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Protein

Concanavalin-A

Gene
N/A
Organism
Canavalia ensiformis (Jack bean) (Dolichos ensiformis)
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

D-mannose specific lectin.

Miscellaneous

Binds one manganese (or another transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi119CalciumBy similarity1
<p>This subsection of the ‘Function’ 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 sitei119Carbohydrate1
Binding sitei139Carbohydrate; via amide nitrogen1
Metal bindingi171Manganese1
Metal bindingi173Calcium1 Publication1
Metal bindingi173Manganese1
Metal bindingi175Calcium; via carbonyl oxygen1 Publication1
Metal bindingi177Calcium1 Publication1
Metal bindingi182Calcium1 Publication1
Metal bindingi182Manganese1
Metal bindingi187Manganese1

<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

<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

LigandCalcium, Lectin, Manganese, Mannose-binding, Metal-binding

Protein family/group databases

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
P02866

<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:
Concanavalin-A
Short name:
Con A
<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>OrganismiCanavalia ensiformis (Jack bean) (Dolichos ensiformis)
<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 identifieri3823 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeindigoferoid/millettioid cladePhaseoleaeCanavalia

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5820

<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 – 291 PublicationAdd BLAST29
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001757730 – 148Concanavalin-A, 2nd partAdd BLAST119
<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_0000017578149 – 1631 PublicationAdd BLAST15
ChainiPRO_0000017579164 – 281Concanavalin-A, 1st partAdd BLAST118
PropeptideiPRO_0000017580282 – 2909

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>Glycosylationi152N-linked (GlcNAc...) asparagine1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The mature chain consists of residues 164-281 followed by 30-148. To form a mature chain the precursor undergoes further post-translational modification after removal of the signal sequence; cleavage after Asn at positions 148, 163, and 281 is followed by transposition and ligation (By formation of a new peptide bond) of residues 164-281 and 30-148.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei148 – 149Cleavage2
Sitei163 – 164Cleavage2
Sitei281 – 282Cleavage2

Keywords - PTMi

Glycoprotein

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P02866, 109 interactors

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P02866

<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

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1APNX-ray2.50A/B28-148[»]
1BXHX-ray2.75A/B/C/D148-164[»]
1C57neutron diffraction2.40A148-164[»]
1CESX-ray2.70A/B28-148[»]
1CJPX-ray2.78A/B/C/D30-148[»]
1CN1X-ray3.20A/B30-281[»]
1CONX-ray2.00A28-148[»]
1CVNX-ray2.30A/B/C/D30-148[»]
1DQ0X-ray1.70A28-148[»]
1DQ1X-ray2.15A28-148[»]
1DQ2X-ray2.05A/B28-148[»]
1DQ4X-ray2.90A/B28-148[»]
1DQ5X-ray2.00A28-148[»]
1DQ6X-ray1.90A28-148[»]
1ENQX-ray2.50A/B/C/D30-148[»]
1ENRX-ray1.83A28-148[»]
1ENSX-ray2.80A/B30-148[»]
1GICX-ray2.00A/B28-148[»]
1GKBX-ray1.56A/B148-164[»]
1HQWX-ray2.40A30-148[»]
1I3HX-ray1.20A28-148[»]
1JBCX-ray1.15A28-148[»]
1JN2X-ray1.90P28-148[»]
1JOJX-ray3.00A/B/C/D28-148[»]
1JUIX-ray2.75A/B/C/D28-148[»]
1JW6X-ray1.93A28-148[»]
1JYCX-ray2.75A/B/C/D28-148[»]
1JYIX-ray2.75A/B/C/D28-148[»]
1NLSX-ray0.94A28-148[»]
1NXDX-ray1.901/2/3/4148-164[»]
1ONAX-ray2.35A/B/C/D30-148[»]
1QGLX-ray2.66A/B30-148[»]
1QNYX-ray1.80A28-148[»]
1SCRX-ray2.00A28-148[»]
1SCSX-ray1.60A28-148[»]
1TEIX-ray2.70A/B/C/D/E/F/G/H28-148[»]
1VALX-ray3.00A/B/C/D30-148[»]
1VAMX-ray2.75A/B/C/D30-148[»]
1XQNneutron diffraction2.50A28-148[»]
2CNAX-ray2.00A28-148[»]
2CTVX-ray1.95A28-148[»]
2ENRX-ray2.35A28-148[»]
2UU8X-ray0.94A148-164[»]
2YZ4neutron diffraction2.20A28-148[»]
3CNAX-ray2.40A30-281[»]
3D4KX-ray1.80A/B/C/D148-164[»]
3ENRX-ray2.40A/B148-164[»]
3NWKX-ray2.09A/B/C/D148-164[»]
4P9WX-ray2.11A/B/C/D28-148[»]
4P9XX-ray2.06A/B/C/D28-148[»]
4P9YX-ray1.89A/B28-148[»]
4PF5X-ray2.04A/B28-148[»]
5CNAX-ray2.00A/B/C/D28-148[»]
5O6NX-ray1.35A148-164[»]
5WEYOther1.80A148-164[»]
5Z5NX-ray2.04A/B/C/D148-164[»]
5Z5PX-ray1.40A/B148-164[»]
5Z5YX-ray1.89A/B148-164[»]
5ZACX-ray2.59A/B/C/D148-164[»]
6AHGX-ray2.83A/B/C148-164[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P02866

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

More...
SMRi
P02866

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P02866

<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

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>Regioni262 – 263Carbohydrate binding2

<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 leguminous lectin family.Curated

Keywords - Domaini

Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06899 lectin_legume_LecRK_Arcelin_Co, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013320 ConA-like_dom_sf
IPR016363 L-lectin
IPR000985 Lectin_LegA_CS
IPR019825 Lectin_legB_Mn/Ca_BS
IPR001220 Legume_lectin_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00139 Lectin_legB, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF002690 L-type_lectin_plant, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49899 SSF49899, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00308 LECTIN_LEGUME_ALPHA, 1 hit
PS00307 LECTIN_LEGUME_BETA, 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>.<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.

P02866-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAISKKSSLF LPIFTFITMF LMVVNKVSSS THETNALHFM FNQFSKDQKD
60 70 80 90 100
LILQGDATTG TDGNLELTRV SSNGSPQGSS VGRALFYAPV HIWESSAVVA
110 120 130 140 150
SFEATFTFLI KSPDSHPADG IAFFISNIDS SIPSGSTGRL LGLFPDANVI
160 170 180 190 200
RNSTTIDFNA AYNADTIVAV ELDTYPNTDI GDPSYPHIGI DIKSVRSKKT
210 220 230 240 250
AKWNMQNGKV GTAHIIYNSV DKRLSAVVSY PNADSATVSY DVDLDNVLPE
260 270 280 290
WVRVGLSAST GLYKETNTIL SWSFTSKLKS NEIPDIATVV
Length:290
Mass (Da):31,480
Last modified:October 3, 2003 - v2
<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:i0F2F7DBBCF547E42
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 conflicti33E → Q AA sequence (PubMed:1112814).Curated1
Sequence conflicti35N → D AA sequence (PubMed:1112814).Curated1
Sequence conflicti62D → E in CAA25787 (PubMed:3965973).Curated1
Sequence conflicti66E → R in CAA25787 (PubMed:3965973).Curated1
Sequence conflicti77Q → E AA sequence (PubMed:1112814).Curated1
Sequence conflicti98 – 101VVAS → TVSA AA sequence (PubMed:1112814).Curated4
Sequence conflicti107T → A AA sequence (PubMed:1112814).Curated1
Sequence conflicti207N → D AA sequence (PubMed:1112813).Curated1
Sequence conflicti245 – 246DN → ND AA sequence (PubMed:1112813).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X01632 mRNA Translation: CAA25787.1
AF308777 mRNA Translation: AAL09432.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A03357 CVJBP

<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

Worthington enzyme manual
Functional Glycomics Gateway - Glycan Binding

Con A (Canavalia ensiformis)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01632 mRNA Translation: CAA25787.1
AF308777 mRNA Translation: AAL09432.1
PIRiA03357 CVJBP

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APNX-ray2.50A/B28-148[»]
1BXHX-ray2.75A/B/C/D148-164[»]
1C57neutron diffraction2.40A148-164[»]
1CESX-ray2.70A/B28-148[»]
1CJPX-ray2.78A/B/C/D30-148[»]
1CN1X-ray3.20A/B30-281[»]
1CONX-ray2.00A28-148[»]
1CVNX-ray2.30A/B/C/D30-148[»]
1DQ0X-ray1.70A28-148[»]
1DQ1X-ray2.15A28-148[»]
1DQ2X-ray2.05A/B28-148[»]
1DQ4X-ray2.90A/B28-148[»]
1DQ5X-ray2.00A28-148[»]
1DQ6X-ray1.90A28-148[»]
1ENQX-ray2.50A/B/C/D30-148[»]
1ENRX-ray1.83A28-148[»]
1ENSX-ray2.80A/B30-148[»]
1GICX-ray2.00A/B28-148[»]
1GKBX-ray1.56A/B148-164[»]
1HQWX-ray2.40A30-148[»]
1I3HX-ray1.20A28-148[»]
1JBCX-ray1.15A28-148[»]
1JN2X-ray1.90P28-148[»]
1JOJX-ray3.00A/B/C/D28-148[»]
1JUIX-ray2.75A/B/C/D28-148[»]
1JW6X-ray1.93A28-148[»]
1JYCX-ray2.75A/B/C/D28-148[»]
1JYIX-ray2.75A/B/C/D28-148[»]
1NLSX-ray0.94A28-148[»]
1NXDX-ray1.901/2/3/4148-164[»]
1ONAX-ray2.35A/B/C/D30-148[»]
1QGLX-ray2.66A/B30-148[»]
1QNYX-ray1.80A28-148[»]
1SCRX-ray2.00A28-148[»]
1SCSX-ray1.60A28-148[»]
1TEIX-ray2.70A/B/C/D/E/F/G/H28-148[»]
1VALX-ray3.00A/B/C/D30-148[»]
1VAMX-ray2.75A/B/C/D30-148[»]
1XQNneutron diffraction2.50A28-148[»]
2CNAX-ray2.00A28-148[»]
2CTVX-ray1.95A28-148[»]
2ENRX-ray2.35A28-148[»]
2UU8X-ray0.94A148-164[»]
2YZ4neutron diffraction2.20A28-148[»]
3CNAX-ray2.40A30-281[»]
3D4KX-ray1.80A/B/C/D148-164[»]
3ENRX-ray2.40A/B148-164[»]
3NWKX-ray2.09A/B/C/D148-164[»]
4P9WX-ray2.11A/B/C/D28-148[»]
4P9XX-ray2.06A/B/C/D28-148[»]
4P9YX-ray1.89A/B28-148[»]
4PF5X-ray2.04A/B28-148[»]
5CNAX-ray2.00A/B/C/D28-148[»]
5O6NX-ray1.35A148-164[»]
5WEYOther1.80A148-164[»]
5Z5NX-ray2.04A/B/C/D148-164[»]
5Z5PX-ray1.40A/B148-164[»]
5Z5YX-ray1.89A/B148-164[»]
5ZACX-ray2.59A/B/C/D148-164[»]
6AHGX-ray2.83A/B/C148-164[»]
ProteinModelPortaliP02866
SMRiP02866
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02866, 109 interactors

Chemistry databases

BindingDBiP02866
ChEMBLiCHEMBL5820

Protein family/group databases

UniLectiniP02866

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02866

Family and domain databases

CDDicd06899 lectin_legume_LecRK_Arcelin_Co, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR016363 L-lectin
IPR000985 Lectin_LegA_CS
IPR019825 Lectin_legB_Mn/Ca_BS
IPR001220 Legume_lectin_dom
PfamiView protein in Pfam
PF00139 Lectin_legB, 1 hit
PIRSFiPIRSF002690 L-type_lectin_plant, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00308 LECTIN_LEGUME_ALPHA, 1 hit
PS00307 LECTIN_LEGUME_BETA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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<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 nameiCONA_CANEN
<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: P02866
Secondary accession number(s): Q947H0
<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: July 21, 1986
Last sequence update: October 3, 2003
Last modified: January 16, 2019
This is version 144 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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