LECR_CLAKE
ID LECR_CLAKE Reviewed; 290 AA.
AC Q39527;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Lectin-related protein;
DE AltName: Full=CLLRP;
DE AltName: Full=LRPCL;
DE Flags: Precursor; Fragment;
OS Cladrastis kentukea (Yellow wood) (Cladrastis lutea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; Cladrastis clade;
OC Cladrastis.
OX NCBI_TaxID=38412;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 37-56.
RC TISSUE=Bark;
RX PubMed=8534854; DOI=10.1007/bf00020986;
RA van Damme E.J.M., Barre A., Bemer V., Rouge P., van Leuven F.,
RA Peumans W.J.;
RT "A lectin and a lectin-related protein are the two most prominent proteins
RT in the bark of yellow wood (Cladrastis lutea).";
RL Plant Mol. Biol. 29:579-598(1995).
CC -!- FUNCTION: Does not have any carbohydrate binding or agglutination
CC activity.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; U21940; AAC49150.1; -; mRNA.
DR PIR; S66355; S66355.
DR AlphaFoldDB; Q39527; -.
DR SMR; Q39527; -.
DR GO; GO:0030246; F:carbohydrate 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 Metal-binding; Signal.
FT SIGNAL <1..36
FT /evidence="ECO:0000269|PubMed:8534854"
FT CHAIN 37..290
FT /note="Lectin-related protein"
FT /id="PRO_0000017653"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 290 AA; 31378 MW; 64F2DBE7B2E20B14 CRC64;
ANSNSRPHLL QTQKPFSVVL AISITFYLLL LNKVNSEEAL SFTFTKFVSN QDELLLQGDA
LVSSKGELQL TRVENGQPIP HSVGRALYSD PVHIWDSSTG SVASFVTSFT FVVEAPNENK
TADGIAFFLA PPDTQVQSLG GFLGLFNSSV YNSSNQILAV EFDTFSNSWD PTARHIGIDV
NSIESTRTAT WGWRNGEVAI VLITYVAPAE TLIASLTYPS SQTSYILSAA VDLKSILPEW
VRVGFSAATG RSAGYVETHD VLSWSFTSTL ETGNSGAKQN NAHLASYALI
