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   27-MAR-2024, entry version 155.
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;
GN   OrderedLocusNames=At3g54960; 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};
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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.Q8VX13; -.
DR   GlyCosmos; Q8VX13; 8 sites, No reported glycans.
DR   PaxDb; 3702-AT3G54960-1; -.
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; AT3G54960; PDIL1-3.
DR   eggNOG; KOG0190; Eukaryota.
DR   InParanoid; Q8VX13; -.
DR   OMA; HANSHHD; -.
DR   OrthoDB; 314307at2759; -.
DR   PhylomeDB; Q8VX13; -.
DR   PRO; PR:Q8VX13; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8VX13; baseline and differential.
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:0034976; P:response to endoplasmic reticulum stress; IEP: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; 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   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF217; PROTEIN DISULFIDE ISOMERASE-LIKE 1-3; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
DR   Genevisible; Q8VX13; AT.
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
//