PDI14_ORYSJ
ID PDI14_ORYSJ Reviewed; 563 AA.
AC Q67IX6; A0A0P0VDI0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein disulfide isomerase-like 1-4;
DE Short=OsPDIL1-4;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide isomerase-like 2-1;
DE Short=OsPDIL2-1;
DE Flags: Precursor;
GN Name=PDIL1-4; Synonyms=PDIL2-1;
GN OrderedLocusNames=Os02g0100100, LOC_Os02g01010;
GN ORFNames=OsJ_04977, OSJNOa183H18.2;
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=16623884; DOI=10.1111/j.1365-313x.2006.02684.x;
RA Mizuno H., Wu J., Kanamori H., Fujisawa M., Namiki N., Saji S.,
RA Katagiri S., Katayose Y., Sasaki T., Matsumoto T.;
RT "Sequencing and characterization of telomere and subtelomere regions on
RT rice chromosomes 1S, 2S, 2L, 6L, 7S, 7L and 8S.";
RL Plant J. 46:206-217(2006).
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 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 [6]
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 [7]
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 [8]
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; AP006851; BAD38565.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07493.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS76496.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE56114.1; -; Genomic_DNA.
DR EMBL; AK071514; BAG92533.1; -; mRNA.
DR RefSeq; XP_015627045.1; XM_015771559.1.
DR AlphaFoldDB; Q67IX6; -.
DR SMR; Q67IX6; -.
DR STRING; 4530.OS02T0100100-01; -.
DR PaxDb; Q67IX6; -.
DR PRIDE; Q67IX6; -.
DR EnsemblPlants; Os02t0100100-01; Os02t0100100-01; Os02g0100100.
DR GeneID; 4327971; -.
DR Gramene; Os02t0100100-01; Os02t0100100-01; Os02g0100100.
DR KEGG; osa:4327971; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_7_0_1; -.
DR InParanoid; Q67IX6; -.
DR OMA; FCDRFLE; -.
DR OrthoDB; 462118at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q67IX6; 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; IPR005788; Disulphide_isomerase.
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 TIGRFAMs; TIGR01126; pdi_dom; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..563
FT /note="Protein disulfide isomerase-like 1-4"
FT /id="PRO_0000400031"
FT DOMAIN 46..180
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 394..523
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 40..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 560..563
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 538..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 444
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 447
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 166
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 445
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 446
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 509
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..105
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 444..447
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 563 AA; 62253 MW; F6862C4A2C65491F CRC64;
MRSRSLLLVA LATLLLHASA SASDDDLDYL IDNADDIPAN DPDGWLQEGS PDDDDDDDLF
HHGQAQDHPI DETHVFLLSA ANFSDFLASH RHVMVEFYAP WCAHCQALAP DYAAAAADLS
PLAHQVALAK VDATEDTDLA QKYDVQGFPT ILFFIDGVPK DYNGARTKEA IVSWVNKKLA
PGVQNITTVD EAEKILTGED KAILAVLDSL SGAHSDEIAA ASRLEDAINF YQTSNPDVAK
LFHLDPAAKR PSLVLLKKQE EEKLTFYDGP FKASAIADFV SANKLPLVNT LTQETAPSIF
DNPIKKQILL FVVANESSKF LPIFKEASKS FKGKLLFVFV ERDNEEVGEP VANYFGITGQ
ETTVLAYTGN EDARNFFLDG EISVENIKRF AEDFLEEKLT PFYKSEPVPE SNEGDVKIVV
GKNLDQIVLD ESKDALLEIY APWCGHCQEL EPTYNKLGKH LRGIDSLVIA KMDGTANEHP
RAKPDGFPTI LFYPAGKKSF EPITFEGDRT VVEMYKFIKK HASIPFKLKR PDSSATKTEK
DQSTASTNLR GERSSGTNFK DEL
