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UniProtKB - Q6ITZ3 (ML4_VISAL)

Entry version 72 (02 Jun 2021)
Sequence version 1 (05 Jul 2004)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.By similarity EC:3.2.2.22

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1591 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		CBM13, Carbohydrate-Binding Module Family 13

UniLectin database of carbohydrate-binding proteins

More...UniLectini		Q6ITZ3

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Beta-galactoside-specific lectin 4
Alternative name(s):
Beta-galactoside-specific lectin IV
Cleaved into the following 2 chains:
Beta-galactoside-specific lectin 4 chain A (EC:3.2.2.22)
Alternative name(s):
Beta-galactoside-specific lectin IV chain A
ML-4 A
ML-IV A
rRNA N-glycosidase
Beta-galactoside-specific lectin 4 chain B
Alternative name(s):
Beta-galactoside-specific lectin IV chain B
ML-4B
ML-IV B
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiViscum album (European mistletoe)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3972 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › Santalales › Viscaceae › Viscum

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_50000934971 – 240Beta-galactoside-specific lectin 4 chain AAdd BLAST240
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000284730241 – 265Connecting peptideCuratedAdd BLAST25
ChainiPRO_5000093498266 – 520Beta-galactoside-specific lectin 4 chain BAdd BLAST255

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi107N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q6ITZ3

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Disulfide-linked dimer of A and B chains.

2 Publications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q6ITZ3

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q6ITZ3

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini269 – 396Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST128
Domaini400 – 520Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST121

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni284 – 286Galactose bindingBy similarity3
Regioni494 – 496Galactose bindingBy similarity3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.Sequence analysis

Keywords - Domaini

Repeat

Family and domain databases

Conserved Domains Database

More...CDDi		cd00161, RICIN, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.420.10, 1 hit
4.10.470.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View 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

The PANTHER Classification System

More...PANTHERi		PTHR33453, PTHR33453, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00652, Ricin_B_lectin, 2 hits
PF00161, RIP, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00396, SHIGARICIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00458, RICIN, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50370, SSF50370, 2 hits
SSF56371, SSF56371, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50231, RICIN_B_LECTIN, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4F9561A0BD92A915
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AY625281 mRNA Translation: AAT37532.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
SMRiQ6ITZ3
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiCBM13, Carbohydrate-Binding Module Family 13
UniLectiniQ6ITZ3

PTM databases

iPTMnetiQ6ITZ3

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
PANTHERiPTHR33453, PTHR33453, 1 hit
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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiML4_VISAL
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6ITZ3
Secondary accession number(s): Q9S7D0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: July 5, 2004
Last modified: June 2, 2021
This is version 72 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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
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