ID   PDI14_ORYSJ             Reviewed;         563 AA.
AC   Q67IX6; A0A0P0VDI0;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   04-NOV-2026, entry version 157.
DE   RecName: Full=Protein disulfide isomerase-like 1-4;
DE            Short=OsPDIL1-4;
DE            EC=5.3.4.1;
DE   AltName: Full=Protein disulfide isomerase-like 2-1;
DE            Short=OsPDIL2-1;
DE   Flags: Precursor;
GN   Name=PDIL1-4; Synonyms=PDIL2-1;
GN   OrderedLocusNames=Os02g0100100, LOC_Os02g01010;
GN   ORFNames=OsJ_04977, OSJNOa183H18.2;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16623884; DOI=10.1111/j.1365-313x.2006.02684.x;
RA   Mizuno H., Wu J., Kanamori H., Fujisawa M., Namiki N., Saji S.,
RA   Katagiri S., Katayose Y., Sasaki T., Matsumoto T.;
RT   "Sequencing and characterization of telomere and subtelomere regions on
RT   rice chromosomes 1S, 2S, 2L, 6L, 7S, 7L and 8S.";
RL   Plant J. 46:206-217(2006).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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: Acts as a protein-folding catalyst that interacts with
CC       nascent polypeptides to catalyze the formation, isomerization, and
CC       reduction or oxidation of disulfide bonds. May play a role in storage
CC       protein biogenesis (By similarity). {ECO:0000250}.
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AP006851; BAD38565.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF07493.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS76496.1; -; Genomic_DNA.
DR   EMBL; CM000139; EEE56114.1; -; Genomic_DNA.
DR   EMBL; AK071514; BAG92533.1; -; mRNA.
DR   AlphaFoldDB; Q67IX6; -.
DR   SMR; Q67IX6; -.
DR   FunCoup; Q67IX6; 2873.
DR   STRING; 39947.Q67IX6; -.
DR   GlyCosmos; Q67IX6; 3 sites, No reported glycans.
DR   PaxDb; 39947-Q67IX6; -.
DR   EnsemblPlants; Os02t0100100-01; Os02t0100100-01; Os02g0100100.
DR   Gramene; Os02t0100100-01; Os02t0100100-01; Os02g0100100.
DR   KEGG; dosa:Os02g0100100; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   HOGENOM; CLU_025879_7_0_1; -.
DR   InParanoid; Q67IX6; -.
DR   OMA; ACCSRGL; -.
DR   OrthoDB; 427280at2759; -.
DR   Proteomes; UP000059680; Chromosome 2.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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   FunFam; 3.40.30.10:FF:000023; Protein disulfide-isomerase; 1.
DR   FunFam; 3.40.30.10:FF:000109; Protein disulfide-isomerase; 1.
DR   FunFam; 3.40.30.10:FF:000134; Protein disulfide-isomerase; 1.
DR   FunFam; 3.40.30.10:FF:000042; protein disulfide-isomerase A2; 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-LIKE 1-4; 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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW   Redox-active center; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..563
FT                   /note="Protein disulfide isomerase-like 1-4"
FT                   /id="PRO_0000400031"
FT   DOMAIN          46..180
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          394..523
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          40..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           560..563
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        529..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        102
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        444
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        447
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            166
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            445
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            446
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            509
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        102..105
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        444..447
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   563 AA;  62253 MW;  F6862C4A2C65491F CRC64;
     MRSRSLLLVA LATLLLHASA SASDDDLDYL IDNADDIPAN DPDGWLQEGS PDDDDDDDLF
     HHGQAQDHPI DETHVFLLSA ANFSDFLASH RHVMVEFYAP WCAHCQALAP DYAAAAADLS
     PLAHQVALAK VDATEDTDLA QKYDVQGFPT ILFFIDGVPK DYNGARTKEA IVSWVNKKLA
     PGVQNITTVD EAEKILTGED KAILAVLDSL SGAHSDEIAA ASRLEDAINF YQTSNPDVAK
     LFHLDPAAKR PSLVLLKKQE EEKLTFYDGP FKASAIADFV SANKLPLVNT LTQETAPSIF
     DNPIKKQILL FVVANESSKF LPIFKEASKS FKGKLLFVFV ERDNEEVGEP VANYFGITGQ
     ETTVLAYTGN EDARNFFLDG EISVENIKRF AEDFLEEKLT PFYKSEPVPE SNEGDVKIVV
     GKNLDQIVLD ESKDALLEIY APWCGHCQEL EPTYNKLGKH LRGIDSLVIA KMDGTANEHP
     RAKPDGFPTI LFYPAGKKSF EPITFEGDRT VVEMYKFIKK HASIPFKLKR PDSSATKTEK
     DQSTASTNLR GERSSGTNFK DEL
//