Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lectin-4

Gene
N/A
Organism
Griffonia simplicifolia (Bandeiraea simplicifolia)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Lectin which has a strong affinity for both the Lewis b and y human blood-group determinants.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi129Manganese1 Publication1
Metal bindingi131Calcium1 Publication1
Metal bindingi131Manganese1 Publication1
Metal bindingi133Calcium1 Publication1
Metal bindingi135Calcium1 Publication1
Metal bindingi140Calcium1 Publication1
Metal bindingi140Manganese1 Publication1
Metal bindingi145Manganese1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lectin-4
Alternative name(s):
GS4
Lectin IV
OrganismiGriffonia simplicifolia (Bandeiraea simplicifolia)
Taxonomic identifieri3850 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaeCaesalpinioideaeCercideaeGriffonia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001050991 – 243Lectin-4Add BLAST243

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid1
Glycosylationi5N-linked (GlcNAc...); in alpha chain1
Glycosylationi18N-linked (GlcNAc...)1

Post-translational modificationi

N-glycosylation of Asn-5 converts form Beta to form Alpha.

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Homodimer of Alpha and Beta forms.1 Publication

Structurei

Secondary structure

1243
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Beta strandi20 – 26Combined sources7
Beta strandi29 – 31Combined sources3
Beta strandi34 – 36Combined sources3
Beta strandi48 – 58Combined sources11
Beta strandi71 – 86Combined sources16
Beta strandi90 – 97Combined sources8
Helixi106 – 108Combined sources3
Turni109 – 111Combined sources3
Turni114 – 118Combined sources5
Helixi120 – 122Combined sources3
Beta strandi126 – 131Combined sources6
Helixi136 – 138Combined sources3
Beta strandi145 – 154Combined sources10
Beta strandi156 – 160Combined sources5
Helixi163 – 166Combined sources4
Beta strandi171 – 179Combined sources9
Turni180 – 183Combined sources4
Beta strandi184 – 191Combined sources8
Beta strandi196 – 202Combined sources7
Helixi205 – 208Combined sources4
Beta strandi211 – 221Combined sources11
Beta strandi223 – 237Combined sources15
Turni239 – 242Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSLX-ray2.00A2-243[»]
1LECX-ray2.00A2-243[»]
1LEDX-ray2.00A2-243[»]
ProteinModelPortaliP24146.
SMRiP24146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24146.

Family & Domainsi

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. L-lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24146-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QNTVNFTYPD FWSYSLKNGT EITFLGDATR IPGALQLTKT DANGNPVRSS
60 70 80 90 100
AGQASYSEPV FLWDSTGKAA SFYTSFTFLL KNYGAPTADG LAFFLAPVDS
110 120 130 140 150
SVKDYGGFLG LFRHETAADP SKNQVVAVEF DTWINKDWND PPYPHIGIDV
160 170 180 190 200
NSIVSVATTR WENDDAYGSS IATAHITYDA RSKILTVLLS YEHGRDYILS
210 220 230 240
HVVDLAKVLP QKVRIGFSAG VGYDEVTYIL SWHFFSTLDG TNK
Length:243
Mass (Da):26,810
Last modified:June 1, 1994 - v3
Checksum:iCFEC0FA389BBBF25
GO

Sequence databases

PIRiS13389.

Cross-referencesi

Sequence databases

PIRiS13389.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSLX-ray2.00A2-243[»]
1LECX-ray2.00A2-243[»]
1LEDX-ray2.00A2-243[»]
ProteinModelPortaliP24146.
SMRiP24146.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP24146.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. L-lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLEC4_GRISI
AccessioniPrimary (citable) accession number: P24146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds one manganese (or another transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.