ID PDI14_ARATH Reviewed; 597 AA.
AC Q9FF55; Q8LAM5;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 164.
DE RecName: Full=Protein disulfide isomerase-like 1-4;
DE Short=AtPDIL1-4;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide isomerase 2;
DE Short=AtPDI2;
DE AltName: Full=Protein disulfide isomerase-like 2-2;
DE Short=AtPDIL2-2;
DE Flags: Precursor;
GN Name=PDIL1-4; Synonyms=PDI2, PDIL2-2; OrderedLocusNames=At5g60640;
GN ORFNames=MUP24.6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP TISSUE SPECIFICITY.
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 [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).
RN [8]
RP FUNCTION, INTERACTION WITH MEE8 AND MED37A/BIP1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21909944; DOI=10.1007/s10059-011-0150-3;
RA Cho E.J., Yuen C.Y., Kang B.H., Ondzighi C.A., Staehelin L.A.,
RA Christopher D.A.;
RT "Protein disulfide isomerase-2 of Arabidopsis mediates protein folding and
RT localizes to both the secretory pathway and nucleus, where it interacts
RT with maternal effect embryo arrest factor.";
RL Mol. Cells 32:459-475(2011).
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.
CC {ECO:0000269|PubMed:21909944}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBUNIT: Interacts with MEE8 and MED37A. {ECO:0000269|PubMed:21909944}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:21909944}. Golgi apparatus
CC {ECO:0000269|PubMed:21909944}. Vacuole {ECO:0000269|PubMed:21909944}.
CC Nucleus {ECO:0000269|PubMed:21909944}. Secreted, cell wall
CC {ECO:0000269|PubMed:21909944}.
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=Q9FF55-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in germinating seedling, including the
CC cotyledons and hypocotyl, in vascular tissues, in pollen grains, root
CC tips, leaf trichomes, developing seeds and siliques.
CC {ECO:0000269|PubMed:18574595, ECO:0000269|PubMed:21909944}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, probably due to functional
CC redundancy. {ECO:0000269|PubMed:21909944}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AB005246; BAB09837.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97360.1; -; Genomic_DNA.
DR EMBL; BT001994; AAN72005.1; -; mRNA.
DR EMBL; BT008359; AAP37718.1; -; mRNA.
DR EMBL; AY087725; AAM65262.1; -; mRNA.
DR RefSeq; NP_851234.1; NM_180903.4. [Q9FF55-1]
DR AlphaFoldDB; Q9FF55; -.
DR SMR; Q9FF55; -.
DR BioGRID; 21429; 25.
DR STRING; 3702.Q9FF55; -.
DR GlyCosmos; Q9FF55; 4 sites, No reported glycans.
DR iPTMnet; Q9FF55; -.
DR SwissPalm; Q9FF55; -.
DR PaxDb; 3702-AT5G60640-1; -.
DR ProteomicsDB; 236290; -. [Q9FF55-1]
DR EnsemblPlants; AT5G60640.1; AT5G60640.1; AT5G60640. [Q9FF55-1]
DR GeneID; 836185; -.
DR Gramene; AT5G60640.1; AT5G60640.1; AT5G60640. [Q9FF55-1]
DR KEGG; ath:AT5G60640; -.
DR Araport; AT5G60640; -.
DR TAIR; AT5G60640; PDIL1-4.
DR eggNOG; KOG0190; Eukaryota.
DR InParanoid; Q9FF55; -.
DR OrthoDB; 314307at2759; -.
DR PhylomeDB; Q9FF55; -.
DR PRO; PR:Q9FF55; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF55; baseline and differential.
DR Genevisible; Q9FF55; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:TAIR.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR NCBIfam; TIGR01126; pdi_dom; 1.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF246; PROTEIN DISULFIDE-ISOMERASE; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell wall; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Isomerase; Nucleus; Redox-active center;
KW Reference proteome; Repeat; Secreted; Signal; Vacuole.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..597
FT /note="Protein disulfide isomerase-like 1-4"
FT /id="PRO_0000400019"
FT DOMAIN 85..208
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 429..550
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 37..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 594..597
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 62..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 471
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 474
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 133
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 134
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 194
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 472
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 473
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 536
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 132..135
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 471..474
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 400
FT /note="P -> H (in Ref. 4; AAM65262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 597 AA; 66357 MW; 5A8FC7E72AA64B2B CRC64;
MAFRVLLLFS LTALLIFSAV SPSFAASSSD DVDDEDLSFL EDLKEDDVPG ADSLSSSTGF
DEFEGGEEED PDMYNDDDDE EGDFSDLGNP DSDPLPTPEI DEKDVVVIKE RNFTDVIENN
QYVLVEFYAP WCGHCQSLAP EYAAAATELK EDGVVLAKID ATEENELAQE YRVQGFPTLL
FFVDGEHKPY TGGRTKETIV TWVKKKIGPG VYNLTTLDDA EKVLTSGNKV VLGYLNSLVG
VEHDQLNAAS KAEDDVNFYQ TVNPDVAKMF HLDPESKRPA LVLVKKEEEK ISHFDGEFVK
SALVSFVSAN KLALVSVFTR ETAPEIFESA IKKQLLLFVT KNESEKVLTE FQEAAKSFKG
KLIFVSVDLD NEDYGKPVAE YFGVSGNGPK LIGYTGNEDP KKYFFDGEIQ SDKIKIFGED
FLNDKLKPFY KSDPIPEKND EDVKIVVGDN FDEIVLDDSK DVLLEVYAPW CGHCQALEPM
YNKLAKHLRS IDSLVITKMD GTTNEHPKAK AEGFPTILFF PAGNKTSEPI TVDTDRTVVA
FYKFLRKHAT IPFKLEKPAS TESPKTAEST PKVETTETKE SPDSTTKSSQ SDSKDEL
//
