Detailed Peptide Information
This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking
| Primary Information |
|---|
| PPepDB ID | PPepDB_4029 |
| Peptide Name | ML1_VISAL |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Viscum album |
| Plant Source (Common Name) | European mistletoe |
| Plant Family | Santalaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | 3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Lectin; Pharmaceutical; Plant defense; Polymorphism; Protein synthesis inhibitor; Repeat; Signal; Toxin | Beta-galactoside-specific lectin 1 precursor (Beta-galactoside-,specific lectin I) (Viscumin) [Contains: Beta-galactoside-specific,lectin 1 chain A isoform 1 (EC 3.2.2.22) (Beta-galactoside-specific,lectin I chain A isoform 1) (MLA) (ML-I A) (rRNA N-glycosidase); Beta-,galactoside-specific lectin 1 chain B (Beta-galactoside-specific,lectin I chain B) (MLB) (ML-I B)]. |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | AAIDVTNLYVVAYQAGDQSYFLRDAPRGAETHLFTGTTRSSLPFNGSYPDADDVTCSASEPTVRIVGRNGMCVDVRDDDFHDGNQIQLWPSKSNNDPNQLDLCMESNGGSVWVETCVISQQNQRWALYGDGSIRPKQNQDQCLTCGRDSVFRFITLLRDYVSSGSFSNEIPLLRQSTIPVSDAQRFVLVELTNEGGDSITINPRSNLVLAASSGIKGTTLTVQTLDYTLGQGWLAGNDTAPREVTIYGFRIRLAIPPGNFVTLTNVRDVIASLAIMLFVCGERPSSSDVRYWPLVIRPVILERYAGHRDQIPLGIDQLIQSVTALRFPGGSTRTQARSILILIQMISEAAMNGHLASRRAWVWYFLMLGQVFGATVKAETKFSYERLRLRVTHQTTGEEYPATGKPNQMWLPVPRFNPILWRARQYINSGASFLPDVYMLELETSWGQQSTQVQQSTDGVFNNPSTVINIVSCSAGSSGQRWVFTNEGAILNLKNGLAMDVAQANPKLRRIIIYWTIKRDGTIRSNGSCLTTYGYTAGVYVMIFDCNTAVREATLWEIWGNGTI |
| Sequence Length | 564 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 62627.91 |
| Monoisotopic Molecular Weight (Da) | 62588.54 |
| Isoelectric Point (pI) | 6.62 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
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| Uniprot | P81446 |
| NCBI | --NA-- |
| EMBL | AY377890 |
| Link to Source Databases | SPdb154144 |
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| Addtional Information | FUNCTION:The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.CATALYTIC ACTIVITY:Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.SUBUNIT:Disulfide-linked dimer of A and B chains.PTM:The A chain of variant MLA' is not glycosylated.PHARMACEUTICAL:Due to its immunomodulative effects it is being studied in clinical trials in cancer patients as it may slow the growth of cancer cells and be an effective treatment for solid tumors.MISCELLANEOUS:Several isoforms exist.SIMILARITY:Belongs to the ribosome-inactivating protein family.Type 2 RIP subfamily.SIMILARITY:Contains 2 ricin B-type lectin domains. |
