ID   PDI15_ORYSJ             Reviewed;         533 AA.
AC   Q5WA72; A0A0P0WSS8;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Protein disulfide isomerase-like 1-5;
DE            Short=OsPDIL1-5;
DE            EC=5.3.4.1;
DE   AltName: Full=Protein disulfide isomerase-like 3-1;
DE            Short=OsPDIL3-1;
DE   Flags: Precursor;
GN   Name=PDIL1-5; Synonyms=PDIL3-1;
GN   OrderedLocusNames=Os06g0163400, LOC_Os06g06790; ORFNames=P0681F10.44;
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].
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}.
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DR   EMBL; AB026295; BAD67648.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF18810.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS96309.1; -; Genomic_DNA.
DR   EMBL; AK073970; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015642967.1; XM_015787481.1.
DR   AlphaFoldDB; Q5WA72; -.
DR   SMR; Q5WA72; -.
DR   STRING; 4530.OS06T0163400-01; -.
DR   PaxDb; Q5WA72; -.
DR   PRIDE; Q5WA72; -.
DR   EnsemblPlants; Os06t0163400-01; Os06t0163400-01; Os06g0163400.
DR   GeneID; 4340223; -.
DR   Gramene; Os06t0163400-01; Os06t0163400-01; Os06g0163400.
DR   KEGG; osa:4340223; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   HOGENOM; CLU_025879_7_0_1; -.
DR   InParanoid; Q5WA72; -.
DR   OMA; FTPWCIN; -.
DR   OrthoDB; 462118at2759; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q5WA72; OS.
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   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   SUPFAM; SSF52833; SSF52833; 4.
DR   PROSITE; PS00014; ER_TARGET; 1.
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..533
FT                   /note="Protein disulfide isomerase-like 1-5"
FT                   /id="PRO_0000400032"
FT   DOMAIN          51..196
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          387..516
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           530..533
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        97
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        436
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        439
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        436..439
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        208
FT                   /note="A -> T (in Ref. 4; AK073970)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  59032 MW;  F435D08CE96793B7 CRC64;
     MRARRVVAAA AVLLLFAVVA VARLDLDDDG DDSEVLDELL AVDEEEERGE LGGGGEAAAA
     EAVRRAQSMV LVLDNDNARR AVEENAEVLL LGYAPWCERS AQLMPRFAEA AAALRAMGSA
     VAFAKLDGER YPKAASAVGV KGFPTVLLFV NGTEHQFTGL HTKDAIVTWV RKKTGAPASR
     IQSKDSAEEF LKKDQTFAVG LFKNFEGAEY EEFVKAATSE NEVQFVETND RNVAKILFPG
     IASEEQFLGL VKSEPEKFEK FNGAFEEKEI IQFVELNKFP LITVFTDLNS GKVYGSPIKL
     QVFTFAEAYD FEDLESMIQE VARGFKTKIM LIYVDTAEEK LAKPFLTLYG LEPEKPTVTA
     FDTSKGTKYL MEAEINAKNL QDFCLSLLEG TLPPYFRSEP VPEEKGPIEK VVGRTFDSSV
     LESPQNVFLE VHAPWCVDCE AISKNVEKLA KHFNDLGQTN LKFARIDASV NEHPKLQINN
     YPTLLLYPAQ DKSNPIKLSK KSNLKDMAKF VKEKLQIADV ETVAAGDIVK DEL