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

Mannose-specific lectin

Gene
N/A
Organism
Galanthus nivalis (Common snowdrop)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mannose-specific lectin.

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Lectin, Mannose-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mannose-specific lectin
Alternative name(s):
Agglutinin
LecGNA 2
OrganismiGalanthus nivalis (Common snowdrop)
Taxonomic identifieri4670 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAmaryllidoideaeGalanthus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Or 23; in 70% of the moleculesAdd
BLAST
Chaini20 – 128109Mannose-specific lectinPRO_0000021586Add
BLAST
Propeptidei129 – 15729Removed in mature formPRO_0000021587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 75

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
157
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 283Combined sources
Beta strandi31 – 333Combined sources
Beta strandi38 – 414Combined sources
Beta strandi44 – 485Combined sources
Beta strandi54 – 585Combined sources
Beta strandi61 – 655Combined sources
Beta strandi76 – 794Combined sources
Beta strandi85 – 884Combined sources
Beta strandi94 – 974Combined sources
Beta strandi107 – 1115Combined sources
Beta strandi117 – 1215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JPCX-ray2.00A24-132[»]
1MSAX-ray2.29A/B/C/D24-132[»]
1NIVX-ray3.00A/C24-132[»]
ProteinModelPortaliP30617.
SMRiP30617. Positions 24-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30617.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 132109Bulb-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 bulb-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.90.10.10. 1 hit.
InterProiIPR001480. Bulb-type_lectin_dom.
[Graphical view]
PfamiPF01453. B_lectin. 1 hit.
[Graphical view]
SMARTiSM00108. B_lectin. 1 hit.
[Graphical view]
SUPFAMiSSF51110. SSF51110. 1 hit.
PROSITEiPS50927. BULB_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P30617-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKASLLILA AIFLGVITPS CLSDNILYSG ETLSTGEFLN YGSFVFIMQE
60 70 80 90 100
DCNLVLYDVD KPIWATNTGG LSRSCFLSMQ TDGNLVVYNP SNKPIWASNT
110 120 130 140 150
GGQNGNYVCI LQKDRNVVIY GTDRWATGTH TGLVGIPASP PSEKYPTAGK

IKLVTAK
Length:157
Mass (Da):16,917
Last modified:April 1, 1993 - v1
Checksum:iB63AE3124DA2252B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211C → Y.
Natural varianti74 – 741S → H.
Natural varianti76 – 761F → Y.
Natural varianti109 – 1091C → S.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55556 mRNA. Translation: AAA33346.1.
PIRiS19735.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55556 mRNA. Translation: AAA33346.1.
PIRiS19735.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JPCX-ray2.00A24-132[»]
1MSAX-ray2.29A/B/C/D24-132[»]
1NIVX-ray3.00A/C24-132[»]
ProteinModelPortaliP30617.
SMRiP30617. Positions 24-132.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP30617.

Family and domain databases

Gene3Di2.90.10.10. 1 hit.
InterProiIPR001480. Bulb-type_lectin_dom.
[Graphical view]
PfamiPF01453. B_lectin. 1 hit.
[Graphical view]
SMARTiSM00108. B_lectin. 1 hit.
[Graphical view]
SUPFAMiSSF51110. SSF51110. 1 hit.
PROSITEiPS50927. BULB_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Biosynthesis, primary structure and molecular cloning of snowdrop (Galanthus nivalis L.) lectin."
    van Damme E.J.M., Kaku H., Perini F., Goldstein I.J., Peeters B., Yagi F., Decock B., Peumans W.J.
    Eur. J. Biochem. 202:23-30(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "The 2.0 A structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: evidence for two unique binding modes."
    Wright C.S., Hester G.
    Structure 4:1339-1352(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiLEC_GALNI
AccessioniPrimary (citable) accession number: P30617
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 14, 2015
This is version 71 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.