Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8LGG0 (FKB12_ARATH)

Last modified November 3, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl isomerase FKBP12
    EC=5.2.1.8
Alternative name(s):
    12 kDa FK506-binding protein
      Short name=12 kDa FKBP
    FKBP-12
    Immunophilin FKBP12
      Short name=AtFKBP12
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
Gene names
Name: FKBP12
Ordered Locus Names: At5g64350
ORF Names: MSJ1.19
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length112 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 By similarity.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Subunit structure

Interacts with FIP37 and with the immunosuppressive drug FK506. Its interaction with FIP37 is inhibited by FK506. Ref.5

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP1 subfamily.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding Ref.5

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FIP37Q9ZSZ83EBI-1641228,EBI-1641243

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 112112Peptidyl-prolyl isomerase FKBP12
PRO_0000075300

Regions

Domain19 – 11294PPIase FKBP-type

Amino acid modifications

Disulfide bond26 ↔ 80 By similarity

Experimental info

Sequence conflict1111V → L in AAM60880. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8LGG0-1 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: C0ED5DFEB6C8E1E2

FASTA11211,988
        10         20         30         40         50         60 
MGVEKQVIRP GNGPKPAPGQ TVTVHCTGFG KDGDLSQKFW STKDEGQKPF SFQIGKGAVI 

        70         80         90        100        110 
KGWDEGVIGM QIGEVARLRC SSDYAYGAGG FPAWGIQPNS VLDFEIEVLS VQ 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of a plant FKBP12 that does not mediate action of FK506 and rapamycin."
Xu Q., Liang S., Kudla J., Luan S.
Plant J. 15:511-519(1998) [PubMed: 9753776] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:401-414(1997) [PubMed: 9501997] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"An Arabidopsis immunophilin, AtFKBP12, binds to AtFIP37 (FKBP interacting protein) in an interaction that is disrupted by FK506."
Faure J.-D., Gingerich D., Howell S.H.
Plant J. 15:783-789(1998) [PubMed: 9807817] [Abstract]
Cited for: INTERACTION WITH FIP37 AND FK506.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

U96924 mRNA. Translation: AAB57847.1.
AB008268 Genomic DNA. Translation: BAB09866.1.
AY059928 mRNA. Translation: AAL24410.1.
AY081564 mRNA. Translation: AAM10126.1.
AY084289 mRNA. Translation: AAM60880.1.
IPIIPI00525181.
RefSeqNP_201240.1.
UniGeneAt.24046

3D structure databases

HSSPHSSP built from PDB template 1KT1 based on UniProtKB Q9XSH5.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8LGG0. 1 interaction.
STRINGQ8LGG0.

Proteomic databases

PRIDEQ8LGG0.

Genome annotation databases

GeneID836556.
GenomeReviewsGene locus AT5G64350 in contig BA000015_GR.
KEGGath:AT5G64350.
NMPDRfig|3702.1.peg.28495.

Organism-specific databases

GeneFarm5056.
TAIRAt5g64350.

Phylogenomic databases

OMAGYLYDES.

Enzyme and pathway databases

BRENDA5.2.1.8. 302.

Gene expression databases

GenevestigatorQ8LGG0.
GermOnlineAT5G64350. Arabidopsis thaliana.

Family and domain databases

InterProIPR001179. PPIase_FKBP.
[Graphical view]
PANTHERPTHR10516. PPIase_FKBP. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFKB12_ARATH
AccessionPrimary (citable) accession number: Q8LGG0
Secondary accession number(s): O04263
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: November 3, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents