PDI23_ORYSJ
ID PDI23_ORYSJ Reviewed; 441 AA.
AC Q67UF5; A0A0P0XND7; Q67UF4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein disulfide isomerase-like 2-3;
DE Short=OsPDIL2-3;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide isomerase-like 5-1;
DE Short=OsPDIL5-1;
DE Flags: Precursor;
GN Name=PDIL2-3; Synonyms=PDIL5-1;
GN OrderedLocusNames=Os09g0451500, LOC_Os09g27830;
GN ORFNames=OJ1163_C07.26, P0488D02.3;
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] (ISOFORMS 1 AND 2).
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).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21278127; DOI=10.1105/tpc.110.079509;
RA Onda Y., Nagamine A., Sakurai M., Kumamaru T., Ogawa M., Kawagoe Y.;
RT "Distinct roles of protein disulfide isomerase and P5 sulfhydryl
RT oxidoreductases in multiple pathways for oxidation of structurally diverse
RT storage proteins in rice.";
RL Plant Cell 23:210-223(2011).
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. {ECO:0000269|PubMed:21278127}.
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
CC {ECO:0000269|PubMed:21278127}. Note=Localizes on the surface of ER-
CC derived type-I protein bodies in the endosperm.
CC {ECO:0000269|PubMed:21278127}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q67UF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q67UF5-2; Sequence=VSP_039982, VSP_039983;
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AP005393; BAD38008.1; -; Genomic_DNA.
DR EMBL; AP005393; BAD38009.1; -; Genomic_DNA.
DR EMBL; AP005559; BAD38214.1; -; Genomic_DNA.
DR EMBL; AP005559; BAD38215.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF25245.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08387.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08388.1; -; Genomic_DNA.
DR EMBL; AK062254; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK072941; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015611801.1; XM_015756315.1. [Q67UF5-1]
DR AlphaFoldDB; Q67UF5; -.
DR SMR; Q67UF5; -.
DR STRING; 4530.OS09T0451500-02; -.
DR PaxDb; Q67UF5; -.
DR PRIDE; Q67UF5; -.
DR EnsemblPlants; Os09t0451500-01; Os09t0451500-01; Os09g0451500. [Q67UF5-2]
DR EnsemblPlants; Os09t0451500-02; Os09t0451500-02; Os09g0451500. [Q67UF5-1]
DR GeneID; 4347226; -.
DR Gramene; Os09t0451500-01; Os09t0451500-01; Os09g0451500. [Q67UF5-2]
DR Gramene; Os09t0451500-02; Os09t0451500-02; Os09g0451500. [Q67UF5-1]
DR KEGG; osa:4347226; -.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_030311_1_0_1; -.
DR InParanoid; Q67UF5; -.
DR OMA; DDIWLVE; -.
DR OrthoDB; 840943at2759; -.
DR BRENDA; 5.3.4.1; 4460.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q67UF5; OS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR044569; PDIA6-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45815; PTHR45815; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 3.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Isomerase;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..441
FT /note="Protein disulfide isomerase-like 2-3"
FT /id="PRO_0000400035"
FT DOMAIN 19..139
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 159..276
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 143..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 198
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 61
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 121
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 258
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 59..62
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 195..198
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 287..395
FT /note="DAMEEKCASAAICFVSFLPDILDSKAEGRNKYLELLLSVAEKFKKSPYSFVW
FT TAAGKQADLEKQVGVGGYGYPAMVALNVKKGAYAPLRSAFQLDEITEFVKEAGRGGK
FT -> VSFRDINKVILLWRQWSGIDVLTRWFGFCRTPWKRNVLLLPFALYLSFQISWIQRP
FT KEETSTLSCYYLLLRNLKRVHTVLSGQLLGSKLILRSKLELVVMAIQRWLLST (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_039982"
FT VAR_SEQ 396..441
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_039983"
FT CONFLICT 388
FT /note="K -> R (in Ref. 4; AK062254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 47334 MW; 9378586020D38ADB CRC64;
MRPAVAAALL LVAAAVAASP VSALYSAGSP VLQFNPNNFK SKVLNSNGVV LVEFFAPWCG
HCQQLTPIWE KAAGVLKGVA TVAALDADAH KELAQEYGIR GFPTIKVFVP GKPPVDYQGA
RDVKPIVEFA LSQVKALLRD RLNGKTSAGS GGKKSGGSSE KTEPSASIEL NSQNFDKLVT
KSKDLWIVEF FAPWCGHCKK LAPEWKKAAK NLKGQVKLGH VDCDAEKSLM SKYKVEGFPT
ILVFGADKES PFPYQGARVA SAIESFALEQ LEANAAPPEV SELTGPDAME EKCASAAICF
VSFLPDILDS KAEGRNKYLE LLLSVAEKFK KSPYSFVWTA AGKQADLEKQ VGVGGYGYPA
MVALNVKKGA YAPLRSAFQL DEITEFVKEA GRGGKGNLPL DGTPTIVQSE PWDGKDGEVI
EEDEFSLEEL MADNSPVNDE L
