P16404 (LEC_ERYCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Lectin Alternative name(s): ECorL
Organism	Erythrina corallodendrum (Coral tree)
Taxonomic identifier	3843 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Erythrina

Protein attributes

Sequence length	281 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Galactose and N-acetyllactosamine specific lectin. Binds to the H-2 blood type determinant fucosyl-N-acetyllactosamine.
Subunit structure	Homodimer.
Post-translational modification	A minor C-terminal proteolytic processing site is observed at position 268.
Miscellaneous	Binds one manganese (or other transition metal) ion and one calcium ion.
Sequence similarities	Belongs to the leguminous lectin family.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Lectin
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.2 Ref.3

Chain

27 – 268

242

Lectin

PRO_0000017617

Propeptide

269 – 281

13

PRO_0000017618

Amino acid modifications

Glycosylation

43

1

N-linked (GlcNAc...) Ref.3

Glycosylation

139

1

N-linked (GlcNAc...)

Natural variations

Natural variant

48

1

G → A.

Natural variant

160

1

P → Q. Ref.3

Natural variant

225

1

D → V.

Experimental info

Sequence conflict

49 – 54

6

AALITQ → DSIPET AA sequence Ref.2

Sequence conflict

139

1

N → F AA sequence Ref.2

Secondary structure

1

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281

Helix Strand Turn

Details...

Beta strand

28 – 36

9

Beta strand

42 – 48

7

Beta strand

58 – 61

4

Beta strand

74 – 81

8

Turn

88 – 90

3

Beta strand

95 – 103

9

Beta strand

109 – 111

3

Beta strand

115 – 123

9

Helix

132 – 134

3

Turn

135 – 137

3

Beta strand

138 – 142

5

Helix

145 – 147

3

Beta strand

150 – 155

6

Beta strand

166 – 177

12

Beta strand

179 – 183

5

Beta strand

192 – 199

8

Turn

200 – 203

4

Beta strand

204 – 210

7

Turn

212 – 214

3

Beta strand

217 – 223

7

Helix

226 – 228

3

Beta strand

232 – 242

11

Beta strand

253 – 263

11

Sequences

	Sequence		Length	Mass (Da)
	P16404 [UniParc]. Last modified July 15, 1998. Version 3. Checksum: 311DE5A43AEF1E67	FASTA	281	30,752
	10 20 30 40 50 60 MATYKLCSVL ALSLTLFLLI LNKVNSVETI SFSFSEFEPG NDNLTLQGAA LITQSGVLQL 70 80 90 100 110 120 TKINQNGMPA WDSTGRTLYA KPVHIWDMTT GTVASFETRF SFSIEQPYTR PLPADGLVFF 130 140 150 160 170 180 MGPTKSKPAQ GYGYLGIFNN SKQDNSYQTL GVEFDTFSNP WDPPQVPHIG IDVNSIRSIK 190 200 210 220 230 240 TQPFQLDNGQ VANVVIKYDA SSKILHAVLV YPSSGAIYTI AEIVDVKQVL PEWVDVGLSG 250 260 270 280 ATGAQRDAAE THDVYSWSFQ ASLPETNDAV IPTSNHNTFA I

References

[1]	"Cloning and sequence analysis of the Erythrina corallodendron lectin cDNA." Arango R., Rozenblatt S., Sharon N. FEBS Lett. 264:109-111(1990) [PubMed: 1692539] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The amino acid sequence of Erythrina corallodendron lectin and its homology with other legume lectins." Adar R., Richardson M., Lis H., Sharon N. FEBS Lett. 257:81-85(1989) [PubMed: 2806566] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-270.
[3]	"C-terminal post-translational proteolysis of plant lectins and their recombinant forms expressed in Escherichia coli. Characterization of 'ragged ends' by mass spectrometry." Young N.M., Watson D.C., Yaguchi M., Adar R., Arango R., Rodriguez-Arango E., Sharon N., Blay P.K., Thibault P. J. Biol. Chem. 270:2563-2570(1995) [PubMed: 7852319] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-55; 77-99; 126-166 AND 247-267, VARIANT GLN-160, PROTEOLYTIC PROCESSING, GLYCOSYLATION.
[4]	"Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose." Shaanan B., Lis H., Sharon N. Science 254:862-866(1991) [PubMed: 1948067] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]	"Structures of the Erythrina corallodendron lectin and of its complexes with mono- and disaccharides." Elgavish S., Shaanan B. J. Mol. Biol. 277:917-932(1998) [PubMed: 9545381] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 27-265.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52782 mRNA. Translation: CAA36986.1.

PIR

S09697.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AX0	X-ray	1.90	A	27-265	[»]
1AX1	X-ray	1.95	A	27-265	[»]
1AX2	X-ray	1.95	A	27-265	[»]
1AXY	X-ray	1.95	A	27-265	[»]
1AXZ	X-ray	1.95	A	27-265	[»]
1FYU	X-ray	2.60	A/B	27-281	[»]
1LTE	X-ray	2.00	A	27-265	[»]
1SFY	X-ray	2.55	A/B/C/D/E/F	27-265	[»]
3N35	X-ray	2.00	A	27-268	[»]
3N36	X-ray	2.30	A	27-268	[»]
3N3H	X-ray	2.00	A	27-268	[»]

ProteinModelPortal

P16404.

SMR

P16404. Positions 27-265.

ModBase

Search...

PTM databases

GlycoSuiteDB

P16404.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR001220. Lectin_legB.
IPR019825. Lectin_legB_Mn/Ca_BS.
[Graphical view]

Gene3D

G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.

Pfam

PF00139. Lectin_legB. 1 hit.
[Graphical view]

PIRSF

PIRSF002690. L-type_lectin_plant. 1 hit.

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LEC_ERYCO

Accession

Primary (citable) accession number: P16404

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	July 15, 1998
Last modified:	June 28, 2011
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program