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   27-MAR-2024, entry version 171.
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.Q9SRG3; -.
DR   GlyCosmos; Q9SRG3; 2 sites, No reported glycans.
DR   iPTMnet; Q9SRG3; -.
DR   PaxDb; 3702-AT1G77510-1; -.
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; AT1G77510; PDIL1-2.
DR   eggNOG; KOG0190; Eukaryota.
DR   HOGENOM; CLU_025879_6_1_1; -.
DR   InParanoid; Q9SRG3; -.
DR   OMA; HEAANQY; -.
DR   OrthoDB; 314307at2759; -.
DR   PhylomeDB; Q9SRG3; -.
DR   PRO; PR:Q9SRG3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SRG3; baseline and differential.
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:0034976; P:response to endoplasmic reticulum stress; IEP:TAIR.
DR   GO; GO:0009644; P:response to high light intensity; IEP:TAIR.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR   NCBIfam; TIGR01126; pdi_dom; 2.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF253; PROTEIN DISULFIDE ISOMERASE-LIKE 1-2; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
DR   Genevisible; Q9SRG3; AT.
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
//