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Protein

Mannose-specific lectin 3

Gene
N/A
Organism
Crocus vernus (Dutch crocus)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Mannose-specific lectin. Has weak agglutinating activity towards trypsin-treated erythrocytes from rabbit but not from human (By similarity).By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin

Keywords - Ligandi

Lectin, Mannose-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mannose-specific lectin 3
Cleaved into the following 2 chains:
OrganismiCrocus vernus (Dutch crocus)
Taxonomic identifieri87752 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesIridaceaeCrocus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003954381 – 111Mannose-specific lectin 3 chain 1Add BLAST111
ChainiPRO_0000395439112 – 224Mannose-specific lectin 3 chain 2Add BLAST113

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 52PROSITE-ProRule annotation1 Publication
Disulfide bondi145 ↔ 170PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterotetramer of 2 domain 1 and 2 domain 2 chains arranged as a dimer of domain 1/domain 2 heterodimers.By similarity

Structurei

Secondary structure

1224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi16 – 19Combined sources4
Beta strandi22 – 26Combined sources5
Beta strandi32 – 35Combined sources4
Beta strandi53 – 56Combined sources4
Beta strandi62 – 65Combined sources4
Beta strandi73 – 79Combined sources7
Beta strandi88 – 91Combined sources4
Beta strandi97 – 100Combined sources4
Beta strandi102 – 106Combined sources5
Beta strandi117 – 121Combined sources5
Beta strandi125 – 127Combined sources3
Beta strandi131 – 134Combined sources4
Beta strandi137 – 141Combined sources5
Beta strandi147 – 151Combined sources5
Turni152 – 155Combined sources4
Beta strandi156 – 160Combined sources5
Beta strandi171 – 174Combined sources4
Beta strandi180 – 183Combined sources4
Beta strandi189 – 192Combined sources4
Beta strandi198 – 200Combined sources3
Beta strandi203 – 206Combined sources4
Beta strandi212 – 215Combined sources4
Beta strandi217 – 222Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MEZX-ray1.94A/C1-110[»]
B/D112-223[»]
SMRiP86626.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP86626.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 111Bulb-type lectin 1PROSITE-ProRule annotationCuratedAdd BLAST110
Domaini117 – 222Bulb-type lectin 2PROSITE-ProRule annotationAdd BLAST106

Sequence similaritiesi

Contains 2 bulb-type lectin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.90.10.10. 2 hits.
InterProiIPR001480. Bulb-type_lectin_dom.
[Graphical view]
PfamiPF01453. B_lectin. 2 hits.
[Graphical view]
SMARTiSM00108. B_lectin. 2 hits.
[Graphical view]
SUPFAMiSSF51110. SSF51110. 2 hits.
PROSITEiPS50927. BULB_LECTIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P86626-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DNNVLLTGDV IHTDNQLSYE SAAFVMQGDC NLVLYNEAGG FQSNTHGRGV
60 70 80 90 100
DCTLRLNNRG QLEIHSANSN TPVWVYPRSV NTVRGNYAAT LGPDQHVTIY
110 120 130 140 150
GPAIWSTPAA ANIPRVRNVL FSSQVMYDNA QLATRDYSLV MRDDCNLVLT
160 170 180 190 200
KGSKTNIVWE SGTSGRGQHC FMRLGHSGEL DITDDRLNTV FVSNTVGQEG
210 220
DYVLILQING QAVVYGPAVW STAA
Length:224
Mass (Da):24,454
Last modified:October 19, 2011 - v3
Checksum:i94C963051247B7C6
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MEZX-ray1.94A/C1-110[»]
B/D112-223[»]
SMRiP86626.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP86626.

Family and domain databases

Gene3Di2.90.10.10. 2 hits.
InterProiIPR001480. Bulb-type_lectin_dom.
[Graphical view]
PfamiPF01453. B_lectin. 2 hits.
[Graphical view]
SMARTiSM00108. B_lectin. 2 hits.
[Graphical view]
SUPFAMiSSF51110. SSF51110. 2 hits.
PROSITEiPS50927. BULB_LECTIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLEC3_CROVR
AccessioniPrimary (citable) accession number: P86626
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: October 19, 2011
Last modified: November 2, 2016
This is version 18 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

On the 2D-gel the determined pI of this protein is: 5.18, its MW is: 48 kDa.

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.