PDI15_ARATH
ID PDI15_ARATH Reviewed; 537 AA.
AC A3KPF5; Q9C818;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Protein disulfide isomerase-like 1-5;
DE Short=AtPDIL1-5;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide isomerase 3;
DE Short=AtPDI3;
DE AltName: Full=Protein disulfide isomerase-like 3-1;
DE Short=AtPDIL3-1;
DE Flags: Precursor;
GN Name=PDIL1-5; Synonyms=PDI3, PDIL3-1; OrderedLocusNames=At1g52260;
GN ORFNames=F19K6.17;
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;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18574595}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51554.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC037424; AAG51554.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32775.1; -; Genomic_DNA.
DR EMBL; BT030322; ABO09885.1; -; mRNA.
DR PIR; F96562; F96562.
DR RefSeq; NP_175636.2; NM_104105.3.
DR AlphaFoldDB; A3KPF5; -.
DR SMR; A3KPF5; -.
DR STRING; 3702.AT1G52260.1; -.
DR iPTMnet; A3KPF5; -.
DR PaxDb; A3KPF5; -.
DR PRIDE; A3KPF5; -.
DR ProteomicsDB; 236378; -.
DR EnsemblPlants; AT1G52260.1; AT1G52260.1; AT1G52260.
DR GeneID; 841656; -.
DR Gramene; AT1G52260.1; AT1G52260.1; AT1G52260.
DR KEGG; ath:AT1G52260; -.
DR Araport; AT1G52260; -.
DR TAIR; locus:2018134; AT1G52260.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_7_0_1; -.
DR InParanoid; A3KPF5; -.
DR OMA; FTPWCIN; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; A3KPF5; -.
DR PRO; PR:A3KPF5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A3KPF5; baseline and differential.
DR Genevisible; A3KPF5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..537
FT /note="Protein disulfide isomerase-like 1-5"
FT /id="PRO_0000400020"
FT DOMAIN 58..184
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 380..526
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 534..537
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 447
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 450
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 447..450
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 537 AA; 60158 MW; 6380842BE6CFB1C4 CRC64;
MSLIPKPISK VSTFTFILLI LLSFTIIIAY SSPDSNVESN EPGFDSDLDQ LLAVDEQLQE
DRPEQQSEAE TVSKAQRIVL ELNGDYTKRV IDGNEFVMVL GYAPWCARSA ELMPRFAEAA
TALKEIGSSV LMAKIDGDRY SKIASELEIK GFPTLLLFVN GTSLTYNGGS SAEDIVIWVQ
KKTGAPIITL NTVDEAPRFL DKYHTFVLGL FEKFEGSEHN EFVKAAKSDD EIQFIETRDS
DVAKLLFPDL KSNNVFIGLV KPEAERYTVY DGSYKMEKIL EFLGSNKFPL FTKLTETNTV
WVYSSPVKLQ VMLFSKADDF QKLAQPLEDI ARKFKSKLMF IYVDITNENL AMPFLILFGI
EAGNKTVVAA FDNNLNSKYL LESDPSPNSI EEFCSGLAHG TVSRYYRSEP VPDNENASIV
TVVGKTFDGL VLNSRENVLL EVHTPWCVNC EALSKQIEKL AKHFKGFENL VFARIDASAN
EHTKLQVDDK YPIILLYKSG EKEKPLKLST KLSAKDIAVF INEELLKPKN GSAKDEL
