Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60)

 PDIA3_HUMAN             Reviewed;         505 AA.
P30101; Q13453; Q14255; Q8IYF8; Q9UMU7;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 4.
25-OCT-2017, entry version 209.
RecName: Full=Protein disulfide-isomerase A3;
EC=5.3.4.1;
AltName: Full=58 kDa glucose-regulated protein;
AltName: Full=58 kDa microsomal protein;
Short=p58;
AltName: Full=Disulfide isomerase ER-60;
AltName: Full=Endoplasmic reticulum resident protein 57;
Short=ER protein 57;
Short=ERp57;
AltName: Full=Endoplasmic reticulum resident protein 60;
Short=ER protein 60;
Short=ERp60;
Flags: Precursor;
Name=PDIA3; Synonyms=ERP57, ERP60, GRP58;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7945384; DOI=10.1006/bbrc.1994.2469;
Hirano N., Shibasaki F., Katoh H., Sakai R., Tanaka T., Nishida J.,
Yazaki Y., Takenawa T., Hirai H.;
"Molecular cloning and characterization of a cDNA for bovine
phospholipase C-alpha: proposal of redesignation of phospholipase C-
alpha.";
Biochem. Biophys. Res. Commun. 204:375-382(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-36 AND 130-144, AND
CATALYTIC ACTIVITY.
TISSUE=Liver;
PubMed=7487104; DOI=10.1006/abbi.1995.0060;
Bourdi M., Demady D., Martin J.L., Jabbour S.K., Martin B.M.,
George J.W., Pohl L.R.;
"cDNA cloning and baculovirus expression of the human liver
endoplasmic reticulum P58: characterization as a protein disulfide
isomerase isoform, but not as a protease or a carnitine
acyltransferase.";
Arch. Biochem. Biophys. 323:397-403(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=8687406; DOI=10.1042/bj3160599;
Koivunen P., Helaakoski T., Annunen P., Veijola J., Raeisaenen S.,
Pihlajaniemi T., Kivirikko K.I.;
"ERp60 does not substitute for protein disulphide isomerase as the
beta-subunit of prolyl 4-hydroxylase.";
Biochem. J. 316:599-605(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8624847; DOI=10.1016/1357-2725(95)00120-4;
Charnock-Jones D.S., Day K., Smith S.K.;
"Cloning, expression and genomic organization of human placental
protein disulfide isomerase (previously identified as phospholipase C
alpha).";
Int. J. Biochem. Cell Biol. 28:81-89(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9205111; DOI=10.1006/geno.1997.4750;
Koivunen P., Horelli-Kuitunen N., Helaakoski T., Karvonen P.,
Jaakkola M., Palotie A., Kivirikko K.I.;
"Structures of the human gene for the protein disulfide isomerase-
related polypeptide ERp60 and a processed gene and assignment of these
genes to 15q15 and 1q21.";
Genomics 42:397-404(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-34 AND 504-505, AND
MUTAGENESIS OF CYS-57; CYS-60; CYS-406 AND CYS-409.
TISSUE=Liver epithelium;
PubMed=9399589; DOI=10.1093/oxfordjournals.jbchem.a021830;
Urade R., Oda T., Ito H., Moriyama T., Utsumi S., Kito M.;
"Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-
Leu (QEDL) motifs of microsomal ER-60 protease.";
J. Biochem. 122:834-842(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, Lung, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 25-54; 62-75 AND 95-104.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[9]
PROTEIN SEQUENCE OF 25-38.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[10]
PROTEIN SEQUENCE OF 25-33.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[11]
PROTEIN SEQUENCE OF 26-42.
TISSUE=Mammary carcinoma;
PubMed=9150946; DOI=10.1002/elps.1150180342;
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E.,
Simpson R.J., Dorow D.S.;
"Two-dimensional electrophoretic analysis of human breast carcinoma
proteins: mapping of proteins that bind to the SH3 domain of mixed
lineage kinase MLK2.";
Electrophoresis 18:588-598(1997).
[12]
PROTEIN SEQUENCE OF 63-73; 95-104; 108-129; 131-140; 259-271; 297-304;
306-329; 336-344; 352-362; 367-397; 434-460 AND 472-482, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[13]
PROTEIN SEQUENCE OF 95-104 AND 472-479.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[14]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=11840567;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line
protein expression map database.";
Proteomics 2:212-223(2002).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[16]
INTERACTION WITH ERP27.
PubMed=16940051; DOI=10.1074/jbc.M604314200;
Alanen H.I., Williamson R.A., Howard M.J., Hatahet F.S., Salo K.E.H.,
Kauppila A., Kellokumpu S., Ruddock L.W.;
"ERp27, a new non-catalytic endoplasmic reticulum-located human
protein disulfide isomerase family member, interacts with ERp57.";
J. Biol. Chem. 281:33727-33738(2006).
[17]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
TISSUE SPECIFICITY.
PubMed=20400973; DOI=10.1038/aja.2010.19;
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B.,
Shivaji S.;
"Glucose-regulated protein precursor (GRP78) and tumor rejection
antigen (GP96) are unique to hamster caput epididymal spermatozoa.";
Asian J. Androl. 12:344-355(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[22]
INTERACTION WITH SERPINA1 AND SERPINA2, AND SUBCELLULAR LOCATION.
PubMed=23826168; DOI=10.1371/journal.pone.0066889;
Marques P.I., Ferreira Z., Martins M., Figueiredo J., Silva D.I.,
Castro P., Morales-Hojas R., Simoes-Correia J., Seixas S.;
"SERPINA2 is a novel gene with a divergent function from SERPINA1.";
PLoS ONE 8:E66889-E66889(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-319, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[25]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-24, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
STRUCTURE BY NMR OF 25-137.
PubMed=16258833; DOI=10.1007/s10858-005-2720-1;
Silvennoinen L., Koivunen P., Myllyharju J., Kilpelaeinen I.,
Permi P.;
"NMR assignment of the N-terminal domain a of the glycoprotein
chaperone ERp57.";
J. Biomol. NMR 33:136-136(2005).
[27]
STRUCTURE BY NMR OF 357-485.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the second thioredoxin domain of human
protein disulfide-isomerase A3.";
Submitted (OCT-2006) to the PDB data bank.
[28]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-376, AND INTERACTION WITH
CANX.
PubMed=16905107; DOI=10.1016/j.str.2006.06.019;
Kozlov G., Maattanen P., Schrag J.D., Pollock S., Cygler M., Nagar B.,
Thomas D.Y., Gehring K.;
"Crystal structure of the bb' domains of the protein disulfide
isomerase ERp57.";
Structure 14:1331-1339(2006).
[29]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-505 IN COMPLEX WITH TAPBP,
SUBUNIT, INTERACTION WITH TAPBP, AND DISULFIDE BONDS.
PubMed=19119025; DOI=10.1016/j.immuni.2008.10.018;
Dong G., Wearsch P.A., Peaper D.R., Cresswell P., Reinisch K.M.;
"Insights into MHC class I peptide loading from the structure of the
tapasin-ERp57 thiol oxidoreductase heterodimer.";
Immunity 30:21-32(2009).
-!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
proteins. {ECO:0000269|PubMed:7487104}.
-!- SUBUNIT: Subunit of the TAP complex, also known as the peptide
loading complex (PLC). Can form disulfide-linked heterodimers with
TAPBP. Interacts with ERP27 and CANX. Interacts with SERPINA2 and
with the S and Z variants of SERPINA1. Interacts with ATP2A2 (By
similarity). {ECO:0000250|UniProtKB:P27773,
ECO:0000269|PubMed:16905107, ECO:0000269|PubMed:16940051,
ECO:0000269|PubMed:19119025, ECO:0000269|PubMed:23826168}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-979862, EBI-979862;
P05067:APP; NbExp=3; IntAct=EBI-979862, EBI-77613;
P18418:Calr (xeno); NbExp=2; IntAct=EBI-979862, EBI-916742;
P24643:CANX (xeno); NbExp=3; IntAct=EBI-979862, EBI-15596385;
P10909:CLU; NbExp=2; IntAct=EBI-979862, EBI-1104674;
Q96HE7:ERO1A; NbExp=3; IntAct=EBI-979862, EBI-2564539;
Q86YB8:ERO1B; NbExp=2; IntAct=EBI-979862, EBI-2806988;
Q13162:PRDX4; NbExp=2; IntAct=EBI-979862, EBI-2211957;
Q13586:STIM1; NbExp=3; IntAct=EBI-979862, EBI-448878;
Q03518:TAP1; NbExp=4; IntAct=EBI-979862, EBI-747259;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:23826168}. Endoplasmic reticulum lumen
{ECO:0000250}. Melanosome {ECO:0000269|PubMed:12643545,
ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry
in melanosome fractions from stage I to stage IV
(PubMed:12643545). {ECO:0000269|PubMed:12643545}.
-!- TISSUE SPECIFICITY: Detected in the flagellum and head region of
spermatozoa (at protein level). {ECO:0000269|PubMed:20400973}.
-!- MASS SPECTROMETRY: Mass=54265.22; Method=MALDI; Range=25-505;
Evidence={ECO:0000269|PubMed:11840567};
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be a phosphatidylinositol 4,5-
bisphosphate phosphodiesterase type I (phospholipase C-alpha).
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D16234; BAA03759.1; -; mRNA.
EMBL; U42068; AAC50331.1; -; mRNA.
EMBL; Z49835; CAA89996.1; -; mRNA.
EMBL; U75885; AAC51518.1; -; Genomic_DNA.
EMBL; U75875; AAC51518.1; JOINED; Genomic_DNA.
EMBL; U75876; AAC51518.1; JOINED; Genomic_DNA.
EMBL; U75877; AAC51518.1; JOINED; Genomic_DNA.
EMBL; U75878; AAC51518.1; JOINED; Genomic_DNA.
EMBL; U75879; AAC51518.1; JOINED; Genomic_DNA.
EMBL; U75880; AAC51518.1; JOINED; Genomic_DNA.
EMBL; U75881; AAC51518.1; JOINED; Genomic_DNA.
EMBL; U75882; AAC51518.1; JOINED; Genomic_DNA.
EMBL; U75883; AAC51518.1; JOINED; Genomic_DNA.
EMBL; U75884; AAC51518.1; JOINED; Genomic_DNA.
EMBL; D83485; BAA11928.1; -; mRNA.
EMBL; BC014433; AAH14433.1; -; mRNA.
EMBL; BC036000; AAH36000.4; -; mRNA.
EMBL; BC071878; AAH71878.1; -; mRNA.
CCDS; CCDS10101.1; -.
PIR; JC5704; JC5704.
PIR; S55507; S55507.
PIR; S63994; S63994.
PIR; S68363; S68363.
RefSeq; NP_005304.3; NM_005313.4.
UniGene; Hs.591095; -.
PDB; 2ALB; NMR; -; A=25-137.
PDB; 2DMM; NMR; -; A=357-485.
PDB; 2H8L; X-ray; 2.00 A; A/B/C=134-376.
PDB; 3F8U; X-ray; 2.60 A; A/C=25-505.
PDBsum; 2ALB; -.
PDBsum; 2DMM; -.
PDBsum; 2H8L; -.
PDBsum; 3F8U; -.
ProteinModelPortal; P30101; -.
SMR; P30101; -.
BioGrid; 109180; 140.
CORUM; P30101; -.
DIP; DIP-29132N; -.
IntAct; P30101; 83.
MINT; MINT-5000005; -.
STRING; 9606.ENSP00000300289; -.
iPTMnet; P30101; -.
PhosphoSitePlus; P30101; -.
SwissPalm; P30101; -.
BioMuta; PDIA3; -.
DMDM; 2507461; -.
DOSAC-COBS-2DPAGE; P30101; -.
REPRODUCTION-2DPAGE; P30101; -.
SWISS-2DPAGE; P30101; -.
UCD-2DPAGE; P30101; -.
EPD; P30101; -.
PaxDb; P30101; -.
PeptideAtlas; P30101; -.
PRIDE; P30101; -.
TopDownProteomics; P30101; -.
DNASU; 2923; -.
Ensembl; ENST00000300289; ENSP00000300289; ENSG00000167004.
GeneID; 2923; -.
KEGG; hsa:2923; -.
CTD; 2923; -.
DisGeNET; 2923; -.
EuPathDB; HostDB:ENSG00000167004.12; -.
GeneCards; PDIA3; -.
HGNC; HGNC:4606; PDIA3.
HPA; CAB011199; -.
HPA; CAB015181; -.
HPA; HPA002645; -.
HPA; HPA003230; -.
MIM; 602046; gene.
neXtProt; NX_P30101; -.
OpenTargets; ENSG00000167004; -.
PharmGKB; PA29000; -.
eggNOG; KOG0190; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00860000133691; -.
HOGENOM; HOG000162459; -.
HOVERGEN; HBG005920; -.
InParanoid; P30101; -.
KO; K08056; -.
OMA; VAIVKMD; -.
OrthoDB; EOG091G05J9; -.
PhylomeDB; P30101; -.
TreeFam; TF106382; -.
BRENDA; 5.3.4.1; 2681.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-901042; Calnexin/calreticulin cycle.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
ChiTaRS; PDIA3; human.
EvolutionaryTrace; P30101; -.
GenomeRNAi; 2923; -.
PRO; PR:P30101; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000167004; -.
CleanEx; HS_PDIA3; -.
ExpressionAtlas; P30101; baseline and differential.
Genevisible; P30101; HS.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome.
GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
GO; GO:0015036; F:disulfide oxidoreductase activity; TAS:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0015037; F:peptide disulfide oxidoreductase activity; IDA:UniProtKB.
GO; GO:0004629; F:phospholipase C activity; TAS:ProtInc.
GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0006457; P:protein folding; TAS:Reactome.
GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL.
GO; GO:0006606; P:protein import into nucleus; TAS:ProtInc.
GO; GO:0006621; P:protein retention in ER lumen; TAS:ProtInc.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR005788; Disulphide_isomerase.
InterPro; IPR005792; Prot_disulphide_isomerase.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 2.
SUPFAM; SSF52833; SSF52833; 4.
TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
TIGRFAMs; TIGR01126; pdi_dom; 2.
PROSITE; PS00194; THIOREDOXIN_1; 2.
PROSITE; PS51352; THIOREDOXIN_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Isomerase; Methylation; Phosphoprotein; Polymorphism;
Redox-active center; Reference proteome; Repeat; Signal.
SIGNAL 1 24 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:1286669,
ECO:0000269|PubMed:7487104,
ECO:0000269|PubMed:9150948,
ECO:0000269|PubMed:9399589}.
CHAIN 25 505 Protein disulfide-isomerase A3.
/FTId=PRO_0000034225.
DOMAIN 25 133 Thioredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 343 485 Thioredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 502 505 Prevents secretion from ER.
{ECO:0000250}.
ACT_SITE 57 57 Nucleophile. {ECO:0000250}.
ACT_SITE 60 60 Nucleophile. {ECO:0000250}.
ACT_SITE 406 406 Nucleophile. {ECO:0000250}.
ACT_SITE 409 409 Nucleophile. {ECO:0000250}.
SITE 58 58 Contributes to redox potential value.
{ECO:0000250}.
SITE 59 59 Contributes to redox potential value.
{ECO:0000250}.
SITE 119 119 Lowers pKa of C-terminal Cys of first
active site. {ECO:0000250}.
SITE 407 407 Contributes to redox potential value.
{ECO:0000250}.
SITE 408 408 Contributes to redox potential value.
{ECO:0000250}.
SITE 471 471 Lowers pKa of C-terminal Cys of second
active site. {ECO:0000250}.
MOD_RES 61 61 N6-methyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 129 129 N6-succinyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 218 218 N6-succinyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 252 252 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 319 319 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 362 362 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 494 494 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27773}.
DISULFID 57 60 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 57 57 Interchain (with C-115 in TAPBP); in
linked form.
{ECO:0000269|PubMed:19119025}.
DISULFID 85 92 {ECO:0000269|PubMed:19119025}.
DISULFID 406 409 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VARIANT 415 415 K -> R (in dbSNP:rs6413485).
/FTId=VAR_020027.
MUTAGEN 57 57 C->A: No loss of activity. No loss of
activity; when associated with A-406.
{ECO:0000269|PubMed:9399589}.
MUTAGEN 57 57 C->S: Activity changed to serine
protease. {ECO:0000269|PubMed:9399589}.
MUTAGEN 60 60 C->S: Activity changed to serine
protease; when associated with S-409.
{ECO:0000269|PubMed:9399589}.
MUTAGEN 406 406 C->A: No loss of activity. No loss of
activity; when associated with A-57.
{ECO:0000269|PubMed:9399589}.
MUTAGEN 406 406 C->S: Activity changed to serine
protease. {ECO:0000269|PubMed:9399589}.
MUTAGEN 409 409 C->S: Activity changed to serine
protease; when associated with S-60.
{ECO:0000269|PubMed:9399589}.
CONFLICT 19 19 A -> G (in Ref. 6; BAA11928).
{ECO:0000305}.
CONFLICT 22 22 A -> V (in Ref. 6; BAA11928).
{ECO:0000305}.
CONFLICT 217 217 D -> Y (in Ref. 1; BAA03759).
{ECO:0000305}.
CONFLICT 225 225 Q -> P (in Ref. 4; CAA89996).
{ECO:0000305}.
CONFLICT 238 238 E -> G (in Ref. 4; CAA89996).
{ECO:0000305}.
CONFLICT 272 272 N -> D (in Ref. 1; BAA03759 and 5;
AAC51518). {ECO:0000305}.
CONFLICT 355 355 D -> G (in Ref. 1; BAA03759).
{ECO:0000305}.
CONFLICT 358 358 D -> G (in Ref. 1; BAA03759).
{ECO:0000305}.
CONFLICT 368 368 E -> D (in Ref. 1; BAA03759).
{ECO:0000305}.
STRAND 27 29 {ECO:0000244|PDB:2ALB}.
TURN 32 34 {ECO:0000244|PDB:3F8U}.
HELIX 35 38 {ECO:0000244|PDB:3F8U}.
HELIX 39 41 {ECO:0000244|PDB:2ALB}.
STRAND 43 53 {ECO:0000244|PDB:3F8U}.
HELIX 58 73 {ECO:0000244|PDB:3F8U}.
TURN 74 77 {ECO:0000244|PDB:3F8U}.
STRAND 80 84 {ECO:0000244|PDB:3F8U}.
TURN 85 87 {ECO:0000244|PDB:3F8U}.
HELIX 89 94 {ECO:0000244|PDB:3F8U}.
STRAND 99 107 {ECO:0000244|PDB:3F8U}.
STRAND 110 114 {ECO:0000244|PDB:3F8U}.
HELIX 121 131 {ECO:0000244|PDB:3F8U}.
STRAND 136 138 {ECO:0000244|PDB:2H8L}.
HELIX 142 149 {ECO:0000244|PDB:2H8L}.
STRAND 151 153 {ECO:0000244|PDB:2H8L}.
STRAND 155 161 {ECO:0000244|PDB:2H8L}.
HELIX 166 177 {ECO:0000244|PDB:2H8L}.
TURN 178 181 {ECO:0000244|PDB:2H8L}.
STRAND 182 187 {ECO:0000244|PDB:2H8L}.
HELIX 190 196 {ECO:0000244|PDB:2H8L}.
STRAND 198 206 {ECO:0000244|PDB:2H8L}.
HELIX 209 211 {ECO:0000244|PDB:2H8L}.
STRAND 218 221 {ECO:0000244|PDB:2H8L}.
HELIX 229 239 {ECO:0000244|PDB:2H8L}.
TURN 240 243 {ECO:0000244|PDB:3F8U}.
TURN 249 251 {ECO:0000244|PDB:2H8L}.
HELIX 252 255 {ECO:0000244|PDB:2H8L}.
STRAND 256 265 {ECO:0000244|PDB:2H8L}.
TURN 269 271 {ECO:0000244|PDB:2H8L}.
HELIX 273 292 {ECO:0000244|PDB:2H8L}.
STRAND 298 303 {ECO:0000244|PDB:2H8L}.
TURN 304 307 {ECO:0000244|PDB:2H8L}.
HELIX 308 311 {ECO:0000244|PDB:2H8L}.
HELIX 312 314 {ECO:0000244|PDB:2H8L}.
STRAND 325 329 {ECO:0000244|PDB:2H8L}.
STRAND 331 333 {ECO:0000244|PDB:3F8U}.
STRAND 335 337 {ECO:0000244|PDB:2H8L}.
HELIX 347 358 {ECO:0000244|PDB:2H8L}.
STRAND 376 381 {ECO:0000244|PDB:3F8U}.
TURN 383 385 {ECO:0000244|PDB:3F8U}.
HELIX 386 390 {ECO:0000244|PDB:3F8U}.
STRAND 396 402 {ECO:0000244|PDB:3F8U}.
HELIX 407 422 {ECO:0000244|PDB:3F8U}.
TURN 423 425 {ECO:0000244|PDB:3F8U}.
STRAND 427 435 {ECO:0000244|PDB:3F8U}.
TURN 436 438 {ECO:0000244|PDB:2DMM}.
STRAND 449 456 {ECO:0000244|PDB:3F8U}.
HELIX 473 483 {ECO:0000244|PDB:3F8U}.
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


Related products :

Catalog number Product name Quantity
E1497b ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Bos taurus,Bovine,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER prot 96T
U1497b CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Bos taurus,Bovine,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER prote 96T
E1497b ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Bos taurus,Bovine,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER 96T
E1497m ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 96T
E1497h ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 96T
U1497r CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 6 96T
E1497r ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 96T
U1497h CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 6 96T
U1497m CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 6 96T
E1497m ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER pro 96T
E1497h ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER pro 96T
E1497r ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER pro 96T
U1497c CLIA Chicken,Endoplasmic reticulum resident protein 57,ER protein 57,ERp57,ERP57,Gallus gallus,Glucose-regulated thiol oxidoreductase 58 kDa protein,GRP58,PDIA3,Protein disulfide-isomerase A3 96T
E1497c ELISA kit Chicken,Endoplasmic reticulum resident protein 57,ER protein 57,ERp57,ERP57,Gallus gallus,Glucose-regulated thiol oxidoreductase 58 kDa protein,GRP58,PDIA3,Protein disulfide-isomerase A3 96T
E1497c ELISA Chicken,Endoplasmic reticulum resident protein 57,ER protein 57,ERp57,ERP57,Gallus gallus,Glucose-regulated thiol oxidoreductase 58 kDa protein,GRP58,PDIA3,Protein disulfide-isomerase A3 96T
EIAAB30361 Endoplasmic reticulum resident protein 70,Endoplasmic reticulum resident protein 72,ER protein 70,ER protein 72,ERp70,ERP70,ERp72,ERP72,ERp-72,Homo sapiens,Human,PDIA4,Protein disulfide-isomerase A4
EIAAB30362 CaBP2,Cabp2,Calcium-binding protein 2,Endoplasmic reticulum resident protein 70,Endoplasmic reticulum resident protein 72,ER protein 70,ER protein 72,ERp70,Erp70,ERp72,ERp-72,Pdia4,Protein disulfide-i
EIAAB44606 Endoplasmic reticulum resident protein 18,Endoplasmic reticulum resident protein 19,ER protein 18,ER protein 19,ERp18,ERp19,Homo sapiens,hTLP19,Human,Thioredoxin domain-containing protein 12,Thioredox
EIAAB30363 Cai,Endoplasmic reticulum resident protein 72,ER protein 72,ERp72,Erp72,ERp-72,Mouse,Mus musculus,Pdia4,Protein disulfide-isomerase A4
EIAAB13274 C12orf8,Endoplasmic reticulum resident protein 28,Endoplasmic reticulum resident protein 29,Endoplasmic reticulum resident protein 31,ERp28,ERP28,ERp29,ERP29,ERp31,Homo sapiens,Human
EIAAB30369 Endoplasmic reticulum protein 5,ER protein 5,ERp5,ERP5,Homo sapiens,Human,P5,PDIA6,Protein disulfide isomerase P5,Protein disulfide-isomerase A6,Thioredoxin domain-containing protein 7,TXNDC7
20-272-190877 ERp57 - Mouse monoclonal [MaP.Erp57] to ERp57; EC 5.3.4.1; Disulfide isomerase ER-60; ERp60; 58 kDa microsomal protein; p58; ERp57; 58 kDa glucose-regulated protein Monoclonal 0.05 mg
18-272-195406 ERp57 - Rabbit polyclonal to ERp57; EC 5.3.4.1; Disulfide isomerase ER-60; ERp60; 58 kDa microsomal protein; p58; ERp57; 58 kDa glucose-regulated protein Polyclonal 0.05 ml
U1061m CLIA Cellular thyroid hormone-binding protein,Endoplasmic reticulum resident protein 59,ER protein 59,ERp59,Mouse,Mus musculus,P4hb,p55,PDI,Pdia1,Prolyl 4-hydroxylase subunit beta,Protein disulfide-is 96T
E1061m ELISA Cellular thyroid hormone-binding protein,Endoplasmic reticulum resident protein 59,ER protein 59,ERp59,Mouse,Mus musculus,P4hb,p55,PDI,Pdia1,Prolyl 4-hydroxylase subunit beta,Protein disulfide-i 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur