FRIL_LABPU
ID FRIL_LABPU Reviewed; 272 AA.
AC Q9ZTA9;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Flt3 receptor-interacting lectin {ECO:0000303|PubMed:9892687};
DE Contains:
DE RecName: Full=Lectin alpha chain {ECO:0000303|PubMed:9892687};
DE Contains:
DE RecName: Full=Lectin beta chain {ECO:0000303|PubMed:9892687};
DE Contains:
DE RecName: Full=Lectin alpha-1 chain {ECO:0000303|PubMed:9892687};
DE Flags: Precursor;
GN Name=FRIL {ECO:0000303|PubMed:9892687};
OS Lablab purpureus (Hyacinth bean) (Dolichos lablab).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Lablab.
OX NCBI_TaxID=35936 {ECO:0000312|EMBL:AAD10734.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 9-38 AND 125-152,
RP GLYCOSYLATION AT ASN-131, FUNCTION, AND BIOTECHNOLOGY.
RC TISSUE=Cotyledon;
RX PubMed=9892687; DOI=10.1073/pnas.96.2.646;
RA Colucci G., Moore J.G., Feldman M., Chrispeels M.J.;
RT "cDNA cloning of FRIL, a lectin from Dolichos lablab, that preserves
RT hematopoietic progenitors in suspension culture.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:646-650(1999).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY,
RP GLYCOSYLATION AT ASN-125 AND ASN-131, AND SUBCELLULAR LOCATION.
RX PubMed=24907509; DOI=10.1016/j.ijbiomac.2014.05.073;
RA B S G.K., Pohlentz G., Schulte M., Mormann M., Nadimpalli S.K.;
RT "N-glycan analysis of mannose/glucose specific lectin from Dolichos lablab
RT seeds.";
RL Int. J. Biol. Macromol. 69:400-407(2014).
RN [3]
RP SUBUNIT, AND FUNCTION.
RX PubMed=9949194; DOI=10.1093/glycob/9.2.173;
RA Mo H., Meah Y., Moore J.G., Goldstein I.J.;
RT "Purification and characterization of Dolichos lablab lectin.";
RL Glycobiology 9:173-179(1999).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=10880759; DOI=10.1016/s0301-472x(00)00163-6;
RA Kollet O., Moore J.G., Aviram R., Ben-Hur H., Liu B.L., Nagler A.,
RA Shultz L., Feldman M., Lapidot T.;
RT "The plant lectin FRIL supports prolonged in vitro maintenance of quiescent
RT human cord blood CD34(+)CD38(-/low)/SCID repopulating stem cells.";
RL Exp. Hematol. 28:726-736(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 9-121 AND 140-272 IN COMPLEX WITH
RP MANNOSE, AND SUBUNIT.
RX PubMed=10843844; DOI=10.1006/jmbi.2000.3785;
RA Hamelryck T.W., Moore J.G., Chrispeels M.J., Loris R., Wyns L.;
RT "The role of weak protein-protein interactions in multivalent lectin-
RT carbohydrate binding: crystal structure of cross-linked FRIL.";
RL J. Mol. Biol. 299:875-883(2000).
CC -!- FUNCTION: Mannose-binding lectin (PubMed:9892687). Accommodates most
CC effectively a non-reducing terminal alpha-d-mannosyl unit. Strongly
CC precipitates murine IgM but not IgG (PubMed:9949194).
CC {ECO:0000269|PubMed:9892687, ECO:0000269|PubMed:9949194}.
CC -!- SUBUNIT: Dimer (alpha/beta)2 (PubMed:9949194). Tetramer (alpha/beta)4
CC (PubMed:10843844). {ECO:0000269|PubMed:10843844,
CC ECO:0000269|PubMed:9949194}.
CC -!- SUBCELLULAR LOCATION: Protein storage vacuole lumen
CC {ECO:0000303|PubMed:24907509}.
CC -!- PTM: Glycosylated at Asn-125 by either a paucimannose type N-glycan
CC (alpha-4) or a single N-acetylglucosamine (alpha-3). Glycosylated at
CC Asn-131 by a paucimannose type N-glycan (alpha-2, alpha-3 and alpha-4).
CC In alpha-2, Asn-125 is deamidated to an Asp, possibly due to the action
CC of intrinsic peptide N-glycosidase (PGNase).
CC {ECO:0000269|PubMed:24907509}.
CC -!- BIOTECHNOLOGY: Preserves hematopoietic progenitors in suspension
CC culture by preventing their proliferation and differentiation even in
CC the presence of a cytokine known for its strong induction of
CC proliferation and differentiation (PubMed:9892687). FRIL's ability to
CC preserve quiescent primitive cells in a reversible manner may
CC significantly expand the time and range of ex vivo manipulations of
CC human stem cells for clinical applications (PubMed:10880759).
CC {ECO:0000269|PubMed:10880759, ECO:0000269|PubMed:9892687}.
CC -!- MISCELLANEOUS: Four different alpha subunits (alpha-1, alpha-2, alpha-3
CC and alpha-4) are observed and their different polypeptide masses might
CC be due to differential C-terminal processing of the corresponding
CC polypeptide or to differential N-glycosylation of subunits. Alpha-1
CC lacks the 8 amino acids N-terminal sequence present in the other alpha
CC subunits. Alpha-2 and Alpha-4 differ in their glycosylation pattern.
CC Alpha-3 et Alpha-4 are N-glycosylated at their N-terminus. The Asn N-
CC terminus of alpha-2 is deamidated into Asp.
CC {ECO:0000269|PubMed:9892687}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
CC -!- CAUTION: The amino acid substitutions in both the subunits found in
CC PubMed:24907509 might have resulted from different cultivars or growing
CC conditions of the plant used in the study.
CC {ECO:0000303|PubMed:24907509}.
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DR EMBL; AF067417; AAD10734.1; -; mRNA.
DR PDB; 1QMO; X-ray; 3.50 A; A/B/C/D=9-121, E/F/G/H=140-272.
DR PDBsum; 1QMO; -.
DR AlphaFoldDB; Q9ZTA9; -.
DR SMR; Q9ZTA9; -.
DR UniLectin; Q9ZTA9; -.
DR iPTMnet; Q9ZTA9; -.
DR EvolutionaryTrace; Q9ZTA9; -.
DR GO; GO:0034495; C:protein storage vacuole lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016363; L-lectin.
DR InterPro; IPR000985; Lectin_LegA_CS.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Lectin; Signal;
KW Vacuole.
FT SIGNAL 1..8
FT /evidence="ECO:0000305|PubMed:9892687"
FT CHAIN 9..124
FT /note="Lectin beta chain"
FT /evidence="ECO:0000305|PubMed:9892687"
FT /id="PRO_0000434745"
FT CHAIN 125..272
FT /note="Lectin alpha chain"
FT /evidence="ECO:0000305|PubMed:9892687"
FT /id="PRO_0000434746"
FT CHAIN 133..272
FT /note="Lectin alpha-1 chain"
FT /evidence="ECO:0000305|PubMed:9892687"
FT /id="PRO_0000434747"
FT BINDING 94
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0007744|PDB:1QMO"
FT BINDING 112
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:10843844,
FT ECO:0007744|PDB:1QMO"
FT BINDING 152
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:10843844,
FT ECO:0007744|PDB:1QMO"
FT BINDING 237..238
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:10843844,
FT ECO:0007744|PDB:1QMO"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24907509"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24907509,
FT ECO:0000269|PubMed:9892687"
FT CONFLICT 34
FT /note="S -> SS (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="V -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000269|PubMed:24907509"
FT CONFLICT 148
FT /note="D -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000269|PubMed:24907509"
FT CONFLICT 206
FT /note="A -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000269|PubMed:24907509"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 71..85
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1QMO"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1QMO"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1QMO"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:1QMO"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1QMO"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1QMO"
FT STRAND 241..255
FT /evidence="ECO:0007829|PDB:1QMO"
SQ SEQUENCE 272 AA; 29900 MW; EA6C004307441495 CRC64;
MFPSKVKSAQ SLSFSFTKFD PNQEDLIFQG HATSTNNVLQ VTKLDSAGNP VSSSAGRVLY
SAPLRLWEDS AVLTSFDTII NFEISTPYTS RIADGLAFFI APPDSVISYH GGFLGLFPNA
NTLNNSSTSE NQTTTKAASS NVVAVEFDTY LNPDYGDPNY IHIGIDVNSI RSKVTAKWDW
QNGKIATAHI SYNSVSKRLS VTSYYAGSKP ATLSYDIELH TVLPEWVRVG LSASTGQDKE
RNTVHSWSFT SSLWTNVAKK ENENKYITRG VL
