P54399 (PDI_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase
Short name=PDI
Short name=dPDI
EC=5.3.4.1

Gene names

Name:	Pdi
ORF Names:	CG6988

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cell pole Inferred from direct assay. Source: FlyBase endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from direct assay. Source: FlyBase fusome Inferred from direct assay. Source: FlyBase lipid particle Inferred from direct assay. Source: FlyBase neuronal cell body Inferred from direct assay. Source: FlyBase nuclear envelope Inferred from direct assay. Source: FlyBase perinuclear region of cytoplasm Inferred from direct assay. Source: FlyBase rough endoplasmic reticulum Inferred from direct assay. Source: FlyBase spindle envelope Inferred from direct assay. Source: FlyBase
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from electronic annotation. Source: EC 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 496	478	Protein disulfide-isomerase		PRO_0000034202
Regions
	Domain	19 – 134	116	Thioredoxin 1
	Domain	349 – 474	126	Thioredoxin 2
	Motif	493 – 496	4	Prevents secretion from ER
	Compositional bias	482 – 489	8	Poly-Glu
Sites
	Active site	56	1	Nucleophile By similarity
	Active site	59	1	Nucleophile By similarity
	Active site	397	1	Nucleophile By similarity
	Active site	400	1	Nucleophile By similarity
	Site	57	1	Contributes to redox potential value By similarity
	Site	58	1	Contributes to redox potential value By similarity
	Site	120	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	398	1	Contributes to redox potential value By similarity
	Site	399	1	Contributes to redox potential value By similarity
	Site	460	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Disulfide bond	56 ↔ 59		Redox-active By similarity
	Disulfide bond	397 ↔ 400		Redox-active By similarity
Natural variations
	Alternative sequence	1 – 306	306	Missing in isoform D.		VSP_035858
Experimental info
	Sequence conflict	406	1	I → T in AAO24936. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EB6E04C4216E7A81	FASTA	496	55,781
	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
	Isoform D [UniParc]. Checksum: A06DC4C1BC98F510	FASTA	190	21,899
	10 20 30 40 50 60 MNKEEVPTIR LIKLEEDMAK YKPESDDLSA ETIEAFLKKF LDGKLKQHLL SQELPEDWDK 70 80 90 100 110 120 NPVKVLVSSN FESVALDKSK SVLVEFYAPW CGHCKQLAPI YDQLAEKYKD NEDIVIAKMD 130 140 150 160 170 180 STANELESIK ISSFPTIKYF RKEDNKVIDF NLDRTLDDFV KFLDANGEVA DSEPVEETEE 190 EEEAPKKDEL

References

	« Hide 'large scale' referencesShow '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: 7787847] [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. , 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: 10731132] [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. , 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: 12537572] [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: 12537569] [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. , 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.
RefSeq	NP_524079.1. NM_079355.2. NP_730033.1. NM_168614.2.
UniGene	Dm.2710.
3D structure databases
ProteinModelPortal	P54399.
SMR	P54399. Positions 26-479.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-21766N.
IntAct	P54399. 5 interactions.
MINT	MINT-314239.
STRING	P54399.
Proteomic databases
PRIDE	P54399.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0075648; FBpp0075401; FBgn0014002.
GeneID	39651.
KEGG	dme:Dmel_CG6988.
Organism-specific databases
CTD	39651.
FlyBase	FBgn0014002. Pdi.
Phylogenomic databases
eggNOG	inNOG05913.
GeneTree	EMGT00050000002774.
InParanoid	P54399.
OMA	DMTKFKP.
OrthoDB	EOG4CJSZK.
PhylomeDB	P54399.
Gene expression databases
ArrayExpress	P54399.
Bgee	P54399.
GermOnline	CG6988. Drosophila melanogaster.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 4 hits.
KO	K09580.
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 4 hits.
TIGRFAMs	TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. Pdi_dom. 2 hits.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	814692.

Entry information

Entry name

PDI_DROME

Accession

Primary (citable) accession number: P54399
Secondary accession number(s): Q53YH5 , Q86PE2, Q8IQL8, Q9VUL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project