P05045 (LEC1_DOLBI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Seed lectin subunit I Short name=SL Cleaved into the following chain: Seed lectin subunit II
Organism	Dolichos biflorus (Horse gram)
Taxonomic identifier	3840 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Vigna › Vigna unguiculata

Protein attributes

Sequence length	275 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	Metalloglycoprotein, containing Ca, Mg, Mn, and Zn and the carbohydrates galactose, glucosamine, mannose, and fucose. It agglutinates erythrocytes of blood group A1. Has a high preference for GalNAc over Gal.
Subunit structure	Homotetramer.
Post-translational modification	Subunit II may arise from subunit I by proteolytic cleavage at the C-terminal end.
Sequence similarities	Belongs to the leguminous lectin family.

Ontologies

Keywords
Domain	Signal
Ligand	Calcium Lectin Mannose-binding
PTM	Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Molecular_function	mannose 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 – 22

22

Chain

23 – 275

253

Seed lectin subunit I

PRO_0000017611

Chain

23 – 265

243

Seed lectin subunit II

PRO_0000017612

Sites

Site

265 – 266

2

Cleavage

Amino acid modifications

Glycosylation

136

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

61 – 67

7

IPTPSSL → FPLRFPS in AAA33141. Ref.1

Sequence conflict

82

1

S → F in AAA33141. Ref.1

Sequence conflict

149

1

F → L in AAA33141. Ref.1

Sequence conflict

199

1

A → V in AAA33141. Ref.1

Sequence conflict

227

1

S → G in AAA33141. Ref.1

Sequence conflict

254

1

K → R in AAA33141. Ref.1

Sequence conflict

268

1

S → R in AAA33141. Ref.1

Secondary structure

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275

Helix Strand Turn

Details...

Beta strand

24 – 32

9

Helix

35 – 37

3

Beta strand

38 – 42

5

Beta strand

45 – 47

3

Beta strand

50 – 52

3

Beta strand

67 – 74

8

Turn

81 – 84

4

Beta strand

88 – 96

9

Beta strand

107 – 115

9

Helix

124 – 126

3

Turn

127 – 129

3

Helix

137 – 139

3

Beta strand

142 – 147

6

Turn

152 – 154

3

Beta strand

160 – 169

10

Beta strand

171 – 175

5

Beta strand

184 – 191

8

Turn

192 – 195

4

Beta strand

196 – 202

7

Helix

204 – 206

3

Beta strand

209 – 215

7

Helix

218 – 221

4

Beta strand

224 – 234

11

Beta strand

245 – 255

11

Beta strand

257 – 259

3

Helix

266 – 273

8

Sequences

	Sequence		Length	Mass (Da)
	P05045 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: D313D73860661A83	FASTA	275	29,406
	10 20 30 40 50 60 MASSTVSVVL SLFLLLLTQA NSANIQSFSF KNFNSPSFIL QGDATVSSGK LQLTKVKENG 70 80 90 100 110 120 IPTPSSLGRA FYSSPIQIYD KSTGAVASWA TSFTVKISAP SKASFADGIA FALVPVGSEP 130 140 150 160 170 180 RRNGGYLGVF DSDVYNNSAQ TVAVEFDTFS NSGWDPSMKH IGIDVNSIKS IATVSWDLAN 190 200 210 220 230 240 GENAEILITY NAATSLLVAS LVHPSRRTSY ILSERVDITN ELPEYVSVGF SATTGLSEGY 250 260 270 IETHDVLSWS FASKLPDDST AEPLDLASYL VRNVL

References

[1]	"Primary structure of the Dolichos biflorus seed lectin." Schnell D.J., Etzler M.E. J. Biol. Chem. 262:7220-7225(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Two lectin genes differentially expressed in Dolichos biflorus differ primarily by a 116-base pair sequence in their 5' flanking regions." Harada J.J., Spadoro-Tank J., Maxwell J.C., Schnell D.J., Etzler M.E. J. Biol. Chem. 265:4997-5001(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus." Hamelryck T.W., Loris R., Bouckaert J., Dao-Thi M.-H., Strecker G., Imberty A., Fernandez E., Wyns L., Etzler M.E. J. Mol. Biol. 286:1161-1177(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02721 mRNA. Translation: AAA33141.1.
M34270 Genomic DNA. Translation: AAA33143.1.

PIR

A29572.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BJQ	X-ray	2.65	A/B/C/D/E/F/G/H	23-275	[»]
1LU1	X-ray	2.60	A	23-275	[»]
1LU2	X-ray	2.80	A/B	23-275	[»]

ProteinModelPortal

P05045.

SMR

P05045. Positions 23-275.

ModBase

Search...

Protein family/group databases

Allergome

3011. Dol b Agglutinin.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.120.200. 1 hit.

InterPro

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

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...

Other

DrugBank

DB00173. Adenine.

EvolutionaryTrace

P05045.

Entry information

Entry name

LEC1_DOLBI

Accession

Primary (citable) accession number: P05045
Secondary accession number(s): Q39666

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	July 15, 1999
Last modified:	April 3, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program