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39 kDa FK506-binding nuclear protein (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase)

 FKB39_DROME             Reviewed;         357 AA.
P54397; Q9VF88;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
05-DEC-2018, entry version 154.
RecName: Full=39 kDa FK506-binding nuclear protein;
EC=5.2.1.8;
AltName: Full=Peptidyl-prolyl cis-trans isomerase;
Short=PPIase;
AltName: Full=Rotamase;
Name=FK506-bp1; Synonyms=FKBP39; ORFNames=CG6226;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Canton-S;
PubMed=7538962; DOI=10.1016/0378-1119(95)00019-3;
Theopold U., Dal Zotto L., Hultmark D.;
"FKBP39, a Drosophila member of a family of proteins that bind the
immunosuppressive drug FK506.";
Gene 156:247-251(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-197, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: PPIases accelerate the folding of proteins. May function
in a signal transduction cascade during early development.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-peptidylproline (omega=180) = [protein]-
peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
ChEBI:CHEBI:83834; EC=5.2.1.8;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed, highest levels in
ovary.
-!- DEVELOPMENTAL STAGE: Expressed during all stages of development
with highest expression in early embryo.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
{ECO:0000305}.
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EMBL; Z46894; CAA86996.1; -; mRNA.
EMBL; AE014297; AAF55171.2; -; Genomic_DNA.
EMBL; AY094814; AAM11167.1; -; mRNA.
PIR; JC4090; JC4090.
RefSeq; NP_524364.2; NM_079640.3.
UniGene; Dm.1208; -.
PDB; 4CA9; NMR; -; A/B/C/D/E=3-92.
PDBsum; 4CA9; -.
ProteinModelPortal; P54397; -.
SMR; P54397; -.
BioGrid; 66923; 85.
DIP; DIP-22384N; -.
IntAct; P54397; 6.
STRING; 7227.FBpp0082574; -.
iPTMnet; P54397; -.
PaxDb; P54397; -.
PRIDE; P54397; -.
EnsemblMetazoa; FBtr0083120; FBpp0082574; FBgn0013269.
GeneID; 41860; -.
KEGG; dme:Dmel_CG6226; -.
CTD; 41860; -.
FlyBase; FBgn0013269; FK506-bp1.
eggNOG; KOG0552; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00940000174423; -.
InParanoid; P54397; -.
KO; K14826; -.
OMA; MSMFWGL; -.
OrthoDB; EOG091G02W1; -.
PhylomeDB; P54397; -.
GenomeRNAi; 41860; -.
PRO; PR:P54397; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0013269; Expressed in 61 organ(s), highest expression level in eye disc (Drosophila).
Genevisible; P54397; DM.
GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005528; F:FK506 binding; IDA:FlyBase.
GO; GO:0070594; F:juvenile hormone response element binding; IDA:FlyBase.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
GO; GO:0035626; P:juvenile hormone mediated signaling pathway; IMP:FlyBase.
GO; GO:0010507; P:negative regulation of autophagy; IMP:FlyBase.
GO; GO:0016242; P:negative regulation of macroautophagy; IMP:FlyBase.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
Pfam; PF00254; FKBP_C; 1.
PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Isomerase; Nucleus; Phosphoprotein;
Reference proteome; Rotamase.
CHAIN 1 357 39 kDa FK506-binding nuclear protein.
/FTId=PRO_0000075310.
DOMAIN 269 357 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
COMPBIAS 89 99 Asp/Glu-rich (highly acidic).
COMPBIAS 119 183 Asp/Glu-rich (highly acidic).
COMPBIAS 186 247 Lys-rich (basic).
MOD_RES 92 92 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 187 187 A -> R (in Ref. 1; CAA86996).
{ECO:0000305}.
STRAND 3 9 {ECO:0000244|PDB:4CA9}.
STRAND 14 18 {ECO:0000244|PDB:4CA9}.
STRAND 23 42 {ECO:0000244|PDB:4CA9}.
STRAND 45 56 {ECO:0000244|PDB:4CA9}.
STRAND 63 65 {ECO:0000244|PDB:4CA9}.
STRAND 69 88 {ECO:0000244|PDB:4CA9}.
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


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