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 DB58

Gene
N/A
Organism
Vigna unguiculata subsp. cylindrica (Horse gram) (Dolichos biflorus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Metalloglycoprotein, containing Ca, Mg, Mn, and Zn and the carbohydrates galactose, glucosamine, mannose, and fucose. It agglutinates erythrocytes of blood group A1.

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Mannose-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lectin DB58
Cleaved into the following 2 chains:
OrganismiVigna unguiculata subsp. cylindrica (Horse gram) (Dolichos biflorus)
Taxonomic identifieri3840 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 275253Lectin DB58 subunit alphaPRO_0000017613Add
BLAST
Chaini23 – 264242Lectin DB58 subunit betaPRO_0000017614Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)
Glycosylationi101 – 1011N-linked (GlcNAc...)

Post-translational modificationi

Leu-264 is missing in a major portion of the beta subunit, suggesting an origin by sequential removal of amino acids rather than a processing by endoproteolytic cleavage.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Heterodimer, composed of an alpha and a beta subunit derived from a single precursor.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 318Combined sources
Beta strandi38 – 425Combined sources
Beta strandi48 – 525Combined sources
Beta strandi67 – 748Combined sources
Turni81 – 833Combined sources
Beta strandi88 – 969Combined sources
Helixi102 – 1043Combined sources
Beta strandi108 – 1158Combined sources
Turni127 – 1293Combined sources
Helixi137 – 1393Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi160 – 16910Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi182 – 19110Combined sources
Turni192 – 1954Combined sources
Beta strandi196 – 2038Combined sources
Helixi204 – 2063Combined sources
Beta strandi208 – 2158Combined sources
Helixi218 – 2214Combined sources
Beta strandi224 – 23310Combined sources
Beta strandi245 – 25511Combined sources
Helixi266 – 2738Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G7YX-ray2.50A/B/C/D/E/F23-275[»]
1LULX-ray3.30A/B/C/D/E/F23-275[»]
ProteinModelPortaliP19588.
SMRiP19588. Positions 23-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19588.

Family & Domainsi

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19588-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSTVSVVL SLFLLLLTQA YSADIQSFSF KNFNSSSFIL QGDATVSSSK
60 70 80 90 100
LRLTKVKGNG LPTLSSLGRA FYSSPIQIYD KSTGAVASWA TSFTANIFAP
110 120 130 140 150
NKSSSADGIA FALVPVGSEP KSNSGFLGVF DSDVYDNSAQ TVAVEFDTFS
160 170 180 190 200
NTDWDPTSRH IGIDVNSIKS IRTASWGLAN GQNAEILITY NAATSLLVAS
210 220 230 240 250
LVHPSRRTSY IVSERVDITN ELPEYVSIGF SATTGLSEGY TETHDVLSWS
260 270
FASKLPDDST TEPLDIASYL VRNVL
Length:275
Mass (Da):29,453
Last modified:July 15, 1999 - v2
Checksum:i53D72ACB02EAE03F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2372LS → FF in AAA33142 (PubMed:2844781).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23216 mRNA. Translation: AAA33142.1.
M34271 Genomic DNA. Translation: AAA33140.1.
PIRiA31972.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23216 mRNA. Translation: AAA33142.1.
M34271 Genomic DNA. Translation: AAA33140.1.
PIRiA31972.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G7YX-ray2.50A/B/C/D/E/F23-275[»]
1LULX-ray3.30A/B/C/D/E/F23-275[»]
ProteinModelPortaliP19588.
SMRiP19588. Positions 23-275.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP19588.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. 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...

Publicationsi

  1. "cDNA cloning, primary structure, and in vitro biosynthesis of the DB58 lectin from Dolichos biflorus."
    Schnell D.J., Etzler M.E.
    J. Biol. Chem. 263:14648-14653(1988) [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. "Isolation and characterization of subunits of DB58, a lectin from the stems and leaves of Dolichos biflorus."
    Etzler M.E.
    Biochemistry 33:9778-9783(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 255-275, PROTEOLYTIC PROCESSING.
    Tissue: Leaf and Stem.
  4. "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 (3.3 ANGSTROMS).

Entry informationi

Entry nameiLEC5_VIGUC
AccessioniPrimary (citable) accession number: P19588
Secondary accession number(s): Q39665
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 15, 1999
Last modified: June 24, 2015
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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 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.