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Q868M7 (Q868M7_CUCEC) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
Gene names
Name:cel3 EMBL BAC75827.1
OrganismCucumaria echinata (Sea cucumber) EMBL BAC75827.1
Taxonomic identifier40245 [NCBI]
Taxonomic lineageEukaryotaMetazoaEchinodermataEleutherozoaEchinozoaHolothuroideaDendrochirotaceaDendrochirotidaCucumariidaeCucumaria

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region131 – 1344N-acetyl-D-galactosamine binding
Region178 – 1792N-acetyl-D-galactosamine binding
Region191 – 1944N-acetyl-D-galactosamine binding
Region219 – 2202N-acetyl-D-galactosamine binding
Region223 – 2242Chloride binding PDB 1VCL

Sites

Metal binding331Calcium 1 PDB 3W9T
Metal binding341Calcium 1; via carbonyl oxygen PDB 3W9T
Metal binding361Calcium 1; via carbonyl oxygen PDB 3W9T
Metal binding421Magnesium 1 PDB 3W9T
Metal binding431Magnesium 1; via amide nitrogen and carbonyl oxygen PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding531Calcium 1 PDB 3W9T
Metal binding821Magnesium 1 PDB 3W9T
Metal binding831Magnesium 1; via carbonyl oxygen PDB 3W9T
Metal binding1311Calcium 2 PDB 3W9T
Metal binding1341Calcium 2 PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding1371Calcium 3; via amide nitrogen and carbonyl oxygen PDB 3W9T
Metal binding1381Calcium 3 PDB 3W9T
Metal binding1401Magnesium 1 PDB 3W9T
Metal binding1411Magnesium 1 PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding1471Calcium 2 PDB 3W9T
Metal binding1511Calcium 2 PDB 3W9T
Metal binding1781Calcium 4 PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding1791Calcium 4; via carbonyl oxygen PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding1811Calcium 4; via carbonyl oxygen PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding1871Magnesium 2 PDB 3W9T
Metal binding1881Magnesium 2; via carbonyl oxygen PDB 3W9T
Metal binding1981Calcium 4 PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding2191Calcium 5 PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding2201Calcium 5; via carbonyl oxygen PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding2221Calcium 5; via carbonyl oxygen PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding2281Magnesium 2 PDB 3W9T
Metal binding2291Magnesium 2; via carbonyl oxygen PDB 3W9T
Metal binding2391Calcium 5 PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding2661Calcium 6 PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding2671Calcium 6; via carbonyl oxygen PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding2691Calcium 6; via carbonyl oxygen PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding2751Magnesium 2 PDB 3W9T
Metal binding2761Magnesium 2; via carbonyl oxygen PDB 3W9T
Metal binding2861Calcium 6 PDB 1VCL PDB 2Z49 PDB 3W9T
Metal binding3831Calcium 7 PDB 3W9T
Binding site191N-acetyl-D-galactosamine
Binding site1171N-acetyl-D-galactosamine; via carbonyl oxygen
Binding site1471N-acetyl-D-galactosamine
Binding site2321N-acetyl-D-galactosamine

Amino acid modifications

Modified residue111Pyrrolidone carboxylic acid

Sequences

Sequence LengthMass (Da)Tools
Q868M7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3E47C608446D40EC

FASTA44248,456
        10         20         30         40         50         60 
MVSLVPCGFA QVLCTNPLDI GELRNYKSKQ CVDIVGNQGS GNIATHDCDG LSDQQIIMCG 

        70         80         90        100        110        120 
DGTIRNEARN YCFTPDGSGN ANVMSSPCTL YPEIPSSQRW RLGRKKAFTD NGGIEQVATE 

       130        140        150        160        170        180 
IINLASGKCL DVEGSDGTGD IGVYDCQNLD DQYFYIRSRG PELFYGRLRN EKSDLCLDVE 

       190        200        210        220        230        240 
GSEGKGNVLM YSCEDNLDQW FRYYENGEIV NAKQGMCLDV EGSDGSGNVG IYRCDDLRDQ 

       250        260        270        280        290        300 
MWSRPNAYCN GDYCSFLNKE SNKCLDVSGD QGTGDVGTWQ CDGLPDQRFK WVFDDWEVPT 

       310        320        330        340        350        360 
ATWNMVGCDQ NGKVSQQISN TISFSSTVTA GVAVEVSSTI EKGVIFAKAS VSVKVTASLS 

       370        380        390        400        410        420 
KAWTNSQSGT TAITYTCDNY DSDEEFTRGC MWQLAIETTE VKSGDLLVWN PQIIKCTRSN 

       430        440 
TAPGCAPFTK CANEDCTFCT DI 

« Hide

References

[1]"Primary structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata and its cDNA: structural similarity to the B-chain from plant lectin, ricin."
Nakano M., Tabata S., Sugihara K., Kouzuma Y., Kimura M., Yamasaki N.
Biochim. Biophys. Acta 1435:167-176(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]Kouzuma Y.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism."
Uchida T., Yamasaki T., Eto S., Sugawara H., Kurisu G., Nakagawa A., Kusunoki M., Hatakeyama T.
J. Biol. Chem. 279:37133-37141(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 11-442 IN COMPLEX WITH CALCIUM; CHLORIDE AND MAGNESIUM, CARBOXYLATION AT GLN-11.
[4]"C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil folds."
Hatakeyama T., Unno H., Kouzuma Y., Uchida T., Eto S., Hidemura H., Kato N., Yonekura M., Kusunoki M.
J. Biol. Chem. 282:37826-37835(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 11-442 IN COMPLEX WITH CALCIUM AND MAGNESIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB109017 mRNA. Translation: BAC75827.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VCLX-ray1.70A/B11-442[»]
2Z48X-ray1.70A/B11-442[»]
2Z49X-ray1.95A/B12-442[»]
3W9TX-ray2.90A/B/C/D/E/F/G12-442[»]
ProteinModelPortalQ868M7.
SMRQ868M7. Positions 12-442.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
TCDB1.C.96.1.1. the haemolytic lectin, cel-iii (cel-iii) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.1750.10. 1 hit.
InterProIPR028988. CEL-III_C.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00652. Ricin_B_lectin. 2 hits.
[Graphical view]
SMARTSM00458. RICIN. 2 hits.
[Graphical view]
SUPFAMSSF111265. SSF111265. 1 hit.
SSF50370. SSF50370. 2 hits.
PROSITEPS50231. RICIN_B_LECTIN. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ868M7.

Entry information

Entry nameQ868M7_CUCEC
AccessionPrimary (citable) accession number: Q868M7
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)