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Protein

Beta-galactoside-specific lectin 1

Gene
N/A
Organism
Viscum album (European mistletoe)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Molt4.3 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei198By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein synthesis inhibitor, Toxin

Keywords - Biological processi

Plant defense

Keywords - Ligandi

Lectin

Enzyme and pathway databases

BRENDAi3.2.2.22. 6669.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactoside-specific lectin 1
Alternative name(s):
Beta-galactoside-specific lectin I
Viscumin
Cleaved into the following 2 chains:
Alternative name(s):
Beta-galactoside-specific lectin I chain A isoform 1
ML-I A
Short name:
MLA
rRNA N-glycosidase
Alternative name(s):
Beta-galactoside-specific lectin I chain B
ML-I B
Short name:
MLB
OrganismiViscum album (European mistletoe)
Taxonomic identifieri3972 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeSantalalesViscaceaeViscum

Pathology & Biotechi

Pharmaceutical usei

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 333 PublicationsAdd BLAST33
ChainiPRO_000003074934 – 287Beta-galactoside-specific lectin 1 chain A isoform 1Add BLAST254
PropeptideiPRO_0000030750288 – 301Connecting peptide1 PublicationAdd BLAST14
ChainiPRO_0000030751302 – 564Beta-galactoside-specific lectin 1 chain BAdd BLAST263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi145N-linked (GlcNAc...)1 Publication1
Disulfide bondi280 ↔ 306Interchain (between A and B chains)PROSITE-ProRule annotation1 Publication
Glycosylationi362N-linked (GlcNAc...)1 Publication1
Disulfide bondi365 ↔ 382PROSITE-ProRule annotation1 Publication
Glycosylationi397N-linked (GlcNAc...)1 Publication1
Glycosylationi437N-linked (GlcNAc...)1 Publication1
Disulfide bondi453 ↔ 466PROSITE-ProRule annotation1 Publication
Disulfide bondi492 ↔ 509PROSITE-ProRule annotation1 Publication

Post-translational modificationi

The A chain of variant MLA' is not glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP81446.

Interactioni

Subunit structurei

Disulfide-linked dimer of A and B chains.3 Publications

Protein-protein interaction databases

MINTiMINT-364969.

Structurei

Secondary structure

1564
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 42Combined sources8
Helixi47 – 61Combined sources15
Beta strandi62 – 67Combined sources6
Beta strandi70 – 73Combined sources4
Beta strandi80 – 82Combined sources3
Beta strandi85 – 93Combined sources9
Beta strandi98 – 104Combined sources7
Turni105 – 107Combined sources3
Beta strandi110 – 115Combined sources6
Beta strandi118 – 121Combined sources4
Helixi129 – 131Combined sources3
Beta strandi137 – 141Combined sources5
Helixi148 – 155Combined sources8
Helixi158 – 160Combined sources3
Helixi165 – 176Combined sources12
Helixi182 – 195Combined sources14
Helixi197 – 201Combined sources5
Helixi203 – 215Combined sources13
Helixi223 – 240Combined sources18
Beta strandi246 – 255Combined sources10
Turni256 – 258Combined sources3
Beta strandi259 – 265Combined sources7
Helixi266 – 268Combined sources3
Turni269 – 272Combined sources4
Beta strandi315 – 317Combined sources3
Helixi318 – 320Combined sources3
Beta strandi322 – 325Combined sources4
Helixi326 – 328Combined sources3
Beta strandi335 – 339Combined sources5
Helixi347 – 349Combined sources3
Beta strandi351 – 353Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi364 – 369Combined sources6
Beta strandi376 – 381Combined sources6
Turni382 – 384Combined sources3
Helixi387 – 390Combined sources4
Beta strandi400 – 402Combined sources3
Turni403 – 406Combined sources4
Beta strandi407 – 410Combined sources4
Beta strandi421 – 423Combined sources3
Helixi429 – 431Combined sources3
Beta strandi434 – 437Combined sources4
Beta strandi442 – 447Combined sources6
Helixi449 – 451Combined sources3
Beta strandi453 – 457Combined sources5
Beta strandi460 – 464Combined sources5
Helixi471 – 473Combined sources3
Beta strandi475 – 477Combined sources3
Beta strandi483 – 485Combined sources3
Beta strandi491 – 494Combined sources4
Beta strandi505 – 509Combined sources5
Helixi514 – 516Combined sources3
Beta strandi518 – 520Combined sources3
Beta strandi526 – 528Combined sources3
Turni529 – 531Combined sources3
Beta strandi534 – 537Combined sources4
Helixi538 – 540Combined sources3
Helixi542 – 544Combined sources3
Beta strandi547 – 550Combined sources4
Helixi556 – 558Combined sources3
Beta strandi561 – 563Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M2TX-ray1.89A34-287[»]
B313-564[»]
1ONKX-ray2.10A34-287[»]
B302-563[»]
1OQLX-ray3.00A34-282[»]
B302-564[»]
1PUMX-ray2.30A44-282[»]
B302-564[»]
1PUUX-ray2.30A44-282[»]
B302-564[»]
1SZ6X-ray2.05A44-282[»]
B302-564[»]
2R9KX-ray2.70A34-287[»]
B302-564[»]
2RG9X-ray1.95A44-282[»]
B302-564[»]
3D7WX-ray2.49A34-287[»]
B302-564[»]
3O5WX-ray2.70A34-287[»]
B302-564[»]
4EB2X-ray1.94A44-282[»]
B302-564[»]
4JKXX-ray2.35A34-282[»]
B302-564[»]
ProteinModelPortaliP81446.
SMRiP81446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81446.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini309 – 436Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST128
Domaini440 – 564Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST125

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni324 – 326Galactose binding3
Regioni536 – 538Galactose binding3

Sequence similaritiesi

Contains 2 ricin B-type lectin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. Ribosome_inactivat_prot.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00652. Ricin_B_lectin. 2 hits.
PF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SMARTiSM00458. RICIN. 2 hits.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 2 hits.
SSF56371. SSF56371. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P81446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGHLASRRA WVWYFLMLGQ VFGATVKAET KFSYERLRLR VTHQTTGEEY
60 70 80 90 100
FRFITLLRDY VSSGSFSNEI PLLRQSTIPV SDAQRFVLVE LTNEGGDSIT
110 120 130 140 150
AAIDVTNLYV VAYQAGDQSY FLRDAPRGAE THLFTGTTRS SLPFNGSYPD
160 170 180 190 200
LERYAGHRDQ IPLGIDQLIQ SVTALRFPGG STRTQARSIL ILIQMISEAA
210 220 230 240 250
RFNPILWRAR QYINSGASFL PDVYMLELET SWGQQSTQVQ QSTDGVFNNP
260 270 280 290 300
IRLAIPPGNF VTLTNVRDVI ASLAIMLFVC GERPSSSDVR YWPLVIRPVI
310 320 330 340 350
ADDVTCSASE PTVRIVGRNG MCVDVRDDDF HDGNQIQLWP SKSNNDPNQL
360 370 380 390 400
WTIKRDGTIR SNGSCLTTYG YTAGVYVMIF DCNTAVREAT LWEIWGNGTI
410 420 430 440 450
INPRSNLVLA ASSGIKGTTL TVQTLDYTLG QGWLAGNDTA PREVTIYGFR
460 470 480 490 500
DLCMESNGGS VWVETCVISQ QNQRWALYGD GSIRPKQNQD QCLTCGRDSV
510 520 530 540 550
STVINIVSCS AGSSGQRWVF TNEGAILNLK NGLAMDVAQA NPKLRRIIIY
560
PATGKPNQMW LPVP
Length:564
Mass (Da):62,628
Last modified:April 17, 2007 - v3
Checksum:i8BC06110DD458A6E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3G → A in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti19 – 20GQ → CL in AAR25545 (PubMed:15182350).Curated2
Sequence conflicti37L → I in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti62S → G AA sequence (PubMed:1450445).Curated1
Sequence conflicti83A → T in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti92T → S in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti94E → Q in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti94E → Q AA sequence (PubMed:8980141).Curated1
Sequence conflicti94E → Q (PubMed:12823544).Curated1
Sequence conflicti96G → Q AA sequence (PubMed:8980141).Curated1
Sequence conflicti99I → V AA sequence (PubMed:8980141).Curated1
Sequence conflicti108L → A AA sequence (PubMed:8980141).Curated1
Sequence conflicti117D → N in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti141S → P in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti181S → N in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti190L → I in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti190L → I in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti193I → V in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti193I → V in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti209A → L in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti209A → Y AA sequence (PubMed:8980141).Curated1
Sequence conflicti241Q → H AA sequence (PubMed:8980141).Curated1
Sequence conflicti241Q → H (PubMed:12823544).Curated1
Sequence conflicti244D → E in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti322C → R AA sequence (PubMed:9618256).Curated1
Sequence conflicti391 – 393LWE → IWQ in AAR25545 (PubMed:15182350).Curated3
Sequence conflicti391 – 393LWE → IWQ in AAL87006 (PubMed:15001393).Curated3
Sequence conflicti391 – 393LWE → IWQ AA sequence (PubMed:9618256).Curated3
Sequence conflicti396G → D AA sequence (PubMed:9618256).Curated1
Sequence conflicti408V → A in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti467V → D AA sequence (PubMed:9618256).Curated1
Sequence conflicti468I → S in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti468I → S in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti468I → S AA sequence (PubMed:9618256).Curated1
Sequence conflicti471 – 474QNQR → KNQGK AA sequence (PubMed:9618256).Curated4
Sequence conflicti495C → S AA sequence (PubMed:9618256).Curated1
Sequence conflicti511 – 515AGSSG → GASGS AA sequence (PubMed:9618256).Curated5
Sequence conflicti538 – 540AQA → KGS in AAL87006 (PubMed:15001393).Curated3
Sequence conflicti546R → Q in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti564P → F AA sequence (PubMed:9618256).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti48E → D in MLA'. 1 Publication1
Natural varianti145N → T in MLA'. 1 Publication1
Natural varianti149P → T in MLA'. 1 Publication1
Natural varianti166 – 167DQ → EE in MLA'. 2
Natural varianti173T → S in MLA'. 1 Publication1
Natural varianti177F → Y in MLA'. 1 Publication1
Natural varianti184T → A in MLA'. 1 Publication1
Natural varianti212Y → D in MLA'. 1 Publication1
Natural varianti217A → E in MLA'. 1 Publication1
Natural varianti223V → M in MLA'. 1 Publication1
Natural varianti251I → F in MLA'. 1 Publication1
Natural varianti256 – 257PP → ST in MLA'. 2
Natural varianti264T → S in MLA'. 1 Publication1
Natural varianti268D → S in MLA'. 1 Publication1
Natural varianti319N → S.1 Publication1
Natural varianti357G → N.1 Publication1
Natural varianti458G → Q.1 Publication1
Natural varianti495C → V.1 Publication1
Natural varianti524G → Y.1 Publication1
Natural varianti531 – 533NGL → KGP.3
Natural varianti531N → S.1 Publication1
Natural varianti531N → T.1 Publication1
Natural varianti532 – 535GLAM → SLMV.4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY377890 Genomic DNA. Translation: AAR25545.1.
AY377891 mRNA. Translation: AAR25546.1.
AY081149 mRNA. Translation: AAL87006.1.
PIRiJW0090.
PD0018.
PD0019.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY377890 Genomic DNA. Translation: AAR25545.1.
AY377891 mRNA. Translation: AAR25546.1.
AY081149 mRNA. Translation: AAL87006.1.
PIRiJW0090.
PD0018.
PD0019.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M2TX-ray1.89A34-287[»]
B313-564[»]
1ONKX-ray2.10A34-287[»]
B302-563[»]
1OQLX-ray3.00A34-282[»]
B302-564[»]
1PUMX-ray2.30A44-282[»]
B302-564[»]
1PUUX-ray2.30A44-282[»]
B302-564[»]
1SZ6X-ray2.05A44-282[»]
B302-564[»]
2R9KX-ray2.70A34-287[»]
B302-564[»]
2RG9X-ray1.95A44-282[»]
B302-564[»]
3D7WX-ray2.49A34-287[»]
B302-564[»]
3O5WX-ray2.70A34-287[»]
B302-564[»]
4EB2X-ray1.94A44-282[»]
B302-564[»]
4JKXX-ray2.35A34-282[»]
B302-564[»]
ProteinModelPortaliP81446.
SMRiP81446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-364969.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Proteomic databases

PRIDEiP81446.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.2.22. 6669.

Miscellaneous databases

EvolutionaryTraceiP81446.

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. Ribosome_inactivat_prot.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00652. Ricin_B_lectin. 2 hits.
PF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SMARTiSM00458. RICIN. 2 hits.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 2 hits.
SSF56371. SSF56371. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiML1_VISAL
AccessioniPrimary (citable) accession number: P81446
Secondary accession number(s): P81830
, Q6H270, Q6H271, Q8RXH6, Q9S7D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 17, 2007
Last modified: November 2, 2016
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Several isoforms exist.

Keywords - Technical termi

3D-structure, Direct protein sequencing, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.