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Reviewed, UniProtKB/Swiss-Prot Q9LEK8 (PIN1_DIGLA)

Last modified January 19, 2010. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase 1
    EC=5.2.1.8
Alternative name(s):
    Rotamase Pin1
    PPIase Pin1
    DlPar13
Gene names
Name: PARV12.8
OrganismDigitalis lanata (Foxglove)
Taxonomic identifier49450 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsLamialesPlantaginaceaeDigitalideaeDigitalis

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds. Ref.1

Catalytic activity

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

Enzyme regulation

Inhibited in vitro by juglone.

Subcellular location

Cytoplasm. Nucleus Ref.1.

Tissue specificity

Expressed in roots, stems, leaves, flowers and seedlings. Ref.1

Post-translational modification

The N-terminus is blocked.

Miscellaneous

Like all plant Pin1-type PPIases, do not contain the N-terminal WW domain found in other eukaryotic parvulins, but contains a four-amino acid insertion next to the phospho-specific recognition site of the active site. These extra amino acids may be important for mediating the substrate interaction of plant enzymes.

Three amino acid residues (P79S, E91D and A95G) differ when compared with the partial sequence of purified protein. The existence of two or more genes coding for this protein is not exluded.

Sequence similarities

Belongs to the ppiC/parvulin rotamase family.

Contains 1 PpiC domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Molecular functionIsomerase
Rotamase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 118118Peptidyl-prolyl cis-trans isomerase 1
PRO_0000193441

Regions

Domain3 – 118116PpiC

Sequences

Sequence LengthMass (Da)Tools
Q9LEK8-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 131B74FB4AC3F229

FASTA11812,834
        10         20         30         40         50         60 
MSSEKVRASH ILIKHQGSRR KSSWKDPDGS LISATTRDDA VSQLQSLRQE LLSDPASFSD 

        70         80         90        100        110 
LASRHSHCSS AKRGGDLGPF GRGQMQKPFE EATFALKVGE ISDIVDTDSG VHIIKRTG 

« Hide

References

[1]"Functional replacement of the essential ess1 in yeast by the plant parvulin DlPar13."
Metzner M., Stoller G., Ruecknagel P., Lu K.P., Fischer G., Luckner M., Kuellertz G.
J. Biol. Chem. 276:13524-13529(2001) [PubMed: 11118437] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
Strain: cv. VIII.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ133755 mRNA. Translation: CAB94994.1.

3D structure databases

SMRQ9LEK8. Positions 2-118.
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.2.1.8. 255268.

Family and domain databases

InterProIPR000297. PPIase_PpiC.
[Graphical view]
PfamPF00639. Rotamase. 1 hit.
[Graphical view]
PROSITEPS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePIN1_DIGLA
AccessionPrimary (citable) accession number: Q9LEK8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 1, 2000
Last modified: January 19, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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