LECA_CYMRO
ID LECA_CYMRO Reviewed; 237 AA.
AC P86184;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Mannose-specific lectin alpha chain {ECO:0000303|Ref.1};
DE Contains:
DE RecName: Full=Mannose-specific lectin beta chain {ECO:0000303|Ref.1};
DE Contains:
DE RecName: Full=Mannose-specific lectin gamma chain {ECO:0000303|Ref.1};
OS Cymbosema roseum (Dioclea purpurea).
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; Cymbosema.
OX NCBI_TaxID=202239;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000269|Ref.1};
RA Rocha B.A.M., Delatorre P., Marinho E.S., Benevides R.G., Moura T.R.,
RA Sousa L.A.G., Nascimento K.S., Sampaio A.H., Cavada B.S.;
RT "Crystal structure of an antiinflammatory legume lectin.";
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin. Also binds derivatives of
CC glucose and mannose such as more complex glycans. {ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.1}.
CC -!- PTM: The beta and gamma chains are produced by partial proteolytic
CC processing of the lectin alpha chain by an asparaginyl endopeptidase.
CC {ECO:0000250|UniProtKB:P81637, ECO:0000269|Ref.1}.
CC -!- MASS SPECTROMETRY: [Mannose-specific lectin alpha chain]: Mass=25326;
CC Mass_error=0.5; Method=Electrospray; Evidence={ECO:0000269|Ref.1};
CC -!- MASS SPECTROMETRY: [Mannose-specific lectin alpha chain]: Mass=25325;
CC Mass_error=1; Method=MALDI; Evidence={ECO:0000269|Ref.1};
CC -!- MISCELLANEOUS: Binds one manganese (or another transition metal) ion
CC and one calcium ion. The metal ions are essential for the saccharide-
CC binding and cell-agglutinating activities (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR PDB; 4MYE; X-ray; 1.65 A; A=1-237.
DR PDBsum; 4MYE; -.
DR AlphaFoldDB; P86184; -.
DR SMR; P86184; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; 2.
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; Calcium; Direct protein sequencing; Lectin; Manganese;
KW Mannose-binding; Metal-binding.
FT CHAIN 1..237
FT /note="Mannose-specific lectin alpha chain"
FT /id="PRO_0000394798"
FT CHAIN 1..118
FT /note="Mannose-specific lectin beta chain"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000394799"
FT CHAIN 119..237
FT /note="Mannose-specific lectin gamma chain"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000394800"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P81637"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81637"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P81637"
FT BINDING 12
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81637"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81637"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81637"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P81637"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P81637"
FT BINDING 34
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 99..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81637"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4MYE"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:4MYE"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:4MYE"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:4MYE"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4MYE"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:4MYE"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4MYE"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4MYE"
SQ SEQUENCE 237 AA; 25326 MW; 58B7174E4089B5A8 CRC64;
ADTIVAVELD SYPNTDIGDP SYPHIGIDIK SIRSKSTARW NMQTGKVGTA HISYNSVAKR
LTAVVSYSGS SSTTVSYDVD LNNVLPEWVR VGLSATTGLY KETNTILSWS FTSKLKTNSI
ADANALHFSF HQFTQNPKDL ILQGDATTDS DGNLELTKVS SSGSPQGSSV GRALFYAPVH
IWESSAVVAS FDATFTFLIK SPDSEPADGI TFFIANTDTS IPSGSSGRLL GLFPDAN
