PDI21_ARATH
ID PDI21_ARATH Reviewed; 361 AA.
AC O22263; Q546R3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein disulfide-isomerase like 2-1;
DE Short=AtPDIL2-1;
DE EC=5.3.4.1;
DE AltName: Full=P5;
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 30;
DE AltName: Full=Protein UNFERTILIZED EMBRYO SAC 5;
DE AltName: Full=Protein disulfide isomerase 11;
DE Short=AtPDI11;
DE AltName: Full=Protein disulfide-isomerase A6;
DE AltName: Full=Protein disulfide-isomerase like 4-1;
DE Short=AtPDIL4-1;
DE Flags: Precursor;
GN Name=PDIL2-1; Synonyms=MEE30, PDI11, PDIL4-1, UNE5;
GN OrderedLocusNames=At2g47470; ORFNames=T30B22.23;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mahon P.;
RT "Arabidopsis thaliana mRNA for ERp72.";
RL Thesis (2000), Cambridge University, United Kingdom.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(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 TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18574595; DOI=10.1007/s00438-008-0356-z;
RA Lu D.-P., Christopher D.A.;
RT "Endoplasmic reticulum stress activates the expression of a sub-group of
RT protein disulfide isomerase genes and AtbZIP60 modulates the response in
RT Arabidopsis thaliana.";
RL Mol. Genet. Genomics 280:199-210(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=19050167; DOI=10.1105/tpc.108.062919;
RA Wang H., Boavida L.C., Ron M., McCormick S.;
RT "Truncation of a protein disulfide isomerase, PDIL2-1, delays embryo sac
RT maturation and disrupts pollen tube guidance in Arabidopsis thaliana.";
RL Plant Cell 20:3300-3311(2008).
RN [9]
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: Protein disulfide isomerase that may be required for proper
CC pollen development, ovule fertilization and embryo development.
CC {ECO:0000269|PubMed:19050167}.
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
CC {ECO:0000269|PubMed:19050167}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O22263-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18574595,
CC ECO:0000269|PubMed:19050167}.
CC -!- DEVELOPMENTAL STAGE: During flower development, expressed at early
CC stage in inner and outer integuments, and nucellar cells. Later,
CC expressed in the integument cells but not in the embryo sac. In the
CC mature ovule, highly expressed in the micropylar region. After
CC fertilization, expressed in the seed integuments but not in the embryo.
CC {ECO:0000269|PubMed:19050167}.
CC -!- INDUCTION: By chemically-induced ER stress response.
CC {ECO:0000269|PubMed:18574595}.
CC -!- DISRUPTION PHENOTYPE: Smaller siliques and reduced seed set. Disrupted
CC pollen tube guidance. {ECO:0000269|PubMed:19050167}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AF083688; AAN60247.1; -; mRNA.
DR EMBL; AJ271470; CAC81060.1; -; mRNA.
DR EMBL; AC002535; AAC62863.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10845.1; -; Genomic_DNA.
DR EMBL; AY074348; AAL67044.1; -; mRNA.
DR EMBL; AY091388; AAM14327.1; -; mRNA.
DR PIR; T00437; T00437.
DR RefSeq; NP_182269.1; NM_130315.5. [O22263-1]
DR AlphaFoldDB; O22263; -.
DR SMR; O22263; -.
DR BioGRID; 4695; 9.
DR IntAct; O22263; 1.
DR STRING; 3702.AT2G47470.1; -.
DR iPTMnet; O22263; -.
DR SwissPalm; O22263; -.
DR SWISS-2DPAGE; O22263; -.
DR PaxDb; O22263; -.
DR PRIDE; O22263; -.
DR ProteomicsDB; 236337; -. [O22263-1]
DR EnsemblPlants; AT2G47470.1; AT2G47470.1; AT2G47470. [O22263-1]
DR GeneID; 819360; -.
DR Gramene; AT2G47470.1; AT2G47470.1; AT2G47470. [O22263-1]
DR KEGG; ath:AT2G47470; -.
DR Araport; AT2G47470; -.
DR TAIR; locus:2062029; AT2G47470.
DR eggNOG; KOG0191; Eukaryota.
DR InParanoid; O22263; -.
DR PhylomeDB; O22263; -.
DR PRO; PR:O22263; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22263; baseline and differential.
DR Genevisible; O22263; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:TAIR.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0048868; P:pollen tube development; IMP:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:TAIR.
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; Endoplasmic reticulum; Isomerase;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..361
FT /note="Protein disulfide-isomerase like 2-1"
FT /id="PRO_0000034242"
FT DOMAIN 23..131
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 132..250
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 174
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 53
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 54
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 117
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 172
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 173
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 236
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 52..55
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 171..174
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 361 AA; 39497 MW; 9F4C7A07B0209DB5 CRC64;
MAKSQIWFGF ALLALLLVSA VADDVVVLTD DSFEKEVGKD KGALVEFYAP WCGHCKKLAP
EYEKLGASFK KAKSVLIAKV DCDEQKSVCT KYGVSGYPTI QWFPKGSLEP QKYEGPRNAE
ALAEYVNKEG GTNVKLAAVP QNVVVLTPDN FDEIVLDQNK DVLVEFYAPW CGHCKSLAPT
YEKVATVFKQ EEGVVIANLD ADAHKALGEK YGVSGFPTLK FFPKDNKAGH DYDGGRDLDD
FVSFINEKSG TSRDSKGQLT SKAGIVESLD ALVKELVAAS EDEKKAVLSR IEEEASTLKG
STTRYGKLYL KLAKSYIEKG SDYASKETER LGRVLGKSIS PVKADELTLK RNILTTFVAS
S
