Reviewed, UniProtKB/Swiss-Prot P48375 (FKB12_DROME)

Names and origin

Protein names

Recommended name:
    12 kDa FK506-binding protein
      Short name=FKBP
    EC=5.2.1.8
Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
    Macrolide-binding protein

Gene names

Name:	FK506-bp2
Synonyms:	FKBP12
ORF Names:	CG11001

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	108 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Binds to ligand-free TGF beta type I receptor, from which it is released upon a ligand-induced, type II receptor mediated phosphorylation of the type I receptor. Binding is inhibitory to the signaling pathways of the TGF beta family ligands. Ref.2
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subcellular location	Cytoplasm. Ref.2
Sequence similarities	Belongs to the FKBP-type PPIase family. FKBP1 subfamily. Contains 1 PPIase FKBP-type domain.
Sequence caution	The sequence AAL48728.1 differs from that shown. Reason: Frameshift at position 108.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase Rotamase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to DNA damage stimulus Inferred from mutant phenotype. Source: FlyBase protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q95RR8	1	EBI-122903,EBI-119468

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 108	108	12 kDa FK506-binding protein		PRO_0000075299
Regions
	Domain	20 – 108	89	PPIase FKBP-type
Experimental info
	Sequence conflict	72	1	R → S Ref.1
	Sequence conflict	72	1	R → S Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P48375-1 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 48BCF993AD262FBA	FASTA	108	11,666
	10 20 30 40 50 60 MGVQVVPIAP GDGSTYPKNG QKVTVHYTGT LDDGTKFDSS RDRNKPFKFT IGKGEVIRGW 70 80 90 100 DEGVAQLSVG QRAKLICSPD YAYGSRGHPG VIPPNSTLTF DVELLKVE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Drosophila homologue of FKBP-12." Mounsey A. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Canton-S. Tissue: Head.
[2]	"The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors." Wang T., Li B.Y., Danielson P.D., Shah P.C., Rockwell S., Lechleider R.J., Martin J., Manganaro T., Donahoe P.K. Cell 86:435-444(1996) [PubMed: 8756725] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[3]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	"A Drosophila full-length cDNA resource." 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. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49079 mRNA. Translation: CAA88904.1. U41441 Genomic DNA. Translation: AAA91178.1. AE013599 Genomic DNA. Translation: AAF57582.1. AY071106 mRNA. Translation: AAL48728.1. Frameshift.
PIR	S54139.
RefSeq	NP_523792.2.
UniGene	Dm.2572
3D structure databases
HSSP	HSSP built from PDB template 1FKL based on UniProtKB P18203.
SMR	P48375. Positions 2-108.
ModBase	Search...
Protein-protein interaction databases
IntAct	P48375. 13 interactions.
STRING	P48375.
Genome annotation databases
Ensembl	FBtr0086515; FBpp0085703; FBgn0013954; Drosophila melanogaster. [Genome view]
GeneID	37214.
KEGG	dme:Dmel_CG11001.
NMPDR	fig|7227.3.peg.6318.
Organism-specific databases
CTD	37214.
FlyBase	FBgn0013954. FK506-bp2.
Phylogenomic databases
HOGENOM	P48375.
OMA	SVDRGSP.
Enzyme and pathway databases
BRENDA	5.2.1.8. 48.
Gene expression databases
GermOnline	CG11001. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001179. PPIase_FKBP. [Graphical view]
PANTHER	PTHR10516. PPIase_FKBP. 1 hit.
Pfam	PF00254. FKBP_C. 1 hit. [Graphical view]
PROSITE	PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	802551.

Entry information

Entry name

FKB12_DROME

Accession

Primary (citable) accession number: P48375
Secondary accession number(s): Q8SZ56, Q9V8S8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	August 30, 2005
Last modified:	November 3, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project