PDIA1_MOUSE
ID PDIA1_MOUSE Reviewed; 509 AA.
AC P09103; Q922C8;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Protein disulfide-isomerase;
DE Short=PDI;
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:P07237};
DE AltName: Full=Cellular thyroid hormone-binding protein;
DE AltName: Full=Endoplasmic reticulum resident protein 59;
DE Short=ER protein 59;
DE Short=ERp59;
DE AltName: Full=Prolyl 4-hydroxylase subunit beta;
DE AltName: Full=p55;
DE Flags: Precursor;
GN Name=P4hb; Synonyms=Pdia1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2830592; DOI=10.1093/nar/16.3.1203;
RA Gong Q.-H., Fukuda T., Parkison C., Cheng S.-Y.;
RT "Nucleotide sequence of a full-length cDNA clone encoding a mouse cellular
RT thyroid hormone binding protein (p55) that is homologous to protein
RT disulfide isomerase and the beta-subunit of prolyl-4-hydroxylase.";
RL Nucleic Acids Res. 16:1203-1203(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2295602; DOI=10.1016/s0021-9258(19)40163-4;
RA Mazzarella R.A., Srinivasan M., Haugejorden S.M., Green M.;
RT "ERp72, an abundant luminal endoplasmic reticulum protein, contains three
RT copies of the active site sequences of protein disulfide isomerase.";
RL J. Biol. Chem. 265:1094-1101(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Bone marrow, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Liver, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH P4HA2.
RX PubMed=7753822; DOI=10.1073/pnas.92.10.4427;
RA Helaakoski T., Annunen P., Vuori K., Macneil I.A., Pihlajaniemi T.,
RA Kivirikko K.I.;
RT "Cloning, baculovirus expression, and characterization of a second mouse
RT prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2
RT tetramer with the protein disulfide-isomerase/beta subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4427-4431(1995).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION AS RECEPTOR FOR LGALS9, AND SUBCELLULAR LOCATION.
RX PubMed=21670307; DOI=10.1073/pnas.1017954108;
RA Bi S., Hong P.W., Lee B., Baum L.G.;
RT "Galectin-9 binding to cell surface protein disulfide isomerase regulates
RT the redox environment to enhance T-cell migration and HIV entry.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10650-10655(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-224 AND LYS-273, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=29858230; DOI=10.15252/embj.201798699;
RA Zhang J., Zhu Q., Wang X., Yu J., Chen X., Wang J., Wang X., Xiao J.,
RA Wang C.C., Wang L.;
RT "Secretory kinase Fam20C tunes endoplasmic reticulum redox state via
RT phosphorylation of Ero1alpha.";
RL EMBO J. 37:0-0(2018).
RN [11]
RP MUTAGENESIS OF SER-359.
RX PubMed=32149426; DOI=10.15252/embj.2019103841;
RA Yu J., Li T., Liu Y., Wang X., Zhang J., Wang X., Shi G., Lou J., Wang L.,
RA Wang C.C., Wang L.;
RT "Phosphorylation switches protein disulfide isomerase activity to maintain
RT proteostasis and attenuate ER stress.";
RL EMBO J. 39:e103841-e103841(2020).
RN [12]
RP INTERACTION WITH ILDR2.
RX PubMed=33863978; DOI=10.1038/s41598-021-87884-7;
RA Watanabe K., Nakayama K., Ohta S., Matsumoto A., Tsuda H., Iwamoto S.;
RT "ILDR2 stabilization is regulated by its interaction with GRP78.";
RL Sci. Rep. 11:8414-8414(2021).
CC -!- FUNCTION: This multifunctional protein catalyzes the formation,
CC breakage and rearrangement of disulfide bonds. At the cell surface,
CC seems to act as a reductase that cleaves disulfide bonds of proteins
CC attached to the cell. May therefore cause structural modifications of
CC exofacial proteins. Inside the cell, seems to form/rearrange disulfide
CC bonds of nascent proteins. At high concentrations and following
CC phosphorylation by FAM20C, functions as a chaperone that inhibits
CC aggregation of misfolded proteins. At low concentrations, facilitates
CC aggregation (anti-chaperone activity). May be involved with other
CC chaperones in the structural modification of the TG precursor in
CC hormone biogenesis. Also acts as a structural subunit of various
CC enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol
CC transfer protein MTTP (By similarity). Receptor for LGALS9; the
CC interaction retains P4HB at the cell surface of Th2 T helper cells,
CC increasing disulfide reductase activity at the plasma membrane,
CC altering the plasma membrane redox state and enhancing cell migration
CC (PubMed:21670307). {ECO:0000250|UniProtKB:P07237,
CC ECO:0000269|PubMed:21670307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P07237};
CC -!- SUBUNIT: Heterodimer; heterodimerizes with the protein microsomal
CC triglyceride transfer MTTP. Homodimer. Monomers and homotetramers may
CC also occur. Interacts with P4HA2, forming a heterotetramer consisting
CC of 2 alpha subunits (P4HA2) and 2 beta (P4HB), where P4HB plays the
CC role of a structural subunit; this tetramer catalyzes the formation of
CC 4-hydroxyproline in collagen (PubMed:7753822). Also constitutes the
CC structural subunit of the microsomal triacylglycerol transfer protein
CC MTTP in mammalian cells. Stabilizes both enzymes and retain them in the
CC ER without contributing to the catalytic activity. Binds UBQLN1.
CC Interacts with ERO1B (By similarity). Interacts with ILDR2
CC (PubMed:33863978). Interacts with ERN1/IRE1A (via N-terminus); the
CC interaction is enhanced by phosphorylation of P4HB by FAM20C in
CC response to endoplasmic reticulum stress and results in attenuation of
CC ERN1 activity (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P07237, ECO:0000269|PubMed:33863978,
CC ECO:0000269|PubMed:7753822}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P07237}. Melanosome
CC {ECO:0000250|UniProtKB:P07237}. Cell membrane
CC {ECO:0000269|PubMed:21670307}; Peripheral membrane protein
CC {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be
CC also secreted or associated with the plasma membrane, where it
CC undergoes constant shedding and replacement from intracellular sources.
CC Localizes near CD4-enriched regions on lymphoid cell surfaces.
CC Colocalizes with MTTP in the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P07237}.
CC -!- TISSUE SPECIFICITY: In the mammary gland, expressed at higher levels in
CC lactating mice than in virgin mice. {ECO:0000269|PubMed:29858230}.
CC -!- PTM: Phosphorylation of Ser-359 by FAM20C is induced by endoplasmic
CC reticulum stress and results in a functional switch from oxidoreductase
CC to molecular chaperone. It also promotes interaction with ERN1.
CC {ECO:0000250|UniProtKB:P07237}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06453; CAA29759.1; -; mRNA.
DR EMBL; J05185; AAA39906.1; -; mRNA.
DR EMBL; AK150002; BAE29230.1; -; mRNA.
DR EMBL; AK150422; BAE29545.1; -; mRNA.
DR EMBL; AK150805; BAE29868.1; -; mRNA.
DR EMBL; AK152141; BAE30979.1; -; mRNA.
DR EMBL; AK152217; BAE31045.1; -; mRNA.
DR EMBL; AK159606; BAE35225.1; -; mRNA.
DR EMBL; AK159965; BAE35520.1; -; mRNA.
DR EMBL; AK168330; BAE40268.1; -; mRNA.
DR EMBL; AK168893; BAE40710.1; -; mRNA.
DR EMBL; AK170603; BAE41907.1; -; mRNA.
DR EMBL; AL663030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008549; AAH08549.1; -; mRNA.
DR EMBL; BC093512; AAH93512.1; -; mRNA.
DR CCDS; CCDS25742.1; -.
DR PIR; A34930; ISMSSS.
DR RefSeq; NP_035162.1; NM_011032.2.
DR AlphaFoldDB; P09103; -.
DR SMR; P09103; -.
DR BioGRID; 202008; 26.
DR CORUM; P09103; -.
DR ELM; P09103; -.
DR IntAct; P09103; 9.
DR MINT; P09103; -.
DR STRING; 10090.ENSMUSP00000026122; -.
DR iPTMnet; P09103; -.
DR PhosphoSitePlus; P09103; -.
DR SwissPalm; P09103; -.
DR COMPLUYEAST-2DPAGE; P09103; -.
DR REPRODUCTION-2DPAGE; P09103; -.
DR SWISS-2DPAGE; P09103; -.
DR CPTAC; non-CPTAC-3844; -.
DR EPD; P09103; -.
DR jPOST; P09103; -.
DR MaxQB; P09103; -.
DR PaxDb; P09103; -.
DR PeptideAtlas; P09103; -.
DR PRIDE; P09103; -.
DR ProteomicsDB; 288020; -.
DR Antibodypedia; 3250; 569 antibodies from 43 providers.
DR DNASU; 18453; -.
DR Ensembl; ENSMUST00000026122; ENSMUSP00000026122; ENSMUSG00000025130.
DR GeneID; 18453; -.
DR KEGG; mmu:18453; -.
DR UCSC; uc007mti.1; mouse.
DR CTD; 5034; -.
DR MGI; MGI:97464; P4hb.
DR VEuPathDB; HostDB:ENSMUSG00000025130; -.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00940000157351; -.
DR HOGENOM; CLU_025879_1_0_1; -.
DR InParanoid; P09103; -.
DR OMA; FCDRFLE; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; P09103; -.
DR TreeFam; TF106381; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-8866423; VLDL assembly.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-8963888; Chylomicron assembly.
DR Reactome; R-MMU-8964041; LDL remodeling.
DR Reactome; R-MMU-9020591; Interleukin-12 signaling.
DR Reactome; R-MMU-9020933; Interleukin-23 signaling.
DR BioGRID-ORCS; 18453; 2 hits in 76 CRISPR screens.
DR ChiTaRS; P4hb; mouse.
DR PRO; PR:P09103; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P09103; protein.
DR Bgee; ENSMUSG00000025130; Expressed in lacrimal gland and 253 other tissues.
DR ExpressionAtlas; P09103; baseline and differential.
DR Genevisible; P09103; MM.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016222; C:procollagen-proline 4-dioxygenase complex; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; ISO:MGI.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:MGI.
DR GO; GO:0016972; F:thiol oxidase activity; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISO:MGI.
DR GO; GO:1902175; P:regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Chaperone; Disulfide bond;
KW Endoplasmic reticulum; Isomerase; Membrane; Phosphoprotein;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..509
FT /note="Protein disulfide-isomerase"
FT /id="PRO_0000034196"
FT DOMAIN 20..136
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 348..477
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 506..509
FT /note="Prevents secretion from ER"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 399
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 402
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 56
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 57
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 122
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 400
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 401
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 463
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 224
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 273
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT DISULFID 55..58
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 399..402
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MUTAGEN 359
FT /note="S->A: Homozygotes are born at Mendelian ratios and
FT have no phenotypic abnormalities from birth to adulthood.
FT Increased ERN1 activity."
FT /evidence="ECO:0000269|PubMed:32149426"
FT CONFLICT 68
FT /note="A -> R (in Ref. 1; CAA29759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 57058 MW; 1FB0AA8ACCDB13EA CRC64;
MLSRALLCLA LAWAARVGAD ALEEEDNVLV LKKSNFEEAL AAHKYLLVEF YAPWCGHCKA
LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG YPTIKFFKNG DTASPKEYTA
GREADDIVNW LKKRTGPAAT TLSDTAAAES LVDSSEVTVI GFFKDVESDS AKQFLLAAEA
IDDIPFGITS NSGVFSKYQL DKDGVVLFKK FDEGRNNFEG EITKEKLLDF IKHNQLPLVI
EFTEQTAPKI FGGEIKTHIL LFLPKSVSDY DGKLSSFKRA AEGFKGKILF IFIDSDHTDN
QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE GKIKPHLMSQ
EVPEDWDKQP VKVLVGANFE EVAFDEKKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE
NIIIAKMDST ANEVEAVKVH SFPTLKFFPA SADRTVIDYN GERTLDGFKK FLESGGQDGA
GDDEDLDLEE ALEPDMEEDD DQKAVKDEL
