Q4IN00 (FKBP2_GIBZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FK506-binding protein 2
EC=5.2.1.8

Alternative name(s):
Peptidyl-prolyl cis-trans isomerase
Short name=PPIase
Rotamase

Gene names

Name:	FPR2
ORF Names:	FGSG_01408

Organism

Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum) [Reference proteome]

Taxonomic identifier

229533 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Gibberella › Gibberella zeae

Protein attributes

Sequence length	195 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by both FK506 and rapamycin By similarity.
Subcellular location	Endoplasmic reticulum By similarity.
Sequence similarities	Belongs to the FKBP-type PPIase family. FKBP2 subfamily. Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Isomerase Rotamase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 195	176	FK506-binding protein 2		PRO_0000233069
Regions
	Domain	39 – 127	89	PPIase FKBP-type
	Motif	192 – 195	4	Prevents secretion from ER Potential

Sequences

	Sequence		Length	Mass (Da)
	Q4IN00 [UniParc]. Last modified April 18, 2006. Version 2. Checksum: 4CDDCC233DFCBF51	FASTA	195	20,421
	10 20 30 40 50 60 MKAALFLSAL ASTAVGVVAE ELKIDVTLPV ICERKTQKGD GVHMHYRGTL KDSGKQFDAS 70 80 90 100 110 120 YDRGTPLSFK VGAGQVIKGW DEGLLDMCIG EKRVLTIPPE FGYGQRAIGP IPAGSTLVFE 130 140 150 160 170 180 TELVGIDGVP KPEKIETKVV EGAESAAEAI SEATEAAATA SQKVAGKVAE AIVDAAKAAK 190 TIIADTDDAP EHEEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization." Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S. , Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C. Science 317:1400-1402(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.
[2]	"Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium." Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E. , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M. Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.
[3]	"Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires." Pemberton T.J. BMC Genomics 7:244-244(2006) [PubMed] [Europe PMC] [Abstract] Cited for: REVISION OF GENE MODEL.

Cross-references

3D structure databases
ProteinModelPortal	Q4IN00.
ModBase	Search...
Protein-protein interaction databases
STRING	5518.FG01408.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	FGSG_01408T0; FGSG_01408P0; FGSG_01408.
Phylogenomic databases
eggNOG	COG0545.
Family and domain databases
InterPro	IPR023566. PPIase_FKBP. IPR001179. PPIase_FKBP_dom. [Graphical view]
PANTHER	PTHR10516. PTHR10516. 1 hit.
Pfam	PF00254. FKBP_C. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FKBP2_GIBZE

Accession

Primary (citable) accession number: Q4IN00

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	April 18, 2006
Last modified:	April 3, 2013
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program