ID   PID13_ORYSJ             Reviewed;         545 AA.
AC   Q69ST6; A0A0P0VKD4; B7ELS1;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 134.
DE   RecName: Full=Protein disulfide isomerase-like 1-3;
DE            Short=OsPDIL1-3;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=PDIL1-3; OrderedLocusNames=Os02g0554900, LOC_Os02g34940;
GN   ORFNames=P0470G10.25;
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=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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-545.
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   [5]
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   [6]
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG93318.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP004876; BAD33310.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09033.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79202.1; -; Genomic_DNA.
DR   EMBL; AK073161; BAG93318.1; ALT_INIT; mRNA.
DR   RefSeq; XP_015626051.1; XM_015770565.1.
DR   AlphaFoldDB; Q69ST6; -.
DR   SMR; Q69ST6; -.
DR   STRING; 39947.Q69ST6; -.
DR   GlyCosmos; Q69ST6; 2 sites, No reported glycans.
DR   PaxDb; 39947-Q69ST6; -.
DR   EnsemblPlants; Os02t0554900-01; Os02t0554900-01; Os02g0554900.
DR   GeneID; 4329652; -.
DR   Gramene; Os02t0554900-01; Os02t0554900-01; Os02g0554900.
DR   KEGG; osa:4329652; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   HOGENOM; CLU_025879_6_1_1; -.
DR   InParanoid; Q69ST6; -.
DR   OMA; HEAANQY; -.
DR   OrthoDB; 314307at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; Q69ST6; baseline and differential.
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   Gene3D; 3.40.30.10; Glutaredoxin; 4.
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   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF206; PROTEIN DISULFIDE ISOMERASE-LIKE 1-3; 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; Q69ST6; 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..?
FT   CHAIN           ?..545
FT                   /note="Protein disulfide isomerase-like 1-3"
FT                   /id="PRO_0000400030"
FT   DOMAIN          55..189
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          403..545
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           542..545
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        453
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        456
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            108
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            109
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            175
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            454
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            455
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            515
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        107..110
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        453..456
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   545 AA;  59075 MW;  362611FD2AD09ED1 CRC64;
     MWPRAPATPP PPPWPSKPSA ASRSALRRLD LDDGRRQGTE GEENHAPLLC SPAMASSTAF
     AAAFALLLLA SSAAAEGEAV LTLDAGNFTE VVGAHDFIVV EFYAPWCGHC NQLAPEYEAA
     AAALRSHDPP VVLAKVDASA DLNRGLAGEH GVQGYPTIRI LRDRGARSHN YAGPRDAAGI
     VAYLKRQAGP ASVEIAASAS PPAADSIAND GVVVVGVFPE LSGSEFESFM AVAEKMRADY
     DFRHTTDAGV LPRGDRTVRG PLVRLFKPFD ELFVDSQDFD RDALEKFIES SGFPTVVTFD
     TSPANQKYLL KYFDNAGTKA MLFLSFSDDR AEEFRTQFHE AANQYSANNI SFLIGDVTAS
     QGAFQYFGLK ESEVPLVFIL ASKSKYIKPT VEPDQILPYL KEFTEGTLAP HVKSEPIPEV
     NDQPVKTVVA DNLREVVFNS GKNVLLEFYA PWCGHCQKLA PILEEVAVSL KDDEDVVIAK
     MDGTANDVPS DFAVEGYPSM YFYSSGGNLL PYDGRTAEEI IDFITKNKGS RPGEATTTES
     VKDEL
//