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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-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi33 – 331Calcium 1
Metal bindingi34 – 341Calcium 1; via carbonyl oxygen
Metal bindingi36 – 361Calcium 1; via carbonyl oxygen
Metal bindingi42 – 421Magnesium 1
Metal bindingi43 – 431Magnesium 1; via amide nitrogen and carbonyl oxygen
Metal bindingi53 – 531Calcium 1
Metal bindingi82 – 821Magnesium 1
Metal bindingi83 – 831Magnesium 1; via carbonyl oxygen
Metal bindingi131 – 1311Calcium 2
Metal bindingi134 – 1341Calcium 2
Metal bindingi137 – 1371Calcium 3; via amide nitrogen and carbonyl oxygenCombined sources
Metal bindingi138 – 1381Calcium 3Combined sources
Metal bindingi140 – 1401Magnesium 1Combined sources
Metal bindingi141 – 1411Magnesium 1
Metal bindingi147 – 1471Calcium 2Combined sources
Metal bindingi151 – 1511Calcium 2
Metal bindingi178 – 1781Calcium 4
Metal bindingi179 – 1791Calcium 4; via carbonyl oxygen
Metal bindingi181 – 1811Calcium 4; via carbonyl oxygen
Metal bindingi187 – 1871Magnesium 2
Metal bindingi188 – 1881Magnesium 2; via carbonyl oxygen
Metal bindingi198 – 1981Calcium 4
Metal bindingi219 – 2191Calcium 5
Metal bindingi220 – 2201Calcium 5; via carbonyl oxygen
Metal bindingi222 – 2221Calcium 5; via carbonyl oxygen
Metal bindingi228 – 2281Magnesium 2
Metal bindingi229 – 2291Magnesium 2; via carbonyl oxygen
Metal bindingi239 – 2391Calcium 5
Metal bindingi266 – 2661Calcium 6
Metal bindingi267 – 2671Calcium 6; via carbonyl oxygen
Metal bindingi269 – 2691Calcium 6; via carbonyl oxygen
Metal bindingi275 – 2751Magnesium 2
Metal bindingi276 – 2761Magnesium 2; via carbonyl oxygen
Metal bindingi286 – 2861Calcium 6
Metal bindingi383 – 3831Calcium 7Combined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

CalciumCombined sources, LectinImported, MagnesiumCombined sources, Metal-bindingCombined sources

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Submitted name:
Hemolytic lectin CEL-IIIImported
Gene namesi
Name:cel3Imported
OrganismiCucumaria echinata (Sea cucumber)Imported
Taxonomic identifieri40245 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEchinodermataEleutherozoaEchinozoaHolothuroideaDendrochirotaceaDendrochirotidaCucumariidaeCucumaria

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Pyrrolidone carboxylic acid
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

Keywords - PTMi

Pyrrolidone carboxylic acid

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ868M7.
SMRiQ868M7. Positions 12-442.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ868M7.

Family & Domainsi

Family and domain databases

Gene3Di3.30.1750.10. 1 hit.
InterProiIPR028988. CEL-III_C.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00652. Ricin_B_lectin. 2 hits.
[Graphical view]
SMARTiSM00458. RICIN. 2 hits.
[Graphical view]
SUPFAMiSSF111265. SSF111265. 1 hit.
SSF50370. SSF50370. 2 hits.
PROSITEiPS50231. RICIN_B_LECTIN. 3 hits.
[Graphical view]

Sequencei

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
Checksum:i3E47C608446D40EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB109017 mRNA. Translation: BAC75827.1.

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:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ868M7.
SMRiQ868M7. Positions 12-442.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ868M7.

Family and domain databases

Gene3Di3.30.1750.10. 1 hit.
InterProiIPR028988. CEL-III_C.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00652. Ricin_B_lectin. 2 hits.
[Graphical view]
SMARTiSM00458. RICIN. 2 hits.
[Graphical view]
SUPFAMiSSF111265. SSF111265. 1 hit.
SSF50370. SSF50370. 2 hits.
PROSITEiPS50231. RICIN_B_LECTIN. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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 AND MAGNESIUM, DISULFIDE BONDS, AND PYRROLIDONE CARBOXYLIC ACID 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, DISULFIDE BONDS.

Entry informationi

Entry nameiQ868M7_CUCEC
AccessioniPrimary (citable) accession number: Q868M7
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: May 27, 2015
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.