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Q38935 (FK151_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP15-1

Short name=PPIase FKBP15-1
EC=5.2.1.8
Alternative name(s):
15 kDa FK506-binding protein
Short name=15 kDa FKBP
FK506-binding protein 15-1
Short name=AtFKBP15-1
FK506-binding protein 2-1
Immunophilin FKBP15-1
Rotamase
Gene names
Name:FKBP15-1
Ordered Locus Names:At3g25220
ORF Names:MJL12.17
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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).

Subcellular location

Endoplasmic reticulum lumen Potential.

Sequence similarities

Belongs to the FKBP-type PPIase family.

Contains 1 PPIase FKBP-type domain.

Sequence caution

The sequence AAC49390.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAM65589.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 153128Peptidyl-prolyl cis-trans isomerase FKBP15-1
PRO_0000025508

Regions

Domain52 – 14089PPIase FKBP-type
Motif150 – 1534Prevents secretion from ER Potential

Experimental info

Sequence conflict721S → I in AAM65589. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q38935 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: 09549E647B738CD9

FASTA15316,355
        10         20         30         40         50         60 
MMSSASAMKA VGFLLLLTIL TLAYAKKSGD VTELQIGVKY KPQKCDLQAH KGDKIKVHYR 

        70         80         90        100        110        120 
GKLTDGTVFD SSFERGDPIE FELGTGQVIP GWDQGLLGAC VGEKRKLKIP SKLGYGDNGS 

       130        140        150 
PPKIPGGATL IFDTELVAVN GEPSSEAKSK NEL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of a FKBP-type immunophilin from higher plants."
Luan S., Kudla J., Gruissem W., Schreiber S.L.
Proc. Natl. Acad. Sci. U.S.A. 93:6964-6969(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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].
[6]"Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis."
He Z., Li L., Luan S.
Plant Physiol. 134:1248-1267(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52046 mRNA. Translation: AAC49390.1. Different initiation.
AB026647 Genomic DNA. Translation: BAB02081.1.
CP002686 Genomic DNA. Translation: AEE76994.1.
AY062776 mRNA. Translation: AAL32854.1.
AY128760 mRNA. Translation: AAM91160.1.
AY088043 mRNA. Translation: AAM65589.1. Different initiation.
PIRS71237.
RefSeqNP_566762.1. NM_113428.3.
UniGeneAt.6372.

3D structure databases

ProteinModelPortalQ38935.
SMRQ38935. Positions 47-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid7446. 5 interactions.
IntActQ38935. 5 interactions.
STRING3702.AT3G25220.1-P.

Proteomic databases

PaxDbQ38935.
PRIDEQ38935.

Protocols and materials databases

DNASU822115.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G25220.1; AT3G25220.1; AT3G25220.
GeneID822115.
KEGGath:AT3G25220.

Organism-specific databases

TAIRAT3G25220.

Phylogenomic databases

eggNOGCOG0545.
HOGENOMHOG000154887.
InParanoidQ38935.
KOK09569.
OMACLNEKRI.
PhylomeDBQ38935.
ProtClustDBCLSN2686604.

Enzyme and pathway databases

BioCycARA:AT3G25220-MONOMER.

Gene expression databases

GenevestigatorQ38935.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFK151_ARATH
AccessionPrimary (citable) accession number: Q38935
Secondary accession number(s): Q8LA41, Q9LSF4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: February 19, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names