LECC1_ARAHY
ID LECC1_ARAHY Reviewed; 280 AA.
AC Q70DJ5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Alpha-methyl-mannoside-specific lectin {ECO:0000303|PubMed:16941222};
DE Short=SL-I {ECO:0000303|PubMed:16941222};
DE Flags: Precursor;
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAE51929.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-36; 44-57; 78-89;
RP 194-209; 233-240 AND 259-270, FUNCTION, SUBUNIT, AND GLYCOSYLATION.
RC STRAIN=cv. ICGS-1; TISSUE=Root {ECO:0000312|EMBL:CAE51929.1};
RX PubMed=16941222; DOI=10.1007/s11103-006-9038-6;
RA Pathak M., Singh B., Sharma A., Agrawal P., Pasha S.B., Das H.R., Das R.H.;
RT "Molecular cloning, expression, and cytokinin (6-benzylaminopurine)
RT antagonist activity of peanut (Arachis hypogaea) lectin SL-I.";
RL Plant Mol. Biol. 62:529-545(2006).
RN [2] {ECO:0000312|EMBL:AAR06177.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. ICGS-1; TISSUE=Root {ECO:0000312|EMBL:AAR06177.1};
RA Das R.H., Das H.R., Pathak M.;
RT "Partial sequence of a cDNA clone having potential to code for a lectin
RT from 6 day-old roots of Arachis hypogaea.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, AND GLYCOSYLATION.
RC STRAIN=cv. JL-24 {ECO:0000269|PubMed:7873922}; TISSUE=Stem;
RX PubMed=7873922; DOI=10.1007/bf00731199;
RA Singh R., Das H.R.;
RT "Purification of lectins from the stems of peanut plants.";
RL Glycoconj. J. 11:282-285(1994).
CC -!- FUNCTION: Alpha-methyl-D-mannoside-specific lectin. Has
CC hemagglutinating activity towards rabbit erythrocytes. Binds to
CC cytokinins and significantly inhibits physiological effects of
CC cytokinin activity such as cotyledon expansion and delayed leaf
CC senescence. {ECO:0000269|PubMed:16941222, ECO:0000269|PubMed:7873922}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16941222}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:7873922,
CC ECO:0000303|PubMed:16941222}.
CC -!- MISCELLANEOUS: The hemagglutination activity of native and recombinant
CC SL-I was not inhibited by cellobiose even at 120 mM, however alpha-
CC methylmannoside and 2-alpha-mannose inhibited hemagglutination at 0.38
CC mM and 0.39 mM respectively. {ECO:0000269|PubMed:16941222}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR EMBL; AJ585523; CAE51929.1; -; mRNA.
DR EMBL; AY431029; AAR06177.1; -; mRNA.
DR AlphaFoldDB; Q70DJ5; -.
DR SMR; Q70DJ5; -.
DR GO; GO:0044373; F:cytokinin binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0080037; P:negative regulation of cytokinin-activated signaling pathway; IDA:UniProtKB.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016363; L-lectin.
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; PS00307; LECTIN_LEGUME_BETA; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hemagglutinin; Lectin; Manganese;
KW Mannose-binding; Metal-binding; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:16941222"
FT CHAIN 27..280
FT /note="Alpha-methyl-mannoside-specific lectin"
FT /evidence="ECO:0000269|PubMed:16941222"
FT /id="PRO_5000072171"
FT BINDING 114
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 134
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 158
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 165
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 166
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 248
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 250
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
SQ SEQUENCE 280 AA; 30765 MW; 2F8E59AB2E628894 CRC64;
MAISKKILPL LSIATIFLLL LNKAHSLGSL SFGYNNFEQG DERNLILQGD ATFSASKGIQ
LTKVDDNGTP AKSTVGRVLH STQVRLWEKS TNRLTNFQAQ FSFVINSPID NGADGIAFFI
AAPDSEIPKN SAGGTLGLSD PSTAQNPSAN QVLAVEFDTF YAQDSNGWDP NYQHIGFDVD
PIKSAATTKW ERRNGQTLNV LVSYDANSKN LQVTASYPDG QSYQVSYNVD LRDYLPEWGR
VGFSAASGQQ YQSHGLQSWS FTSTLLYTSP HYLKLGRFMI
