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P81460

- CONA_CANLI

UniProt

P81460 - CONA_CANLI

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Protein

Concanavalin-A

Gene
N/A
Organism
Canavalia lineata (Beach bean) (Dolichos lineatus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Glucose/D-mannose specific lectin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81ManganeseBy similarity
Metal bindingi10 – 101CalciumBy similarity
Metal bindingi10 – 101ManganeseBy similarity
Metal bindingi12 – 121Calcium; via carbonyl oxygenBy similarity
Binding sitei12 – 121CarbohydrateBy similarity
Metal bindingi14 – 141CalciumBy similarity
Metal bindingi19 – 191CalciumBy similarity
Metal bindingi19 – 191ManganeseBy similarity
Metal bindingi24 – 241ManganeseBy similarity
Metal bindingi208 – 2081CalciumBy similarity
Binding sitei228 – 2281Carbohydrate; via amide nitrogenBy similarity

GO - Molecular functioni

  1. mannose binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Manganese, Mannose-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Concanavalin-A
Short name:
Con A
OrganismiCanavalia lineata (Beach bean) (Dolichos lineatus)
Taxonomic identifieri28957 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Concanavalin-APRO_0000105087Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi15 – 173Combined sources
Beta strandi24 – 3310Combined sources
Beta strandi35 – 395Combined sources
Beta strandi46 – 5510Combined sources
Turni56 – 594Combined sources
Beta strandi60 – 667Combined sources
Beta strandi72 – 787Combined sources
Helixi81 – 833Combined sources
Beta strandi87 – 9610Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi105 – 11612Combined sources
Beta strandi124 – 1329Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1574Combined sources
Turni161 – 1633Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi187 – 19913Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi209 – 2168Combined sources
Helixi227 – 2293Combined sources
Turni230 – 2323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CWMX-ray1.95A1-237[»]
2CY6X-ray2.00A/D1-237[»]
2CYFX-ray1.80A1-237[»]
3SNMX-ray2.15A1-237[»]
4DPNX-ray2.55A/D1-237[»]
4I30X-ray1.89A1-237[»]
ProteinModelPortaliP81460.
SMRiP81460. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81460.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1002Carbohydrate bindingBy similarity

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81460-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA
60 70 80 90 100
HIIYNSVGKR LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY
110 120 130 140 150
KETNTILSWS FTSKLKSNST HETNALHFVF NQFSKDQKDL ILQGDATTGT
160 170 180 190 200
DGNLELTRVS SNGSPQGNSV GRALFYAPVH IWESSAVVAS FDATFTFLIK
210 220 230
SSDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
Length:237
Mass (Da):25,497
Last modified:December 15, 1998 - v1
Checksum:i2D31C2BD3D30D66A
GO

Sequence databases

PIRiA59415.

Cross-referencesi

Sequence databases

PIRi A59415.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CWM X-ray 1.95 A 1-237 [» ]
2CY6 X-ray 2.00 A/D 1-237 [» ]
2CYF X-ray 1.80 A 1-237 [» ]
3SNM X-ray 2.15 A 1-237 [» ]
4DPN X-ray 2.55 A/D 1-237 [» ]
4I30 X-ray 1.89 A 1-237 [» ]
ProteinModelPortali P81460.
SMRi P81460. Positions 1-237.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P81460.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
InterProi IPR013320. ConA-like_dom.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view ]
Pfami PF00139. Lectin_legB. 2 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary structures of concanavalin A-like lectins from seeds of two species of Canavalia."
    Fujimura S., Terada S., Jayavardhanan K.K., Panikkar K.R., Kimoto E.
    Phytochemistry 33:985-987(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiCONA_CANLI
AccessioniPrimary (citable) accession number: P81460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: November 26, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds one manganese (or another transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities.

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