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P54399 (PDI_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase

Short name=PDI
Short name=dPDI
EC=5.3.4.1
Gene names
Name:Pdi
ORF Names:CG6988
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Participates in the folding of proteins containing disulfide bonds By similarity.

Catalytic activity

Catalyzes the rearrangement of -S-S- bonds in proteins.

Subunit structure

Homodimer By similarity.

Subcellular location

Endoplasmic reticulum lumen Potential.

Tissue specificity

Expressed in all head and body tissues. Ref.1

Developmental stage

Ubiquitously expressed during development. Ref.1

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence caution

The sequence AAO24936.1 differs from that shown. Reason: Frameshift at position 362.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DomainRedox-active center
Repeat
Signal
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

peptidyl-proline hydroxylation

Inferred from Biological aspect of Ancestor. Source: GOC

protein folding

Inferred from Biological aspect of Ancestor. Source: GOC

regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to endoplasmic reticulum stress

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcell pole

Inferred from direct assay PubMed 17914057. Source: FlyBase

cytoplasm

Inferred from direct assay PubMed 19303437. Source: FlyBase

endoplasmic reticulum

Inferred from direct assay PubMed 11514618PubMed 17914057. Source: FlyBase

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay PubMed 16670001. Source: FlyBase

fusome

Inferred from direct assay PubMed 18355804. Source: FlyBase

lipid particle

Inferred from direct assay PubMed 16543254. Source: FlyBase

neuronal cell body

Inferred from direct assay PubMed 17470283. Source: FlyBase

nuclear envelope

Inferred from direct assay PubMed 16847576. Source: FlyBase

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17470283. Source: FlyBase

rough endoplasmic reticulum

Inferred from direct assay PubMed 17327273. Source: FlyBase

spindle envelope

Inferred from direct assay PubMed 17914057. Source: FlyBase

   Molecular_functionprotein disulfide isomerase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P54399-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform D (identifier: P54399-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-306: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 496478Protein disulfide-isomerase
PRO_0000034202

Regions

Domain19 – 134116Thioredoxin 1
Domain349 – 474126Thioredoxin 2
Motif493 – 4964Prevents secretion from ER
Compositional bias482 – 4898Poly-Glu

Sites

Active site561Nucleophile By similarity
Active site591Nucleophile By similarity
Active site3971Nucleophile By similarity
Active site4001Nucleophile By similarity
Site571Contributes to redox potential value By similarity
Site581Contributes to redox potential value By similarity
Site1201Lowers pKa of C-terminal Cys of first active site By similarity
Site3981Contributes to redox potential value By similarity
Site3991Contributes to redox potential value By similarity
Site4601Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond56 ↔ 59Redox-active By similarity
Disulfide bond397 ↔ 400Redox-active By similarity

Natural variations

Alternative sequence1 – 306306Missing in isoform D.
VSP_035858

Experimental info

Sequence conflict4061I → T in AAO24936. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EB6E04C4216E7A81

FASTA49655,781
        10         20         30         40         50         60 
MKFLICALFL AASYVAASAE AEVKVEEGVL VATVDNFKQL IADNEFVLVE FYAPWCGHCK 

        70         80         90        100        110        120 
ALAPEYAKAA QQLAEKESPI KLAKVDATVE GELAEQYAVR GYPTLKFFRS GSPVEYSGGR 

       130        140        150        160        170        180 
QAADIIAWVT KKTGPPAKDL TSVADAEQFL KDNEIAIIGF FKDLESEEAK TFTKVANALD 

       190        200        210        220        230        240 
SFVFGVSSNA DVIAKYEAKD NGVVLFKPFD DKKSVFEGEL NEENLKKFAQ VQSLPLIVDF 

       250        260        270        280        290        300 
NHESASKIFG GSIKSHLLFF VSREGGHIEK YVDPLKEIAK KYRDDILFVT ISSDEEDHTR 

       310        320        330        340        350        360 
IFEFFGMNKE EVPTIRLIKL EEDMAKYKPE SDDLSAETIE AFLKKFLDGK LKQHLLSQEL 

       370        380        390        400        410        420 
PEDWDKNPVK VLVSSNFESV ALDKSKSVLV EFYAPWCGHC KQLAPIYDQL AEKYKDNEDI 

       430        440        450        460        470        480 
VIAKMDSTAN ELESIKISSF PTIKYFRKED NKVIDFNLDR TLDDFVKFLD ANGEVADSEP 

       490 
VEETEEEEEA PKKDEL 

« Hide

Isoform D [UniParc].

Checksum: A06DC4C1BC98F510
Show »

FASTA19021,899

References

« Hide 'large scale' references
[1]"A Drosophila gene that encodes a member of the protein disulfide isomerase/phospholipase C-alpha family."
McKay R.R., Zhu L., Shortridge R.D.
Insect Biochem. Mol. Biol. 25:647-654(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Head.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
[5]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
Strain: Berkeley.
Tissue: Embryo and Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18973 mRNA. Translation: AAA86480.1.
AE014296 Genomic DNA. Translation: AAF49659.1.
AE014296 Genomic DNA. Translation: AAN11793.1.
BT001544 mRNA. Translation: AAN71299.1.
BT003181 mRNA. Translation: AAO24936.1. Frameshift.
BT011488 mRNA. Translation: AAR99146.1.
BT012439 mRNA. Translation: AAS93710.1.
RefSeqNP_524079.1. NM_079355.3. [P54399-1]
NP_730033.1. NM_168614.3. [P54399-2]
UniGeneDm.2710.

3D structure databases

ProteinModelPortalP54399.
SMRP54399. Positions 26-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid64973. 82 interactions.
DIPDIP-21766N.
IntActP54399. 5 interactions.
MINTMINT-314239.

Proteomic databases

PaxDbP54399.
PRIDEP54399.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075648; FBpp0075401; FBgn0014002. [P54399-1]
GeneID39651.
KEGGdme:Dmel_CG6988.
UCSCCG6988-RD. d. melanogaster.

Organism-specific databases

CTD39651.
FlyBaseFBgn0014002. Pdi.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00740000115202.
InParanoidP54399.
KOK09580.
OMACHHFLEG.
OrthoDBEOG7VHSX1.
PhylomeDBP54399.

Gene expression databases

BgeeP54399.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPdi. drosophila.
GenomeRNAi39651.
NextBio814692.
PROP54399.

Entry information

Entry namePDI_DROME
AccessionPrimary (citable) accession number: P54399
Secondary accession number(s): Q53YH5 expand/collapse secondary AC list , Q86PE2, Q8IQL8, Q9VUL7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase