PDI54_ORYSJ
ID PDI54_ORYSJ Reviewed; 485 AA.
AC Q69SA9; A0A0P0X7L3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein disulfide isomerase-like 5-4;
DE Short=OsPDIL5-4;
DE AltName: Full=Protein disulfide isomerase-like 8-1;
DE Short=OsPDIL8-1;
DE Flags: Precursor;
GN Name=PDIL5-4; Synonyms=PDIL8-1;
GN OrderedLocusNames=Os07g0524100, LOC_Os07g34030;
GN ORFNames=OsJ_24505, OSJNBb0052O11.108;
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 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 [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.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AP005105; BAD30858.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21735.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01838.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE67299.1; -; Genomic_DNA.
DR EMBL; AK099660; BAG94243.1; -; mRNA.
DR RefSeq; XP_015647888.1; XM_015792402.1.
DR AlphaFoldDB; Q69SA9; -.
DR STRING; 4530.OS07T0524100-01; -.
DR PaxDb; Q69SA9; -.
DR PRIDE; Q69SA9; -.
DR EnsemblPlants; Os07t0524100-01; Os07t0524100-01; Os07g0524100.
DR GeneID; 4343420; -.
DR Gramene; Os07t0524100-01; Os07t0524100-01; Os07g0524100.
DR KEGG; osa:4343420; -.
DR eggNOG; KOG2667; Eukaryota.
DR HOGENOM; CLU_034705_3_0_1; -.
DR InParanoid; Q69SA9; -.
DR OMA; GNFHVHL; -.
DR OrthoDB; 1318747at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q69SA9; OS.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR045888; Erv.
DR InterPro; IPR012936; Erv_C.
DR InterPro; IPR039542; Erv_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10984; PTHR10984; 1.
DR Pfam; PF07970; COPIIcoated_ERV; 1.
DR Pfam; PF13850; ERGIC_N; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT CHAIN ?..485
FT /note="Protein disulfide isomerase-like 5-4"
FT /id="PRO_0000400039"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 114..263
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 485 AA; 54434 MW; 010BFDDE156B6227 CRC64;
MISSSKLKSV DFYRKIPRDL TEASLSGAGL SIVAALAMVF LFGMELSNYL AVNTSTSVIV
DRSSDGEFLR IDFNLSFPAL SCEFASVDVS DVLGTNRLNI TKTVRKYSID RNLVPTGSEF
HPGPIPTVSK HGDDVEENHD DGSVPLSSRN FDSYSHQYPV LVVNFYAPWC YWSNRLKPSW
EKTAKIMRER YDPEMDGRII LAKVDCTEEI DLCRRHHIQG YPSIRIFRKG SDLKENQGHH
DHESYYGDRD TESLVAAMET YVANIPKDAH VLALEDKSNK TVDPAKRPAP LTSGCRIEGF
VRVKKVPGSV VISARSGSHS FDPSQINVSH YVTQFSFGKR LSAKMFNELK RLTPYVGGHH
DRLAGQSYIV KHGDVNANVT IEHYLQIVKT ELVTLRSSKE LKLVEEYEYT AHSSLVHSFY
VPVVKFHFEP SPMQVLVTEL PKSFSHFITN VCAIIGGVFT VAGILDSIFH NTLRLVKKVE
LGKNI
