PDI12_ARATH
ID PDI12_ARATH Reviewed; 508 AA.
AC Q9SRG3; Q0WV97;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Protein disulfide isomerase-like 1-2;
DE Short=AtPDIL1-2;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide-isomerase 2;
DE Short=PDI 2;
DE AltName: Full=Protein disulfide-isomerase 6;
DE Short=AtPDI6;
DE Flags: Precursor;
GN Name=PDIL1-2; Synonyms=PDI6; OrderedLocusNames=At1g77510;
GN ORFNames=T5M16.10;
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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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, 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 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 -!- INDUCTION: By chemically-induced ER stress response.
CC {ECO:0000269|PubMed:18574595}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AC010704; AAG51673.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35987.1; -; Genomic_DNA.
DR EMBL; AK226862; BAE98951.1; -; mRNA.
DR PIR; E96804; E96804.
DR RefSeq; NP_177875.1; NM_106400.3.
DR AlphaFoldDB; Q9SRG3; -.
DR SMR; Q9SRG3; -.
DR BioGRID; 29306; 8.
DR STRING; 3702.AT1G77510.1; -.
DR iPTMnet; Q9SRG3; -.
DR PaxDb; Q9SRG3; -.
DR PRIDE; Q9SRG3; -.
DR ProteomicsDB; 236377; -.
DR EnsemblPlants; AT1G77510.1; AT1G77510.1; AT1G77510.
DR GeneID; 844087; -.
DR Gramene; AT1G77510.1; AT1G77510.1; AT1G77510.
DR KEGG; ath:AT1G77510; -.
DR Araport; AT1G77510; -.
DR TAIR; locus:2204670; AT1G77510.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_6_1_1; -.
DR InParanoid; Q9SRG3; -.
DR OMA; ISQPNWT; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q9SRG3; -.
DR PRO; PR:Q9SRG3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRG3; baseline and differential.
DR Genevisible; Q9SRG3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:TAIR.
DR GO; GO:0010205; P:photoinhibition; IMP:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:TAIR.
DR GO; GO:0009644; P:response to high light intensity; IEP:TAIR.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..508
FT /note="Protein disulfide isomerase-like 1-2"
FT /id="PRO_0000034206"
FT DOMAIN 25..140
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 336..480
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 474..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 505..508
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 61
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 402
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 126
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 403
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 404
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 466
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..61
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 402..405
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 508 AA; 56365 MW; B6300A31DFD2AB62 CRC64;
MAFKGFACFS ILLLLSLFVS SIRSEETKEF VLTLDHSNFT ETISKHDFIV VEFYAPWCGH
CQKLAPEYEK AASELSSHNP PLALAKIDAS EEANKEFANE YKIQGFPTLK ILRNGGKSVQ
DYNGPREAEG IVTYLKKQSG PASVEIKSAD SATEVVGEKN VVAVGVFPKL SGDEFDSFMA
LAEKLRADYD FAHTLDAKFL PRGESVEGPA VRLFKPFDEL FVDSKDFNGE ALEKFVKESS
IPLVTVFDSD PNNHPYVAKF FESPATKAMM FVNFTGATAE ALKSKYREVA TSNKDQSLAF
LVGDAESSQG AFQYFGLEES QVPLIIIQTP DNKKYLKVNV EVDQIESWFK DFQDGKVAVH
KKSQPIPAEN NEPVKVVVAE SLDDIVFKSG KNVLIEFYAP WCGHCQKLAP ILDEVALSFQ
NDPSVIIAKL DATANDIPSD TFDVKGFPTI YFRSASGNVV VYEGDRTKED FINFVEKNSE
KKPTSHGEES TKSEEPKKTE ETAAKDEL
