PID13_ORYSJ
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 25-MAY-2022, entry version 128.
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; 4530.OS02T0554900-01; -.
DR PaxDb; 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; FPEPRAN; -.
DR OrthoDB; 462118at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q69ST6; baseline and differential.
DR Genevisible; Q69ST6; 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; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
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..?
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
