ID   PDI53_ORYSJ             Reviewed;         425 AA.
AC   Q0E0I1;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Protein disulfide isomerase-like 5-3;
DE            Short=OsPDIL5-3;
DE   AltName: Full=Protein disulfide isomerase-like 7-2;
DE            Short=OsPDIL7-2;
DE   Flags: Precursor;
GN   Name=PDIL5-3; Synonyms=PDIL7-2;
GN   OrderedLocusNames=Os02g0550300, LOC_Os02g34530; ORFNames=OsJ_07093;
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 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   [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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AP008208; BAF09007.1; -; Genomic_DNA.
DR   EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000139; EAZ23399.1; -; Genomic_DNA.
DR   RefSeq; XP_015627163.1; XM_015771677.1.
DR   AlphaFoldDB; Q0E0I1; -.
DR   SMR; Q0E0I1; -.
DR   STRING; 4530.OS02T0550300-00; -.
DR   PaxDb; Q0E0I1; -.
DR   PRIDE; Q0E0I1; -.
DR   GeneID; 4329624; -.
DR   KEGG; osa:4329624; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   HOGENOM; CLU_054116_0_0_1; -.
DR   InParanoid; Q0E0I1; -.
DR   OrthoDB; 746938at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q0E0I1; OS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Membrane; Redox-active center; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..425
FT                   /note="Protein disulfide isomerase-like 5-3"
FT                   /id="PRO_0000400038"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..153
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        75
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            76
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            77
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            139
FT                   /note="Lowers pKa of C-terminal Cys of active site"
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..78
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   425 AA;  47104 MW;  DE05133A6295AD96 CRC64;
     MGKPTLPPVV VVVVLLLLVV VLPATTCGAD AGGGGEAEEF QIPRDGRVLE LDDGNFDAAV
     RAAGLLFVDF YAPWCGHCKR LAPQLDEAAP VLAGLSTPIV VAKVNADKYK KLGSKYGVDG
     FPTLMLFDHG TPTEYTGSRK ADLLVENLKK LVAPDVSVLE SDSAIKSFVE DAGMGFPLFL
     GFGVDESLIV EYGAKYKNRA WFSVAKDFSE DMMVFYDFDK VPALVSVNPK YREQSIFYGP
     FDDGAFLEDF IRNSLLPLVV PMNRETVKML NDDGRKVVLM ILQDDESDEN SPRLIKVLRS
     AASANRDLVF GYVGVNQWEE FTETFDVKSS ELPTMIVWDK KEEYEIVEGS ERLEEGDYGS
     QISRFLEGYR AGRTIKKKVG DRSPTLLGVN AVYILVFLVA VLVLLMYFSG QGEEDQRPRQ
     RAHED