Beta-galactoside-specific lectin 3 precursor - Viscum album (European mistletoe)

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Reviewed, UniProtKB/Swiss-Prot P82683 (ML3_VISAL)

Last modified January 19, 2010. Version 39. History...

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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 names	Recommended name: Beta-galactoside-specific lectin 3 Alternative name(s): Beta-galactoside-specific lectin III Beta-galactoside-specific lectin II Cleaved into the following 2 chains: 1- Recommended name: Beta-galactoside-specific lectin 3 chain A isoform 1 EC=3.2.2.22 Alternative name(s): ML-3 A Beta-galactoside-specific lectin III chain A isoform 1 ML-III A Lectin chain A isoform 2 rRNA N-glycosidase 2- Recommended name: Beta-galactoside-specific lectin 3 chain B Alternative name(s): ML-3 B Beta-galactoside-specific lectin III chain B ML-III 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

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Protein attributes

Sequence length	569 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.3 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.
Miscellaneous	Several isoforms exist.
Sequence similarities	Belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily. Contains 2 ricin B-type lectin domains.
Mass spectrometry	Molecular mass is 59300 Da from positions 34 - 569. Determined by MALDI. Ref.5

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Ontologies

Keywords
Biological process	Plant defense
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Lectin
Molecular function	Hydrolase Protein synthesis inhibitor Toxin
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense 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 function	rRNA 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 33

Ref.3 Ref.4 Ref.2

Chain

34 – 287

254

Beta-galactoside-specific lectin 3 chain A isoform 1

PRO_0000221393

Propeptide

288 – 307

Connecting peptide

PRO_0000284729

Chain

308 – 569

262

Beta-galactoside-specific lectin 3 chain B

PRO_0000221394

Regions

Domain

314 – 441

128

Ricin B-type lectin 1

Domain

445 – 568

124

Ricin B-type lectin 2

Region

329 – 331

Galactose binding

Region

541 – 543

Galactose binding

Sites

Active site

198

By similarity

Amino acid modifications

Glycosylation

402

N-linked (GlcNAc...) Ref.5

Glycosylation

442

N-linked (GlcNAc...) Ref.5

Disulfide bond

280 ↔ 311

Interchain (between A and B chains) Probable

Disulfide bond

327 ↔ 346

By similarity

Disulfide bond

370 ↔ 387

By similarity

Disulfide bond

458 ↔ 471

By similarity

Disulfide bond

497 ↔ 514

By similarity

Natural variations

Natural variant

127

D → R

Natural variant

131

R → T

Natural variant

138

T → A

Natural variant

358

I → F

Natural variant

430

Q → L

Natural variant

569

P → F

Experimental info

Sequence conflict

G → R in AAR25548. Ref.1

Sequence conflict

I → M in AAR25548. Ref.1

Sequence conflict

A → R in AAR25548. Ref.1

Sequence conflict

D → E AA sequence Ref.3

Sequence conflict

D → E AA sequence Ref.4

Sequence conflict

S → G AA sequence Ref.4

Sequence conflict

Q → E in AAL87005. Ref.3

Sequence conflict

127

D → N AA sequence Ref.2

Sequence conflict

190

I → L AA sequence Ref.2

Sequence conflict

191

I → V in AAR25548. Ref.1

Sequence conflict

244

D → Y in AAR25548. Ref.1

Sequence conflict

281 – 282

RD → GE AA sequence Ref.2

Sequence conflict

281 – 282

RD → GE in AAL87005. Ref.3

Sequence conflict

475

T → K in AAR25548. Ref.1

Sequence conflict

475

T → K AA sequence Ref.5

Sequence conflict

479

N → D AA sequence Ref.5

Sequence conflict

500

C → S in AAR25548. Ref.1

Sequence conflict

506

A → S in AAR25548. Ref.1

Sequence conflict

506

A → S AA sequence Ref.5

Sequence conflict

535

N → K in AAR25548. Ref.1

Sequence conflict

568

V → L in AAR25548. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P82683-1 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 7860722EA6425D3E
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FASTA

569

62,686

        10         20         30         40         50         60 
MNAVMDSRGA WVSCFLILGL VFGATVKAET KFSYERLRLR VTHQTTGDEY FRFITLLRDY 

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

       130        140        150        160        170        180 
FLRDAPDGAE RHLFTGTTRS SLPFTGSYTD LERYAGHRDQ IPLGIEELIQ SVSALRYPGG 

       190        200        210        220        230        240 
STRAQARSII ILIQMISEAA RFNPIFWRVR QDINSGESFL PDMYMLELET SWGQQSTQVQ 

       250        260        270        280        290        300 
QSTDGVFNNP FRLAISTGNF VTLSNVRDVI ASLAIMLFVC RDRPSSSEVR YWPLVIRPVL 

       310        320        330        340        350        360 
ENSGAVDDVT CTASEPTVRI VGRDGLCVDV RDGKFHNGNP IQLSPCKSNT DPNQLWTIRR 

       370        380        390        400        410        420 
DGTIRSNGRC LTTYGYTAGV YVMIFDCNTA VREATLWQIW GNGTIINPRS NLVLGAASGS 

       430        440        450        460        470        480 
SGTTLTVQTQ VYSLGQGWLA GNDTAPREVT IYGFRDLCME ANGASVWVET CGSSTENQNW 

       490        500        510        520        530        540 
ALYGDGSIRP KQNQDQCLTC QGDSVATVIN IVSCSAGSSG QRWVFTNEGT ILNLNNGLVM 

       550        560 
DVAQSNPSLR RIIIYPATGN PNQMWLPVP

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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]	"Complete structure determination of the A chain of mistletoe lectin III from Viscum album L. ssp. album." Wacker R., Stoeva S., Pfuller K., Pfuller U., Voelter W. J. Pept. Sci. 10:138-148(2004) [PubMed: 15113086] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-287, VARIANTS ARG-127; THR-131 AND ALA-138.
[3]	"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 34-282, PROTEIN SEQUENCE OF 34-53, FUNCTION. Tissue: Leaf.
[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 structure determination of N-acetyl-D-galactosamine-binding mistletoe lectin-3 from Viscum album L. album." Wacker R., Stoeva S., Betzel C., Voelter W. J. Pept. Sci. 11:289-302(2005) [PubMed: 15635663] [Abstract] Cited for: PROTEIN SEQUENCE OF 308-569, MASS SPECTROMETRY, VARIANTS PHE-358; LEU-430 AND PHE-569, GLYCOSYLATION AT ASN-402 AND ASN-442. Tissue: Leaf.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AY377892 Genomic DNA. Translation: AAR25547.1. AY377893 mRNA. Translation: AAR25548.1. AY081148 mRNA. Translation: AAL87005.1.
3D structure databases
SMR	P82683. Positions 34-280, 43-313, 272-525, 307-569.
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. 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]
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...

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Entry information

Entry name

ML3_VISAL

Accession

Primary (citable) accession number: P82683
Secondary accession number(s): P87800

Q9S7D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2003
Last sequence update:	April 17, 2007
Last modified:	January 19, 2010
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents