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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 – 81Manganese By similarity
Metal bindingi10 – 101Calcium By similarity
Metal bindingi10 – 101Manganese By similarity
Metal bindingi12 – 121Calcium; via carbonyl oxygen By similarity
Binding sitei12 – 121Carbohydrate By similarity
Metal bindingi14 – 141Calcium By similarity
Metal bindingi19 – 191Calcium By similarity
Metal bindingi19 – 191Manganese By similarity
Metal bindingi24 – 241Manganese By similarity
Metal bindingi208 – 2081Calcium By similarity
Binding sitei228 – 2281Carbohydrate; via amide nitrogen By similarity

GO - Molecular functioni

  1. mannose binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: UniProtKB
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 – 107
Helixi15 – 173
Beta strandi24 – 3310
Beta strandi35 – 395
Beta strandi46 – 5510
Turni56 – 594
Beta strandi60 – 667
Beta strandi72 – 787
Helixi81 – 833
Beta strandi87 – 9610
Beta strandi98 – 1003
Beta strandi105 – 11612
Beta strandi124 – 1329
Beta strandi140 – 1445
Beta strandi150 – 1523
Beta strandi154 – 1574
Turni161 – 1633
Beta strandi170 – 1778
Beta strandi187 – 19913
Beta strandi203 – 2053
Beta strandi209 – 2168
Helixi227 – 2293
Turni230 – 2323

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP81460.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the leguminous lectin family.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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

ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA    50
HIIYNSVGKR LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY 100
KETNTILSWS FTSKLKSNST HETNALHFVF NQFSKDQKDL ILQGDATTGT 150
DGNLELTRVS SNGSPQGNSV GRALFYAPVH IWESSAVVAS FDATFTFLIK 200
SSDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN 237
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:
PDBe
RCSB PDB
PDBj
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 IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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: June 11, 2014
This is version 80 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

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