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Entry version 77 (02 Jun 2021)
Sequence version 1 (01 May 1997)
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Protein

Jacalin-related lectin Calsepa

Gene
N/A
Organism
Calystegia sepium (Hedge bindweed) (Convolvulus sepium)
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

Mannose-binding lectin (PubMed:9111143, PubMed:18266762, PubMed:14561768, PubMed:26971576, PubMed:28973127).

Preferentially binds mannose at concentrations ranging between 5 and 25 mM, but binds also glucose. Has a marked preference for methylated sugar derivatives, such as alpha-MeMan and alpha-MeGlc, at concentration down to 5 mM (PubMed:14561768).

Binds to N-glycans, but not to glycolipid-type or other type of glycans (PubMed:28973127).

Binds N-linked high-mannose-type glycans (PubMed:18266762, PubMed:28973127).

Has a preference for smaller (Man2-Man6) high-mannose-type glycans to larger (Man7-Man9) ones. Recognizes both alpha1-6 extended and alpha1-3 extended monoantennary glycans. The addition of alpha1-2Man to the Man-alpha1-3Man-beta branch results in a significant loss of affinity, but beta1-2GlcNAc has some affinity. Has less affinity for biantennary glycans (PubMed:18266762).

However, affinity is significant for the biantennary complex-type N-glycans with bisecting GlcNAc (PubMed:18266762, PubMed:26971576, PubMed:28973127).

No affinity is observed for tri- and tetra-antennary glycans (PubMed:18266762).

Binds bisected glycans of the mouse brain. Selectively binds to bisecting N-glycans which are in back-fold conformation, and does not favor a glycan with an extend conformation (PubMed:26971576).

Has hemagglutinating activity against rabbit erythrocytes at 0.3 µg/ml and against trypsin-treated human erythrocytes at 5 µg/ml. Has mitogenic activity in murine cells (PubMed:9111143).

5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Hemagglutinating activity is most inhibited by methyl alpha-mannopyranoside. This activity is inhibited to a less extent (about a third of the inhibition of that of methyl alpha-mannopyranoside) by methyl alpha-glucoside, other alpha-glucosides, such as maltose, isomaltose, panose or palatinose, and alpha-glucosides modified at the second position, such as methyl 2-deoxy-alpha-arabinoglucopyranoside or methyl 2-acetamido-2-deoxy alpha-glucopyranoside. Mildly inhibited by free monosaccharides, with glucose presenting at least 20-fold less inhibitory effect on hemagglutinating activity than mannose. Glycoproteins are somewhat inhibitory, the best being asialothyroglobulin and ovomucoid. Not inhibited by isomaltitol, sucrose or trehalose.1 Publication

<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

GO - Biological processi

<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

LigandLectin

Protein family/group databases

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
P93114

<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:
Jacalin-related lectin Calsepa7 Publications
Alternative name(s):
Agglutinin6 Publications
Mannose/maltose-specific lectin1 Publication
<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>OrganismiCalystegia sepium (Hedge bindweed) (Convolvulus sepium)Imported
<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 identifieri47519 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeConvolvuleaeCalystegia

<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

Keywords - Cellular componenti

Cytoplasm

<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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Can be used for the isolation of glycoproteins from humans, plants and fungi. Is a powerful T-cell mitogen in the mouse, and can thus be used as an alternative to concanavalin A for the mitogenic proliferation of murine lymphocytes (PubMed:9111143). Identified as one of the several suitable fluorescently labeled lectins that can be used in a combination for the visualization and quantification of extracellular glycoconjugates in dental supragingival biofilms grown for 48 hours in situ in the absence of dietary carbohydrates (PubMed:28748044). Used in lectin-based microarrays to detect altered glycosylation in cancer tissue (PubMed:32143591).3 Publications

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCurated
<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_00004504392 – 153Jacalin-related lectin CalsepaCuratedAdd BLAST152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Not glycosylated.1 Publication

Keywords - PTMi

Acetylation

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Rhizome (at protein level) (PubMed:8955378, PubMed:9111143, PubMed:15299962, PubMed:10908718, PubMed:14561768). Detected in the cortex and the pith of rhizome. Not detected in vascular tissues, pericycle, endodermis or rhizodermis (PubMed:10908718).5 Publications

<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

Homodimer.

3 Publications

GO - Molecular functioni

<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

1153
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

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SMRi
P93114

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P93114

<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>Domaini6 – 152Jacalin-type lectinPROSITE-ProRule annotationAdd BLAST147

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>Regioni17 – 18N-glycan bindingCombined sources2 Publications2
Regioni95 – 96N-glycan bindingCombined sources2 Publications2
Regioni140 – 144N-glycan bindingCombined sources2 Publications5

<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 jacalin lectin family.PROSITE-ProRule annotationCurated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09612, Jacalin, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.100.10.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001229, Jacalin-like_lectin_dom
IPR033734, Jacalin-like_lectin_dom_plant
IPR036404, Jacalin-like_lectin_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF01419, Jacalin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00915, Jacalin, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51101, SSF51101, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51752, JACALIN_LECTIN, 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%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.

P93114-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAVPMDTISG PWGNNGGNFW SFRPVNKINQ IVISYGGGGN NPIALTFSST
60 70 80 90 100
KADGSKDTIT VGGGGPDSIT GTEMVNIGTD EYLTGISGTF GIYLDNNVLR
110 120 130 140 150
SITFTTNLKA HGPYGQKVGT PFSSANVVGN EIVGFLGRSG YYVDAIGTYN

RHK
Length:153
Mass (Da):16,063
Last modified:May 1, 1997 - 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:iD94A5F2A8FED39AE
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 16092 Da. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U56820 mRNA Translation: AAC49564.1

<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
U56820 mRNA Translation: AAC49564.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OUWX-ray1.37A/B/C/D2-153[»]
5AV7X-ray1.85A/B/C/D3-153[»]
5XFIX-ray1.65A/B1-153[»]
SMRiP93114
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

UniLectiniP93114

Miscellaneous databases

EvolutionaryTraceiP93114

Family and domain databases

CDDicd09612, Jacalin, 1 hit
Gene3Di2.100.10.30, 1 hit
InterProiView protein in InterPro
IPR001229, Jacalin-like_lectin_dom
IPR033734, Jacalin-like_lectin_dom_plant
IPR036404, Jacalin-like_lectin_dom_sf
PfamiView protein in Pfam
PF01419, Jacalin, 1 hit
SMARTiView protein in SMART
SM00915, Jacalin, 1 hit
SUPFAMiSSF51101, SSF51101, 1 hit
PROSITEiView protein in PROSITE
PS51752, JACALIN_LECTIN, 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 nameiLECC_CALSE
<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: P93114
<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: August 12, 2020
Last sequence update: May 1, 1997
Last modified: June 2, 2021
This is version 77 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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