PDI22_ARATH
ID PDI22_ARATH Reviewed; 447 AA.
AC Q9MAU6;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein disulfide-isomerase like 2-2;
DE Short=AtPDIL2-2;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide-isomerase 10;
DE Short=PDI10;
DE AltName: Full=Protein disulfide-isomerase like 5-1;
DE Short=AtPDIL5-1;
DE Flags: Precursor;
GN Name=PDIL2-2; Synonyms=PDI10, PDIL5-1; OrderedLocusNames=At1g04980;
GN ORFNames=F13M7.3;
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] OF 5-447.
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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF40463.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC004809; AAF40463.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE27773.1; -; Genomic_DNA.
DR EMBL; AY099813; AAM20664.1; -; mRNA.
DR PIR; D86183; D86183.
DR RefSeq; NP_171990.3; NM_100376.5.
DR AlphaFoldDB; Q9MAU6; -.
DR SMR; Q9MAU6; -.
DR STRING; 3702.AT1G04980.1; -.
DR PaxDb; Q9MAU6; -.
DR PRIDE; Q9MAU6; -.
DR ProteomicsDB; 236330; -.
DR EnsemblPlants; AT1G04980.1; AT1G04980.1; AT1G04980.
DR GeneID; 839355; -.
DR Gramene; AT1G04980.1; AT1G04980.1; AT1G04980.
DR KEGG; ath:AT1G04980; -.
DR Araport; AT1G04980; -.
DR TAIR; locus:2010577; AT1G04980.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_030311_1_0_1; -.
DR InParanoid; Q9MAU6; -.
DR OMA; DDIWLVE; -.
DR OrthoDB; 840943at2759; -.
DR PhylomeDB; Q9MAU6; -.
DR PRO; PR:Q9MAU6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAU6; baseline and differential.
DR Genevisible; Q9MAU6; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:TAIR.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:TAIR.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR044569; PDIA6-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45815; PTHR45815; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 3.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..447
FT /note="Protein disulfide-isomerase like 2-2"
FT /id="PRO_0000400022"
FT DOMAIN 27..139
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 161..275
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 146..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 444..447
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 65
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 200
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 63
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 64
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 124
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 198
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 199
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 260
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..65
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 197..200
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 447 AA; 48403 MW; 9B942A605CB863BF CRC64;
MERKMYKSTV FPICCLLFAL FDRGNALYGS SSPVLQLTPS NFKSKVLNSN GVVLVEFFAP
WCGHCQSLTP TWEKVASTLK GIATVAAIDA DAHKSVSQDY GVRGFPTIKV FVPGKPPIDY
QGARDAKSIS QFAIKQIKAL LKDRLDGKTS GTKNGGGSSE KKKSEPSASV ELNSSNFDEL
VTESKELWIV EFFAPWCGHC KKLAPEWKKA ANNLKGKVKL GHVNCDAEQS IKSRFKVQGF
PTILVFGSDK SSPVPYEGAR SASAIESFAL EQLESNAGPA EVTELTGPDV MEDKCGSAAI
CFVSFLPDIL DSKAEGRNKY LEMLLSVADK FKKDPYGFVW VAAGKQPDLE KRVGVGGYGY
PAMVALNAKK GAYAPLKSGF EVKHLKDFVK EAAKGGKGNL PIDGTMEIVK TEAWDGKDGE
VVDADEFSLE DLMGNDDEAS TESKDDL
