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).
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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 |
molecule |
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Pfam: |
PF00652
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[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
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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