PDI52_ARATH
ID PDI52_ARATH Reviewed; 440 AA.
AC Q94F09; Q9LQG5;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein disulfide-isomerase 5-2;
DE Short=AtPDIL5-2;
DE AltName: Full=Protein disulfide-isomerase 7-1;
DE Short=AtPDIL7-1;
DE AltName: Full=Protein disulfide-isomerase 8;
DE Short=PDI8;
DE Flags: Precursor;
GN Name=PDIL5-2; Synonyms=PDI8, PDIL7-1; OrderedLocusNames=At1g35620;
GN ORFNames=F15O4.20;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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 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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79381.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007887; AAF79381.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31818.1; -; Genomic_DNA.
DR EMBL; AF386986; AAK62431.1; -; mRNA.
DR EMBL; BT008751; AAP49513.1; -; mRNA.
DR RefSeq; NP_564462.1; NM_103262.5.
DR AlphaFoldDB; Q94F09; -.
DR SMR; Q94F09; -.
DR BioGRID; 25693; 7.
DR IntAct; Q94F09; 7.
DR STRING; 3702.AT1G35620.1; -.
DR iPTMnet; Q94F09; -.
DR PaxDb; Q94F09; -.
DR PRIDE; Q94F09; -.
DR ProteomicsDB; 236804; -.
DR EnsemblPlants; AT1G35620.1; AT1G35620.1; AT1G35620.
DR GeneID; 840461; -.
DR Gramene; AT1G35620.1; AT1G35620.1; AT1G35620.
DR KEGG; ath:AT1G35620; -.
DR Araport; AT1G35620; -.
DR TAIR; locus:2014681; AT1G35620.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_054116_0_0_1; -.
DR InParanoid; Q94F09; -.
DR OMA; MWRGNPV; -.
DR OrthoDB; 746938at2759; -.
DR PhylomeDB; Q94F09; -.
DR PRO; PR:Q94F09; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94F09; baseline and differential.
DR Genevisible; Q94F09; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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; IBA:GO_Central.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Redox-active center; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..440
FT /note="Protein disulfide-isomerase 5-2"
FT /id="PRO_0000400025"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 24..139
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 406..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 61
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 64
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 62
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 63
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 125
FT /note="Lowers pKa of C-terminal Cys of active site"
FT /evidence="ECO:0000250"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..64
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 440 AA; 49851 MW; 7609CAF70D38D00A CRC64;
MRSLKLLLCW ISFLTLSISI SASSDDQFTL DGTVLELTDS NFDSAISTFD CIFVDFYAPW
CGHCKRLNPE LDAAAPILAK LKQPIVIAKL NADKYSRLAR KIEIDAFPTL MLYNHGVPME
YYGPRKADLL VRYLKKFVAP DVAVLESDST VKEFVEDAGT FFPVFIGFGL NESIISGLGR
KYKKKAWFAV SKEVSEDTMV SYDFDKAPAL VANHPTYNEH SVFYGPFEDG FLEEFVKQSF
LPLILPINHD TLKLLKDDER KIVLTIVEDE THESLEKLYK ALRAAAHANR DLVFGYVGVK
QFEEFVDSFH VDKKTNLPKI VVWDGDEEYD QVTGIETITQ EEDHLTQVSR FLEGYREGRT
EKKKINGPSF MGFINSMIGI RSVYILVFLV AVIMMLRSLG QVEEPTGVRT ATAVRERVDQ
ATTVPEDESS EHKPSDKKED
