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LEC_LENCC
ID   LEC_LENCC               Reviewed;         275 AA.
AC   Q93WH6; Q93X50;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Lectin;
DE   Contains:
DE     RecName: Full=Lectin beta chain;
DE   Contains:
DE     RecName: Full=Lectin alpha chain;
DE   Flags: Precursor;
OS   Lens culinaris subsp. culinaris (Cultivated lentil) (Lens esculenta).
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; Hologalegina; IRL clade; Fabeae; Lens.
OX   NCBI_TaxID=362247;
RN   [1] {ECO:0000312|EMBL:CAC42123.2}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Eston {ECO:0000312|EMBL:CAC42124.2}, and
RC   cv. Laird {ECO:0000312|EMBL:CAC42123.2};
RC   TISSUE=Leaf {ECO:0000312|EMBL:CAC42123.2};
RX   PubMed=15067396; DOI=10.1007/s00122-003-1520-9;
RA   Galasso I., Lioi L., Lanave C., Bollini R., Sparvoli F.;
RT   "Identification and isolation of lectin nucleotide sequences and species
RT   relationships in the genus Lens (Miller).";
RL   Theor. Appl. Genet. 108:1098-1102(2004).
CC   -!- FUNCTION: D-mannose specific lectin. {ECO:0000250|UniProtKB:P02867}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000250}.
CC   -!- PTM: The mature form consists of two chains, alpha and beta, produced
CC       by cleavage of the immature protein. These remain cleaved, yet fold
CC       together to form one subunit (By similarity).
CC       {ECO:0000250|UniProtKB:P02870}.
CC   -!- MISCELLANEOUS: Binds two manganese (or other transition metal) ions and
CC       two calcium ions per heterotetramer. The metal ions are essential for
CC       the saccharide-binding activity (By similarity).
CC       {ECO:0000250|UniProtKB:P02870}.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR   EMBL; AJ318216; CAC42122.1; -; Genomic_DNA.
DR   EMBL; AJ318217; CAC42123.2; -; Genomic_DNA.
DR   EMBL; AJ318218; CAC42124.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q93WH6; -.
DR   SMR; Q93WH6; -.
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   3: Inferred from homology;
KW   Calcium; Lectin; Manganese; Mannose-binding; Metal-binding; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   CHAIN           31..210
FT                   /note="Lectin beta chain"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT                   /id="PRO_0000223510"
FT   PROPEP          211..217
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT                   /id="PRO_0000223511"
FT   CHAIN           218..269
FT                   /note="Lectin alpha chain"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT                   /id="PRO_0000223512"
FT   PROPEP          270..275
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT                   /id="PRO_0000223513"
FT   BINDING         111
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   BINDING         129
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   BINDING         151
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   BINDING         151
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   BINDING         153
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   BINDING         166
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   BINDING         246
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250"
FT   SITE            210..211
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   SITE            217..218
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P02870"
FT   CONFLICT        46
FT                   /note="K -> Q (in Ref. 1; CAC42122)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   275 AA;  30280 MW;  4345F4322F1C75F0 CRC64;
     MASLQTQMIS FYLIFLSILL TTIFFFKVNS TETTSFSITK FSPDQKNLIF QGDGYTTKGK
     LTLTKAVKST VGRALYSTPI HIWDRDTGNV ANFVTSFTFV IDAPSSYNVA DGFTFFIAPV
     DTKPQTGGGY LGVFNSKEYD KTSQTVAVEF DTFYNAAWDP SNKERHIGID VNSIKSVNTK
     SWNLQNGERA NVVIAFNAAT NVLTVTLTYP NSLEEENVTS YTLNEVVPLK DVVPEWVRIG
     FSATTGAEFA AHEVHSWSFH SELGGTSSSK QAADA
 
 
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