P-POD: Princeton Protein Orthology Database: GO3/Para384

This family has 39 members: 6 Arabidopsis thaliana, 4 Caenorhabditis elegans, 6 Danio rerio, 1 Dictyostelium discoideum, 2 Drosophila melanogaster, 5 Gallus gallus, 4 Homo sapiens, 4 Mus musculus, 4 Rattus norvegicus, 2 Saccharomyces cerevisiae, 1 Schizosaccharomyces pombe.

Interactive Java Applets: Notung Tree Analysis · Jalview Alignment

GO3/Para384
39 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_188232.2 · TAIR:locus:2093447 (AT3G16110 · ATPDI4 · ATPDIL1-6 · PDI4 · MSL1.15)ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 4 · PROTEIN DISULFIDE ISOMERASE 4 · PDI-LIKE 1-6⌘
A. thalianaNCBI:NP_175636.2 · TAIR:locus:2018134 (F19K6_17 · F19K6.17 · PDI3 · ATPDI3 · ATPDIL1-5 · AT1G52260)PROTEIN DISULFIDE ISOMERASE 3 · ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 3 · PDI-LIKE 1-5⌘
A. thalianaNCBI:NP_851234.1 · TAIR:locus:2175811 (MUP24.6 · AT5G60640 · PDI2 · ATPDIL1-4 · ATPDI2 · MUP24_6)PROTEIN DISULFIDE ISOMERASE 2 · PDI-LIKE 1-4 · ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 2⌘
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_191056.2 · TAIR:locus:2082712 (ATPDIL1-3 · ATPDI1 · AT3G54960 · PDI1 · T15C9.4)PDI-LIKE 1-3 · ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 1 · PROTEIN DISULFIDE ISOMERASE 1⌘
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:WBGene00003962 (C14B1.1 · pdi-1) · UniProtKB:Q17967⌘
C. elegansWB:WBGene00003963 (C07A12.4 · pdi-2) · UniProtKB:Q17770⌘
C. elegansWB:WBGene00015752 (C14B9.2) · UniProtKB:P34329⌘
C. elegansWB:WBGene00003964 (H06O01.1 · pdi-3) · UniProtKB:O17908⌘
D. rerioENSEMBL:ENSDARP00000068966
D. rerioZFIN:ZDB-GENE-040801-20 (zgc:100906) · UniProtKB:Q6DEI4⌘
D. rerioZFIN:ZDB-GENE-060421-2552 (zgc:136472) · UniProtKB:Q6DG87⌘
D. rerioZFIN:ZDB-GENE-040426-2238 (zgc:77086) · UniProtKB:Q6NXB9⌘
D. rerioUniProtKB:Q7ZVH2 · ZFIN:ZDB-GENE-030131-5493 (pdia4)protein disulfide isomerase associated 4⌘
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. melanogasterUniProtKB:P54399 · FB:FBgn0014002 (dpdi · EP(3)1022 · Dpdi · CG6988 · Pdi · pdi · PDI)Protein disulfide isomerase · disulfide isomerase · protein disulfide isomerase · protein-disulfide isomerase⌘
D. melanogasterFB:FBgn0033663 (Erp60 · CG8983 · anon-fast-evolving-3D9 · D-ERp60 · ERp60 · anon-EST:fe3D9 · Ov6) · UniProtKB:Q3YMU0⌘
G. gallusNCBI:XP_420095 · ENTREZ:374091
G. gallusNCBI:XP_428969 · ENTREZ:431417
G. gallusENTREZ:396376 · UniProtKB:P12244 (GSBP_CHICK · P12244 · IPI00597613)Dolichyl-diphosphooligosaccharide--protein glycotransferase⌘
G. gallusENTREZ:373899 · UniProtKB:Q8JG64 (GRP58 · ERP57 · PDIA3_CHICK · IPI00575271 · PDIA3 · Q8JG64)Protein disulfide-isomerase A3⌘
G. gallusUniProtKB:Q5ZK20 (Q5ZK20 · RCJMB04_13l7 · IPI00589958) · ENTREZ:420785⌘
H. sapiensENSEMBL:ENSG00000185624 · UniProtKB:P07237 (PDIA1 · PDIA1_HUMAN · P4HB · PDI · P07237 · ERBA2L · PO4DB · IPI00010796)Protein disulfide-isomerase⌘
H. sapiensENSEMBL:ENSG00000167004 · UniProtKB:P30101 (PDIA3_HUMAN · IPI00025252 · GRP58 · ERP60 · P30101 · ERP57 · PDIA3)Protein disulfide-isomerase A3⌘
H. sapiensENSEMBL:ENSG00000155660 · UniProtKB:P13667 (PDIA4 · PDIA4_HUMAN · ERP72 · P13667 · ERP70 · IPI00009904)Protein disulfide-isomerase A4⌘
H. sapiensENSEMBL:ENSG00000169340 · UniProtKB:Q8N807 (Q8N807 · PDILT_HUMAN · IPI00646007 · PDILT)Protein disulfide-isomerase-like protein of the testis⌘
M. musculusUniProtKB:P09103 · MGI:MGI:97464 (Thbp · ERp59 · P4hb)prolyl 4-hydroxylase, beta polypeptide · protein disulfide isomerase⌘
M. musculusUniProtKB:P27773 · MGI:MGI:95834 (Grp58 · ERp57 · Erp · Pdia3 · PDI · Plca · ERp60 · ERp61 · PDI-Q2)protein disulfide isomerase associated 3⌘
M. musculusUniProtKB:P08003 · MGI:MGI:104864 (ERp72 · Pdia4 · Cai)protein disulfide isomerase associated 4⌘
M. musculusUniProtKB:Q9DAN1 · MGI:MGI:1919080 (Pdilt · PDILT)protein disulfide isomerase-like, testis expressed⌘
R. norvegicusUniProtKB:P04785 · RGD:3244 (P4hb)prolyl 4-hydroxylase, beta polypeptide⌘
R. norvegicusUniProtKB:P11598 · RGD:68430 (Pdia3)protein disulfide isomerase family A, member 3⌘
R. norvegicusUniProtKB:P38659 · RGD:619835 (Pdia4)protein disulfide isomerase family A, member 4⌘
R. norvegicusUniProtKB:Q5XI02 · RGD:1307822 (Pdilt)protein disulfide isomerase-like protein of the testis⌘
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
Send questions, suggestions, and comments to: yfgdb@genomics.princeton.edu