PDI21_ORYSJ
ID PDI21_ORYSJ Reviewed; 366 AA.
AC Q75M08; A0A0P0WI54; B7ENX8; Q5WMX4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein disulfide isomerase-like 2-1;
DE Short=OsPDIL2-1;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide isomerase-like 4-1;
DE Short=OsPDIL4-1;
DE Flags: Precursor;
GN Name=PDIL2-1; Synonyms=PDIL4-1;
GN OrderedLocusNames=Os05g0156300, LOC_Os05g06430;
GN ORFNames=OsJ_17181, P0431G05.14, P0676G05.4;
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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 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] (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 [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: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q75M08-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q75M08-2; Sequence=VSP_039981;
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AC087425; AAS55771.2; -; Genomic_DNA.
DR EMBL; AC087551; AAV32227.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16610.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92362.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92363.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE62391.1; -; Genomic_DNA.
DR EMBL; AK062024; BAG88199.1; -; mRNA.
DR EMBL; AK098931; BAG93817.1; -; mRNA.
DR EMBL; AK099341; BAG94075.1; -; mRNA.
DR EMBL; AK103944; BAG96336.1; -; mRNA.
DR RefSeq; XP_015640374.1; XM_015784888.1. [Q75M08-2]
DR RefSeq; XP_015640375.1; XM_015784889.1. [Q75M08-1]
DR AlphaFoldDB; Q75M08; -.
DR SMR; Q75M08; -.
DR STRING; 4530.OS05T0156300-01; -.
DR PaxDb; Q75M08; -.
DR PRIDE; Q75M08; -.
DR EnsemblPlants; Os05t0156300-01; Os05t0156300-01; Os05g0156300. [Q75M08-2]
DR EnsemblPlants; Os05t0156300-02; Os05t0156300-02; Os05g0156300. [Q75M08-1]
DR EnsemblPlants; Os05t0156300-03; Os05t0156300-03; Os05g0156300. [Q75M08-1]
DR GeneID; 4337858; -.
DR Gramene; Os05t0156300-01; Os05t0156300-01; Os05g0156300. [Q75M08-2]
DR Gramene; Os05t0156300-02; Os05t0156300-02; Os05g0156300. [Q75M08-1]
DR Gramene; Os05t0156300-03; Os05t0156300-03; Os05g0156300. [Q75M08-1]
DR KEGG; osa:4337858; -.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_038617_1_0_1; -.
DR InParanoid; Q75M08; -.
DR OMA; WCRHCKK; -.
DR OrthoDB; 840943at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q75M08; baseline and differential.
DR Genevisible; Q75M08; OS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; 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 CDD; cd00238; ERp29c; 1.
DR Gene3D; 1.20.1150.12; -; 1.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR011679; ERp29_C.
DR InterPro; IPR036356; ERp29_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF07749; ERp29; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF47933; SSF47933; 1.
DR SUPFAM; SSF52833; SSF52833; 2.
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; Isomerase; Redox-active center;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..366
FT /note="Protein disulfide isomerase-like 2-1"
FT /id="PRO_0000400033"
FT DOMAIN 30..138
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 139..257
FT /note="Thioredoxin 2"
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 ACT_SITE 178
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 181
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 124
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 179
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 243
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 178..181
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 311
FT /note="K -> NR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_039981"
SQ SEQUENCE 366 AA; 39913 MW; 1D77D174B2937995 CRC64;
MATPQISRKA LASLLLLVAA AAAVSTASAD DVLALTESTF EKEVGQDRAA LVEFYAPWCG
HCKKLAPEYE KLGASFKKAK SVLIAKVDCD EHKSVCSKYG VSGYPTIQWF PKGSLEPKKY
EGQRTAEALA EYVNSEAATN VKIAAVPSSV VVLTPETFDS VVLDETKDVL VEFYAPWCGH
CKHLAPIYEK LASVYKQDEG VVIANLDADK HTALAEKYGV SGFPTLKFFP KGNKAGEDYD
GGRELDDFVK FINEKCGTSR DSKGQLTSEA GIVESLAPLV KEFLGAANDK RKEALSKMEE
DVAKLTGPAA KYGKIYVNSA KKIMEKGSEY TKKESERLQR MLEKSISPSK ADEFVIKKNI
LSTFSS
