PDI_DROME
ID PDI_DROME Reviewed; 496 AA.
AC P54399; Q53YH5; Q86PE2; Q8IQL8; Q9VUL7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein disulfide-isomerase;
DE Short=PDI;
DE Short=dPDI;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN Name=Pdi; ORFNames=CG6988;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Head;
RX PubMed=7787847; DOI=10.1016/0965-1748(95)00001-c;
RA McKay R.R., Zhu L., Shortridge R.D.;
RT "A Drosophila gene that encodes a member of the protein disulfide
RT isomerase/phospholipase C-alpha family.";
RL Insect Biochem. Mol. Biol. 25:647-654(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC bonds. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P54399-1; Sequence=Displayed;
CC Name=D;
CC IsoId=P54399-2; Sequence=VSP_035858;
CC -!- TISSUE SPECIFICITY: Expressed in all head and body tissues.
CC {ECO:0000269|PubMed:7787847}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed during development.
CC {ECO:0000269|PubMed:7787847}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO24936.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U18973; AAA86480.1; -; mRNA.
DR EMBL; AE014296; AAF49659.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11793.1; -; Genomic_DNA.
DR EMBL; BT001544; AAN71299.1; -; mRNA.
DR EMBL; BT003181; AAO24936.1; ALT_FRAME; mRNA.
DR EMBL; BT011488; AAR99146.1; -; mRNA.
DR EMBL; BT012439; AAS93710.1; -; mRNA.
DR RefSeq; NP_001287070.1; NM_001300141.1. [P54399-1]
DR RefSeq; NP_524079.1; NM_079355.3. [P54399-1]
DR AlphaFoldDB; P54399; -.
DR SMR; P54399; -.
DR BioGRID; 64973; 85.
DR DIP; DIP-21766N; -.
DR IntAct; P54399; 21.
DR STRING; 7227.FBpp0075401; -.
DR PaxDb; P54399; -.
DR PRIDE; P54399; -.
DR DNASU; 39651; -.
DR EnsemblMetazoa; FBtr0075648; FBpp0075401; FBgn0286818. [P54399-1]
DR EnsemblMetazoa; FBtr0346644; FBpp0312224; FBgn0286818. [P54399-1]
DR GeneID; 39651; -.
DR KEGG; dme:Dmel_CG6988; -.
DR UCSC; CG6988-RD; d. melanogaster.
DR CTD; 39651; -.
DR FlyBase; FBgn0286818; Pdi.
DR VEuPathDB; VectorBase:FBgn0286818; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_1_0_1; -.
DR InParanoid; P54399; -.
DR OMA; FCDRFLE; -.
DR PhylomeDB; P54399; -.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR Reactome; R-DME-8964041; LDL remodeling.
DR BioGRID-ORCS; 39651; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Pdi; fly.
DR GenomeRNAi; 39651; -.
DR PRO; PR:P54399; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0286818; Expressed in saliva-secreting gland and 26 other tissues.
DR ExpressionAtlas; P54399; baseline and differential.
DR Genevisible; P54399; DM.
DR GO; GO:0060187; C:cell pole; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0045169; C:fusome; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0070732; C:spindle envelope; IDA:FlyBase.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISS:FlyBase.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Isomerase;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..496
FT /note="Protein disulfide-isomerase"
FT /id="PRO_0000034202"
FT DOMAIN 19..134
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 349..474
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 473..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 493..496
FT /note="Prevents secretion from ER"
FT COMPBIAS 476..496
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 397
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 400
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 57
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 398
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 399
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 460
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 56..59
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 397..400
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 1..306
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_035858"
FT CONFLICT 406
FT /note="I -> T (in Ref. 5; AAO24936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 55781 MW; EB6E04C4216E7A81 CRC64;
MKFLICALFL AASYVAASAE AEVKVEEGVL VATVDNFKQL IADNEFVLVE FYAPWCGHCK
ALAPEYAKAA QQLAEKESPI KLAKVDATVE GELAEQYAVR GYPTLKFFRS GSPVEYSGGR
QAADIIAWVT KKTGPPAKDL TSVADAEQFL KDNEIAIIGF FKDLESEEAK TFTKVANALD
SFVFGVSSNA DVIAKYEAKD NGVVLFKPFD DKKSVFEGEL NEENLKKFAQ VQSLPLIVDF
NHESASKIFG GSIKSHLLFF VSREGGHIEK YVDPLKEIAK KYRDDILFVT ISSDEEDHTR
IFEFFGMNKE EVPTIRLIKL EEDMAKYKPE SDDLSAETIE AFLKKFLDGK LKQHLLSQEL
PEDWDKNPVK VLVSSNFESV ALDKSKSVLV EFYAPWCGHC KQLAPIYDQL AEKYKDNEDI
VIAKMDSTAN ELESIKISSF PTIKYFRKED NKVIDFNLDR TLDDFVKFLD ANGEVADSEP
VEETEEEEEA PKKDEL
