P02867 (LEC_PEA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lectin

Cleaved into the following 2 chains:

1. Lectin beta chain
2. Lectin alpha chain

Gene names

Name:	LECA
Synonyms:	PSL1

Organism

Pisum sativum (Garden pea)

Taxonomic identifier

3888 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

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	D-mannose specific lectin.
Subunit structure	Tetramer of two alpha and two beta chains.
Miscellaneous	Binds one manganese (or other transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities.
Sequence similarities	Belongs to the leguminous lectin family.

Ontologies

Keywords
Domain	Signal
Ligand	Calcium Lectin Manganese Mannose-binding Metal-binding
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular_function	mannose binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion 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 – 30

30

Chain

31 – 217

187

Lectin beta chain

PRO_0000017623

Chain

218 – 275

58

Lectin alpha chain

PRO_0000017624

Sites

Metal binding

149

1

Manganese By similarity

Metal binding

151

1

Calcium By similarity

Metal binding

151

1

Manganese By similarity

Metal binding

153

1

Calcium; via carbonyl oxygen By similarity

Metal binding

155

1

Calcium By similarity

Metal binding

159

1

Calcium By similarity

Metal binding

159

1

Manganese By similarity

Metal binding

166

1

Manganese By similarity

Amino acid modifications

Glycosylation

217

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

269

1

Missing Ref.4

Secondary structure

1

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275

Helix Strand Turn

Details...

Beta strand

32 – 41

10

Beta strand

48 – 52

5

Beta strand

55 – 57

3

Beta strand

59 – 64

6

Beta strand

71 – 78

8

Turn

85 – 87

3

Beta strand

92 – 102

11

Beta strand

112 – 119

8

Helix

128 – 130

3

Turn

131 – 133

3

Helix

141 – 143

3

Beta strand

146 – 151

6

Turn

156 – 158

3

Beta strand

166 – 175

10

Beta strand

177 – 181

5

Beta strand

189 – 197

9

Turn

198 – 201

4

Beta strand

202 – 209

8

Beta strand

219 – 226

8

Helix

229 – 231

3

Beta strand

235 – 244

10

Beta strand

246 – 248

3

Beta strand

251 – 263

13

Sequences

	Sequence		Length	Mass (Da)
	P02867 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: FD7BE8E00A811222	FASTA	275	30,270
	10 20 30 40 50 60 MASLQTQMIS FYAIFLSILL TTILFFKVNS TETTSFLITK FSPDQQNLIF QGDGYTTKEK 70 80 90 100 110 120 LTLTKAVKNT VGRALYSSPI HIWDRETGNV ANFVTSFTFV INAPNSYNVA DGFTFFIAPV 130 140 150 160 170 180 DTKPQTGGGY LGVFNSAEYD KTTQTVAVEF DTFYNAAWDP SNRDRHIGID VNSIKSVNTK 190 200 210 220 230 240 SWKLQNGEEA NVVIAFNAAT NVLTVSLTYP NSLEEENVTS YTLSDVVSLK DVVPEWVRIG 250 260 270 FSATTGAEYA AHEVLSWSFH SELSGTSSSK QAADA

References

[1]	"Sequence of the seed lectin gene from pea (Pisum sativum L.)." Gatehouse J.A., Bown D., Evans I.M., Gatehouse L.N., Jobes D., Preston P., Croy R.R.D. Nucleic Acids Res. 15:7642-7642(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Feltham First. Tissue: Seed.
[2]	"The pea lectin gene family contains only one functional gene." Kaminski P.A., Buffard D., Strosberg A.D. Plant Mol. Biol. 9:497-507(1987) [AGRICOLA] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE.
[3]	"The biosynthesis and primary structure of pea seed lectin." Higgins T.J.V., Chandler P.M., Zurawski G., Button S.C., Spencer D. J. Biol. Chem. 258:9544-9549(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. P1/G086.
[4]	de Pater B.S., Pham K.T., Katagiri F., Chua N.H., Kijne J.W. Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Feltham First.
[5]	"The complete amino acid sequence of the alpha-subunit of pea lectin, Pisum sativum." Richardson C., Behnke W.D., Freisheim J.H., Blumenthal K.M. Biochim. Biophys. Acta 537:310-319(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 218-271.
[6]	"The crystal structure of pea lectin at 3.0-A resolution." Einspahr H., Parks E.H., Suguna K., Subramanian E., Suddath F.L. J. Biol. Chem. 261:16518-16527(1986) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[7]	"X-ray crystal structure of a pea lectin-trimannoside complex at 2.6-A resolution." Rini J.M., Hardman K.D., Einspahr H., Suddath F.L., Carver J.P. J. Biol. Chem. 268:10126-10132(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[8]	"The structure of the pea lectin-D-mannopyranose complex at a 2.1 A resolution." Ruzeinikov S.N., Mikhailova I.Y., Tsygannik I.N., Pangborn W., Duax W., Pletnev V.Z. Russ. J. Bioorg. Chem. 24:277-279(1998) Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]	"Mutational analysis of pea lectin. Substitution of Asn125 for Asp in the monosaccharide-binding site eliminates mannose/glucose-binding activity." van Eijsden R.R., Hoedemaeker F.J., Diaz C.L., Lugtenberg B.J.J., de Pater B.S., Kijne J.W. Plant Mol. Biol. 20:1049-1058(1992) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00440 Genomic DNA. Translation: CAA68497.1.
M18160 mRNA. Translation: AAA33676.1.
J01254 mRNA. No translation available.
X66368 Genomic DNA. Translation: CAA47011.1.

PIR

LNPM. A26844.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BQP	X-ray	2.10	A/C	31-211	[»]
			B/D	218-264	[»]
1HKD	X-ray	2.09	A/C	31-211	[»]
			B/D	218-269	[»]
1OFS	X-ray	1.80	A/C	31-217	[»]
			B/D	218-265	[»]
1RIN	X-ray	2.60	A/C	31-210	[»]
			B/D	218-266	[»]
2BQP	X-ray	1.90	A/B	31-264	[»]
2LTN	X-ray	1.70	A/C	31-211	[»]
			B/D	218-269	[»]

ProteinModelPortal

P02867.

SMR

P02867. Positions 31-266.

ModBase

Search...

Protein family/group databases

Allergome

8818. Pis s 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

EvolutionaryTrace

P02867.

Entry information

Entry name

LEC_PEA

Accession

Primary (citable) accession number: P02867

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program