P38911 (FKBP3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FK506-binding nuclear protein
EC=5.2.1.8

Alternative name(s):
FKBP-70
Nucleolar proline isomerase
Peptidyl-prolyl cis-trans isomerase
Short name=PPIase
Proline rotamase

Gene names

Name:	FPR3
Synonyms:	NPI46
Ordered Locus Names:	YML074C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. FK506- and rapamycin-binding protein. Specifically binds nuclear localization sequences. May be involved in the assembly or folding of ribosomal proteins.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by both FK506 and rapamycin.
Subunit structure	Interacts with NOP53. Ref.9
Subcellular location	Nucleus › nucleolus.
Post-translational modification	Phosphorylated at tyrosine and dephosphorylated by the phosphotyrosine-specific phosphoprotein phosphatase PTP1. Ref.7
Miscellaneous	Present with 9490 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily. Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
Cellular component	Nucleus
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone peptidyl-prolyl isomerization Inferred from Biological aspect of Ancestor. Source: RefGenome meiotic recombination checkpoint Inferred from mutant phenotype PubMed 16179256. Source: SGD protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	membrane Inferred from Biological aspect of Ancestor. Source: RefGenome nucleolus Inferred from direct assay Ref.3Ref.2. Source: SGD
Molecular_function	FK506 binding Inferred from Biological aspect of Ancestor. Source: RefGenome peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.3Ref.1Ref.2. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 411	411	FK506-binding nuclear protein		PRO_0000075313
Regions
	Domain	324 – 411	88	PPIase FKBP-type
	Motif	256 – 271	16	Nuclear localization signal Potential
	Compositional bias	60 – 87	28	Asp/Glu-rich (highly acidic)
	Compositional bias	88 – 99	12	Lys-rich (highly basic)
	Compositional bias	101 – 119	19	Asp/Glu-rich (highly acidic)
	Compositional bias	173 – 248	76	Asp/Glu-rich (highly acidic)
	Compositional bias	250 – 298	49	Lys-rich (highly basic)
Amino acid modifications
	Modified residue	80	1	Phosphoserine Ref.10 Ref.11
	Modified residue	81	1	Phosphoserine Ref.10 Ref.11
	Modified residue	184	1	Phosphotyrosine; by CK2 Ref.7
	Modified residue	186	1	Phosphoserine; by CK2 Ref.7
Experimental info
	Sequence conflict	122	1	L → P in AAB04165. Ref.1
	Sequence conflict	240	1	E → EEE Ref.1
	Sequence conflict	335	1	L → F in AAB04165. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38911 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: A01D24DE0078FE11	FASTA	411	46,553
	10 20 30 40 50 60 MSDLLPLATY SLNVEPYTPV PAIDVTMPIT VRITMAALNP EAIDEENKPS TLRIIKRNPD 70 80 90 100 110 120 FEDDDFLGGD FDEDEIDEES SEEEEEEKTQ KKKKSKGKKA ESESEDDEED DDEDDEFQES 130 140 150 160 170 180 VLLTLSPEAQ YQQSLDLTIT PEEEVQFIVT GSYAISLSGN YVKHPFDTPM GVEGEDEDED 190 200 210 220 230 240 ADIYDSEDYD LTPDEDEIIG DDMDDLDDEE EEEVRIEEVQ EEDEEDNDGE EEQEEEEEEE 250 260 270 280 290 300 QKEEVKPEPK KSKKEKKRKH EEKEEEKKAK KVKKVEFKKD LEEGPTKPKS KKEQDKHKPK 310 320 330 340 350 360 SKVLEGGIVI EDRTIGDGPQ AKRGARVGMR YIGKLKNGKV FDKNTSGKPF AFKLGRGEVI 370 380 390 400 410 KGWDIGVAGM SVGGERRIII PAPYAYGKQA LPGIPANSEL TFDVKLVSMK N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification of FKBP-70, a novel immunophilin from Saccharomyces cerevisiae, and cloning of its structural gene, FPR3." Manning-Krieg U.C., Henriquez R., Cammas F., Graff P., Gaveriaux S., Movva N.R. FEBS Lett. 352:98-103(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Yeast NPI46 encodes a novel prolyl cis-trans isomerase that is located in the nucleolus." Shan X., Xue Z., Melese T. J. Cell Biol. 126:853-862(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus." Benton B.M., Zang J.-H., Thorner J. J. Cell Biol. 127:623-639(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: YNN 214.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[7]	"Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3." Wilson L.K., Dhillon N., Thorner J., Martin G.S. J. Biol. Chem. 272:12961-12967(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-184 AND SER-186.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein." Sydorskyy Y., Dilworth D.J., Halloran B., Yi E.C., Makhnevych T., Wozniak R.W., Aitchison J.D. Biochem. J. 388:819-826(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NOP53, MASS SPECTROMETRY.
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-81, MASS SPECTROMETRY. Strain: ADR376.
[11]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-81, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L34569 Genomic DNA. Translation: AAB04165.1. X79379 Genomic DNA. Translation: CAA55924.1. S73876 Genomic DNA. Translation: AAB31995.1. Z46373 Genomic DNA. Translation: CAA86504.1. AY693136 Genomic DNA. Translation: AAT93155.1. BK006946 Genomic DNA. Translation: DAA09823.1.
PIR	S48647.
RefSeq	NP_013637.1. NM_001182433.1.
3D structure databases
ProteinModelPortal	P38911.
SMR	P38911. Positions 295-410.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6578N.
IntAct	P38911. 59 interactions.
MINT	MINT-673400.
STRING	4932.YML074C.
Proteomic databases
PaxDb	P38911.
PeptideAtlas	P38911.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML074C; YML074C; YML074C.
GeneID	854901.
KEGG	sce:YML074C.
Organism-specific databases
CYGD	YML074c.
SGD	S000004539. FPR3.
Phylogenomic databases
eggNOG	COG0545.
GeneTree	ENSGT00680000100845.
HOGENOM	HOG000216214.
KO	K14826.
OMA	NTVAMRY.
OrthoDB	EOG4VT96G.
Gene expression databases
Genevestigator	P38911.
GermOnline	YML074C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR026257. FK506_BP. IPR023566. PPIase_FKBP. IPR001179. PPIase_FKBP_dom. [Graphical view]
PANTHER	PTHR10516. PTHR10516. 1 hit.
Pfam	PF00254. FKBP_C. 1 hit. [Graphical view]
PIRSF	PIRSF001473. FK506-bp_FPR3. 1 hit.
PROSITE	PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977879.

Entry information

Entry name

FKBP3_YEAST

Accession

Primary (citable) accession number: P38911
Secondary accession number(s): D6W0K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program