FKB39_DROME
ID FKB39_DROME Reviewed; 357 AA.
AC P54397; Q9VF88;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=39 kDa FK506-binding nuclear protein;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
GN Name=FK506-bp1; Synonyms=FKBP39; ORFNames=CG6226;
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].
RC STRAIN=Canton-S;
RX PubMed=7538962; DOI=10.1016/0378-1119(95)00019-3;
RA Theopold U., Dal Zotto L., Hultmark D.;
RT "FKBP39, a Drosophila member of a family of proteins that bind the
RT immunosuppressive drug FK506.";
RL Gene 156:247-251(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.
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].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-197, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. May function in a
CC signal transduction cascade during early development.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, highest levels in ovary.
CC -!- DEVELOPMENTAL STAGE: Expressed during all stages of development with
CC highest expression in early embryo.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
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DR EMBL; Z46894; CAA86996.1; -; mRNA.
DR EMBL; AE014297; AAF55171.2; -; Genomic_DNA.
DR EMBL; AY094814; AAM11167.1; -; mRNA.
DR PIR; JC4090; JC4090.
DR RefSeq; NP_524364.2; NM_079640.3.
DR PDB; 4CA9; NMR; -; A/B/C/D/E=3-92.
DR PDBsum; 4CA9; -.
DR AlphaFoldDB; P54397; -.
DR BMRB; P54397; -.
DR SASBDB; P54397; -.
DR SMR; P54397; -.
DR BioGRID; 66923; 85.
DR DIP; DIP-22384N; -.
DR IntAct; P54397; 6.
DR STRING; 7227.FBpp0082574; -.
DR iPTMnet; P54397; -.
DR PaxDb; P54397; -.
DR PRIDE; P54397; -.
DR DNASU; 41860; -.
DR EnsemblMetazoa; FBtr0083120; FBpp0082574; FBgn0013269.
DR GeneID; 41860; -.
DR KEGG; dme:Dmel_CG6226; -.
DR CTD; 41860; -.
DR FlyBase; FBgn0013269; FK506-bp1.
DR VEuPathDB; VectorBase:FBgn0013269; -.
DR eggNOG; KOG0552; Eukaryota.
DR GeneTree; ENSGT00940000174423; -.
DR HOGENOM; CLU_022297_0_0_1; -.
DR InParanoid; P54397; -.
DR OMA; CPPHMAY; -.
DR OrthoDB; 402681at2759; -.
DR PhylomeDB; P54397; -.
DR SignaLink; P54397; -.
DR BioGRID-ORCS; 41860; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41860; -.
DR PRO; PR:P54397; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0013269; Expressed in eye disc (Drosophila) and 59 other tissues.
DR Genevisible; P54397; DM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005528; F:FK506 binding; IDA:FlyBase.
DR GO; GO:0070594; F:juvenile hormone response element binding; IDA:FlyBase.
DR GO; GO:0005527; F:macrolide binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0035626; P:juvenile hormone mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:FlyBase.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:FlyBase.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR041232; NPL.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR023566; PPIase_Fpr3/Fpr4-like.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF17800; NPL; 1.
DR PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Nucleus; Phosphoprotein; Reference proteome;
KW Rotamase.
FT CHAIN 1..357
FT /note="39 kDa FK506-binding nuclear protein"
FT /id="PRO_0000075310"
FT DOMAIN 269..357
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 113..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 187
FT /note="A -> R (in Ref. 1; CAA86996)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4CA9"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:4CA9"
FT STRAND 23..42
FT /evidence="ECO:0007829|PDB:4CA9"
FT STRAND 45..56
FT /evidence="ECO:0007829|PDB:4CA9"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4CA9"
FT STRAND 69..88
FT /evidence="ECO:0007829|PDB:4CA9"
SQ SEQUENCE 357 AA; 39344 MW; EF0AB7831738BB30 CRC64;
MSMFWGLNMK PERKYSQTII KSFHISGVAL DKGQEAKLYL AAEKQEYIVA TVTKAIPQVA
LDLNFSKGDR IMFYTAGDAS VSLLGYLHDI DSEDDEDDDQ MTIENLLNSK AIKNSKKSED
DEDENESGEE DEEDTDDDSQ IIEEYESFLE NGEEEDDDDV DEDNEESGEE DEQDSDDSEA
EEEQPKAKVA KLSPGASAKK SGKEQNGVAK KEEAKQQQKK KEKPEAKKEQ PKAKEPAKQQ
PASKDPRTIT GGVKIVDQVV GKGEEAKQGK RVSVYYIGRL QSNNKTFDSL LKGKPFKFAL
GGGEVIKGWD VGVAGMKVGG KRVITCPPHM AYGARGAPPK IGPNSTLVFE VELKAVH
