LECA_LABPU
ID LECA_LABPU Reviewed; 237 AA.
AC P38662;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Lectin;
DE Contains:
DE RecName: Full=Lectin alpha chain;
DE Contains:
DE RecName: Full=Lectin beta chain;
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;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=cv. Lignosus; TISSUE=Seed;
RX PubMed=8034631; DOI=10.1016/s0021-9258(17)32237-8;
RA Gowda L.R., Savithri H.S., Rajagopal Rao D.;
RT "The complete primary structure of a unique mannose/glucose-specific lectin
RT from field bean (Dolichos lab lab).";
RL J. Biol. Chem. 269:18789-18793(1994).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin. Requires Ca(2+) and
CC Mn(2+) ions for full activity.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC -!- PTM: The N-terminus of alpha chain is blocked. The alpha and beta
CC chains are produced by proteolytic processing, with probably the loss
CC of intervening amino acid(s).
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PIR; A54864; A54864.
DR PIR; B54864; B54864.
DR AlphaFoldDB; P38662; -.
DR SMR; P38662; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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 Calcium; Direct protein sequencing; Glycoprotein; Lectin; Manganese;
KW Mannose-binding; Metal-binding.
FT CHAIN 1..105
FT /note="Lectin beta chain"
FT /id="PRO_0000017615"
FT CHAIN 106..237
FT /note="Lectin alpha chain"
FT /id="PRO_0000017616"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MOD_RES 106
FT /note="Blocked amino end (Ile)"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 237 AA; 25719 MW; BEB7E84DC2895327 CRC64;
AQSLSFSFTK FDPNQEDLIF QGTATSKLDS AGNPVSSSAG RVLYSAPLRL WEDSAVLTSF
DPTIYIFTNY TSRIADGLAF IAPPDSVISY HGGFLGLFPN AAESGIAESN VVAVEFDTDY
LNPDYGDPNY IHIGIDVNSI RSKVTASWDW QNGKIATAHI SYNSVSKRLS VTTYYPGRGK
PATSYDIELH TVLPEWVRVG LSASTGQNIE RNTVHSWSFT SSLWTNVAKV GVASISG
