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Protein

Lectin-D2

Gene
N/A
Organism
Phytolacca americana (American pokeweed) (Phytolacca decandra)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

N-acetyl-D-glucosamine binding lectin. Shows no hemagglutinating activity towards rabbit erythrocytes and weak activity towards trypsin-treated erythrocytes. Has mitogenic activity towards human peripheral blood lymphocytes (HPBL).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201Carbohydrate1 Publication
Binding sitei22 – 221Carbohydrate1 Publication
Binding sitei24 – 241Carbohydrate1 Publication
Binding sitei31 – 311Carbohydrate1 Publication
Binding sitei43 – 431Carbohydrate1 Publication
Binding sitei61 – 611Carbohydrate1 Publication
Binding sitei63 – 631Carbohydrate1 Publication
Binding sitei65 – 651Carbohydrate1 Publication
Binding sitei72 – 721Carbohydrate1 Publication

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • chitin binding Source: UniProtKB

GO - Biological processi

  • positive regulation of mitotic nuclear division Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Mitogen

Keywords - Ligandi

Chitin-binding, Lectin

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Lectin-D2
Alternative name(s):
PL-D2
OrganismiPhytolacca americana (American pokeweed) (Phytolacca decandra)
Taxonomic identifieri3527 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesPhytolaccaceaePhytolacca

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8282Lectin-D2PRO_0000124812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 19PROSITE-ProRule annotation2 Publications
Disulfide bondi13 ↔ 25PROSITE-ProRule annotation2 Publications
Disulfide bondi18 ↔ 32PROSITE-ProRule annotation2 Publications
Disulfide bondi36 ↔ 40PROSITE-ProRule annotation2 Publications
Disulfide bondi45 ↔ 60PROSITE-ProRule annotation2 Publications
Disulfide bondi54 ↔ 66PROSITE-ProRule annotation2 Publications
Disulfide bondi59 ↔ 73PROSITE-ProRule annotation2 Publications
Disulfide bondi77 ↔ 81PROSITE-ProRule annotation2 Publications

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1
82
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Helixi14 – 163Combined sources
Beta strandi25 – 284Combined sources
Helixi29 – 324Combined sources
Turni40 – 434Combined sources
Helixi47 – 493Combined sources
Beta strandi64 – 674Combined sources
Helixi70 – 734Combined sources
Beta strandi74 – 763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UHAX-ray1.50A1-82[»]
1ULMX-ray1.80A/B1-82[»]
1ULNX-ray1.65A1-82[»]
ProteinModelPortaliP83790.
SMRiP83790. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83790.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4242Chitin-binding type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini43 – 8240Chitin-binding type-1 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 chitin-binding type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di3.30.60.10. 2 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 2 hits.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 2 hits.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 2 hits.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
APECGERASG KRCPNGKCCS QWGYCGTTDN YCGQGCQSQC DYWRCGRDFG
60 70 80
GRLCEEDMCC SKYGWCGYSD DHCEDGCQSQ CD
Length:82
Mass (Da):9,103
Last modified:March 15, 2004 - v1
Checksum:i1E65B08E58A80037
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UHAX-ray1.50A1-82[»]
1ULMX-ray1.80A/B1-82[»]
1ULNX-ray1.65A1-82[»]
ProteinModelPortaliP83790.
SMRiP83790. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP83790.

Family and domain databases

Gene3Di3.30.60.10. 2 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 2 hits.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 2 hits.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 2 hits.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Amino acid sequence and some properties of lectin-D from the roots of pokeweed (Phytolacca americana)."
    Yamaguchi K., Mori A., Funatsu G.
    Biosci. Biotechnol. Biochem. 60:1380-1382(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION.
    Tissue: Root1 Publication.
  2. "Mitogenic properties of pokeweed lectin-D isoforms on human peripheral blood lymphocytes: non-mitogen PL-D1 and mitogen PL-D2."
    Yamaguchi K., Uechi M., Katakura Y., Oda T., Ishiguro M.
    Biosci. Biotechnol. Biochem. 68:1591-1593(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  3. "Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed."
    Hayashida M., Fujii T., Hamasu M., Ishiguro M., Hata Y.
    J. Mol. Biol. 334:551-565(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH TRI-N-ACETYLCHITOTRIOSE.
  4. "Structures of two lectins from the roots of pokeweed (Phytolacca americana)."
    Fujii T., Hayashida M., Hamasu M., Ishiguro M., Hata Y.
    Acta Crystallogr. D 60:665-673(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Entry informationi

Entry nameiLED2_PHYAM
AccessioniPrimary (citable) accession number: P83790
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: March 15, 2004
Last modified: December 9, 2015
This is version 57 of the entry and version 1 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

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.