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PDI51_ORYSJ
ID   PDI51_ORYSJ             Reviewed;         147 AA.
AC   Q10N04; A0A0P0VW92;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Protein disulfide isomerase-like 5-1;
DE            Short=OsPDIL5-1;
DE   AltName: Full=Protein disulfide isomerase-like 6-1;
DE            Short=OsPDIL6-1;
DE   Flags: Precursor;
GN   Name=PDIL5-1; Synonyms=PDIL6-1;
GN   OrderedLocusNames=Os03g0287900, LOC_Os03g17860;
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=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
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 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   [6]
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   [7]
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   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; DP000009; ABF95370.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF11695.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS83643.1; -; Genomic_DNA.
DR   EMBL; AK063663; BAG88812.1; -; mRNA.
DR   RefSeq; XP_015628450.1; XM_015772964.1.
DR   AlphaFoldDB; Q10N04; -.
DR   SMR; Q10N04; -.
DR   STRING; 4530.OS03T0287900-01; -.
DR   PaxDb; Q10N04; -.
DR   PRIDE; Q10N04; -.
DR   EnsemblPlants; Os03t0287900-01; Os03t0287900-01; Os03g0287900.
DR   GeneID; 4332486; -.
DR   Gramene; Os03t0287900-01; Os03t0287900-01; Os03g0287900.
DR   KEGG; osa:4332486; -.
DR   eggNOG; KOG0191; Eukaryota.
DR   HOGENOM; CLU_090389_4_2_1; -.
DR   InParanoid; Q10N04; -.
DR   OMA; HAYPTFK; -.
DR   OrthoDB; 1481386at2759; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; Q10N04; OS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Redox-active center; Reference proteome; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..147
FT                   /note="Protein disulfide isomerase-like 5-1"
FT                   /id="PRO_0000400036"
FT   DOMAIN          30..137
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        59
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            123
FT                   /note="Lowers pKa of C-terminal Cys of active site"
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..62
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   147 AA;  16282 MW;  8000AE54D767CF1C CRC64;
     MDLAPGRRAR LLVALALVVL VALAARSGAE VITLTEETFS DKIKEKDTVW FVKFCVPWCK
     HCKNLGTLWE DLGKVMEGAD EIEIGQVDCG VSKPVCSKVD IHSYPTFKVF YEGEEVAKYK
     GPRNVESLKN FVSDEAEKAG EAKLQDS
 
 
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