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UniProtKB - P06750 (AGGL_RICCO)

Entry version 136 (02 Jun 2021)
Sequence version 1 (01 Jan 1988)
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Protein

Agglutinin

Gene
N/A
Organism
Ricinus communis (Castor bean)
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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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. EC:3.2.2.22

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei74Carbohydrate; via amide nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei104By similarity1
Active sitei147By similarity1
Active sitei200By similarity1
Active sitei203By similarity1
Binding sitei312Carbohydrate; via carbonyl oxygenCombined sources1 Publication1
Binding sitei337CarbohydrateCombined sources1 Publication1
Binding sitei342CarbohydrateCombined sources1 Publication1
Binding sitei348CarbohydrateCombined sources1 Publication1
Binding sitei381CarbohydrateCombined sources1 Publication1
Binding sitei397CarbohydrateCombined sources1 Publication1
Binding sitei437CarbohydrateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi104 – 105AMPBy similarity2
Nucleotide bindingi145 – 147AMPBy similarity3

<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, Nucleotide-binding

Protein family/group databases

Carbohydrate-Active enZymes

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

UniLectin database of carbohydrate-binding proteins

More...UniLectini		P06750

<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_and_taxonomy_section">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:
Agglutinin
Alternative name(s):
RCA
Cleaved into the following 2 chains:
Agglutinin A chain (EC:3.2.2.22)
Alternative name(s):
rRNA N-glycosidase
Agglutinin B chain
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiRicinus communis (Castor bean)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri3988 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 › rosids › fabids › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
<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_000003072625 – 290Agglutinin A chainAdd BLAST266
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_0000030727291 – 302Linker peptide2 PublicationsAdd BLAST12
ChainiPRO_0000030728303 – 564Agglutinin B chain1 PublicationAdd BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi34N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi259N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi282 ↔ 306Interchain (between A and B chains)PROSITE-ProRule annotation1 Publication
Disulfide bondi322 ↔ 341PROSITE-ProRule annotation1 Publication
Disulfide bondi365 ↔ 382PROSITE-ProRule annotation1 Publication
Glycosylationi397N-linked (GlcNAc...) asparagine1
Glycosylationi437N-linked (GlcNAc...) asparagine1
Disulfide bondi453 ↔ 466PROSITE-ProRule annotation1 Publication
Disulfide bondi492 ↔ 509PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		10, 3 N-Linked glycans

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		3988.XP_002534220.1

<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

1564
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		P06750

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		P06750

<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_and_domains_section">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>Domaini309 – 436Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST128
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati319 – 3611-alphaAdd BLAST43
Repeati362 – 4021-betaAdd BLAST41
Repeati405 – 4371-gammaAdd BLAST33
Domaini439 – 563Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST125
Repeati450 – 4852-alphaAdd BLAST36
Repeati489 – 5282-betaAdd BLAST40
Repeati531 – 5582-gammaAdd BLAST28

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>Regioni32 – 34Carbohydrate bindingCombined sources1 Publication3
Regioni164 – 169Carbohydrate bindingBy similarity6
Regioni218 – 220Carbohydrate bindingBy similarity3
Regioni324 – 328Carbohydrate bindingCombined sources1 Publication5
Regioni536 – 539Carbohydrate bindingBy similarity4
Regioni553 – 557Carbohydrate bindingBy similarity5

<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

In the N-terminal section; belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QUVN, Eukaryota

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
IPR017988, Ribosome_inactivat_prot_CS
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
PS00275, SHIGA_RICIN, 1 hit

<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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P06750-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYAVATWLCF GSTSGWSFTL EDNNIFPKQY PIINFTTADA TVESYTNFIR 
        60         70         80         90        100
AVRSHLTTGA DVRHEIPVLP NRVGLPISQR FILVELSNHA ELSVTLALDV 
       110        120        130        140        150
TNAYVVGCRA GNSAYFFHPD NQEDAEAITH LFTDVQNSFT FAFGGNYDRL 
       160        170        180        190        200
EQLGGLRENI ELGTGPLEDA ISALYYYSTC GTQIPTLARS FMVCIQMISE 
       210        220        230        240        250
AARFQYIEGE MRTRIRYNRR SAPDPSVITL ENSWGRLSTA IQESNQGAFA 
       260        270        280        290        300
SPIQLQRRNG SKFNVYDVSI LIPIIALMVY RCAPPPSSQF SLLIRPVVPN 
       310        320        330        340        350
FNADVCMDPE PIVRIVGRNG LCVDVTGEEF FDGNPIQLWP CKSNTDWNQL 
       360        370        380        390        400
WTLRKDSTIR SNGKCLTISK SSPRQQVVIY NCSTATVGAT RWQIWDNRTI 
       410        420        430        440        450
INPRSGLVLA ATSGNSGTKL TVQTNIYAVS QGWLPTNNTQ PFVTTIVGLY 
       460        470        480        490        500
GMCLQANSGK VWLEDCTSEK AEQQWALYAD GSIRPQQNRD NCLTTDANIK 
       510        520        530        540        550
GTVVKILSCG PASSGQRWMF KNDGTILNLY NGLVLDVRRS DPSLKQIIVH 
       560 
PFHGNLNQIW LPLF
Length:564
Mass (Da):62,851
Last modified:January 1, 1988 - 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:iD455F2A72F609759
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 conflicti331F → T AA sequence (Ref. 2) Curated1
Sequence conflicti362N → D AA sequence (Ref. 2) Curated1
Sequence conflicti374R → G AA sequence (Ref. 2) Curated1
Sequence conflicti404R → T AA sequence (Ref. 2) Curated1
Sequence conflicti552F → V AA sequence (Ref. 2) 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
M12089 mRNA Translation: AAA33869.1
S40368 mRNA Translation: AAB22584.1

Protein sequence database of the Protein Information Resource

More...PIRi		A24261, RLCSAG

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Functional Glycomics Gateway - Glycan Binding

RCA

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12089 mRNA Translation: AAA33869.1
S40368 mRNA Translation: AAB22584.1
PIRiA24261, RLCSAG

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
1RZOX-ray2.63A/C25-286[»]
B/D303-564[»]
SMRiP06750
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi3988.XP_002534220.1

Protein family/group databases

CAZyiCBM13, Carbohydrate-Binding Module Family 13
UniLectiniP06750

PTM databases

GlyConnecti10, 3 N-Linked glycans

Phylogenomic databases

eggNOGiENOG502QUVN, Eukaryota

Miscellaneous databases

EvolutionaryTraceiP06750

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
IPR017988, Ribosome_inactivat_prot_CS
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
PS00275, SHIGA_RICIN, 1 hit

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 nameiAGGL_RICCO
<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: P06750
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 2, 2021
This is version 136 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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