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Protein

Galectin-3

Gene

Cgl3

Organism
Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds complex carbohydrates, such as chitooligosaccharides. Does not bind lactose. May play a role in fruiting body formation.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45Carbohydrate1
Binding sitei64Carbohydrate1
Binding sitei73Carbohydrate1
Binding sitei81Carbohydrate1
Binding sitei84Carbohydrate1
Binding sitei138Carbohydrate1

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Galectin-3
Alternative name(s):
Cgl-III
Galectin III
Gene namesi
Name:Cgl3
OrganismiCoprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
Taxonomic identifieri5346 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43I → A: Abolishes chitooligosaccharide binding; when associated with A-45. 1 Publication1
Mutagenesisi45N → A: Abolishes chitooligosaccharide binding; when associated with A-43. 1 Publication1
Mutagenesisi81R → A: Alters binding specificity, leading to lactose binding and reduced affinity for chitooligosaccharide. 1 Publication1
Mutagenesisi81R → W: Alters binding specificity, leading to lactose binding and loss of chitooligosaccharide binding. 1 Publication1
Mutagenesisi138N → A: Abolishes chitooligosaccharide binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003332631 – 164Galectin-3Add BLAST164

Expressioni

Inductioni

Induced during fruiting body formation.2 Publications

Keywords - Developmental stagei

Fruiting body

Interactioni

Subunit structurei

Homotetramer. Oligomerization is required for carbohydrate binding (By similarity).By similarity

Structurei

Secondary structure

1164
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Beta strandi9 – 12Combined sources4
Beta strandi22 – 26Combined sources5
Turni39 – 41Combined sources3
Beta strandi46 – 52Combined sources7
Beta strandi57 – 64Combined sources8
Turni65 – 68Combined sources4
Beta strandi69 – 75Combined sources7
Beta strandi85 – 88Combined sources4
Turni90 – 92Combined sources3
Beta strandi100 – 105Combined sources6
Beta strandi107 – 114Combined sources8
Beta strandi117 – 123Combined sources7
Beta strandi130 – 137Combined sources8
Beta strandi147 – 154Combined sources8
Helixi156 – 159Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R0FX-ray2.00A/B1-164[»]
2R0HX-ray1.90A/B/C/D1-164[»]
ProteinModelPortaliQ206Z5.
SMRiQ206Z5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ206Z5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 154GalectinPROSITE-ProRule annotationAdd BLAST146

Sequence similaritiesi

Contains 1 galectin domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410K266. Eukaryota.
ENOG4110BR0. LUCA.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51304. GALECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q206Z5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFHILRLEST VDLSEPLKDN GIIVFQSDKL DLEPSPNLGP TGIDNTNVNL
60 70 80 90 100
INAKGDVLLH IGIRRRENAF VFNSIPYGES RGPEERIPLE GTFGDRRDPS
110 120 130 140 150
ITIFDHPDRY QIMIDYKTVY YYKKRLEGRC EKVSYKINEG QTPPFSDVLG
160
VTVLYFANVM PRAN
Length:164
Mass (Da):18,735
Last modified:April 18, 2006 - v1
Checksum:i4AAF6E1507F88617
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ408306 Genomic DNA. Translation: ABD64675.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ408306 Genomic DNA. Translation: ABD64675.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R0FX-ray2.00A/B1-164[»]
2R0HX-ray1.90A/B/C/D1-164[»]
ProteinModelPortaliQ206Z5.
SMRiQ206Z5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410K266. Eukaryota.
ENOG4110BR0. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ206Z5.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51304. GALECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCGL3_COPCI
AccessioniPrimary (citable) accession number: Q206Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 18, 2006
Last modified: November 2, 2016
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.