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Protein

Beta-galactoside-specific lectin 4

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.By similarity2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 15911 Publication

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

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactoside-specific lectin 4
Alternative name(s):
Beta-galactoside-specific lectin IV
Cleaved into the following 2 chains:
Alternative name(s):
Beta-galactoside-specific lectin IV chain A
ML-4 A
ML-IV A
rRNA N-glycosidase
Alternative name(s):
Beta-galactoside-specific lectin IV chain B
ML-4B
ML-IV B
OrganismiViscum album (European mistletoe)
Taxonomic identifieri3972 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeSantalalesViscaceaeViscum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Beta-galactoside-specific lectin 4 chain APRO_5000093497Add
BLAST
Propeptidei241 – 26525Connecting peptideCuratedPRO_0000284730Add
BLAST
Chaini266 – 520255Beta-galactoside-specific lectin 4 chain BPRO_5000093498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi107 – 1071N-linked (GlcNAc...)1 Publication
Disulfide bondi240 ↔ 266Interchain (between A and B chains)PROSITE-ProRule annotation2 Publications
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence analysis
Disulfide bondi325 ↔ 342PROSITE-ProRule annotation1 Publication
Glycosylationi357 – 3571N-linked (GlcNAc...)1 Publication
Glycosylationi397 – 3971N-linked (GlcNAc...)1 Publication
Disulfide bondi413 ↔ 426PROSITE-ProRule annotation1 Publication
Disulfide bondi451 ↔ 467PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Disulfide-linked dimer of A and B chains.2 Publications

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi14 – 2815Combined sources
Beta strandi29 – 346Combined sources
Beta strandi37 – 404Combined sources
Beta strandi43 – 453Combined sources
Beta strandi50 – 5910Combined sources
Beta strandi64 – 707Combined sources
Turni71 – 733Combined sources
Beta strandi76 – 805Combined sources
Beta strandi82 – 876Combined sources
Beta strandi98 – 1014Combined sources
Helixi110 – 1178Combined sources
Helixi120 – 1223Combined sources
Beta strandi125 – 1273Combined sources
Helixi128 – 13811Combined sources
Helixi144 – 15613Combined sources
Helixi159 – 1624Combined sources
Helixi164 – 17613Combined sources
Helixi184 – 1907Combined sources
Helixi193 – 20210Combined sources
Beta strandi204 – 21411Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi221 – 2255Combined sources
Helixi226 – 2294Combined sources
Turni230 – 2323Combined sources
Beta strandi275 – 2773Combined sources
Helixi278 – 2803Combined sources
Beta strandi281 – 2855Combined sources
Helixi286 – 2883Combined sources
Beta strandi295 – 2995Combined sources
Helixi307 – 3093Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi315 – 3173Combined sources
Beta strandi319 – 3213Combined sources
Beta strandi324 – 3296Combined sources
Beta strandi336 – 3405Combined sources
Turni342 – 3443Combined sources
Helixi347 – 3504Combined sources
Beta strandi360 – 3623Combined sources
Turni363 – 3664Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi381 – 3833Combined sources
Helixi389 – 3913Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi402 – 4087Combined sources
Helixi409 – 4113Combined sources
Beta strandi412 – 4176Combined sources
Beta strandi420 – 4256Combined sources
Beta strandi428 – 4303Combined sources
Beta strandi434 – 4374Combined sources
Turni438 – 4403Combined sources
Beta strandi441 – 4466Combined sources
Beta strandi450 – 4534Combined sources
Beta strandi455 – 4606Combined sources
Beta strandi463 – 4675Combined sources
Helixi472 – 4743Combined sources
Beta strandi476 – 4783Combined sources
Beta strandi484 – 4863Combined sources
Turni487 – 4893Combined sources
Beta strandi492 – 4954Combined sources
Helixi498 – 5003Combined sources
Beta strandi503 – 5064Combined sources
Helixi512 – 5143Combined sources
Beta strandi516 – 5194Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ6ITZ3.
SMRiQ6ITZ3. Positions 1-240, 266-520.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6ITZ3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini269 – 396128Ricin B-type lectin 1PROSITE-ProRule annotationAdd
BLAST
Domaini400 – 520121Ricin B-type lectin 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni284 – 2863Galactose bindingBy similarity
Regioni494 – 4963Galactose bindingBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

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.

Q6ITZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
YERLDLDVTS QTTGEEYFRF ITLLRDYVSS GSFSNEIPLL RQSGGGVEAA
60 70 80 90 100
RFVLVELTNE GGDSITAAID VTNLYVVAYQ AGSQSYFLSG PGTHLFTGTT
110 120 130 140 150
RSSLPFNGSY PDLEQYAGHR KQIPLGIDQL IQSVTALRFP GNTRTQARSI
160 170 180 190 200
LILIQMISEA ARFNPILWRA RQYINSGASF LPDVYMLELE TSWGQQSTQV
210 220 230 240 250
QQSTEGVFNN PIRLAIPGNF VTLTNVRDVI ASLAIMLFVC GERPSSSDVR
260 270 280 290 300
YWPLVIRPVI ADDVTCSASE PTVRIVGRNG MNVDVRDDDF HDGNQIQLWP
310 320 330 340 350
SKSNNDPNQL WTIKRDGTIR SNGSCLTTYG YTAGVYVMIF DCNTAVREAT
360 370 380 390 400
IWQIWGNGTI INPRSNLALA ASSGIKGTTL TVQTLDYTLG QGWLAGNDTA
410 420 430 440 450
PREVTIYGFN DLCMESNGGS VWVETCVSQQ NDRWALYGDG SIRPEQNQDQ
460 470 480 490 500
CLTSGRDSVA GINIVSCSGG SSGQRWVFTN EGAILNLKNG LAMDVANPGL
510 520
GQIIIYPATG KPNQMWLPVP
Length:520
Mass (Da):56,957
Last modified:July 5, 2004 - v1
Checksum:i4F9561A0BD92A915
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51D → R AA sequence (PubMed:15001393).Curated
Sequence conflicti5 – 51D → R AA sequence (PubMed:1450445).Curated
Sequence conflicti7 – 71D → R AA sequence (PubMed:15001393).Curated
Sequence conflicti7 – 71D → R AA sequence (PubMed:1450445).Curated
Sequence conflicti10 – 101S → H AA sequence (PubMed:15001393).Curated
Sequence conflicti10 – 101S → H AA sequence (PubMed:1450445).Curated
Sequence conflicti29 – 291S → H AA sequence (PubMed:1450445).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY625281 mRNA. Translation: AAT37532.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY625281 mRNA. Translation: AAT37532.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ6ITZ3.
SMRiQ6ITZ3. Positions 1-240, 266-520.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ6ITZ3.

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 nameiML4_VISAL
AccessioniPrimary (citable) accession number: Q6ITZ3
Secondary accession number(s): Q9S7D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: July 5, 2004
Last modified: October 14, 2015
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Several isoforms exist.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.