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Protein

Flt3 receptor-interacting lectin

Gene

FRIL

Organism
Lablab purpureus (Hyacinth bean) (Dolichos lablab)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mannose-binding lectin (PubMed:9892687). Accommodates most effectively a non-reducing terminal alpha-d-mannosyl unit. Strongly precipitates murine IgM but not IgG (PubMed:9949194).2 Publications

Miscellaneous

Four different alpha subunits (alpha-1, alpha-2, alpha-3 and alpha-4) are observed and their different polypeptide masses might be due to differential C-terminal processing of the corresponding polypeptide or to differential N-glycosylation of subunits. Alpha-1 lacks the 8 amino acids N-terminal sequence present in the other alpha subunits. Alpha-2 and Alpha-4 differ in their glycosylation pattern. Alpha-3 et Alpha-4 are N-glycosylated at their N-terminus. The Asn N-terminus of alpha-2 is deamidated into Asp.1 Publication

Caution

The amino acid substitutions in both the subunits found in PubMed:24907509 might have resulted from different cultivars or growing conditions of the plant used in the study.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei94MannoseCombined sources1
Binding sitei112Mannose; via amide nitrogenCombined sources1 Publication1
Binding sitei152MannoseCombined sources1 Publication1

GO - Molecular functioni

Keywordsi

LigandLectin

Protein family/group databases

UniLectiniQ9ZTA9

Names & Taxonomyi

Protein namesi
Recommended name:
Flt3 receptor-interacting lectin1 Publication
Cleaved into the following 3 chains:
Lectin alpha chain1 Publication
Lectin beta chain1 Publication
Lectin alpha-1 chain1 Publication
Gene namesi
Name:FRIL1 Publication
OrganismiLablab purpureus (Hyacinth bean) (Dolichos lablab)Imported
Taxonomic identifieri35936 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeindigoferoid/millettioid cladePhaseoleaeLablab

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Biotechnological usei

Preserves hematopoietic progenitors in suspension culture by preventing their proliferation and differentiation even in the presence of a cytokine known for its strong induction of proliferation and differentiation (PubMed:9892687). FRIL's ability to preserve quiescent primitive cells in a reversible manner may significantly expand the time and range of ex vivo manipulations of human stem cells for clinical applications (PubMed:10880759).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 81 Publication8
ChainiPRO_00004347459 – 124Lectin beta chain1 PublicationAdd BLAST116
ChainiPRO_0000434746125 – 272Lectin alpha chain1 PublicationAdd BLAST148
ChainiPRO_0000434747133 – 272Lectin alpha-1 chain1 PublicationAdd BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi125N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi131N-linked (GlcNAc...) asparagine2 Publications1

Post-translational modificationi

Glycosylated at Asn-125 by either a paucimannose type N-glycan (alpha-4) or a single N-acetylglucosamine (alpha-3). Glycosylated at Asn-131 by a paucimannose type N-glycan (alpha-2, alpha-3 and alpha-4). In alpha-2, Asn-125 is deamidated to an Asp, possibly due to the action of intrinsic peptide N-glycosidase (PGNase).1 Publication

Keywords - PTMi

Glycoprotein

PTM databases

iPTMnetiQ9ZTA9

Interactioni

Subunit structurei

Dimer (alpha/beta)2 (PubMed:9949194). Tetramer (alpha/beta)4 (PubMed:10843844).2 Publications

Structurei

Secondary structure

1272
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9ZTA9
SMRiQ9ZTA9
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZTA9

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni237 – 238Mannose bindingCombined sources1 Publication2

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd06899 lectin_legume_LecRK_Arcelin_Co, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR016363 L-lectin
IPR000985 Lectin_LegA_CS
IPR019825 Lectin_legB_Mn/Ca_BS
IPR001220 Legume_lectin_dom
PfamiView protein in Pfam
PF00139 Lectin_legB, 1 hit
PIRSFiPIRSF002690 L-type_lectin_plant, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00308 LECTIN_LEGUME_ALPHA, 1 hit
PS00307 LECTIN_LEGUME_BETA, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q9ZTA9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFPSKVKSAQ SLSFSFTKFD PNQEDLIFQG HATSTNNVLQ VTKLDSAGNP
60 70 80 90 100
VSSSAGRVLY SAPLRLWEDS AVLTSFDTII NFEISTPYTS RIADGLAFFI
110 120 130 140 150
APPDSVISYH GGFLGLFPNA NTLNNSSTSE NQTTTKAASS NVVAVEFDTY
160 170 180 190 200
LNPDYGDPNY IHIGIDVNSI RSKVTAKWDW QNGKIATAHI SYNSVSKRLS
210 220 230 240 250
VTSYYAGSKP ATLSYDIELH TVLPEWVRVG LSASTGQDKE RNTVHSWSFT
260 270
SSLWTNVAKK ENENKYITRG VL
Length:272
Mass (Da):29,900
Last modified:May 1, 1999 - v1
Checksum:iEA6C004307441495
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34S → SS AA sequence (PubMed:9892687).Curated1
Sequence conflicti41V → L AA sequence (PubMed:24907509).1 Publication1
Sequence conflicti148D → K AA sequence (PubMed:9892687).Curated1
Sequence conflicti203S → T AA sequence (PubMed:24907509).1 Publication1
Sequence conflicti206A → P AA sequence (PubMed:24907509).1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067417 mRNA Translation: AAD10734.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067417 mRNA Translation: AAD10734.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QMOX-ray3.50A/B/C/D9-121[»]
E/F/G/H140-272[»]
ProteinModelPortaliQ9ZTA9
SMRiQ9ZTA9
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

UniLectiniQ9ZTA9

PTM databases

iPTMnetiQ9ZTA9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZTA9

Family and domain databases

CDDicd06899 lectin_legume_LecRK_Arcelin_Co, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR016363 L-lectin
IPR000985 Lectin_LegA_CS
IPR019825 Lectin_legB_Mn/Ca_BS
IPR001220 Legume_lectin_dom
PfamiView protein in Pfam
PF00139 Lectin_legB, 1 hit
PIRSFiPIRSF002690 L-type_lectin_plant, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00308 LECTIN_LEGUME_ALPHA, 1 hit
PS00307 LECTIN_LEGUME_BETA, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFRIL_LABPU
AccessioniPrimary (citable) accession number: Q9ZTA9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 11, 2015
Last sequence update: May 1, 1999
Last modified: September 12, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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