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Q38935

- FK151_ARATH

UniProt

Q38935 - FK151_ARATH

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Protein

Peptidyl-prolyl cis-trans isomerase FKBP15-1

Gene

FKBP15-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. FK506 binding Source: RefGenome
  2. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome

GO - Biological processi

  1. peptidyl-proline modification Source: RefGenome
  2. protein folding Source: UniProtKB-KW
  3. protein peptidyl-prolyl isomerization Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciARA:AT3G25220-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP15-1 (EC:5.2.1.8)
Short name:
PPIase FKBP15-1
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 namesi
Name:FKBP15-1
Ordered Locus Names:At3g25220
ORF Names:MJL12.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G25220.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: TAIR
  2. membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 153128Peptidyl-prolyl cis-trans isomerase FKBP15-1PRO_0000025508Add
BLAST

Proteomic databases

PaxDbiQ38935.
PRIDEiQ38935.

Expressioni

Gene expression databases

GenevestigatoriQ38935.

Interactioni

Protein-protein interaction databases

BioGridi7446. 5 interactions.
IntActiQ38935. 7 interactions.
STRINGi3702.AT3G25220.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ38935.
SMRiQ38935. Positions 47-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 14089PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi150 – 1534Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the FKBP-type PPIase family.Curated
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0545.
HOGENOMiHOG000154887.
InParanoidiQ38935.
KOiK09569.
OMAiCLNEKRI.
PhylomeDBiQ38935.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q38935-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMSSASAMKA VGFLLLLTIL TLAYAKKSGD VTELQIGVKY KPQKCDLQAH
60 70 80 90 100
KGDKIKVHYR GKLTDGTVFD SSFERGDPIE FELGTGQVIP GWDQGLLGAC
110 120 130 140 150
VGEKRKLKIP SKLGYGDNGS PPKIPGGATL IFDTELVAVN GEPSSEAKSK

NEL
Length:153
Mass (Da):16,355
Last modified:September 19, 2002 - v2
Checksum:i09549E647B738CD9
GO

Sequence cautioni

The sequence AAC49390.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAM65589.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721S → I in AAM65589. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS71237.
RefSeqiNP_566762.1. NM_113428.3.
UniGeneiAt.6372.

Genome annotation databases

EnsemblPlantsiAT3G25220.1; AT3G25220.1; AT3G25220.
GeneIDi822115.
KEGGiath:AT3G25220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRi S71237.
RefSeqi NP_566762.1. NM_113428.3.
UniGenei At.6372.

3D structure databases

ProteinModelPortali Q38935.
SMRi Q38935. Positions 47-139.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 7446. 5 interactions.
IntActi Q38935. 7 interactions.
STRINGi 3702.AT3G25220.1-P.

Proteomic databases

PaxDbi Q38935.
PRIDEi Q38935.

Protocols and materials databases

DNASUi 822115.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G25220.1 ; AT3G25220.1 ; AT3G25220 .
GeneIDi 822115.
KEGGi ath:AT3G25220.

Organism-specific databases

TAIRi AT3G25220.

Phylogenomic databases

eggNOGi COG0545.
HOGENOMi HOG000154887.
InParanoidi Q38935.
KOi K09569.
OMAi CLNEKRI.
PhylomeDBi Q38935.

Enzyme and pathway databases

BioCyci ARA:AT3G25220-MONOMER.

Gene expression databases

Genevestigatori Q38935.

Family and domain databases

InterProi IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view ]
PANTHERi PTHR10516. PTHR10516. 1 hit.
Pfami PF00254. FKBP_C. 1 hit.
[Graphical view ]
PROSITEi PS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiFK151_ARATH
AccessioniPrimary (citable) accession number: Q38935
Secondary accession number(s): Q8LA41, Q9LSF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: October 29, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3