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Entry version 76 (17 Jun 2020)
Sequence version 1 (01 Jun 2003)
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Protein
Submitted name:

Hemolytic lectin CEL-III

Gene

cel3

Organism
Cucumaria echinata (Sea cucumber)
Status
Unreviewed-Annotation score:

Annotation score:1 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei19N-acetyl-D-galactosamineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi33Calcium 1Combined sources1
Metal bindingi34Calcium 1; via carbonyl oxygenCombined sources1
Metal bindingi36Calcium 1; via carbonyl oxygenCombined sources1
Metal bindingi42Magnesium 1Combined sources1
Metal bindingi43Magnesium 1; via carbonyl oxygenCombined sources1
Metal bindingi53Calcium 1Combined sources1
Metal bindingi82Magnesium 1Combined sources1
Metal bindingi83Magnesium 1; via carbonyl oxygenCombined sources1
Binding sitei117N-acetyl-D-galactosamine; via carbonyl oxygenCombined sources1
Metal bindingi131Calcium 2Combined sources1
Metal bindingi134Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi137Calcium 3; via amide nitrogenCombined sources1
Metal bindingi138Calcium 3; via amide nitrogen and carbonyl oxygenCombined sources1
Metal bindingi141Magnesium 1; via carbonyl oxygenCombined sources1
Metal bindingi147Calcium 2Combined sources1
Metal bindingi151Calcium 2Combined sources1
Metal bindingi178Calcium 4Combined sources1
Metal bindingi179Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi181Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi187Magnesium 2Combined sources1
Metal bindingi187Magnesium 3Combined sources1
Metal bindingi188Magnesium 2; via carbonyl oxygenCombined sources1
Metal bindingi198Calcium 4Combined sources1
Metal bindingi219Calcium 5Combined sources1
Metal bindingi220Calcium 5; via carbonyl oxygenCombined sources1
Metal bindingi221Calcium 6Combined sources1
Metal bindingi222Calcium 5; via carbonyl oxygenCombined sources1
Metal bindingi228Magnesium 2Combined sources1
Metal bindingi229Magnesium 2; via carbonyl oxygenCombined sources1
Metal bindingi229Magnesium 3; via carbonyl oxygenCombined sources1
Binding sitei232N-acetyl-D-galactosamineCombined sources1
Metal bindingi239Calcium 5Combined sources1
Metal bindingi266Calcium 7Combined sources1
Metal bindingi267Calcium 7; via carbonyl oxygenCombined sources1
Metal bindingi269Calcium 7; via carbonyl oxygenCombined sources1
Metal bindingi275Magnesium 2Combined sources1
Metal bindingi276Magnesium 2; via carbonyl oxygenCombined sources1
Metal bindingi276Magnesium 3; via carbonyl oxygenCombined sources1
Metal bindingi286Calcium 7Combined sources1
Metal bindingi383Calcium 8Combined sources1

<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

LigandCalciumCombined sources, LectinImported, MagnesiumCombined sources, Metal-bindingCombined sources

Protein family/group databases

Carbohydrate-Active enZymes

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

Transport Classification Database

More...
TCDBi
1.C.96.1.1 the haemolytic lectin, cel-iii (cel-iii) family

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
Q868M7

<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
Submitted name:
Hemolytic lectin CEL-IIIImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cel3Imported
<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>OrganismiCucumaria echinata (Sea cucumber)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 identifieri40245 [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 lineageiEukaryotaMetazoaEchinodermataEleutherozoaEchinozoaHolothuroideaDendrochirotaceaDendrochirotidaCucumariidaeCucumaria

<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

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi14 ↔ 59Combined sources
Disulfide bondi31 ↔ 48Combined sources
Disulfide bondi72 ↔ 88Combined sources
Disulfide bondi129 ↔ 146Combined sources
Disulfide bondi176 ↔ 193Combined sources
Disulfide bondi217 ↔ 234Combined sources
Disulfide bondi249 ↔ 254Combined sources
Disulfide bondi264 ↔ 281Combined sources
Disulfide bondi308 ↔ 390Combined sources
Disulfide bondi377 ↔ 416Combined sources
Disulfide bondi425 ↔ 439Combined sources
Disulfide bondi431 ↔ 436Combined sources

<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

3D structure databases

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

More...
SMRi
Q868M7

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
Q868M7

<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>Domaini28 – 102Ricin B-type lectinInterPro annotationAdd BLAST75
Domaini115 – 245Ricin B-type lectinInterPro annotationAdd BLAST131
Domaini261 – 293Ricin B-type lectinInterPro annotationAdd BLAST33

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>Regioni131 – 134N-acetyl-D-galactosamine bindingCombined sources4
Regioni144 – 147N-acetyl-D-galactosamine bindingCombined sources4
Regioni178 – 179N-acetyl-D-galactosamine bindingCombined sources2
Regioni191 – 194N-acetyl-D-galactosamine bindingCombined sources4
Regioni219 – 222N-acetyl-D-galactosamine bindingCombined sources4

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00161 RICIN, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1750.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR028988 CEL-III_C_sf
IPR041014 CEL_III_C
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18054 CEL_III_C, 1 hit
PF00652 Ricin_B_lectin, 2 hits

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
SSF111265 SSF111265, 1 hit
SSF50370 SSF50370, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50231 RICIN_B_LECTIN, 3 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.

Q868M7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVSLVPCGFA QVLCTNPLDI GELRNYKSKQ CVDIVGNQGS GNIATHDCDG
60 70 80 90 100
LSDQQIIMCG DGTIRNEARN YCFTPDGSGN ANVMSSPCTL YPEIPSSQRW
110 120 130 140 150
RLGRKKAFTD NGGIEQVATE IINLASGKCL DVEGSDGTGD IGVYDCQNLD
160 170 180 190 200
DQYFYIRSRG PELFYGRLRN EKSDLCLDVE GSEGKGNVLM YSCEDNLDQW
210 220 230 240 250
FRYYENGEIV NAKQGMCLDV EGSDGSGNVG IYRCDDLRDQ MWSRPNAYCN
260 270 280 290 300
GDYCSFLNKE SNKCLDVSGD QGTGDVGTWQ CDGLPDQRFK WVFDDWEVPT
310 320 330 340 350
ATWNMVGCDQ NGKVSQQISN TISFSSTVTA GVAVEVSSTI EKGVIFAKAS
360 370 380 390 400
VSVKVTASLS KAWTNSQSGT TAITYTCDNY DSDEEFTRGC MWQLAIETTE
410 420 430 440
VKSGDLLVWN PQIIKCTRSN TAPGCAPFTK CANEDCTFCT DI
Length:442
Mass (Da):48,456
Last modified:June 1, 2003 - 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:i3E47C608446D40EC
GO

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
AB109017 mRNA Translation: BAC75827.1

<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
AB109017 mRNA Translation: BAC75827.1

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
1VCLX-ray1.70A/B11-442[»]
2Z48X-ray1.70A/B11-442[»]
2Z49X-ray1.95A/B11-442[»]
3W9TX-ray2.90A/B/C/D/E/F/G11-442[»]
SMRiQ868M7
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiCBM13 Carbohydrate-Binding Module Family 13
TCDBi1.C.96.1.1 the haemolytic lectin, cel-iii (cel-iii) family
UniLectiniQ868M7

Miscellaneous databases

EvolutionaryTraceiQ868M7

Family and domain databases

CDDicd00161 RICIN, 2 hits
Gene3Di3.30.1750.10, 1 hit
InterProiView protein in InterPro
IPR028988 CEL-III_C_sf
IPR041014 CEL_III_C
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PfamiView protein in Pfam
PF18054 CEL_III_C, 1 hit
PF00652 Ricin_B_lectin, 2 hits
SMARTiView protein in SMART
SM00458 RICIN, 2 hits
SUPFAMiSSF111265 SSF111265, 1 hit
SSF50370 SSF50370, 2 hits
PROSITEiView protein in PROSITE
PS50231 RICIN_B_LECTIN, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiQ868M7_CUCEC
<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: Q868M7
<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/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: June 17, 2020
This is version 76 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 statusiUnreviewed (UniProtKB/TrEMBL)

<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-structureCombined sources
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