LEC1_CRAMO
ID LEC1_CRAMO Reviewed; 234 AA.
AC P83721;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Mannose/glucose-specific lectin Cramoll;
DE AltName: Full=Iso1;
DE Contains:
DE RecName: Full=Cramoll alpha chain;
DE Contains:
DE RecName: Full=Cramoll beta chain;
DE Flags: Fragments;
OS Cratylia mollis (Camaratu bean).
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; Cratylia.
OX NCBI_TaxID=252530 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBUNIT, METAL-BINDING, AND X-RAY CRYSTALLOGRAPHY (1.77
RP ANGSTROMS).
RC TISSUE=Seed {ECO:0000269|PubMed:12966038};
RX PubMed=12966038; DOI=10.1093/glycob/cwg115;
RA De Souza G.A., Oliveira P.S.L., Trapani S., Santos A.C.O., Rosa J.C.,
RA Laure H.J., Faca V.M., Correia M.T.S., Tavares G.A., Oliva G.,
RA Coelho L.C.B.B., Greene L.J.;
RT "Amino acid sequence and tertiary structure of Cratylia mollis seed
RT lectin.";
RL Glycobiology 13:961-972(2003).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=8579345; DOI=10.1007/bf02786865;
RA Correia M.T.S., Coelho L.C.B.B.;
RT "Purification of a glucose/mannose specific lectin, isoform 1, from seeds
RT of Cratylia mollis Mart. (Camaratu bean).";
RL Appl. Biochem. Biotechnol. 55:261-273(1995).
CC -!- FUNCTION: Glucose/D-mannose specific lectin.
CC {ECO:0000269|PubMed:8579345}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12966038}.
CC -!- PTM: The alpha and beta chains are produced by partial proteolytic
CC processing of the lectin precursor by an asparaginyl endopeptidase.
CC {ECO:0000303|PubMed:12966038}.
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.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 1MVQ; X-ray; 1.77 A; A=1-234.
DR PDBsum; 1MVQ; -.
DR AlphaFoldDB; P83721; -.
DR SMR; P83721; -.
DR UniLectin; P83721; -.
DR EvolutionaryTrace; P83721; -.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
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; 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..116
FT /note="Cramoll alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000017591"
FT CHAIN 117..234
FT /note="Cramoll beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000017592"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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 BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 34
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 99..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 225
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT NON_CONS 114..115
FT /evidence="ECO:0000303|PubMed:12966038"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1MVQ"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1MVQ"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1MVQ"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:1MVQ"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 184..195
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1MVQ"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:1MVQ"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1MVQ"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:1MVQ"
SQ SEQUENCE 234 AA; 25130 MW; 6DC1F3FF1D3C1C58 CRC64;
ADTIVAVELD TYPNTDIGDP SYQHIGINIK SIRSKATTRW DVQNGKVGTA HISYNSVAKR
LSAVVSYPGG SSATVSYDVD LNNILPEWVR VGLSASTGLY KETNTILSWS FTSKSNSTAD
AQSLHFTFNQ FSQSPKDLIL QGDASTDSDG NLQLTRVSNG SPQSDSVGRA LYYAPVHIWD
KSAVVASFDA TFTFLIKSPD REIADGIAFF IANTDSSIPH GSGGRLLGLF PDAN
