Entry sw: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   18-JAN-2017, entry version 146.
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;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., 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.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in the folding of proteins containing
CC       disulfide bonds. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000255|PROSITE-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         Note=No experimental confirmation available.;
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   -!- SIMILARITY: Contains 2 thioredoxin domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00691}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO24936.1; Type=Frameshift; Positions=362; Evidence={ECO:0000305};
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   UniGene; Dm.2710; -.
DR   ProteinModelPortal; P54399; -.
DR   SMR; P54399; -.
DR   BioGrid; 64973; 83.
DR   DIP; DIP-21766N; -.
DR   IntAct; P54399; 21.
DR   MINT; MINT-314239; -.
DR   STRING; 7227.FBpp0075401; -.
DR   PaxDb; P54399; -.
DR   PRIDE; P54399; -.
DR   EnsemblMetazoa; FBtr0075648; FBpp0075401; FBgn0014002. [P54399-1]
DR   EnsemblMetazoa; FBtr0346644; FBpp0312224; FBgn0014002. [P54399-1]
DR   GeneID; 39651; -.
DR   KEGG; dme:Dmel_CG6988; -.
DR   UCSC; CG6988-RD; d. melanogaster.
DR   CTD; 39651; -.
DR   FlyBase; FBgn0014002; Pdi.
DR   eggNOG; KOG0190; Eukaryota.
DR   eggNOG; COG0526; LUCA.
DR   InParanoid; P54399; -.
DR   KO; K09580; -.
DR   OMA; IEKYVDP; -.
DR   OrthoDB; EOG091G08WM; -.
DR   PhylomeDB; P54399; -.
DR   Reactome; R-DME-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-DME-174800; Chylomicron-mediated lipid transport.
DR   Reactome; R-DME-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-DME-8866423; VLDL biosynthesis.
DR   ChiTaRS; Pdi; fly.
DR   GenomeRNAi; 39651; -.
DR   PRO; PR:P54399; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0014002; -.
DR   ExpressionAtlas; P54399; 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; IDA: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:0005811; C:lipid particle; 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; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0019511; P:peptidyl-proline hydroxylation; IEA:GOC.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:1902175; P:regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR   Gene3D; 3.40.30.10; -; 4.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
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; Complete proteome; Disulfide bond;
KW   Endoplasmic reticulum; Isomerase; Redox-active center;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    496       Protein disulfide-isomerase.
FT                                /FTId=PRO_0000034202.
FT   DOMAIN       19    134       Thioredoxin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   DOMAIN      349    474       Thioredoxin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   MOTIF       493    496       Prevents secretion from ER.
FT   COMPBIAS    482    489       Poly-Glu.
FT   ACT_SITE     56     56       Nucleophile. {ECO:0000250}.
FT   ACT_SITE     59     59       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    397    397       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    400    400       Nucleophile. {ECO:0000250}.
FT   SITE         57     57       Contributes to redox potential value.
FT                                {ECO:0000250}.
FT   SITE         58     58       Contributes to redox potential value.
FT                                {ECO:0000250}.
FT   SITE        120    120       Lowers pKa of C-terminal Cys of first
FT                                active site. {ECO:0000250}.
FT   SITE        398    398       Contributes to redox potential value.
FT                                {ECO:0000250}.
FT   SITE        399    399       Contributes to redox potential value.
FT                                {ECO:0000250}.
FT   SITE        460    460       Lowers pKa of C-terminal Cys of second
FT                                active site. {ECO:0000250}.
FT   DISULFID     56     59       Redox-active. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   DISULFID    397    400       Redox-active. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   VAR_SEQ       1    306       Missing (in isoform D).
FT                                {ECO:0000303|Ref.5}.
FT                                /FTId=VSP_035858.
FT   CONFLICT    406    406       I -> T (in Ref. 5; AAO24936).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       349    474       iprf:THIOREDOXIN_2 [T]
FT   MYHIT        29    131       ipfam:Thioredoxin [T]
FT   MYHIT        10    134       iprf:THIOREDOXIN_2 [T]
FT   MYHIT       369    471       ipfam:Thioredoxin [T]
FT   MYHIT       389    407       ipat:THIOREDOXIN_1 [T]
FT   MYHIT        48     66       ipat:THIOREDOXIN_1 [T]
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
//