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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)DescriptionActionsGraphical viewLength
Active sitei1591 Publication1

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)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...)1 Publication1
Disulfide bondi240 ↔ 266Interchain (between A and B chains)PROSITE-ProRule annotation2 Publications
Glycosylationi322N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi325 ↔ 342PROSITE-ProRule annotation1 Publication
Glycosylationi357N-linked (GlcNAc...)1 Publication1
Glycosylationi397N-linked (GlcNAc...)1 Publication1
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

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Helixi14 – 28Combined sources15
Beta strandi29 – 34Combined sources6
Beta strandi37 – 40Combined sources4
Beta strandi43 – 45Combined sources3
Beta strandi50 – 59Combined sources10
Beta strandi64 – 70Combined sources7
Turni71 – 73Combined sources3
Beta strandi76 – 80Combined sources5
Beta strandi82 – 87Combined sources6
Beta strandi98 – 101Combined sources4
Helixi110 – 117Combined sources8
Helixi120 – 122Combined sources3
Beta strandi125 – 127Combined sources3
Helixi128 – 138Combined sources11
Helixi144 – 156Combined sources13
Helixi159 – 162Combined sources4
Helixi164 – 176Combined sources13
Helixi184 – 190Combined sources7
Helixi193 – 202Combined sources10
Beta strandi204 – 214Combined sources11
Beta strandi217 – 219Combined sources3
Beta strandi221 – 225Combined sources5
Helixi226 – 229Combined sources4
Turni230 – 232Combined sources3
Beta strandi275 – 277Combined sources3
Helixi278 – 280Combined sources3
Beta strandi281 – 285Combined sources5
Helixi286 – 288Combined sources3
Beta strandi295 – 299Combined sources5
Helixi307 – 309Combined sources3
Beta strandi311 – 313Combined sources3
Beta strandi315 – 317Combined sources3
Beta strandi319 – 321Combined sources3
Beta strandi324 – 329Combined sources6
Beta strandi336 – 340Combined sources5
Turni342 – 344Combined sources3
Helixi347 – 350Combined sources4
Beta strandi360 – 362Combined sources3
Turni363 – 366Combined sources4
Beta strandi367 – 370Combined sources4
Beta strandi381 – 383Combined sources3
Helixi389 – 391Combined sources3
Beta strandi394 – 397Combined sources4
Beta strandi402 – 408Combined sources7
Helixi409 – 411Combined sources3
Beta strandi412 – 417Combined sources6
Beta strandi420 – 425Combined sources6
Beta strandi428 – 430Combined sources3
Beta strandi434 – 437Combined sources4
Turni438 – 440Combined sources3
Beta strandi441 – 446Combined sources6
Beta strandi450 – 453Combined sources4
Beta strandi455 – 460Combined sources6
Beta strandi463 – 467Combined sources5
Helixi472 – 474Combined sources3
Beta strandi476 – 478Combined sources3
Beta strandi484 – 486Combined sources3
Turni487 – 489Combined sources3
Beta strandi492 – 495Combined sources4
Helixi498 – 500Combined sources3
Beta strandi503 – 506Combined sources4
Helixi512 – 514Combined sources3
Beta strandi516 – 519Combined sources4

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...

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

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)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.

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.

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: November 2, 2016
This is version 58 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.