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Protein

Beta-galactoside-specific lectin 4

Gene
N/A
Organism
Viscum album (European mistletoe)
Status
Reviewed-Annotation score: -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

Miscellaneous

Several isoforms exist.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1591 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protein synthesis inhibitor, Toxin
Biological processPlant defense
LigandLectin

Protein family/group databases

CAZyiCBM13 Carbohydrate-Binding Module Family 13
UniLectiniQ6ITZ3

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)DescriptionActionsGraphical viewLength
ChainiPRO_50000934971 – 240Beta-galactoside-specific lectin 4 chain AAdd BLAST240
PropeptideiPRO_0000284730241 – 265Connecting peptideCuratedAdd BLAST25
ChainiPRO_5000093498266 – 520Beta-galactoside-specific lectin 4 chain BAdd BLAST255

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi107N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi240 ↔ 266Interchain (between A and B chains)PROSITE-ProRule annotation2 Publications
Glycosylationi322N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi325 ↔ 342PROSITE-ProRule annotation1 Publication
Glycosylationi357N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi397N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi413 ↔ 426PROSITE-ProRule annotation1 Publication
Disulfide bondi451 ↔ 467PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

iPTMnetiQ6ITZ3

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ6ITZ3
SMRiQ6ITZ3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6ITZ3

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini269 – 396Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST128
Domaini400 – 520Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST121

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni284 – 286Galactose bindingBy similarity3
Regioni494 – 496Galactose bindingBy similarity3

Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

CDDicd00161 RICIN, 2 hits
Gene3Di3.40.420.10, 1 hit
4.10.470.10, 1 hit
InterProiView protein in InterPro
IPR036041 Ribosome-inact_prot_sf
IPR017989 Ribosome_inactivat_1/2
IPR001574 Ribosome_inactivat_prot
IPR016138 Ribosome_inactivat_prot_sub1
IPR016139 Ribosome_inactivat_prot_sub2
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PfamiView protein in Pfam
PF00652 Ricin_B_lectin, 2 hits
PF00161 RIP, 1 hit
PRINTSiPR00396 SHIGARICIN
SMARTiView protein in SMART
SM00458 RICIN, 2 hits
SUPFAMiSSF50370 SSF50370, 2 hits
SSF56371 SSF56371, 1 hit
PROSITEiView protein in PROSITE
PS50231 RICIN_B_LECTIN, 2 hits

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)DescriptionActionsGraphical viewLength
Sequence conflicti5D → R AA sequence (PubMed:15001393).Curated1
Sequence conflicti5D → R AA sequence (PubMed:1450445).Curated1
Sequence conflicti7D → R AA sequence (PubMed:15001393).Curated1
Sequence conflicti7D → R AA sequence (PubMed:1450445).Curated1
Sequence conflicti10S → H AA sequence (PubMed:15001393).Curated1
Sequence conflicti10S → H AA sequence (PubMed:1450445).Curated1
Sequence conflicti29S → H AA sequence (PubMed:1450445).Curated1

Sequence databases

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

Similar proteinsi

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
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13 Carbohydrate-Binding Module Family 13
UniLectiniQ6ITZ3

PTM databases

iPTMnetiQ6ITZ3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ6ITZ3

Family and domain databases

CDDicd00161 RICIN, 2 hits
Gene3Di3.40.420.10, 1 hit
4.10.470.10, 1 hit
InterProiView protein in InterPro
IPR036041 Ribosome-inact_prot_sf
IPR017989 Ribosome_inactivat_1/2
IPR001574 Ribosome_inactivat_prot
IPR016138 Ribosome_inactivat_prot_sub1
IPR016139 Ribosome_inactivat_prot_sub2
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PfamiView protein in Pfam
PF00652 Ricin_B_lectin, 2 hits
PF00161 RIP, 1 hit
PRINTSiPR00396 SHIGARICIN
SMARTiView protein in SMART
SM00458 RICIN, 2 hits
SUPFAMiSSF50370 SSF50370, 2 hits
SSF56371 SSF56371, 1 hit
PROSITEiView protein in PROSITE
PS50231 RICIN_B_LECTIN, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiML4_VISAL
AccessioniPrimary (citable) accession number: Q6ITZ3
Secondary accession number(s): Q9S7D0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: July 5, 2004
Last modified: July 18, 2018
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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