P02873 (LEA1_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase inhibitor 1
Short name=Alpha-AI-1
Short name=Alpha-AI1

Alternative name(s):
Lectin

Cleaved into the following 2 chains:

1. Alpha-amylase inhibitor 1 chain 1
2. Alpha-amylase inhibitor 1 chain 2

Gene names

Name:	LLP
Synonyms:	Alpha-AI1

Organism

Phaseolus vulgaris (Kidney bean) (French bean)

Taxonomic identifier

3885 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	246 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	Lectin and alpha-amylase inhibitor. Acts as a defensive protein against insects. Ref.6
Subunit structure	Heterodimer of chain 1 and chain 2. Ref.6
Post-translational modification	Proteolytic processing yields active form.
Biotechnological use	Sold as a diet aid under the name of 'Phaseolamin' or 'Phase 2'.
Sequence similarities	Belongs to the leguminous lectin family.

Ontologies

Keywords
Domain	Signal
Ligand	Lectin
Molecular function	Alpha-amylase inhibitor
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular_function	alpha-amylase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW carbohydrate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.4 Ref.5 Ref.6

Chain

24 – 100

77

Alpha-amylase inhibitor 1 chain 1

PRO_0000017627

Chain

101 – 239

139

Alpha-amylase inhibitor 1 chain 2

PRO_0000017628

Propeptide

240 – 246

7

PRO_0000017629

Amino acid modifications

Glycosylation

35

1

N-linked (GlcNAc...) Ref.8

Glycosylation

88

1

N-linked (GlcNAc...) Ref.8

Glycosylation

163

1

N-linked (GlcNAc...) Ref.8

Experimental info

Sequence conflict

30

1

I → N AA sequence Ref.5

Sequence conflict

73

1

Q → R in CAD28835. Ref.3

Sequence conflict

142

1

K → E in CAD28835. Ref.3

Sequence conflict

196

1

D → N Ref.2

Secondary structure

1

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246

Helix Strand Turn

Details...

Beta strand

28 – 33

6

Helix

36 – 38

3

Beta strand

39 – 47

9

Beta strand

53 – 58

6

Beta strand

60 – 70

11

Beta strand

72 – 75

4

Turn

77 – 79

3

Beta strand

84 – 94

11

Beta strand

103 – 111

9

Beta strand

121 – 126

6

Turn

127 – 130

4

Beta strand

131 – 136

6

Beta strand

139 – 145

7

Helix

148 – 150

3

Turn

151 – 153

3

Beta strand

156 – 163

8

Turn

164 – 167

4

Beta strand

168 – 174

7

Turn

176 – 178

3

Beta strand

181 – 187

7

Helix

193 – 195

3

Beta strand

196 – 206

11

Helix

209 – 211

3

Beta strand

215 – 226

12

Sequences

	Sequence		Length	Mass (Da)
	P02873 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: EA56F15EF1F78788	FASTA	246	27,207
	10 20 30 40 50 60 MIMASSKLLS LALFLALLSH ANSATETSFI IDAFNKTNLI LQGDATVSSN GNLQLSYNSY 70 80 90 100 110 120 DSMSRAFYSA PIQIRDSTTG NVASFDTNFT MNIRTHRQAN SAVGLDFVLV PVQPESKGDT 130 140 150 160 170 180 VTVEFDTFLS RISIDVNNND IKSVPWDVHD YDGQNAEVRI TYNSSTKVFS VSLSNPSTGK 190 200 210 220 230 240 SNNVSTTVEL EKEVYDWVSV GFSATSGAYQ WSYETHDVLS WSFSSKFINL KDQKSERSNI VLNKIL

References

[1]	"Structure of a chromosomal Phaseolus vulgaris lectin gene and its transcript." Hoffman L.M. J. Mol. Appl. Genet. 2:447-453(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Tendergreen.
[2]	"Molecular cloning of Phaseolus vulgaris lectin mRNA and use of cDNA as a probe to estimate lectin transcript levels in various tissues." Hoffman L.M., Ma Y., Barker R.F. Nucleic Acids Res. 10:7819-7828(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Tendergreen.
[3]	"Arcelin and other members of lectin family in wild Phaseolus vulgaris." Lioi L., Galasso I., Lanave C., Sparvoli F., Bollini R. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-246. Tissue: Leaf.
[4]	"A lectin gene encodes the alpha-amylase inhibitor of the common bean." Moreno J., Chrispeels M.J. Proc. Natl. Acad. Sci. U.S.A. 86:7885-7889(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-34 AND 101-115. Strain: cv. Greensleeves. Tissue: Seed.
[5]	"Isolation and characterization of the subunits of a heat-labile alpha-amylase inhibitor from Phaseolus vulgaris white kidney bean." Yamaguchi H. Biosci. Biotechnol. Biochem. 57:297-302(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-32 AND 101-109. Strain: cv. Tebo. Tissue: Seed.
[6]	Kluh I., Horn M., Voburka Z. Submitted (DEC-2003) to UniProtKB Cited for: PROTEIN SEQUENCE OF 24-99 AND 101-231, FUNCTION, SUBUNIT, GLYCOSYLATION. Strain: cv. Magna. Tissue: Seed.
[7]	"Location of the active site of the bean alpha-amylase inhibitor and involvement of a Trp, Arg, Tyr triad." Mirkov T.E., Evans S.V., Wahlstrom J., Gomez L., Young N.M., Chrispeels M.J. Glycobiology 5:45-50(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Post-translational processing of two alpha-amylase inhibitors and an arcelin from the common bean, Phaseolus vulgaris." Young N.M., Thibault P., Watson D.C., Chrispeels M.J. FEBS Lett. 446:203-206(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF C-TERMINAL, GLYCOSYLATION AT ASN-35; ASN-88 AND ASN-163.
[9]	"Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex." Bompard-Gilles C., Rousseau P., Rouge P., Payan F. Structure 4:1441-1452(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF COMPLEX WITH PIG ALPHA-AMYLASE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01261 Genomic DNA. Translation: AAA33769.1.
AJ439614 Genomic DNA. Translation: CAD28835.1.

PIR

LNFB. A03365.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DHK	X-ray	1.85	B	24-246	[»]
1VIW	X-ray	3.00	B	24-228	[»]

ProteinModelPortal

P02873.

SMR

P02873. Positions 24-228.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-88091.

Protein family/group databases

Allergome

2946. Pha v aAI.
8208. Pha v aAI.0101.

PTM databases

GlycoSuiteDB

P02873.

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

P02873.

Entry information

Entry name

LEA1_PHAVU

Accession

Primary (citable) accession number: P02873
Secondary accession number(s): Q8RVY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program