PDI54_ARATH
ID PDI54_ARATH Reviewed; 480 AA.
AC Q9T042; Q8LFW3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Protein disulfide-isomerase 5-4;
DE Short=AtPDIL5-4;
DE AltName: Full=Protein disulfide-isomerase 7;
DE Short=PDI7;
DE AltName: Full=Protein disulfide-isomerase 8-2;
DE Short=AtPDIL8-2;
DE Flags: Precursor;
GN Name=PDIL5-4; Synonyms=PDI7, PDIL8-2; OrderedLocusNames=At4g27080;
GN ORFNames=T24A18.30;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] OF 164-480.
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, 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 [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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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=Q9T042-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18574595}.
CC -!- INDUCTION: Slightly down-regulated by chemically-induced ER stress
CC response. {ECO:0000269|PubMed:18574595}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AL035680; CAB38838.1; -; Genomic_DNA.
DR EMBL; AL161566; CAB79563.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85297.1; -; Genomic_DNA.
DR EMBL; AY054496; AAK96687.1; -; mRNA.
DR EMBL; AY093266; AAM13265.1; -; mRNA.
DR EMBL; AY084612; AAM67352.1; -; mRNA.
DR PIR; T06038; T06038.
DR RefSeq; NP_567765.2; NM_118842.4. [Q9T042-1]
DR AlphaFoldDB; Q9T042; -.
DR BioGRID; 14103; 1.
DR STRING; 3702.AT4G27080.2; -.
DR PaxDb; Q9T042; -.
DR PRIDE; Q9T042; -.
DR ProteomicsDB; 236336; -. [Q9T042-1]
DR EnsemblPlants; AT4G27080.1; AT4G27080.1; AT4G27080. [Q9T042-1]
DR GeneID; 828816; -.
DR Gramene; AT4G27080.1; AT4G27080.1; AT4G27080. [Q9T042-1]
DR KEGG; ath:AT4G27080; -.
DR Araport; AT4G27080; -.
DR eggNOG; KOG2667; Eukaryota.
DR HOGENOM; CLU_034705_3_0_1; -.
DR InParanoid; Q9T042; -.
DR OMA; GNFHVHL; -.
DR PhylomeDB; Q9T042; -.
DR PRO; PR:Q9T042; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T042; baseline and differential.
DR Genevisible; Q9T042; AT.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR045888; Erv.
DR InterPro; IPR012936; Erv_C.
DR InterPro; IPR039542; Erv_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10984; PTHR10984; 1.
DR Pfam; PF07970; COPIIcoated_ERV; 1.
DR Pfam; PF13850; ERGIC_N; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Redox-active center; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..?
FT CHAIN ?..480
FT /note="Protein disulfide-isomerase 5-4"
FT /id="PRO_0000400027"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 120..263
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 173
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 249
FT /note="Lowers pKa of C-terminal Cys of active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 170..173
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 453
FT /note="V -> A (in Ref. 4; AAM67352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 53893 MW; 9123D67830F93E5C CRC64;
MVSTSKIKSV DFYRKIPRDL TEASLSGAGL SIIAALSMIF LFGMELNNYL AVSTSTSVIV
DRSADGDFLR LDFNISFPSL SCEFASVDVS DVLGTNRLNV TKTIRKFSID SNMRPTGSEF
HAGEVLSLIN HGDETGEEIV EDSVPLTGRN FDTFTHQFPI LVVNFYAPWC YWCNLLKPSW
EKAAKQIKER YDPEMDGRVI LAKVDCTQEG DLCRRNHIQG YPSIRIFRKG SDLKDDNAHH
DHESYYGDRD TESLVKMVVS LVEPIHLEPH NLALEDKSDN SSRTLKKAPS TGGCRVEGYM
RVKKVPGNLM VSARSGSHSF DSSQMNMSHV VNHLSFGRRI MPQKFSEFKR LSPYLGLSHD
RLDGRSFINQ RDLGPNVTIE HYLQIVKTEV VKSNGQALVE AYEYTAHSSV AHSYYLPVAK
FHFELSPMQV LITENSKSFS HFITNVCAII GGVFTVAGIL DSILHHSMTL MKKIELGKNF
