AGGL_SCLSC
ID AGGL_SCLSC Reviewed; 153 AA.
AC A7XUK7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Agglutinin {ECO:0000312|EMBL:ABE97202.1};
DE Short=SSA {ECO:0000303|PubMed:17294128};
OS Sclerotinia sclerotiorum (White mold) (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=5180;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABE97202.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=S1954 {ECO:0000269|PubMed:17294128};
RC TISSUE=Sclerotium {ECO:0000269|PubMed:17294128};
RX PubMed=17294128; DOI=10.1007/s10719-006-9022-z;
RA Van Damme E.J., Nakamura-Tsuruta S., Hirabayashi J., Rouge P.,
RA Peumans W.J.;
RT "The Sclerotinia sclerotiorum agglutinin represents a novel family of
RT fungal lectins remotely related to the Clostridium botulinum non-toxin
RT haemagglutinin HA33/A.";
RL Glycoconj. J. 24:143-156(2007).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-20, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=12901882; DOI=10.1016/s0006-291x(03)01406-2;
RA Candy L., Van Damme E.J., Peumans W.J., Menu-Bouaouiche L., Erard M.,
RA Rouge P.;
RT "Structural and functional characterization of the GalNAc/Gal-specific
RT lectin from the phytopathogenic ascomycete Sclerotinia sclerotiorum (Lib.)
RT de Bary.";
RL Biochem. Biophys. Res. Commun. 308:396-402(2003).
RN [3] {ECO:0000305, ECO:0000312|PDB:2X2T}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH
RP GALACTOSE-BETA-1,3-N-ACETYL-D-GALACTOSAMINE, FUNCTION, AND SUBUNIT.
RX PubMed=20566411; DOI=10.1016/j.jmb.2010.05.038;
RA Sulzenbacher G., Roig-Zamboni V., Peumans W.J., Rouge P., Van Damme E.J.,
RA Bourne Y.;
RT "Crystal structure of the GalNAc/Gal-specific agglutinin from the
RT phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel
RT adaptation of a beta-trefoil domain.";
RL J. Mol. Biol. 400:715-723(2010).
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. {ECO:0000269|PubMed:12901882,
CC ECO:0000269|PubMed:17294128, ECO:0000269|PubMed:20566411}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12901882,
CC ECO:0000269|PubMed:20566411}.
CC -!- MASS SPECTROMETRY: Mass=16618; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12901882};
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DR EMBL; DQ468383; ABE97202.1; -; mRNA.
DR PDB; 2X2S; X-ray; 1.60 A; A/B/C/D=1-153.
DR PDB; 2X2T; X-ray; 1.97 A; A=1-153.
DR PDBsum; 2X2S; -.
DR PDBsum; 2X2T; -.
DR AlphaFoldDB; A7XUK7; -.
DR SMR; A7XUK7; -.
DR UniLectin; A7XUK7; -.
DR VEuPathDB; FungiDB:sscle_01g001830; -.
DR OMA; YEIVPYQ; -.
DR EvolutionaryTrace; A7XUK7; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lectin.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12901882"
FT CHAIN 2..153
FT /note="Agglutinin"
FT /evidence="ECO:0000269|PubMed:12901882"
FT /id="PRO_0000424170"
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:0000269|PubMed:20566411,
FT ECO:0007744|PDB:2X2T"
FT BINDING 46
FT /ligand="beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:546807"
FT /evidence="ECO:0000269|PubMed:20566411,
FT ECO:0007744|PDB:2X2T"
FT CONFLICT 2
FT /note="G -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="K -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:2X2S"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2X2S"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2X2T"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2X2S"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2X2S"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:2X2S"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2X2S"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2X2S"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2X2S"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2X2S"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2X2S"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:2X2S"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2X2S"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2X2S"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2X2S"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2X2S"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2X2S"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:2X2S"
SQ SEQUENCE 153 AA; 16740 MW; BDAC0EF1FA1ED374 CRC64;
MGFKGVGTYE IVPYQAPSLN LNAWEGKLEP GAVVRTYTRG DKPSDNAKWQ VALVAGSGDS
AEYLIINVHS GYFLTATKEN HIVSTPQISP TDPSARWTIK PATTHQYEVF TINNKVSELG
QLTVKDYSTH SGADVLSASA KTADNQKWYF DAK
