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Reviewed, UniProtKB/Swiss-Prot Q6ITZ3 (ML4_VISAL)

Last modified July 28, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Beta-galactoside-specific lectin 4
Alternative name(s):
    Beta-galactoside-specific lectin IV
Cleaved into the following 2 chains:
    1- Recommended name:
            Beta-galactoside-specific lectin 4 chain A
              EC=3.2.2.22
        Alternative name(s):
            ML-4 A
            Beta-galactoside-specific lectin IV chain A
            ML-IV A
            rRNA N-glycosidase
    2- Recommended name:
            Beta-galactoside-specific lectin 4 chain B
        Alternative name(s):
            ML-4B
            Beta-galactoside-specific lectin IV chain B
            ML-IV B
OrganismViscum album (European mistletoe)
Taxonomic identifier3972 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Santalales › Santalaceae › Viscum

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Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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). Inhibits growth of the human tumor cell line Molt4. Ref.1 Ref.2 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. Ref.3 Ref.4

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Beta-galactoside-specific lectin 4 chain A
PRO_5000093497
Propeptide241 – 26525Connecting peptide
PRO_0000284730
Chain266 – 520255Beta-galactoside-specific lectin 4 chain B
PRO_5000093498

Regions

Domain269 – 396128Ricin B-type lectin 1
Domain400 – 520121Ricin B-type lectin 2
Region284 – 2863Galactose binding By similarity UniProtKB P81446
Region494 – 4963Galactose binding By similarity UniProtKB P81446

Sites

Active site1591 Ref.4

Amino acid modifications

Glycosylation1071N-linked (GlcNAc...) Ref.3
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Ref.3
Glycosylation3971N-linked (GlcNAc...) Ref.3
Disulfide bond240 ↔ 266Interchain (between A and B chains) Ref.3 Ref.4
Disulfide bond325 ↔ 342 Ref.4
Disulfide bond413 ↔ 426 Ref.4
Disulfide bond451 ↔ 467 Ref.4

Experimental info

Sequence conflict51D → R AA sequence Ref.1
Sequence conflict51D → R AA sequence Ref.2
Sequence conflict71D → R AA sequence Ref.1
Sequence conflict71D → R AA sequence Ref.2
Sequence conflict101S → H AA sequence Ref.1
Sequence conflict101S → H AA sequence Ref.2
Sequence conflict291S → H AA sequence Ref.2

Secondary structure

1 ............................................................................................................. 520
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q6ITZ3-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4F9561A0BD92A915

FASTA52056,957
        10         20         30         40         50         60 
YERLDLDVTS QTTGEEYFRF ITLLRDYVSS GSFSNEIPLL RQSGGGVEAA RFVLVELTNE 

        70         80         90        100        110        120 
GGDSITAAID VTNLYVVAYQ AGSQSYFLSG PGTHLFTGTT RSSLPFNGSY PDLEQYAGHR 

       130        140        150        160        170        180 
KQIPLGIDQL IQSVTALRFP GNTRTQARSI LILIQMISEA ARFNPILWRA RQYINSGASF 

       190        200        210        220        230        240 
LPDVYMLELE TSWGQQSTQV QQSTEGVFNN PIRLAIPGNF VTLTNVRDVI ASLAIMLFVC 

       250        260        270        280        290        300 
GERPSSSDVR YWPLVIRPVI ADDVTCSASE PTVRIVGRNG MNVDVRDDDF HDGNQIQLWP 

       310        320        330        340        350        360 
SKSNNDPNQL WTIKRDGTIR SNGSCLTTYG YTAGVYVMIF DCNTAVREAT IWQIWGNGTI 

       370        380        390        400        410        420 
INPRSNLALA ASSGIKGTTL TVQTLDYTLG QGWLAGNDTA PREVTIYGFN DLCMESNGGS 

       430        440        450        460        470        480 
VWVETCVSQQ NDRWALYGDG SIRPEQNQDQ CLTSGRDSVA GINIVSCSGG SSGQRWVFTN 

       490        500        510        520 
EGAILNLKNG LAMDVANPGL GQIIIYPATG KPNQMWLPVP

« Hide

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References

[1]"Purification and characterization of four isoforms of Himalayan mistletoe ribosome-inactivating protein from Viscum album having unique sugar affinity."
Mishra V., Sharma R.S., Yadav S., Babu C.R., Singh T.P.
Arch. Biochem. Biophys. 423:288-301(2004) [PubMed: 15001393] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-20, FUNCTION.
Tissue: Leaf.
[2]"Identity of the N-terminal sequences of the three A chains of mistletoe (Viscum album L.) lectins: homology with ricin-like plant toxins and single-chain ribosome-inhibiting proteins."
Dietrich J.B., Ribereau-Gayon G., Jung M.L., Franz H., Beck J.P., Anton R.
Anticancer Drugs 3:507-511(1992) [PubMed: 1450445] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-29, FUNCTION.
[3]"Crystal structure of mistletoe lectin I from Viscum album."
Krauspenhaar R., Eschenburg S., Perbandt M., Kornilov V., Konareva N., Mikailova I., Stoeva S., Wacker R., Maier T., Singh T.P., Mikhailov A., Voelter W., Betzel C.
Biochem. Biophys. Res. Commun. 257:418-424(1999) [PubMed: 10198229] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-240 AND 266-520, SUBUNIT, GLYCOSYLATION AT ASN-107; ASN-357 AND ASN-397.
[4]"Structure of a novel ribosome-inactivating protein from a hemi-parasitic plant inhabiting the northwestern Himalayas."
Mishra V., Ethayathulla A.S., Sharma R.S., Yadav S., Krauspenhaar R., Betzel C., Babu C.R., Singh T.P.
Acta Crystallogr. D 60:2295-2304(2004) [PubMed: 15583377] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 1-240 AND 266-520, SUBUNIT, ACTIVE SITE, DISULFIDE BONDS.
[5]"Crystal structure of Himalayan mistletoe rip reveals the presence of a natural inhibitor and a new functionally active sugar-binding site."
Mishra V., Bilgrami S., Sharma R.S., Kaur P., Yadav S., Krauspenhaar R., Betzel C., Voelter W., Babu C.R., Singh T.P.
Submitted (DEC-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-240 AND 266-520.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AY625281 mRNA. Translation: AAT37532.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CE7X-ray2.70A1-240[»]
B266-519[»]
1PC8X-ray3.80A1-240[»]
B266-520[»]
1TFMX-ray2.80A1-240[»]
B266-520[»]
1YF8X-ray2.80A1-240[»]
B266-520[»]
2MLLX-ray2.70A1-240[»]
B266-519[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.

Enzyme and pathway databases

BRENDA3.2.2.22. 273578.

Family and domain databases

InterProIPR001574. Ribosome_inactivat_prot.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
IPR000772. Ricin_B_lectin.
[Graphical view]
Gene3DG3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit.
G3DSA:4.10.470.10. Ribosome_inactivat_prot_sub2. 1 hit.
PfamPF00652. Ricin_B_lectin. 2 hits.
PF00161. RIP. 1 hit.
[Graphical view]
PRINTSPR00396. SHIGARICIN.
SMARTSM00458. RICIN. 2 hits.
[Graphical view]
PROSITEPS50231. RICIN_B_LECTIN. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameML4_VISAL
AccessionPrimary (citable) accession number: Q6ITZ3
Secondary accession number(s): Q9S7D0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: July 5, 2004
Last modified: July 28, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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