PDI11_ORYSJ
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 03-AUG-2022, entry version 135.
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; 4530.OS11T0199200-01; -.
DR PaxDb; Q53LQ0; -.
DR PRIDE; 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; YIAKHAT; -.
DR OrthoDB; 462118at2759; -.
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 Genevisible; Q53LQ0; OS.
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 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 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
