PDI52_ORYSJ
ID PDI52_ORYSJ Reviewed; 423 AA.
AC Q0JD42; A0A0P0WAQ8; Q7XQN8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein disulfide isomerase-like 5-2;
DE Short=OsPDIL5-2;
DE AltName: Full=Protein disulfide isomerase-like 7-1;
DE Short=OsPDIL7-1;
DE Flags: Precursor;
GN Name=PDIL5-2; Synonyms=PDIL7-1;
GN OrderedLocusNames=Os04g0432500, LOC_Os04g35290; ORFNames=OSJNBa0084A10.17;
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE03042.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL606458; CAE03042.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF14745.2; -; Genomic_DNA.
DR EMBL; AP014960; BAS89277.1; -; Genomic_DNA.
DR EMBL; AK069367; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015637134.1; XM_015781648.1.
DR AlphaFoldDB; Q0JD42; -.
DR SMR; Q0JD42; -.
DR STRING; 4530.OS04T0432500-01; -.
DR PaxDb; Q0JD42; -.
DR PRIDE; Q0JD42; -.
DR EnsemblPlants; Os04t0432500-01; Os04t0432500-01; Os04g0432500.
DR GeneID; 4335881; -.
DR Gramene; Os04t0432500-01; Os04t0432500-01; Os04g0432500.
DR KEGG; osa:4335881; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_054116_0_0_1; -.
DR InParanoid; Q0JD42; -.
DR OMA; MWRGNPV; -.
DR OrthoDB; 746938at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q0JD42; baseline and differential.
DR Genevisible; Q0JD42; OS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Membrane; Redox-active center;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..423
FT /note="Protein disulfide isomerase-like 5-2"
FT /id="PRO_0000400037"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 36..149
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 71
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 74
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 72
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 73
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 135
FT /note="Lowers pKa of C-terminal Cys of active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..74
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 136
FT /note="K -> E (in Ref. 5; AK069367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47056 MW; 3D56FF8BFCB51A32 CRC64;
MAATTTRPLP LLLLLLLPPL LLLLLSFHAA AAAAAEEFPR DGRVIELDES SFEAALGAID
YLFVDFYAPW CGHCKRLAPE LDEAAPVLAG LSEPIIVAKV NADKYRKLGS KYGVDGFPTL
MLFIHGVPIE YTGSRKADLL VRNLNKFVAP DVSILESDSA IKSFVENAGT SFPMFIGFGV
NESLIAGYGG KYKKRAWFAV AKDFSEDFMV TYDFDKVPAL VSLHPKYKEQ SVFYGPFEGS
FLEDFIRQSL LPLTVPINTE TLKMLDDDDR KVVLAILEDD SDETSSQLVK VLRSAANANR
DLVFGYVGIK QWDEFVETFD ISKSSQLPKL IVWDRNEEYE VVEGSEKLEE GDQASQISQF
LEGYRAGRTT KKKVSGPSFM GFLNSLVSLN SLYILICVFA LLGVMIYFTG QDDTPQVRRA
HEE
