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1.C.96.1.1
The haemolytic lectin, CEL-III (Uchida et al. 2004)CEL-III heptamerizes via a large structural transition from alpha-helices to a beta-barrel during the transmembrane pore-formation process (Unno et al. 2014).

Accession Number:Q868M7
Protein Name:Hemolytic lectin CEL-III
Length:442
Molecular Weight:48456.00
Species:Cucumaria echinata (Sea cucumber) [40245]
Location1 / Topology2 / Orientation3: Cytoplasmic vesicle1 / Multi-pass membrane protein2
Substrate small molecules

Cross database links:

Pfam: PF00652   

Gene Ontology

GO:0005529 F:sugar binding

References (2)

[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.et.al.   10561549
[2] “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.et.al.   15194688
Structure:
1VCL   2Z48   2Z49   3W9T     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MVSLVPCGFA QVLCTNPLDI GELRNYKSKQ CVDIVGNQGS GNIATHDCDG LSDQQIIMCG 
61:	DGTIRNEARN YCFTPDGSGN ANVMSSPCTL YPEIPSSQRW RLGRKKAFTD NGGIEQVATE 
121:	IINLASGKCL DVEGSDGTGD IGVYDCQNLD DQYFYIRSRG PELFYGRLRN EKSDLCLDVE 
181:	GSEGKGNVLM YSCEDNLDQW FRYYENGEIV NAKQGMCLDV EGSDGSGNVG IYRCDDLRDQ 
241:	MWSRPNAYCN GDYCSFLNKE SNKCLDVSGD QGTGDVGTWQ CDGLPDQRFK WVFDDWEVPT 
301:	ATWNMVGCDQ NGKVSQQISN TISFSSTVTA GVAVEVSSTI EKGVIFAKAS VSVKVTASLS 
361:	KAWTNSQSGT TAITYTCDNY DSDEEFTRGC MWQLAIETTE VKSGDLLVWN PQIIKCTRSN 
421:	TAPGCAPFTK CANEDCTFCT DI