MASCOT Search Results
Protein View: PDIA3_HUMAN
Protein disulfide-isomerase A3 OS=Homo sapiens GN=PDIA3 PE=1 SV=4
AC P30101; Q13453; Q14255; Q8IYF8; Q9UMU7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 4.
DT 09-DEC-2015, entry version 189.
DE RecName: Full=Protein disulfide-isomerase A3;
DE EC=5.3.4.1;
DE AltName: Full=58 kDa glucose-regulated protein;
DE AltName: Full=58 kDa microsomal protein;
DE Short=p58;
DE AltName: Full=Disulfide isomerase ER-60;
DE AltName: Full=Endoplasmic reticulum resident protein 57;
DE Short=ER protein 57;
DE Short=ERp57;
DE AltName: Full=Endoplasmic reticulum resident protein 60;
DE Short=ER protein 60;
DE Short=ERp60;
DE Flags: Precursor;
GN Name=PDIA3; Synonyms=ERP57, ERP60, GRP58;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7945384; DOI=10.1006/bbrc.1994.2469;
RA Hirano N., Shibasaki F., Katoh H., Sakai R., Tanaka T., Nishida J.,
RA Yazaki Y., Takenawa T., Hirai H.;
RT "Molecular cloning and characterization of a cDNA for bovine
RT phospholipase C-alpha: proposal of redesignation of phospholipase C-
RT alpha.";
RL Biochem. Biophys. Res. Commun. 204:375-382(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-36 AND 130-144, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=7487104; DOI=10.1006/abbi.1995.0060;
RA Bourdi M., Demady D., Martin J.L., Jabbour S.K., Martin B.M.,
RA George J.W., Pohl L.R.;
RT "cDNA cloning and baculovirus expression of the human liver
RT endoplasmic reticulum P58: characterization as a protein disulfide
RT isomerase isoform, but not as a protease or a carnitine
RT acyltransferase.";
RL Arch. Biochem. Biophys. 323:397-403(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8687406;
RA Koivunen P., Helaakoski T., Annunen P., Veijola J., Raeisaenen S.,
RA Pihlajaniemi T., Kivirikko K.I.;
RT "ERp60 does not substitute for protein disulphide isomerase as the
RT beta-subunit of prolyl 4-hydroxylase.";
RL Biochem. J. 316:599-605(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8624847; DOI=10.1016/1357-2725(95)00120-4;
RA Charnock-Jones D.S., Day K., Smith S.K.;
RT "Cloning, expression and genomic organization of human placental
RT protein disulfide isomerase (previously identified as phospholipase C
RT alpha).";
RL Int. J. Biochem. Cell Biol. 28:81-89(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9205111; DOI=10.1006/geno.1997.4750;
RA Koivunen P., Horelli-Kuitunen N., Helaakoski T., Karvonen P.,
RA Jaakkola M., Palotie A., Kivirikko K.I.;
RT "Structures of the human gene for the protein disulfide isomerase-
RT related polypeptide ERp60 and a processed gene and assignment of these
RT genes to 15q15 and 1q21.";
RL Genomics 42:397-404(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-34 AND 504-505, AND
RP MUTAGENESIS OF CYS-57; CYS-60; CYS-406 AND CYS-409.
RC TISSUE=Liver epithelium;
RX PubMed=9399589; DOI=10.1093/oxfordjournals.jbchem.a021830;
RA Urade R., Oda T., Ito H., Moriyama T., Utsumi S., Kito M.;
RT "Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-
RT Leu (QEDL) motifs of microsomal ER-60 protease.";
RL J. Biochem. 122:834-842(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, Lung, and Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 25-54; 62-75 AND 95-104.
RC TISSUE=Colon carcinoma;
RX PubMed=9150948; DOI=10.1002/elps.1150180344;
RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT "A two-dimensional gel database of human colon carcinoma proteins.";
RL Electrophoresis 18:605-613(1997).
RN [9]
RP PROTEIN SEQUENCE OF 25-38.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP PROTEIN SEQUENCE OF 25-33.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [11]
RP PROTEIN SEQUENCE OF 26-42.
RC TISSUE=Mammary carcinoma;
RX PubMed=9150946; DOI=10.1002/elps.1150180342;
RA Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E.,
RA Simpson R.J., Dorow D.S.;
RT "Two-dimensional electrophoretic analysis of human breast carcinoma
RT proteins: mapping of proteins that bind to the SH3 domain of mixed
RT lineage kinase MLK2.";
RL Electrophoresis 18:588-598(1997).
RN [12]
RP PROTEIN SEQUENCE OF 63-73; 95-104; 108-129; 131-140; 259-271; 297-304;
RP 306-329; 336-344; 352-362; 367-397; 434-460 AND 472-482, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [13]
RP PROTEIN SEQUENCE OF 95-104 AND 472-479.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [14]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line
RT protein expression map database.";
RL Proteomics 2:212-223(2002).
RN [15]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [16]
RP INTERACTION WITH ERP27.
RX PubMed=16940051; DOI=10.1074/jbc.M604314200;
RA Alanen H.I., Williamson R.A., Howard M.J., Hatahet F.S., Salo K.E.H.,
RA Kauppila A., Kellokumpu S., Ruddock L.W.;
RT "ERp27, a new non-catalytic endoplasmic reticulum-located human
RT protein disulfide isomerase family member, interacts with ERp57.";
RL J. Biol. Chem. 281:33727-33738(2006).
RN [17]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP TISSUE SPECIFICITY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B.,
RA Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection
RT antigen (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
RA Fischer-Posovszky P., Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion
RT profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [22]
RP INTERACTION WITH SERPINA1 AND SERPINA2, AND SUBCELLULAR LOCATION.
RX PubMed=23826168; DOI=10.1371/journal.pone.0066889;
RA Marques P.I., Ferreira Z., Martins M., Figueiredo J., Silva D.I.,
RA Castro P., Morales-Hojas R., Simoes-Correia J., Seixas S.;
RT "SERPINA2 is a novel gene with a divergent function from SERPINA1.";
RL PLoS ONE 8:E66889-E66889(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-319, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-24, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [25]
RP STRUCTURE BY NMR OF 25-137.
RX PubMed=16258833; DOI=10.1007/s10858-005-2720-1;
RA Silvennoinen L., Koivunen P., Myllyharju J., Kilpelaeinen I.,
RA Permi P.;
RT "NMR assignment of the N-terminal domain a of the glycoprotein
RT chaperone ERp57.";
RL J. Biomol. NMR 33:136-136(2005).
RN [26]
RP STRUCTURE BY NMR OF 357-485.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the second thioredoxin domain of human
RT protein disulfide-isomerase A3.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-376, AND INTERACTION WITH
RP CANX.
RX PubMed=16905107; DOI=10.1016/j.str.2006.06.019;
RA Kozlov G., Maattanen P., Schrag J.D., Pollock S., Cygler M., Nagar B.,
RA Thomas D.Y., Gehring K.;
RT "Crystal structure of the bb' domains of the protein disulfide
RT isomerase ERp57.";
RL Structure 14:1331-1339(2006).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-505 IN COMPLEX WITH TAPBP,
RP SUBUNIT, INTERACTION WITH TAPBP, AND DISULFIDE BONDS.
RX PubMed=19119025; DOI=10.1016/j.immuni.2008.10.018;
RA Dong G., Wearsch P.A., Peaper D.R., Cresswell P., Reinisch K.M.;
RT "Insights into MHC class I peptide loading from the structure of the
RT tapasin-ERp57 thiol oxidoreductase heterodimer.";
RL Immunity 30:21-32(2009).
CC -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC proteins. {ECO:0000269|PubMed:7487104}.
CC -!- SUBUNIT: Subunit of the TAP complex, also known as the peptide
CC loading complex (PLC). Can form disulfide-linked heterodimers with
CC TAPBP. Interacts with ERP27 and CANX. Interacts with SERPINA2 and
CC with the S and Z variants of SERPINA1.
CC {ECO:0000269|PubMed:16905107, ECO:0000269|PubMed:16940051,
CC ECO:0000269|PubMed:19119025, ECO:0000269|PubMed:23826168}.
CC -!- INTERACTION:
CC P05067:APP; NbExp=3; IntAct=EBI-979862, EBI-77613;
CC P18418:Calr (xeno); NbExp=2; IntAct=EBI-979862, EBI-916742;
CC P10909:CLU; NbExp=2; IntAct=EBI-979862, EBI-1104674;
CC Q96HE7:ERO1L; NbExp=3; IntAct=EBI-979862, EBI-2564539;
CC Q86YB8:ERO1LB; NbExp=2; IntAct=EBI-979862, EBI-2806988;
CC Q13162:PRDX4; NbExp=2; IntAct=EBI-979862, EBI-2211957;
CC Q13586:STIM1; NbExp=3; IntAct=EBI-979862, EBI-448878;
CC Q03518:TAP1; NbExp=4; IntAct=EBI-979862, EBI-747259;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Endoplasmic reticulum
CC lumen {ECO:0000250}. Melanosome. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- TISSUE SPECIFICITY: Detected in the flagellum and head region of
CC spermatozoa (at protein level). {ECO:0000269|PubMed:20400973}.
CC -!- MASS SPECTROMETRY: Mass=54265.22; Method=MALDI; Range=25-505;
CC Evidence={ECO:0000269|PubMed:11840567};
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SIMILARITY: Contains 2 thioredoxin domains. {ECO:0000255|PROSITE-
CC ProRule:PRU00691}.
CC -!- CAUTION: Was originally thought to be a phosphatidylinositol 4,5-
CC bisphosphate phosphodiesterase type I (phospholipase C-alpha).
CC {ECO:0000305}.
DR EMBL; D16234; BAA03759.1; -; mRNA.
DR EMBL; U42068; AAC50331.1; -; mRNA.
DR EMBL; Z49835; CAA89996.1; -; mRNA.
DR EMBL; U75885; AAC51518.1; -; Genomic_DNA.
DR EMBL; U75875; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; U75876; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; U75877; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; U75878; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; U75879; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; U75880; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; U75881; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; U75882; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; U75883; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; U75884; AAC51518.1; JOINED; Genomic_DNA.
DR EMBL; D83485; BAA11928.1; -; mRNA.
DR EMBL; BC014433; AAH14433.1; -; mRNA.
DR EMBL; BC036000; AAH36000.4; -; mRNA.
DR EMBL; BC071878; AAH71878.1; -; mRNA.
DR CCDS; CCDS10101.1; -.
DR PIR; JC5704; JC5704.
DR PIR; S55507; S55507.
DR PIR; S63994; S63994.
DR PIR; S68363; S68363.
DR RefSeq; NP_005304.3; NM_005313.4.
DR UniGene; Hs.591095; -.
DR PDB; 2ALB; NMR; -; A=25-137.
DR PDB; 2DMM; NMR; -; A=357-485.
DR PDB; 2H8L; X-ray; 2.00 A; A/B/C=134-376.
DR PDB; 3F8U; X-ray; 2.60 A; A/C=25-505.
DR PDBsum; 2ALB; -.
DR PDBsum; 2DMM; -.
DR PDBsum; 2H8L; -.
DR PDBsum; 3F8U; -.
DR ProteinModelPortal; P30101; -.
DR SMR; P30101; 25-493.
DR BioGrid; 109180; 106.
DR DIP; DIP-29132N; -.
DR IntAct; P30101; 61.
DR MINT; MINT-5000005; -.
DR STRING; 9606.ENSP00000300289; -.
DR PhosphoSite; P30101; -.
DR BioMuta; PDIA3; -.
DR DMDM; 2507461; -.
DR DOSAC-COBS-2DPAGE; P30101; -.
DR REPRODUCTION-2DPAGE; P30101; -.
DR SWISS-2DPAGE; P30101; -.
DR UCD-2DPAGE; P30101; -.
DR PaxDb; P30101; -.
DR PRIDE; P30101; -.
DR DNASU; 2923; -.
DR Ensembl; ENST00000300289; ENSP00000300289; ENSG00000167004.
DR GeneID; 2923; -.
DR KEGG; hsa:2923; -.
DR UCSC; uc001zsu.3; human.
DR CTD; 2923; -.
DR GeneCards; PDIA3; -.
DR HGNC; HGNC:4606; PDIA3.
DR HPA; CAB011199; -.
DR HPA; CAB015181; -.
DR HPA; HPA002645; -.
DR HPA; HPA003230; -.
DR MIM; 602046; gene.
DR neXtProt; NX_P30101; -.
DR PharmGKB; PA29000; -.
DR eggNOG; KOG0190; Eukaryota.
DR eggNOG; COG0526; LUCA.
DR HOGENOM; HOG000162459; -.
DR HOVERGEN; HBG005920; -.
DR InParanoid; P30101; -.
DR KO; K08056; -.
DR OMA; QINFAIA; -.
DR OrthoDB; EOG7VHSX1; -.
DR PhylomeDB; P30101; -.
DR TreeFam; TF106382; -.
DR BRENDA; 5.3.4.1; 2681.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-901042; Calnexin/calreticulin cycle.
DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR ChiTaRS; PDIA3; human.
DR EvolutionaryTrace; P30101; -.
DR GenomeRNAi; 2923; -.
DR NextBio; 11593; -.
DR PRO; PR:P30101; -.
DR Proteomes; UP000005640; Chromosome 15.
DR Bgee; P30101; -.
DR CleanEx; HS_PDIA3; -.
DR ExpressionAtlas; P30101; baseline and differential.
DR Genevisible; P30101; HS.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; TAS:ParkinsonsUK-UCL.
DR GO; GO:0004629; F:phospholipase C activity; TAS:ProtInc.
DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; TAS:ProtInc.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0055114; P:oxidation-reduction process; TAS:GOC.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL.
DR GO; GO:0006606; P:protein import into nucleus; TAS:ProtInc.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR GO; GO:0006621; P:protein retention in ER lumen; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; TAS:GOC.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.40.30.10; -; 3.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Isomerase; Phosphoprotein; Polymorphism; Redox-active center;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1 24 {ECO:0000244|PubMed:25944712,
FT ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:1286669,
FT ECO:0000269|PubMed:7487104,
FT ECO:0000269|PubMed:9150948,
FT ECO:0000269|PubMed:9399589}.
FT CHAIN 25 505 Protein disulfide-isomerase A3.
FT /FTId=PRO_0000034225.
FT DOMAIN 25 133 Thioredoxin 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00691}.
FT DOMAIN 343 485 Thioredoxin 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00691}.
FT MOTIF 502 505 Prevents secretion from ER.
FT {ECO:0000250}.
FT ACT_SITE 57 57 Nucleophile. {ECO:0000250}.
FT ACT_SITE 60 60 Nucleophile. {ECO:0000250}.
FT ACT_SITE 406 406 Nucleophile. {ECO:0000250}.
FT ACT_SITE 409 409 Nucleophile. {ECO:0000250}.
FT SITE 58 58 Contributes to redox potential value.
FT {ECO:0000250}.
FT SITE 59 59 Contributes to redox potential value.
FT {ECO:0000250}.
FT SITE 119 119 Lowers pKa of C-terminal Cys of first
FT active site. {ECO:0000250}.
FT SITE 407 407 Contributes to redox potential value.
FT {ECO:0000250}.
FT SITE 408 408 Contributes to redox potential value.
FT {ECO:0000250}.
FT SITE 471 471 Lowers pKa of C-terminal Cys of second
FT active site. {ECO:0000250}.
FT MOD_RES 129 129 N6-succinyllysine.
FT {ECO:0000250|UniProtKB:P27773}.
FT MOD_RES 152 152 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P27773}.
FT MOD_RES 218 218 N6-succinyllysine.
FT {ECO:0000250|UniProtKB:P27773}.
FT MOD_RES 252 252 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P27773}.
FT MOD_RES 319 319 Phosphothreonine.
FT {ECO:0000244|PubMed:24275569}.
FT MOD_RES 362 362 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P27773}.
FT MOD_RES 494 494 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P27773}.
FT DISULFID 57 60 Redox-active. {ECO:0000255|PROSITE-
FT ProRule:PRU00691}.
FT DISULFID 57 57 Interchain (with C-115 in TAPBP); in
FT linked form.
FT {ECO:0000269|PubMed:19119025}.
FT DISULFID 85 92 {ECO:0000269|PubMed:19119025}.
FT DISULFID 406 409 Redox-active. {ECO:0000255|PROSITE-
FT ProRule:PRU00691}.
FT VARIANT 415 415 K -> R (in dbSNP:rs6413485).
FT /FTId=VAR_020027.
FT MUTAGEN 57 57 C->A: No loss of activity. No loss of
FT activity; when associated with A-406.
FT {ECO:0000269|PubMed:9399589}.
FT MUTAGEN 57 57 C->S: Activity changed to serine
FT protease. {ECO:0000269|PubMed:9399589}.
FT MUTAGEN 60 60 C->S: Activity changed to serine
FT protease; when associated with S-409.
FT {ECO:0000269|PubMed:9399589}.
FT MUTAGEN 406 406 C->A: No loss of activity. No loss of
FT activity; when associated with A-57.
FT {ECO:0000269|PubMed:9399589}.
FT MUTAGEN 406 406 C->S: Activity changed to serine
FT protease. {ECO:0000269|PubMed:9399589}.
FT MUTAGEN 409 409 C->S: Activity changed to serine
FT protease; when associated with S-60.
FT {ECO:0000269|PubMed:9399589}.
FT CONFLICT 19 19 A -> G (in Ref. 6; BAA11928).
FT {ECO:0000305}.
FT CONFLICT 22 22 A -> V (in Ref. 6; BAA11928).
FT {ECO:0000305}.
FT CONFLICT 217 217 D -> Y (in Ref. 1; BAA03759).
FT {ECO:0000305}.
FT CONFLICT 225 225 Q -> P (in Ref. 4; CAA89996).
FT {ECO:0000305}.
FT CONFLICT 238 238 E -> G (in Ref. 4; CAA89996).
FT {ECO:0000305}.
FT CONFLICT 272 272 N -> D (in Ref. 1; BAA03759 and 5;
FT AAC51518). {ECO:0000305}.
FT CONFLICT 355 355 D -> G (in Ref. 1; BAA03759).
FT {ECO:0000305}.
FT CONFLICT 358 358 D -> G (in Ref. 1; BAA03759).
FT {ECO:0000305}.
FT CONFLICT 368 368 E -> D (in Ref. 1; BAA03759).
FT {ECO:0000305}.
FT STRAND 27 29 {ECO:0000244|PDB:2ALB}.
FT TURN 32 34 {ECO:0000244|PDB:3F8U}.
FT HELIX 35 38 {ECO:0000244|PDB:3F8U}.
FT HELIX 39 41 {ECO:0000244|PDB:2ALB}.
FT STRAND 43 53 {ECO:0000244|PDB:3F8U}.
FT HELIX 58 73 {ECO:0000244|PDB:3F8U}.
FT TURN 74 77 {ECO:0000244|PDB:3F8U}.
FT STRAND 80 84 {ECO:0000244|PDB:3F8U}.
FT TURN 85 87 {ECO:0000244|PDB:3F8U}.
FT HELIX 89 94 {ECO:0000244|PDB:3F8U}.
FT STRAND 99 107 {ECO:0000244|PDB:3F8U}.
FT STRAND 110 114 {ECO:0000244|PDB:3F8U}.
FT HELIX 121 131 {ECO:0000244|PDB:3F8U}.
FT STRAND 136 138 {ECO:0000244|PDB:2H8L}.
FT HELIX 142 149 {ECO:0000244|PDB:2H8L}.
FT STRAND 151 153 {ECO:0000244|PDB:2H8L}.
FT STRAND 155 161 {ECO:0000244|PDB:2H8L}.
FT HELIX 166 177 {ECO:0000244|PDB:2H8L}.
FT TURN 178 181 {ECO:0000244|PDB:2H8L}.
FT STRAND 182 187 {ECO:0000244|PDB:2H8L}.
FT HELIX 190 196 {ECO:0000244|PDB:2H8L}.
FT STRAND 198 206 {ECO:0000244|PDB:2H8L}.
FT HELIX 209 211 {ECO:0000244|PDB:2H8L}.
FT STRAND 218 221 {ECO:0000244|PDB:2H8L}.
FT HELIX 229 239 {ECO:0000244|PDB:2H8L}.
FT TURN 240 243 {ECO:0000244|PDB:3F8U}.
FT TURN 249 251 {ECO:0000244|PDB:2H8L}.
FT HELIX 252 255 {ECO:0000244|PDB:2H8L}.
FT STRAND 256 265 {ECO:0000244|PDB:2H8L}.
FT TURN 269 271 {ECO:0000244|PDB:2H8L}.
FT HELIX 273 292 {ECO:0000244|PDB:2H8L}.
FT STRAND 298 303 {ECO:0000244|PDB:2H8L}.
FT TURN 304 307 {ECO:0000244|PDB:2H8L}.
FT HELIX 308 311 {ECO:0000244|PDB:2H8L}.
FT HELIX 312 314 {ECO:0000244|PDB:2H8L}.
FT STRAND 325 329 {ECO:0000244|PDB:2H8L}.
FT STRAND 331 333 {ECO:0000244|PDB:3F8U}.
FT STRAND 335 337 {ECO:0000244|PDB:2H8L}.
FT HELIX 347 358 {ECO:0000244|PDB:2H8L}.
FT STRAND 376 381 {ECO:0000244|PDB:3F8U}.
FT TURN 383 385 {ECO:0000244|PDB:3F8U}.
FT HELIX 386 390 {ECO:0000244|PDB:3F8U}.
FT STRAND 396 402 {ECO:0000244|PDB:3F8U}.
FT HELIX 407 422 {ECO:0000244|PDB:3F8U}.
FT TURN 423 425 {ECO:0000244|PDB:3F8U}.
FT STRAND 427 435 {ECO:0000244|PDB:3F8U}.
FT TURN 436 438 {ECO:0000244|PDB:2DMM}.
FT STRAND 449 456 {ECO:0000244|PDB:3F8U}.
FT HELIX 473 483 {ECO:0000244|PDB:3F8U}.
SQ SEQUENCE 505 AA; 56782 MW; 529E5B6692D0D7E9 CRC64;
MRLRRLALFP GVALLLAAAR LAAASDVLEL TDDNFESRIS DTGSAGLMLV EFFAPWCGHC
KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT
ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASIVGFF DDSFSEAHSE FLKAASNLRD
NYRFAHTNVE SLVNEYDDNG EGIILFRPSH LTNKFEDKTV AYTEQKMTSG KIKKFIQENI
FGICPHMTED NKDLIQGKDL LIAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA
VASRKTFSHE LSDFGLESTA GEIPVVAIRT AKGEKFVMQE EFSRDGKALE RFLQDYFDGN
LKRYLKSEPI PESNDGPVKV VVAENFDEIV NNENKDVLIE FYAPWCGHCK NLEPKYKELG
EKLSKDPNIV IAKMDATAND VPSPYEVRGF PTIYFSPANK KLNPKKYEGG RELSDFISYL
QREATNPPVI QEEKPKKKKK AQEDL