FKB59_DROME
ID FKB59_DROME Reviewed; 439 AA.
AC Q9VL78; Q9U4N1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=FK506-binding protein 59 {ECO:0000312|FlyBase:FBgn0029174};
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
DE AltName: Full=dFKBP59;
GN Name=Fkbp59 {ECO:0000312|FlyBase:FBgn0029174};
GN ORFNames=CG4535 {ECO:0000312|FlyBase:FBgn0029174};
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] {ECO:0000305, ECO:0000312|EMBL:AAF18387.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAF18387.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:10767531};
RX PubMed=10767531; DOI=10.1016/s0378-1119(00)00058-5;
RA Zaffran S.;
RT "Molecular cloning and embryonic expression of dFKBP59, a novel Drosophila
RT FK506-binding protein.";
RL Gene 246:103-109(2000).
RN [2] {ECO:0000312|EMBL:AAF52818.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF52818.1}
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] {ECO:0000312|EMBL:AAL13958.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL13958.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH INAD AND TRPL.
RX PubMed=11514552; DOI=10.1074/jbc.m104125200;
RA Goel M., Garcia R., Estacion M., Schilling W.P.;
RT "Regulation of Drosophila TRPL channels by immunophilin FKBP59.";
RL J. Biol. Chem. 276:38762-38773(2001).
CC -!- FUNCTION: May have a role in phototransduction; inhibits or prevents
CC Ca(2+) induced stimulation of the trpl ion channel.
CC {ECO:0000269|PubMed:11514552}.
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; Evidence={ECO:0000255};
CC -!- SUBUNIT: Interacts with inaD and trpl, and may be part of the inaD
CC signaling complex. {ECO:0000269|PubMed:11514552}.
CC -!- TISSUE SPECIFICITY: Expression in the embryo is limited to three
CC tissues: lymph glands, Garland cells and oenocyte cells.
CC {ECO:0000269|PubMed:10767531}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. First
CC expressed at a high level in 0-2 hours embryos. Expression then
CC gradually increases through the end of embryogenesis and laval
CC development. Detected at lower levels in third-instar larvae and pupal
CC stages. Expressed at a high level in adult females and at a lower level
CC in adult males. {ECO:0000269|PubMed:10767531}.
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DR EMBL; AF163664; AAF18387.1; -; mRNA.
DR EMBL; AE014134; AAF52818.1; -; Genomic_DNA.
DR EMBL; AY058729; AAL13958.1; -; mRNA.
DR RefSeq; NP_001285784.1; NM_001298855.1.
DR RefSeq; NP_524895.2; NM_080156.4.
DR AlphaFoldDB; Q9VL78; -.
DR SMR; Q9VL78; -.
DR BioGRID; 70920; 8.
DR IntAct; Q9VL78; 3.
DR STRING; 7227.FBpp0079468; -.
DR PaxDb; Q9VL78; -.
DR PRIDE; Q9VL78; -.
DR DNASU; 47762; -.
DR EnsemblMetazoa; FBtr0079872; FBpp0079468; FBgn0029174.
DR EnsemblMetazoa; FBtr0342837; FBpp0309663; FBgn0029174.
DR GeneID; 47762; -.
DR KEGG; dme:Dmel_CG4535; -.
DR CTD; 47762; -.
DR FlyBase; FBgn0029174; Fkbp59.
DR VEuPathDB; VectorBase:FBgn0029174; -.
DR eggNOG; KOG0543; Eukaryota.
DR HOGENOM; CLU_013615_13_1_1; -.
DR InParanoid; Q9VL78; -.
DR OMA; ELEMLGW; -.
DR OrthoDB; 897391at2759; -.
DR PhylomeDB; Q9VL78; -.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-3371568; Attenuation phase.
DR Reactome; R-DME-8939211; ESR-mediated signaling.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR SignaLink; Q9VL78; -.
DR BioGRID-ORCS; 47762; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 47762; -.
DR PRO; PR:Q9VL78; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0029174; Expressed in embryonic/larval hemocyte (Drosophila) and 38 other tissues.
DR ExpressionAtlas; Q9VL78; baseline and differential.
DR Genevisible; Q9VL78; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016027; C:inaD signaling complex; IPI:UniProtKB.
DR GO; GO:0005528; F:FK506 binding; ISS:FlyBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IPI:UniProtKB.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:FlyBase.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 2.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00254; FKBP_C; 2.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Isomerase; Reference proteome; Repeat; Rotamase; Sensory transduction;
KW TPR repeat; Vision.
FT CHAIN 1..439
FT /note="FK506-binding protein 59"
FT /id="PRO_0000075312"
FT DOMAIN 32..120
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 149..235
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 252..285
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 297..330
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 331..364
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT CONFLICT 67
FT /note="N -> E (in Ref. 1; AAF18387)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="I -> V (in Ref. 1; AAF18387)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="H -> P (in Ref. 1; AAF18387)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="L -> W (in Ref. 1; AAF18387)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="V -> F (in Ref. 1; AAF18387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 48795 MW; 5D08DBB1569B42F8 CRC64;
MPEGNKIDLS GDGGVLKEIL KEGTGTETPH SGCTVSLHYT GRLVDGTEFD SSLSRNEPFE
FSLGKGNVIK AFDMGVATMK LGERCFLTCA PNYAYGAAGS PPAIPPDATL IFELEMLGWK
GEDLSPNQDG SIDRTILEAS DKKRTPSDGA FVKAHISGSF EGRVFEDRDV EFDYGEGKAI
GIIDGVEIAL EKMNVGETSR IKIQAKYAFG AKGNEEFKIP PNATVEYTVK LVDCGKGLEE
WKLSDEERLA EAKVYKEKGT NYFKKENWAL AIKMYTKCKN ILPTTVHTNE EVKKIKVATH
SNIALCHQKS NDHFEAKQEC NEVLALDKNN VKALYRRGQC NLTINELEDA LEDFQKVIQL
EPGNKAAANQ VIICKQKLKE SKNKEKKLYA NMFTKLAAND KETEPPRETD VLSKCGEWSE
EDAKREAELT LERDNIIMI
