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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)DescriptionActionsGraphical viewLength
Binding sitei20Carbohydrate1 Publication1
Binding sitei22Carbohydrate1 Publication1
Binding sitei24Carbohydrate1 Publication1
Binding sitei31Carbohydrate1 Publication1
Binding sitei43Carbohydrate1 Publication1
Binding sitei61Carbohydrate1 Publication1
Binding sitei63Carbohydrate1 Publication1
Binding sitei65Carbohydrate1 Publication1
Binding sitei72Carbohydrate1 Publication1

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionMitogen
LigandChitin-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)DescriptionActionsGraphical viewLength
ChainiPRO_00001248121 – 82Lectin-D2Add BLAST82

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

182
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Helixi14 – 16Combined sources3
Beta strandi25 – 28Combined sources4
Helixi29 – 32Combined sources4
Turni40 – 43Combined sources4
Helixi47 – 49Combined sources3
Beta strandi64 – 67Combined sources4
Helixi70 – 73Combined sources4
Beta strandi74 – 76Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP83790.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 42Chitin-binding type-1 1PROSITE-ProRule annotationAdd BLAST42
Domaini43 – 82Chitin-binding type-1 2PROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di3.30.60.10. 2 hits.
InterProiView protein in InterPro
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
PfamiView protein in Pfam
PF00187. Chitin_bind_1. 2 hits.
PRINTSiPR00451. CHITINBINDNG.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000609. Chitin_bd_1. 2 hits.
SMARTiView protein in SMART
SM00270. ChtBD1. 2 hits.
SUPFAMiSSF57016. SSF57016. 2 hits.
PROSITEiView protein in PROSITE
PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 2 hits.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UHAX-ray1.50A1-82[»]
1ULMX-ray1.80A/B1-82[»]
1ULNX-ray1.65A1-82[»]
ProteinModelPortaliP83790.
SMRiP83790.
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.
InterProiView protein in InterPro
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
PfamiView protein in Pfam
PF00187. Chitin_bind_1. 2 hits.
PRINTSiPR00451. CHITINBINDNG.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000609. Chitin_bd_1. 2 hits.
SMARTiView protein in SMART
SM00270. ChtBD1. 2 hits.
SUPFAMiSSF57016. SSF57016. 2 hits.
PROSITEiView protein in PROSITE
PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiLED2_PHYAM
AccessioniPrimary (citable) accession number: P83790
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: March 15, 2004
Last modified: February 15, 2017
This is version 60 of the entry and version 1 of the sequence. See 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

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.