PDI53_ARATH
ID PDI53_ARATH Reviewed; 483 AA.
AC Q9LJU2;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein disulfide-isomerase 5-3;
DE Short=AtPDIL5-3;
DE AltName: Full=Protein disulfide-isomerase 12;
DE Short=PDI12;
DE AltName: Full=Protein disulfide-isomerase 8-1;
DE Short=AtPDIL8-1;
DE Flags: Precursor;
GN Name=PDIL5-3; Synonyms=PDI12, PDIL8-1; OrderedLocusNames=At3g20560;
GN ORFNames=K10D20.9;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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.
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 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 -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AP000410; BAB01164.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76398.1; -; Genomic_DNA.
DR EMBL; AY050453; AAK91468.1; -; mRNA.
DR RefSeq; NP_566664.1; NM_112948.3.
DR AlphaFoldDB; Q9LJU2; -.
DR SMR; Q9LJU2; -.
DR STRING; 3702.AT3G20560.1; -.
DR iPTMnet; Q9LJU2; -.
DR PaxDb; Q9LJU2; -.
DR PRIDE; Q9LJU2; -.
DR ProteomicsDB; 236376; -.
DR EnsemblPlants; AT3G20560.1; AT3G20560.1; AT3G20560.
DR GeneID; 821603; -.
DR Gramene; AT3G20560.1; AT3G20560.1; AT3G20560.
DR KEGG; ath:AT3G20560; -.
DR Araport; AT3G20560; -.
DR TAIR; locus:2085750; AT3G20560.
DR eggNOG; KOG2667; Eukaryota.
DR HOGENOM; CLU_034705_3_0_1; -.
DR InParanoid; Q9LJU2; -.
DR OMA; NINHGEE; -.
DR OrthoDB; 1318747at2759; -.
DR PhylomeDB; Q9LJU2; -.
DR PRO; PR:Q9LJU2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJU2; baseline and differential.
DR Genevisible; Q9LJU2; 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 GO; GO:0003756; F:protein disulfide isomerase activity; ISS:TAIR.
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 Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..?
FT CHAIN ?..483
FT /note="Protein disulfide-isomerase 5-3"
FT /id="PRO_0000400026"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 133..263
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 279
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"
SQ SEQUENCE 483 AA; 53996 MW; CB96EA1262F1A770 CRC64;
MVSSTKLKSV DFYRKIPRDL TEASLSGAGL SIVAALFMMF LFGMELSSYL EVNTTTAVIV
DKSSDGDFLR IDFNISFPAL SCEFASVDVS DVLGTNRLNI TKTVRKFPID PHLRSTGAEF
HSGLALHNIN HGEETKEEFP DGAIPLTSAS FEALSHHFPI LVVNFNAPWC YWSNRLKPSW
EKAANIIKQR YDPEADGRVL LGNVDCTEEP ALCKRNHIQG YPSIRIFRKG SDLREDHGHH
EHESYYGDRD TDSIVKMVEG LVAPIHPETH KVALDGKSND TVKHLKKGPV TGGCRVEGYV
RVKKVPGNLV ISAHSGAHSF DSSQMNMSHV VSHFSFGRMI SPRLLTDMKR LLPYLGLSHD
RLDGKAFINQ HEFGANVTIE HYLQTVKTEV ITRRSGQEHS LIEEYEYTAH SSVAQTYYLP
VAKFHFELSP MQILITENPK SFSHFITNLC AIIGGVFTVA GILDSIFHNT VRLVKKVELG
KNI
