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Reviewed, UniProtKB/Swiss-Prot P81446 (ML1_VISAL)

Last modified January 19, 2010. Version 80. 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 1
Alternative name(s):
    Beta-galactoside-specific lectin I
    Viscumin
Cleaved into the following 2 chains:
    1- Recommended name:
            Beta-galactoside-specific lectin 1 chain A isoform 1
              EC=3.2.2.22
        Alternative name(s):
            Beta-galactoside-specific lectin I chain A isoform 1
            ML-I A
              Short name=MLA
            rRNA N-glycosidase
    2- Recommended name:
            Beta-galactoside-specific lectin 1 chain B
        Alternative name(s):
            Beta-galactoside-specific lectin I chain B
            ML-I B
              Short name=MLB
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 length564 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 Ref.4

Catalytic activity

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

Subunit structure

Disulfide-linked dimer of A and B chains. Ref.8

Post-translational modification

The A chain of variant MLA' is not glycosylated. Ref.8

Pharmaceutical use

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.

Sequence similarities

Belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.

Contains 2 ricin B-type lectin domains.

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Ontologies

Keywords
   Biological processPlant defense
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   LigandLectin
   Molecular functionHydrolase
Protein synthesis inhibitor
Toxin
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Pharmaceutical
Gene Ontology (GO)
   Biological processdefense response

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionrRNA N-glycosylase activity

Inferred from electronic annotation. Source: EC

sugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.2 Ref.4 Ref.3
Chain34 – 287254Beta-galactoside-specific lectin 1 chain A isoform 1
PRO_0000030749
Propeptide288 – 30114Connecting peptide
PRO_0000030750
Chain302 – 564263Beta-galactoside-specific lectin 1 chain B
PRO_0000030751

Regions

Domain309 – 436128Ricin B-type lectin 1
Domain440 – 564125Ricin B-type lectin 2
Region324 – 3263Galactose binding
Region536 – 5383Galactose binding

Sites

Active site1981 By similarity

Amino acid modifications

Glycosylation1451N-linked (GlcNAc...) Ref.8
Glycosylation3621N-linked (GlcNAc...) Ref.8
Glycosylation3971N-linked (GlcNAc...) Ref.8
Glycosylation4371N-linked (GlcNAc...) Ref.8
Disulfide bond280 ↔ 306Interchain (between A and B chains) Ref.8
Disulfide bond365 ↔ 382 Ref.8
Disulfide bond453 ↔ 466 Ref.8
Disulfide bond492 ↔ 509 Ref.8

Natural variations

Natural variant481E → D in MLA'. Ref.3
Natural variant1451N → T in MLA'. Ref.3
Natural variant1491P → T in MLA'. Ref.3
Natural variant166 – 1672DQ → EE in MLA'.
Natural variant1731T → S in MLA'. Ref.3
Natural variant1771F → Y in MLA'. Ref.3
Natural variant1841T → A in MLA'. Ref.3
Natural variant2121Y → D in MLA'. Ref.3
Natural variant2171A → E in MLA'. Ref.3
Natural variant2231V → M in MLA'. Ref.3
Natural variant2511I → F in MLA'. Ref.3
Natural variant256 – 2572PP → ST in MLA'.
Natural variant2641T → S in MLA'. Ref.3
Natural variant2681D → S in MLA'. Ref.3
Natural variant3191N → S
Natural variant3571G → N
Natural variant4581G → Q
Natural variant4951C → V
Natural variant5241G → Y
Natural variant531 – 5333NGL → KGP
Natural variant5311N → S
Natural variant5311N → T
Natural variant532 – 5354GLAM → SLMV

Experimental info

Sequence conflict31G → A in AAR25545. Ref.1
Sequence conflict19 – 202GQ → CL in AAR25545. Ref.1
Sequence conflict371L → I in AAR25546. Ref.1
Sequence conflict621S → G AA sequence Ref.4
Sequence conflict831A → T in AAR25546. Ref.1
Sequence conflict921T → S in AAR25546. Ref.1
Sequence conflict941E → Q in AAR25545. Ref.1
Sequence conflict941E → Q AA sequence Ref.3
Sequence conflict941E → Q Ref.8
Sequence conflict961G → Q AA sequence Ref.3
Sequence conflict991I → V AA sequence Ref.3
Sequence conflict1081L → A AA sequence Ref.3
Sequence conflict1171D → N in AAR25546. Ref.1
Sequence conflict1411S → P in AAR25546. Ref.1
Sequence conflict1811S → N in AAL87006. Ref.2
Sequence conflict1901L → I in AAR25545. Ref.1
Sequence conflict1901L → I in AAR25546. Ref.1
Sequence conflict1931I → V in AAR25545. Ref.1
Sequence conflict1931I → V in AAR25546. Ref.1
Sequence conflict2091A → L in AAR25546. Ref.1
Sequence conflict2091A → Y AA sequence Ref.3
Sequence conflict2411Q → H AA sequence Ref.3
Sequence conflict2411Q → H Ref.8
Sequence conflict2441D → E in AAL87006. Ref.2
Sequence conflict3221C → R AA sequence Ref.5
Sequence conflict391 – 3933LWE → IWQ in AAR25545. Ref.1
Sequence conflict391 – 3933LWE → IWQ in AAL87006. Ref.2
Sequence conflict391 – 3933LWE → IWQ AA sequence Ref.5
Sequence conflict3961G → D AA sequence Ref.5
Sequence conflict4081V → A in AAL87006. Ref.2
Sequence conflict4671V → D AA sequence Ref.5
Sequence conflict4681I → S in AAR25545. Ref.1
Sequence conflict4681I → S in AAL87006. Ref.2
Sequence conflict4681I → S AA sequence Ref.5
Sequence conflict471 – 4744QNQR → KNQGK AA sequence Ref.5
Sequence conflict4951C → S AA sequence Ref.5
Sequence conflict511 – 5155AGSSG → GASGS AA sequence Ref.5
Sequence conflict538 – 5403AQA → KGS in AAL87006. Ref.2
Sequence conflict5461R → Q in AAL87006. Ref.2
Sequence conflict5641P → F AA sequence Ref.5

Secondary structure

1 ........................................................................................................... 564
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P81446-1 [UniParc].

Last modified April 17, 2007. Version 3.
Checksum: 8BC06110DD458A6E

FASTA56462,628
        10         20         30         40         50         60 
MNGHLASRRA WVWYFLMLGQ VFGATVKAET KFSYERLRLR VTHQTTGEEY FRFITLLRDY 

        70         80         90        100        110        120 
VSSGSFSNEI PLLRQSTIPV SDAQRFVLVE LTNEGGDSIT AAIDVTNLYV VAYQAGDQSY 

       130        140        150        160        170        180 
FLRDAPRGAE THLFTGTTRS SLPFNGSYPD LERYAGHRDQ IPLGIDQLIQ SVTALRFPGG 

       190        200        210        220        230        240 
STRTQARSIL ILIQMISEAA RFNPILWRAR QYINSGASFL PDVYMLELET SWGQQSTQVQ 

       250        260        270        280        290        300 
QSTDGVFNNP IRLAIPPGNF VTLTNVRDVI ASLAIMLFVC GERPSSSDVR YWPLVIRPVI 

       310        320        330        340        350        360 
ADDVTCSASE PTVRIVGRNG MCVDVRDDDF HDGNQIQLWP SKSNNDPNQL WTIKRDGTIR 

       370        380        390        400        410        420 
SNGSCLTTYG YTAGVYVMIF DCNTAVREAT LWEIWGNGTI INPRSNLVLA ASSGIKGTTL 

       430        440        450        460        470        480 
TVQTLDYTLG QGWLAGNDTA PREVTIYGFR DLCMESNGGS VWVETCVISQ QNQRWALYGD 

       490        500        510        520        530        540 
GSIRPKQNQD QCLTCGRDSV STVINIVSCS AGSSGQRWVF TNEGAILNLK NGLAMDVAQA 

       550        560 
NPKLRRIIIY PATGKPNQMW LPVP

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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.
[2]"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] OF 34-564, PROTEIN SEQUENCE OF 34-53, FUNCTION.
Tissue: Leaf.
[3]"Complete amino acid sequence of the A chain of mistletoe lectin I."
Soler M.H., Stoeva S., Schwamborn C., Wilhelm S., Stiefel T., Voelter W.
FEBS Lett. 399:153-157(1996) [PubMed: 8980141] [Abstract]
Cited for: PROTEIN SEQUENCE OF 34-287 (CHAIN A), VARIANTS ASP-48; THR-145; THR-149; 166-GLU-GLU-167; SER-173; TYR-177; ALA-184; ASP-212; GLU-217; MET-223; PHE-251; 256-SER-THR-257; SER-264 AND SER-268.
[4]"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 34-62, FUNCTION.
[5]"Complete amino acid sequence of the B chain of mistletoe lectin I."
Soler M.H., Stoeva S., Voelter W.
Biochem. Biophys. Res. Commun. 246:596-601(1998) [PubMed: 9618256] [Abstract]
Cited for: PROTEIN SEQUENCE OF 302-564 (CHAIN B), VARIANTS SER-319; ASN-357; GLN-458; VAL-495; TYR-524; SER-531; THR-531; 531-LYS--PRO-533 AND 532-SER--VAL-535.
[6]"Primary structure and molecular modeling of mistletoe lectin I from Viscum album."
Eschenburg S., Krauspenhaar R., Mikhailov A., Stoeva S., Betzel C., Voelter W.
Biochem. Biophys. Res. Commun. 247:367-372(1998) [PubMed: 9642133] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 34-287 AND 302-564.
[7]"Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 A resolution."
Krauspenhaar R., Rypniewski W., Kalkura N., Moore K., DeLucas L., Stoeva S., Mikhailov A., Voelter W., Betzel C.
Acta Crystallogr. D 58:1704-1707(2002) [PubMed: 12351890] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 34-287 AND 302-564 IN COMPLEX WITH AMP.
[8]"Crystal structure at 3 A of mistletoe lectin I, a dimeric type-II ribosome-inactivating protein, complexed with galactose."
Niwa H., Tonevitsky A.G., Agapov I.I., Saward S., Pfueller U., Palmer R.A.
Eur. J. Biochem. 270:2739-2749(2003) [PubMed: 12823544] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 34-282 AND 302-564 IN COMPLEX WITH GALACTOSE, SUBUNIT, GLYCOSYLATION AT ASN-145; ASN-362; ASN-397 AND ASN-437, DISULFIDE BONDS.
[9]"Mistletoe lectin I in complex with galactose and lactose reveals distinct sugar-binding properties."
Mikeska R., Wacker R., Arni R., Singh T.P., Mikhailov A., Gabdoulkhakov A., Voelter W., Betzel C.
Acta Crystallogr. F 61:17-25(2005) [PubMed: 16508080] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 34-282 AND 302-564 IN COMPLEX WITH LACTOSE AND GALACTOSE.
[10]"Mistletoe lectin I From Viscum album."
Gabdoulkhakov A.G., Savoshkina Y., Krauspenhaar R., Stoeva S., Konareva N., Kornilov V., Kornev A.N., Voelter W., Nikonov S.V., Betzel C., Mikhailov A.M.
Submitted (FEB-2003) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 34-287 AND 302-563.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY377890 Genomic DNA. Translation: AAR25545.1.
AY377891 mRNA. Translation: AAR25546.1.
AY081149 mRNA. Translation: AAL87006.1.
PIRJW0090.
PD0018.
PD0019.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2TX-ray1.89A34-287[»]
B304-564[»]
1ONKX-ray2.10A34-287[»]
B302-563[»]
1OQLX-ray3.00A34-282[»]
B302-564[»]
1PUMX-ray2.30A34-282[»]
B302-564[»]
1PUUX-ray2.30A34-282[»]
B302-564[»]
1SZ6X-ray2.05A34-282[»]
B302-564[»]
2R9KX-ray2.70A34-287[»]
B304-564[»]
2RG9X-ray1.95A34-282[»]
B302-564[»]
3D7WX-ray2.49A34-287[»]
B302-564[»]
SMRP81446. Positions 43-309, 272-520.
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.
IPR008997. Ricin_B-rel_lectin.
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.
PS00275. SHIGA_RICIN. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameML1_VISAL
AccessionPrimary (citable) accession number: P81446
Secondary accession number(s): P81830 expand/collapse secondary AC list , Q6H270, Q6H271, Q8RXH6, Q9S7D0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 17, 2007
Last modified: January 19, 2010
This is version 80 of the entry and version 3 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