P-POD: Princeton Protein Orthology Database: GO3/OrthoMCL1183

This family has 16 members: 2 Arabidopsis thaliana, 1 Caenorhabditis elegans, 3 Danio rerio, 1 Dictyostelium discoideum, 1 Drosophila melanogaster, 1 Escherichia coli, 1 Gallus gallus, 1 Homo sapiens, 1 Mus musculus, 1 Rattus norvegicus, 2 Saccharomyces cerevisiae, 1 Schizosaccharomyces pombe.

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GO3/OrthoMCL1183
16 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_177875.1 · TAIR:locus:2204670 (ATPDI6 · T5M16_10 · AT1G77510 · T5M16.10 · PDI6 · ATPDIL1-2)PROTEIN DISULFIDE ISOMERASE 6 · PDI-LIKE 1-2⌘
A. thalianaNCBI:NP_173594.1 · TAIR:locus:2036906 (F8K7.19 · ATPDI5 · PDI5 · ATPDIL1-1 · F8K7_19 · AT1G21750)ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 5 · PDI-LIKE 1-1 · PROTEIN DISULFIDE ISOMERASE 5⌘
C. elegansWB:WBGene00003964 (H06O01.1 · pdi-3) · UniProtKB:O17908⌘
D. rerioZFIN:ZDB-GENE-040801-20 (zgc:100906) · UniProtKB:Q6DEI4⌘
D. rerioUniProtKB:Q6NXB9 · ZFIN:ZDB-GENE-040426-2238 (zgc:77086)⌘
D. rerioUniProtKB:Q803D7 · ZFIN:ZDB-GENE-031002-9 (pdia3)protein disulfide isomerase family A, member 3⌘
D. discoideumUniProtKB:Q54EN4 · dictyBase:DDB_G0291434 (PDI · pdi2)protein disulfide isomerase⌘
D. melanogasterFB:FBgn0033663 (Erp60 · CG8983 · anon-fast-evolving-3D9 · D-ERp60 · ERp60 · anon-EST:fe3D9 · Ov6) · UniProtKB:Q3YMU0⌘
E. coliUniProtKB:P0AGG4 · ECOLI:OX-THIOREDOXIN2-MONOMER (trxC · yfiG · ECK2580 · b2582)oxidized thioredoxin 2⌘
G. gallusENTREZ:373899 · UniProtKB:Q8JG64 (GRP58 · ERP57 · PDIA3_CHICK · IPI00575271 · PDIA3 · Q8JG64)Protein disulfide-isomerase A3⌘
H. sapiensENSEMBL:ENSG00000167004 · UniProtKB:P30101 (PDIA3_HUMAN · IPI00025252 · GRP58 · ERP60 · P30101 · ERP57 · PDIA3)Protein disulfide-isomerase A3⌘
M. musculusUniProtKB:P27773 · MGI:MGI:95834 (Grp58 · ERp57 · Erp · Pdia3 · PDI · Plca · ERp60 · ERp61 · PDI-Q2)protein disulfide isomerase associated 3⌘
R. norvegicusUniProtKB:P11598 · RGD:68430 (Pdia3)protein disulfide isomerase family A, member 3⌘
S. cerevisiaeUniProtKB:P32474 · SGD:S000002926 (YDR518W · EUG1)Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p⌘
S. cerevisiaeUniProtKB:P17967 · SGD:S000000548 (MFP1 · YCL043C · PDI1 · TRG1)Protein disulfide isomerase, multifunctional protein resident in the endoplasmic reticulum lumen, essential for the formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds⌘
S. pombeUniProtKB:Q10057 · GeneDB_Spombe:SPAC1F5.02 (SPAC1F5.02)protein disulfide isomerase⌘
ProteinPublicationCurator Notes
UniProtKB:P17967 · SGD:S000000548PMID:8385117 Günther R, et al. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J Biol Chem. 1993 Apr 15;268(11):7728-32.The M. musculus protein P08003 complements a homologous mutation in S. cerevisiae. This paper shows that murine ERp72 (P08003) partially complements a yeast pdi1 null mutant.
UniProtKB:P17967 · SGD:S000000548PMID:7499282 Laboissiere MC, et al. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem. 1995 Nov 24;270(47):28006-9.The R. norvegicus protein PDI complements a homologous mutation in S. cerevisiae.
UniProtKB:P17967 · SGD:S000000548PMID:15377672 Xiao R, et al. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J Biol Chem. 2004 Nov 26;279(48):49780-6.The R. norvegicus protein PDI complements a homologous mutation in S. cerevisiae. This paper shows that rat PDI partially complements a yeast pdi1 null mutant.
UniProtKB:P17967 · SGD:S000000548PMID:16889384 Zhang W, et al. Enhanced secretion of heterologous proteins in Pichia pastoris following overexpression of Saccharomyces cerevisiae chaperone proteins. Biotechnol Prog. 2006 Jul-Aug;22(4):1090-5.The S. cerevisiae protein PDI1 was expressed in P. pastoris, but complementation was not directly tested. This paper shows heterologous overexpression of S. cerevisiae PDI1 in P. pastoris.
UniProtKB:P17967 · SGD:S000000548PMID:8385117 Günther R, et al. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J Biol Chem. 1993 Apr 15;268(11):7728-32.The R. norvegicus protein ERp61 does not complement a homologous mutation in S. cerevisiae.
UniProtKB:P17967 · SGD:S000000548PMID:8385117 Günther R, et al. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J Biol Chem. 1993 Apr 15;268(11):7728-32.The M. musculus protein P09103 complements a homologous mutation in S. cerevisiae. This paper shows that murine ERp59/PDI (P09103) partially complements a yeast pdi1 null mutant.
DescriptionSuffix
Sequences in this family.fasta
mafft aligned Fasta file.afasta
phyml newick file.newick
Notung rooted & rearranged newick file.newick.rooting.0.rearrange.0
Notung Homolog Table.newick.rooting.0.rearrange.0.homologs.csv
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