LECC_CALSE
ID LECC_CALSE Reviewed; 153 AA.
AC P93114;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Jacalin-related lectin Calsepa {ECO:0000303|PubMed:10908718, ECO:0000303|PubMed:15299962, ECO:0000303|PubMed:26971576, ECO:0000303|PubMed:28748044, ECO:0000303|PubMed:28973127, ECO:0000303|PubMed:8955378, ECO:0000303|PubMed:9111143};
DE AltName: Full=Agglutinin {ECO:0000303|PubMed:10908718, ECO:0000303|PubMed:14561768, ECO:0000303|PubMed:18266762, ECO:0000303|PubMed:32143591, ECO:0000303|PubMed:8955378, ECO:0000303|PubMed:9111143};
DE AltName: Full=Mannose/maltose-specific lectin {ECO:0000303|PubMed:8955378};
OS Calystegia sepium (Hedge bindweed) (Convolvulus sepium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Convolvuleae; Calystegia.
OX NCBI_TaxID=47519 {ECO:0000312|EMBL:AAC49564.1};
RN [1] {ECO:0000312|EMBL:AAC49564.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Rhizome {ECO:0000303|PubMed:8955378, ECO:0000312|EMBL:AAC49564.1};
RX PubMed=8955378; DOI=10.1016/s0014-5793(96)01211-2;
RA Van Damme E.J., Barre A., Verhaert P., Rouge P., Peumans W.J.;
RT "Molecular cloning of the mitogenic mannose/maltose-specific rhizome lectin
RT from Calystegia sepium.";
RL FEBS Lett. 397:352-356(1996).
RN [2]
RP PROTEIN SEQUENCE OF 6-25 AND 75-94, FUNCTION, ACTIVITY REGULATION, SUBUNIT,
RP TISSUE SPECIFICITY, AND BIOTECHNOLOGY.
RX PubMed=9111143; DOI=10.1023/a:1018502107707;
RA Peumans W.J., Winter H.C., Bemer V., Van Leuven F., Goldstein I.J.,
RA Truffa-Bachi P., Van Damme E.J.;
RT "Isolation of a novel plant lectin with an unusual specificity from
RT Calystegia sepium.";
RL Glycoconj. J. 14:259-265(1997).
RN [3]
RP CRYSTALLIZATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=15299962; DOI=10.1107/s0907444996010955;
RA Wright L.M., Wood S.D., Reynolds C.D., Rizkallah P.J., Van Damme E.J.,
RA Peumans W.J.;
RT "Crystallization and preliminary X-ray analysis of a novel plant lectin
RT from Calystegia sepium.";
RL Acta Crystallogr. D 53:220-221(1997).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10908718; DOI=10.1016/s0014-5793(00)01801-9;
RA Peumans W.J., Hause B., Van Damme E.J.;
RT "The galactose-binding and mannose-binding jacalin-related lectins are
RT located in different sub-cellular compartments.";
RL FEBS Lett. 477:186-192(2000).
RN [5]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=18266762; DOI=10.1111/j.1742-4658.2008.06282.x;
RA Nakamura-Tsuruta S., Uchiyama N., Peumans W.J., Van Damme E.J., Totani K.,
RA Ito Y., Hirabayashi J.;
RT "Analysis of the sugar-binding specificity of mannose-binding-type Jacalin-
RT related lectins by frontal affinity chromatography--an approach to
RT functional classification.";
RL FEBS J. 275:1227-1239(2008).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=28748044; DOI=10.1080/20002297.2017.1345581;
RA Tawakoli P.N., Neu T.R., Busck M.M., Kuhlicke U., Schramm A., Attin T.,
RA Wiedemeier D.B., Schlafer S.;
RT "Visualizing the dental biofilm matrix by means of fluorescence lectin-
RT binding analysis.";
RL J. Oral Microbiol. 9:1345581-1345581(2017).
RN [7]
RP BIOTECHNOLOGY.
RX PubMed=32143591; DOI=10.1186/s12885-020-6699-5;
RA Takayama H., Ohta M., Iwashita Y., Uchida H., Shitomi Y., Yada K.,
RA Inomata M.;
RT "Altered glycosylation associated with dedifferentiation of hepatocellular
RT carcinoma: a lectin microarray-based study.";
RL BMC Cancer 20:192-192(2020).
RN [8] {ECO:0007744|PDB:1OUW}
RP X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 2-153, FUNCTION, SUBSTRATE
RP SPECIFICITY, SUBUNIT, TISSUE SPECIFICITY, ACETYLATION AT ALA-2, CIRCULAR
RP DICHROISM ANALYSIS, AND 3D-STRUCTURE MODELING IN COMPLEX WITH
RP CARBOHYDRATES.
RX PubMed=14561768; DOI=10.1074/jbc.m308218200;
RA Bourne Y., Roig-Zamboni V., Barre A., Peumans W.J., Astoul C.H.,
RA Van Damme E.J., Rouge P.;
RT "The crystal structure of the Calystegia sepium agglutinin reveals a novel
RT quaternary arrangement of lectin subunits with a beta-prism fold.";
RL J. Biol. Chem. 279:527-533(2004).
RN [9] {ECO:0007744|PDB:5AV7}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 3-153 IN COMPLEX WITH BISECTED
RP BIANTENNARY GLYCAN, FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=26971576; DOI=10.1038/srep22973;
RA Nagae M., Kanagawa M., Morita-Matsumoto K., Hanashima S., Kizuka Y.,
RA Taniguchi N., Yamaguchi Y.;
RT "Atomic visualization of a flipped-back conformation of bisected glycans
RT bound to specific lectins.";
RL Sci. Rep. 6:22973-22973(2016).
RN [10] {ECO:0007744|PDB:5XFI}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NON-BISECTED
RP BIANTENNARY GLYCAN, FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=28973127; DOI=10.1093/glycob/cwx081;
RA Nagae M., Mishra S.K., Hanashima S., Tateno H., Yamaguchi Y.;
RT "Distinct roles for each N-glycan branch interacting with mannose-binding
RT type Jacalin-related lectins Orysata and Calsepa.";
RL Glycobiology 27:1120-1133(2017).
CC -!- FUNCTION: Mannose-binding lectin (PubMed:9111143, PubMed:18266762,
CC PubMed:14561768, PubMed:26971576, PubMed:28973127). Preferentially
CC binds mannose at concentrations ranging between 5 and 25 mM, but binds
CC also glucose. Has a marked preference for methylated sugar derivatives,
CC such as alpha-MeMan and alpha-MeGlc, at concentration down to 5 mM
CC (PubMed:14561768). Binds to N-glycans, but not to glycolipid-type or
CC other type of glycans (PubMed:28973127). Binds N-linked high-mannose-
CC type glycans (PubMed:18266762, PubMed:28973127). Has a preference for
CC smaller (Man(2)-Man(6)) high-mannose-type glycans to larger (Man(7)-
CC Man(9)) ones. Recognizes both alpha1-6 extended and alpha1-3 extended
CC monoantennary glycans. The addition of alpha1-2Man to the Man-alpha1-
CC 3Man-beta branch results in a significant loss of affinity, but beta1-
CC 2GlcNAc has some affinity. Has less affinity for biantennary glycans
CC (PubMed:18266762). However, affinity is significant for the biantennary
CC complex-type N-glycans with bisecting GlcNAc (PubMed:18266762,
CC PubMed:26971576, PubMed:28973127). No affinity is observed for tri- and
CC tetra-antennary glycans (PubMed:18266762). Binds bisected glycans of
CC the mouse brain. Selectively binds to bisecting N-glycans which are in
CC back-fold conformation, and does not favor a glycan with an extend
CC conformation (PubMed:26971576). Has hemagglutinating activity against
CC rabbit erythrocytes at 0.3 ug/ml and against trypsin-treated human
CC erythrocytes at 5 ug/ml. Has mitogenic activity in murine cells
CC (PubMed:9111143). {ECO:0000269|PubMed:14561768,
CC ECO:0000269|PubMed:18266762, ECO:0000269|PubMed:26971576,
CC ECO:0000269|PubMed:28973127, ECO:0000269|PubMed:9111143}.
CC -!- ACTIVITY REGULATION: Hemagglutinating activity is most inhibited by
CC methyl alpha-mannopyranoside. This activity is inhibited to a less
CC extent (about a third of the inhibition of that of methyl alpha-
CC mannopyranoside) by methyl alpha-glucoside, other alpha-glucosides,
CC such as maltose, isomaltose, panose or palatinose, and alpha-glucosides
CC modified at the second position, such as methyl 2-deoxy-alpha-
CC arabinoglucopyranoside or methyl 2-acetamido-2-deoxy alpha-
CC glucopyranoside. Mildly inhibited by free monosaccharides, with glucose
CC presenting at least 20-fold less inhibitory effect on hemagglutinating
CC activity than mannose. Glycoproteins are somewhat inhibitory, the best
CC being asialothyroglobulin and ovomucoid. Not inhibited by isomaltitol,
CC sucrose or trehalose. {ECO:0000269|PubMed:9111143}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14561768,
CC ECO:0000269|PubMed:15299962, ECO:0000269|PubMed:9111143}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10908718}.
CC -!- TISSUE SPECIFICITY: Rhizome (at protein level) (PubMed:8955378,
CC PubMed:9111143, PubMed:15299962, PubMed:10908718, PubMed:14561768).
CC Detected in the cortex and the pith of rhizome. Not detected in
CC vascular tissues, pericycle, endodermis or rhizodermis
CC (PubMed:10908718). {ECO:0000269|PubMed:10908718,
CC ECO:0000269|PubMed:14561768, ECO:0000269|PubMed:15299962,
CC ECO:0000269|PubMed:8955378, ECO:0000269|PubMed:9111143}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:9111143}.
CC -!- MASS SPECTROMETRY: Mass=16092; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:8955378};
CC -!- BIOTECHNOLOGY: Can be used for the isolation of glycoproteins from
CC humans, plants and fungi. Is a powerful T-cell mitogen in the mouse,
CC and can thus be used as an alternative to concanavalin A for the
CC mitogenic proliferation of murine lymphocytes (PubMed:9111143).
CC Identified as one of the several suitable fluorescently labeled lectins
CC that can be used in a combination for the visualization and
CC quantification of extracellular glycoconjugates in dental supragingival
CC biofilms grown for 48 hours in situ in the absence of dietary
CC carbohydrates (PubMed:28748044). Used in lectin-based microarrays to
CC detect altered glycosylation in cancer tissue (PubMed:32143591).
CC {ECO:0000269|PubMed:28748044, ECO:0000269|PubMed:32143591,
CC ECO:0000269|PubMed:9111143}.
CC -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01088, ECO:0000305}.
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DR EMBL; U56820; AAC49564.1; -; mRNA.
DR PDB; 1OUW; X-ray; 1.37 A; A/B/C/D=2-153.
DR PDB; 5AV7; X-ray; 1.85 A; A/B/C/D=3-153.
DR PDB; 5XFI; X-ray; 1.65 A; A/B=1-153.
DR PDBsum; 1OUW; -.
DR PDBsum; 5AV7; -.
DR PDBsum; 5XFI; -.
DR AlphaFoldDB; P93114; -.
DR SMR; P93114; -.
DR UniLectin; P93114; -.
DR EvolutionaryTrace; P93114; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
DR CDD; cd09612; Jacalin; 1.
DR Gene3D; 2.100.10.30; -; 1.
DR InterPro; IPR001229; Jacalin-like_lectin_dom.
DR InterPro; IPR033734; Jacalin-like_lectin_dom_plant.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR Pfam; PF01419; Jacalin; 1.
DR SMART; SM00915; Jacalin; 1.
DR SUPFAM; SSF51101; SSF51101; 1.
DR PROSITE; PS51752; JACALIN_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Lectin.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..153
FT /note="Jacalin-related lectin Calsepa"
FT /evidence="ECO:0000305"
FT /id="PRO_0000450439"
FT DOMAIN 6..152
FT /note="Jacalin-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT REGION 17..18
FT /note="N-glycan binding"
FT /evidence="ECO:0000269|PubMed:26971576,
FT ECO:0000269|PubMed:28973127, ECO:0007744|PDB:5AV7,
FT ECO:0007744|PDB:5XFI"
FT REGION 95..96
FT /note="N-glycan binding"
FT /evidence="ECO:0000269|PubMed:26971576,
FT ECO:0000269|PubMed:28973127, ECO:0007744|PDB:5AV7,
FT ECO:0007744|PDB:5XFI"
FT REGION 140..144
FT /note="N-glycan binding"
FT /evidence="ECO:0000269|PubMed:26971576,
FT ECO:0000269|PubMed:28973127, ECO:0007744|PDB:5AV7,
FT ECO:0007744|PDB:5XFI"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:14561768,
FT ECO:0007744|PDB:1OUW"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1OUW"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1OUW"
FT STRAND 131..151
FT /evidence="ECO:0007829|PDB:1OUW"
SQ SEQUENCE 153 AA; 16063 MW; D94A5F2A8FED39AE CRC64;
MAVPMDTISG PWGNNGGNFW SFRPVNKINQ IVISYGGGGN NPIALTFSST KADGSKDTIT
VGGGGPDSIT GTEMVNIGTD EYLTGISGTF GIYLDNNVLR SITFTTNLKA HGPYGQKVGT
PFSSANVVGN EIVGFLGRSG YYVDAIGTYN RHK
