ID   LECA_CASCR              Reviewed;         309 AA.
AC   P82859;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Agglutinin;
DE   AltName: Full=CCA;
OS   Castanea crenata (Japanese chestnut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Fagaceae; Castanea.
OX   NCBI_TaxID=103480;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC   STRAIN=cv. Kunimi; TISSUE=Seed;
RX   PubMed=11006076; DOI=10.1006/bbrc.2000.3420;
RA   Nomura K., Nakamura S., Fujitake M., Nakanishi T.;
RT   "Complete amino acid sequence of Japanese chestnut agglutinin.";
RL   Biochem. Biophys. Res. Commun. 276:23-28(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cotyledon;
RX   PubMed=11820938; DOI=10.1093/oxfordjournals.jbchem.a003094;
RA   Nakamura S., Ikegami A., Matsumura Y., Nakanishi T., Nomura K.;
RT   "Molecular cloning and expression of the mannose/glucose specific lectin
RT   from Castanea crenata cotyledons.";
RL   J. Biochem. 131:241-246(2002).
RN   [3]
RP   FUNCTION.
RC   STRAIN=cv. Kunimi; TISSUE=Cotyledon;
RX   PubMed=9779592; DOI=10.1016/s0031-9422(97)00924-2;
RA   Nomura K., Ashida H., Uemura N., Kushibe S., Ozaki T., Yoshida M.;
RT   "Purification and characterization of a mannose/glucose-specific lectin
RT   from Castanea crenata.";
RL   Phytochemistry 49:667-673(1998).
RN   [4]
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).
CC   -!- FUNCTION: D-mannose/D-glucose-binding lectin (PubMed:9779592). Binds N-
CC       linked high-mannose-type glycans. Has a preference for smaller (Man(2)-
CC       Man(6)) high-mannose-type glycans to larger (Man(7)-Man(9)) ones.
CC       Recognizes both alpha1-6 extended and alpha1-3 extended monoantennary
CC       glycans. The addition of alpha1-2Man to the Man-alpha1-3Man-beta branch
CC       results in a significant loss of affinity, but beta1-2GlcNAc has some
CC       affinity. Has less affinity for biantennary glycans, and affinity is
CC       very weak for the biantennary complex-type N-glycans with bisecting
CC       GlcNAc. No affinity is observed for tri- and tetra-antennary glycans
CC       (PubMed:18266762). Has mitogenic and hemagglutinating activities
CC       (PubMed:9779592). {ECO:0000269|PubMed:18266762,
CC       ECO:0000269|PubMed:9779592}.
CC   -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01088, 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   EMBL; AF319617; AAG40322.1; -; mRNA.
DR   PIR; JC7806; JC7806.
DR   AlphaFoldDB; P82859; -.
DR   SMR; P82859; -.
DR   iPTMnet; P82859; -.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR   GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR   GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR   GO; GO:0030247; F:polysaccharide binding; IDA:UniProtKB.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
DR   CDD; cd09612; Jacalin; 2.
DR   Gene3D; 2.100.10.30; -; 2.
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; 2.
DR   SMART; SM00915; Jacalin; 2.
DR   SUPFAM; SSF51101; SSF51101; 2.
DR   PROSITE; PS51752; JACALIN_LECTIN; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Chitin-binding; Direct protein sequencing; Hemagglutinin;
KW   Lectin; Mannose-binding; Mitogen; Repeat.
FT   CHAIN           1..309
FT                   /note="Agglutinin"
FT                   /id="PRO_0000072802"
FT   DOMAIN          4..148
FT                   /note="Jacalin-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT   DOMAIN          163..308
FT                   /note="Jacalin-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:11006076"
SQ   SEQUENCE   309 AA;  33383 MW;  70B025197975319D CRC64;
     MEEFLTVGLW GGEGGDRWSF VVNNGGIIGM EIVHANGIAS ITFKCGDEYG VLQHSRKFGG
     TGEGWKTDKI SLNWPEEYLT SISGTVADLW QHIIIRSISF KTNKGTEYGP YGVVTGQPFS
     YSTEGGVIVG FHGRSGTLLD AIGAYVKIPQ KKDNTLKMAL PVPRGPGPWG GHGGMEWDDG
     VFPAIRELHL YVGDSVIHAI RVSYQSKDGE PLLSPKHGGE GGEPIDPIKL EVSKEFLIRI
     AGFYGPVEGS GSFKALRSIT FYTNKAKYGP YGDEIGQAFT SSVAPGRVVG FHGRSGAYLD
     AIGVHMEYF