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[1]
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NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
STRAIN=cv. VIII;
DOI=10.1074/jbc.M007005200; PubMed=11118437 [NCBI, ExPASy, EBI, Israel, Japan]
Metzner M.,
Stoller G.,
Ruecknagel P.,
Lu K.P.,
Fischer G.,
Luckner M.,
Kuellertz G.;
"Functional replacement of the essential ess1 in yeast by the plant parvulin DlPar13.";
J. Biol. Chem. 276:13524-13529(2001).
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- FUNCTION: Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds.
- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0).
- ENZYME REGULATION: Inhibited in vitro by juglone.
- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and seedlings.
- PTM: 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.
- MISCELLANEOUS: 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.
- SIMILARITY: Belongs to the ppiC/parvulin rotamase family.
- SIMILARITY: Contains 1 PpiC domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 118 AA [This is the length of the unprocessed precursor] |
Molecular weight: 12834 Da [This is the MW of the unprocessed precursor] |
CRC64: 131B74FB4AC3F229 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSSEKVRASH ILIKHQGSRR KSSWKDPDGS LISATTRDDA VSQLQSLRQE LLSDPASFSD
70 80 90 100 110
LASRHSHCSS AKRGGDLGPF GRGQMQKPFE EATFALKVGE ISDIVDTDSG VHIIKRTG
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Q9LEK8 in FASTA format |
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