AGGL_SCLS1
ID AGGL_SCLS1 Reviewed; 153 AA.
AC A7EWX9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Agglutinin {ECO:0000250|UniProtKB:A7XUK7};
GN ORFNames=SS1G_09838;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1] {ECO:0000312|EMBL:EDN93971.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Lectin that primarily recognizes glycans with a non-reducing
CC terminal N-acetylgalactosamine (GalNAc), with a preference for the
CC alpha- over the beta-anomer. Can also bind non-reducing terminal
CC galactose (Gal) residues but with a lower affinity. Strongly interacts
CC with glycolipid type glycans with terminal non-reducing Gal or GalNAc
CC but fails to bind sialylated or fucosylated forms of the same glycans.
CC Strongly interacts with galactosylated N-glycans, displaying highest
CC affinity for alpha-1-3 branched mono-antennary N-glycans but also
CC binding to multi-antennary glycans (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A7XUK7}.
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DR EMBL; CH476634; EDN93971.1; -; Genomic_DNA.
DR RefSeq; XP_001589205.1; XM_001589155.1.
DR AlphaFoldDB; A7EWX9; -.
DR SMR; A7EWX9; -.
DR GeneID; 5485273; -.
DR KEGG; ssl:SS1G_09838; -.
DR VEuPathDB; FungiDB:sscle_01g001830; -.
DR InParanoid; A7EWX9; -.
DR OMA; YEIVPYQ; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
PE 3: Inferred from homology;
KW Lectin; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:A7XUK7"
FT CHAIN 2..153
FT /note="Agglutinin"
FT /evidence="ECO:0000250|UniProtKB:A7XUK7"
FT /id="PRO_0000424171"
FT DOMAIN 58..153
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255"
FT BINDING 22..25
FT /ligand="beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:546807"
FT /evidence="ECO:0000250|UniProtKB:A7XUK7"
FT BINDING 46
FT /ligand="beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:546807"
FT /evidence="ECO:0000250|UniProtKB:A7XUK7"
SQ SEQUENCE 153 AA; 16740 MW; BDAC0EF1FA1ED374 CRC64;
MGFKGVGTYE IVPYQAPSLN LNAWEGKLEP GAVVRTYTRG DKPSDNAKWQ VALVAGSGDS
AEYLIINVHS GYFLTATKEN HIVSTPQISP TDPSARWTIK PATTHQYEVF TINNKVSELG
QLTVKDYSTH SGADVLSASA KTADNQKWYF DAK