PDI13_ARATH
ID PDI13_ARATH Reviewed; 579 AA.
AC Q8VX13; B3H5N9; Q9SV44;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Protein disulfide isomerase-like 1-3;
DE Short=AtPDIL1-3;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide isomerase 1;
DE Short=AtPDI1;
DE AltName: Full=Protein disulfide isomerase-like 2-1;
DE Short=AtPDIL2-1;
DE Flags: Precursor;
GN Name=PDIL1-3; Synonyms=PDI1, PDI72, PDIL2-1; OrderedLocusNames=At3g54960;
GN ORFNames=F28P10.60, T15C9.4;
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] (ISOFORM 1).
RA Mahon P.;
RT "Arabidopsis thaliana mRNA for ERp72.";
RL Thesis (2000), Cambridge University, United Kingdom.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VX13-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VX13-2; Sequence=VSP_039979, VSP_039980;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18574595}.
CC -!- INDUCTION: By chemically-induced ER stress response.
CC {ECO:0000269|PubMed:18574595}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41088.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK318844; BAH56959.1; -; mRNA.
DR EMBL; AJ271376; CAC81067.1; -; mRNA.
DR EMBL; AL049655; CAB41088.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL132970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE79318.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79319.1; -; Genomic_DNA.
DR EMBL; AY093115; AAM13114.1; -; mRNA.
DR EMBL; BT000172; AAN15491.1; -; mRNA.
DR PIR; T06724; T06724.
DR RefSeq; NP_001118842.1; NM_001125370.1. [Q8VX13-2]
DR RefSeq; NP_191056.2; NM_115353.5. [Q8VX13-1]
DR AlphaFoldDB; Q8VX13; -.
DR SMR; Q8VX13; -.
DR BioGRID; 9977; 15.
DR IntAct; Q8VX13; 1.
DR STRING; 3702.AT3G54960.1; -.
DR PaxDb; Q8VX13; -.
DR PRIDE; Q8VX13; -.
DR ProteomicsDB; 236386; -. [Q8VX13-1]
DR EnsemblPlants; AT3G54960.1; AT3G54960.1; AT3G54960. [Q8VX13-1]
DR EnsemblPlants; AT3G54960.2; AT3G54960.2; AT3G54960. [Q8VX13-2]
DR GeneID; 824661; -.
DR Gramene; AT3G54960.1; AT3G54960.1; AT3G54960. [Q8VX13-1]
DR Gramene; AT3G54960.2; AT3G54960.2; AT3G54960. [Q8VX13-2]
DR KEGG; ath:AT3G54960; -.
DR Araport; AT3G54960; -.
DR TAIR; locus:2082712; AT3G54960.
DR eggNOG; KOG0190; Eukaryota.
DR InParanoid; Q8VX13; -.
DR OMA; HANSHHD; -.
DR PhylomeDB; Q8VX13; -.
DR PRO; PR:Q8VX13; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VX13; baseline and differential.
DR Genevisible; Q8VX13; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:TAIR.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
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; Glycoprotein;
KW Isomerase; Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..579
FT /note="Protein disulfide isomerase-like 1-3"
FT /id="PRO_5000065917"
FT DOMAIN 81..204
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 416..546
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 44..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 576..579
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 564..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 131
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 467
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 470
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 190
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 468
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 469
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 532
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 128..131
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 467..470
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 507..518
FT /note="ADGFPTILFFPG -> VIKKKELRKSFW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039979"
FT VAR_SEQ 519..579
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039980"
SQ SEQUENCE 579 AA; 64212 MW; 0DF50E500B24B829 CRC64;
MASSSTSISL LLFVSFILLL VNSRAENASS GSDLDEELAF LAAEESKEQS HGGGSYHEEE
HDHQHRDFEN YDDLEQGGGE FHHGDHGYEE EPLPPVDEKD VAVLTKDNFT EFVGNNSFAM
VEFYAPWCGA CQALTPEYAA AATELKGLAA LAKIDATEEG DLAQKYEIQG FPTVFLFVDG
EMRKTYEGER TKDGIVTWLK KKASPSIHNI TTKEEAERVL SAEPKLVFGF LNSLVGSESE
ELAAASRLED DLSFYQTASP DIAKLFEIET QVKRPALVLL KKEEEKLARF DGNFTKTAIA
EFVSANKVPL VINFTREGAS LIFESSVKNQ LILFAKANES EKHLPTLREV AKSFKGKFVF
VYVQMDNEDY GEAVSGFFGV TGAAPKVLVY TGNEDMRKFI LDGELTVNNI KTLAEDFLAD
KLKPFYKSDP LPENNDGDVK VIVGNNFDEI VLDESKDVLL EIYAPWCGHC QSFEPIYNKL
GKYLKGIDSL VVAKMDGTSN EHPRAKADGF PTILFFPGGN KSFDPIAVDV DRTVVELYKF
LKKHASIPFK LEKPATPEPV ISTMKSDEKI EGDSSKDEL
