FKB12_DROME
ID FKB12_DROME Reviewed; 108 AA.
AC P48375; Q8SZ56; Q9V8S8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase Fkbp12 {ECO:0000303|PubMed:8756725, ECO:0000312|FlyBase:FBgn0013954};
DE Short=PPIase Fkbp12 {ECO:0000303|PubMed:8756725};
DE EC=5.2.1.8;
DE AltName: Full=12 kDa FK506-binding protein {ECO:0000305};
DE Short=12 kDa FKBP {ECO:0000305};
DE AltName: Full=Macrolide-binding protein;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
GN Name=Fkbp12 {ECO:0000303|PubMed:8756725, ECO:0000312|FlyBase:FBgn0013954};
GN Synonyms=FK506-bp2 {ECO:0000312|FlyBase:FBgn0013954};
GN ORFNames=CG11001 {ECO:0000312|FlyBase:FBgn0013954};
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; TISSUE=Head;
RA Mounsey A.;
RT "Drosophila homologue of FKBP-12.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8756725; DOI=10.1016/s0092-8674(00)80116-6;
RA Wang T., Li B.Y., Danielson P.D., Shah P.C., Rockwell S., Lechleider R.J.,
RA Martin J., Manganaro T., Donahoe P.K.;
RT "The immunophilin FKBP12 functions as a common inhibitor of the TGF beta
RT family type I receptors.";
RL Cell 86:435-444(1996).
RN [3]
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 [4]
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 [5]
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).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Binds to ligand-free TGF beta type I receptor, from
CC which it is released upon a ligand-induced, type II receptor mediated
CC phosphorylation of the type I receptor. Binding is inhibitory to the
CC signaling pathways of the TGF beta family ligands.
CC {ECO:0000269|PubMed:8756725}.
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: Cytoplasm {ECO:0000269|PubMed:8756725}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48728.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z49079; CAA88904.1; -; mRNA.
DR EMBL; U41441; AAA91178.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57582.1; -; Genomic_DNA.
DR EMBL; AY071106; AAL48728.1; ALT_FRAME; mRNA.
DR PIR; S54139; S54139.
DR RefSeq; NP_523792.2; NM_079068.5.
DR AlphaFoldDB; P48375; -.
DR SMR; P48375; -.
DR BioGRID; 62878; 72.
DR IntAct; P48375; 1.
DR STRING; 7227.FBpp0085703; -.
DR PaxDb; P48375; -.
DR PRIDE; P48375; -.
DR DNASU; 37214; -.
DR EnsemblMetazoa; FBtr0086515; FBpp0085703; FBgn0013954.
DR GeneID; 37214; -.
DR KEGG; dme:Dmel_CG11001; -.
DR CTD; 37214; -.
DR FlyBase; FBgn0013954; Fkbp12.
DR VEuPathDB; VectorBase:FBgn0013954; -.
DR eggNOG; KOG0544; Eukaryota.
DR GeneTree; ENSGT00940000153311; -.
DR HOGENOM; CLU_013615_12_1_1; -.
DR InParanoid; P48375; -.
DR OMA; GQTFPKT; -.
DR OrthoDB; 1328688at2759; -.
DR PhylomeDB; P48375; -.
DR Reactome; R-DME-166208; mTORC1-mediated signalling.
DR Reactome; R-DME-2025928; Calcineurin activates NFAT.
DR SignaLink; P48375; -.
DR BioGRID-ORCS; 37214; 1 hit in 3 CRISPR screens.
DR ChiTaRS; FK506-bp2; fly.
DR GenomeRNAi; 37214; -.
DR PRO; PR:P48375; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0013954; Expressed in cleaving embryo and 28 other tissues.
DR ExpressionAtlas; P48375; baseline and differential.
DR Genevisible; P48375; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:FlyBase.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IPI:FlyBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:FlyBase.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..108
FT /note="Peptidyl-prolyl cis-trans isomerase Fkbp12"
FT /id="PRO_0000075299"
FT DOMAIN 20..108
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 72
FT /note="R -> S (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 108 AA; 11666 MW; 48BCF993AD262FBA CRC64;
MGVQVVPIAP GDGSTYPKNG QKVTVHYTGT LDDGTKFDSS RDRNKPFKFT IGKGEVIRGW
DEGVAQLSVG QRAKLICSPD YAYGSRGHPG VIPPNSTLTF DVELLKVE
