTL
     KIFRNQGKNI QEYKGPREAE GIVEYLKKQV GPASKEIKSP EDATNLIDDK KIYIVGIFSE
     LSGTEYTNFI EVAEKLRSDY DFGHTLHANH LPRGDAAVER PLVRLFKPFD ELVVDSKDFD
     VTALEKFIDA SSTPKVVTFD KNPDNHPYLL KFFQSSAAKA MLFLNFSTGP FESFKSVYYG
     AAEEFKDKEI KFLIGDIEAS QGAFQYFGLR EDQVPLIIIQ DGESKKFLKA HVEPDQIVSW
     LKEYFDGKLS PFRKSEPIPE VNDEPVKVVV ADNVHDFVFK SGKNVLVEFY APWCGHCKKL
     APILDEAATT LKSDKDVVIA KMDATANDVP SEFDVQGYPT LYFVTPSGKM VPYESGRTAD
     EIVDFIKKNK ETAGQAKEKA ESAPAEPLKD EL
//