PDI16_ARATH
ID PDI16_ARATH Reviewed; 534 AA.
AC Q66GQ3; Q56YD5; Q9LW75;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Protein disulfide isomerase-like 1-6;
DE Short=AtPDIL1-6;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide isomerase 4;
DE Short=AtPDI4;
DE AltName: Full=Protein disulfide isomerase-like 3-2;
DE Short=AtPDIL3-2;
DE Flags: Precursor;
GN Name=PDIL1-6; Synonyms=PDI4, PDIL3-2; OrderedLocusNames=At3g16110;
GN ORFNames=MSL1.15;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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).
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. {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: Endoplasmic reticulum lumen {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18574595}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02677.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB012247; BAB02677.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75772.1; -; Genomic_DNA.
DR EMBL; BT015349; AAU05472.1; -; mRNA.
DR EMBL; BT015798; AAU93570.1; -; mRNA.
DR EMBL; AK221388; BAD94313.1; -; mRNA.
DR RefSeq; NP_188232.2; NM_112481.4.
DR AlphaFoldDB; Q66GQ3; -.
DR SMR; Q66GQ3; -.
DR STRING; 3702.AT3G16110.1; -.
DR iPTMnet; Q66GQ3; -.
DR PaxDb; Q66GQ3; -.
DR PRIDE; Q66GQ3; -.
DR ProteomicsDB; 236387; -.
DR EnsemblPlants; AT3G16110.1; AT3G16110.1; AT3G16110.
DR GeneID; 820856; -.
DR Gramene; AT3G16110.1; AT3G16110.1; AT3G16110.
DR KEGG; ath:AT3G16110; -.
DR Araport; AT3G16110; -.
DR TAIR; locus:2093447; AT3G16110.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_7_0_1; -.
DR InParanoid; Q66GQ3; -.
DR OMA; SNENLAM; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q66GQ3; -.
DR PRO; PR:Q66GQ3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q66GQ3; baseline and differential.
DR Genevisible; Q66GQ3; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:TAIR.
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; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..534
FT /note="Protein disulfide isomerase-like 1-6"
FT /id="PRO_0000400021"
FT DOMAIN 56..182
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 407..524
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 531..534
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 446
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 449
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 446..449
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 326
FT /note="L -> P (in Ref. 4; BAD94313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 59571 MW; 66FA90F57CF5FF85 CRC64;
MLTKPKPNSK FSILFTFLLL LSFLIFVARS SDVAVEAGSE EELDDLEQLL AVDEQLQEER
PEQQSEAETV SKAQRIVVEL NGDNTKRLID GNEYVMVLGY APWCARSAEL MPRFAEAATD
LKEIGSSVLM AKIDGERYSK VASQLEIKGF PTLLLFVNGT SQSYTGGFSS EEIVIWVQKK
TGASTIKLDT VDEASGFLKK HHTFILGLFE KSEDSSGHDE FVKAASLDNE IQFVETSSID
VAKLLFPNLK TNNVFVGLVK TEAEKYTSYD GPCQAEKIVE FLNSNKFPLV TKLTESNTVR
VYSSPVKLQV MVFSKTDDFE SLAQPLEDIA RKFKSKLMLI YIDISNENLA MPFLTLFGIE
DAKKTVVAAF DNNLNSKYLL ESDPSPSNIE EFCFGLAHGT VSAYYKSQPI PDNQNASVVA
VVGRTFDEVV LRSSENVLLE VHTPWCINCE ALSKQVEKLS QHFKGFENLV FARIDASANE
HPKLTVDDYP TILLYKTGEK ENPLKLSTKS SAKDMAVLIN KELKWKDQSG KDEL
