Reviewed,
UniProtKB/Swiss-Prot Q6H266 (ML2_VISAL)
Last modified
June 16, 2009.
Version 28.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Beta-galactoside-specific lectin 2 Alternative name(s): Beta-galactoside-specific lectin II Beta-galactoside-specific lectin III Cleaved into the following 2 chains: 1- Recommended name: Beta-galactoside-specific lectin 2 chain A EC=3.2.2.22 Alternative name(s): ML-2 A Beta-galactoside-specific lectin II chain A ML-II A rRNA N-glycosidase 2- Recommended name: Beta-galactoside-specific lectin 2 chain B Alternative name(s): ML-2B Beta-galactoside-specific lectin II chain B ML-II B |
| Organism | Viscum album (European mistletoe) |
| Taxonomic identifier | 3972 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Santalales › Santalaceae › Viscum |
Protein attributes
| Sequence length | 567 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| 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). Ref.1 UniProtKB P81446 |
| Catalytic activity | Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. UniProtKB P81446 |
| Subunit structure | Disulfide-linked dimer of A and B chains By similarity. UniProtKB P81446 |
| Miscellaneous | Several isoforms exist. Ref.1 |
| Sequence similarities | Belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily. Contains 2 ricin B-type lectin domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Plant defense |
| Domain | Repeat Signal |
| Ligand | Lectin |
| Molecular function | Hydrolase Protein synthesis inhibitor Toxin |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | defense response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of translationInferred from electronic annotation. Source: UniProtKB-KW pathogenesisInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | rRNA N-glycosylase activity Inferred from electronic annotation. Source: EC sugar bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 33 | 33 | Potential | ||||||||
| Chain | 34 – 287 | 254 | Beta-galactoside-specific lectin 2 chain A | PRO_5000092109 | |||||||
| Propeptide | 288 – 301 | 14 | Connecting peptide By similarity UniProtKB P81446 | PRO_0000284728 | |||||||
| Chain | 302 – 567 | 266 | Beta-galactoside-specific lectin 2 chain B | PRO_5000092110 | |||||||
Regions | |||||||||||
| Domain | 309 – 439 | 131 | Ricin B-type lectin 1 | ||||||||
| Domain | 443 – 566 | 124 | Ricin B-type lectin 2 | ||||||||
| Region | 324 – 326 | 3 | Galactose binding By similarity UniProtKB P81446 | ||||||||
| Region | 539 – 541 | 3 | Galactose binding By similarity UniProtKB P81446 | ||||||||
Sites | |||||||||||
| Active site | 198 | 1 | By similarity UniProtKB Q6ITZ3 | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 145 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 362 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 440 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 280 ↔ 306 | Interchain (between A and B chains) By similarity UniProtKB P81446 | |||||||||
| Disulfide bond | 322 ↔ 341 | By similarity UniProtKB Q6ITZ3 | |||||||||
| Disulfide bond | 365 ↔ 382 | By similarity UniProtKB P81446 | |||||||||
| Disulfide bond | 456 ↔ 469 | By similarity UniProtKB P81446 | |||||||||
| Disulfide bond | 495 ↔ 512 | By similarity UniProtKB P81446 | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 18 | 1 | V → L in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 26 | 1 | A → T in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 30 | 1 | S → T in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 44 | 1 | K → E in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 63 | 1 | I → M in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 95 | 1 | W → G in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 127 | 1 | H → D in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 199 | 1 | A → V in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 246 | 1 | V → I in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 289 | 1 | V → A in AAR25551. Ref.1 | ||||||||
| Sequence conflict | 314 | 1 | R → Q in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 331 | 1 | R → H in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 364 – 365 | 2 | SC → RF in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 393 | 1 | Q → L in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 430 | 1 | D → Y in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 442 | 1 | T → I in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 468 | 1 | S → T in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 505 | 1 | S → F in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 556 | 1 | S → N in AAR25549. Ref.1 | ||||||||
| Sequence conflict | 566 | 1 | V → M in AAR25549. Ref.1 | ||||||||
Sequences
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References
| [1] | "Cloning and characterization of the genes encoding toxic lectins in mistletoe (Viscum album L)." Kourmanova A.G., Soudarkina O.J., Olsnes S., Kozlov J.V. Eur. J. Biochem. 271:2350-2360(2004) [PubMed: 15182350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION. Tissue: Leaf. |
Cross-references
Sequence databases | |
|---|---|
| AY377894 Genomic DNA. Translation: AAR25549.1. AY377895 Genomic DNA. Translation: AAR25550.1. AY377896 mRNA. Translation: AAR25551.1. | |
3D structure databases | |
| SMR | Q6H266. Positions 34-280, 302-567. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM13. Carbohydrate-Binding Module Family 13. |
Enzyme and pathway databases | |
| BRENDA | 3.2.2.22. 273578. |
Family and domain databases | |
| InterPro | IPR001574. Ribosome_inactivat_prot. IPR017988. Ribosome_inactivat_prot_CS. IPR016138. Ribosome_inactivat_prot_sub1. IPR016139. Ribosome_inactivat_prot_sub2. IPR017989. Ribosome_inactivat_prot_subgr. IPR000772. Ricin_B_lectin. [Graphical view] |
| Gene3D | G3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit. G3DSA:4.10.470.10. Ribosome_inactivat_prot_sub2. 1 hit. |
| Pfam | PF00652. Ricin_B_lectin. 2 hits. PF00161. RIP. 1 hit. [Graphical view] |
| PRINTS | PR00396. SHIGARICIN. |
| SMART | SM00458. RICIN. 2 hits. [Graphical view] |
| PROSITE | PS50231. RICIN_B_LECTIN. 2 hits. PS00275. SHIGA_RICIN. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ML2_VISAL | ||||||||
| Accession | Primary (citable) accession number: Q6H266 Secondary accession number(s): Q6H265, Q6H267 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


