{PDOC51752}
{PS51752; JACALIN_LECTIN}
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* Jacalin-type lectin domain profile *
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Lectins, a  well-known class of carbohydrate-binding proteins, are known to be
important in  a  variety  of  biological  processes,  mediated  through  their
carbohydrate specificities. Plant lectins are broadly divided into six classes
based on  their  subunit  folds.  These  are legume lectins (see <PDOC00278>),
jacalin-related lectins   (JRLs),   monocot   mannose-binding   lectins   (see
<PDOC50927>), trefoil lectins, cyanovirin-N lectin, and hevein domain lectins.
JRLs derive  their  name  from jacalin, the first member to be identified from
the seed of jackfruit. Based on the known sugar specificities, lectins in this
family can  be  broadly  divided  into two classes: (1) the galactose-specific
lectins and (2) the mannose/glucose-specific lectins [1,2,3,4,5].

The ~135-150  amino  acid  residue  jacalin-type  lectin domain adopts a beta-
prism-I fold  comprised  of  three Greek keys (four stranded beta-sheets) (see
<PDB:3APA>) [4].

Some proteins known to contain a jacalin-type lectin domain are listed below:

 - Artocarpus integrifolia (jackfruit) jacalin.
 - Artocarpus ntegrifolia (jackfruit) artocarpin.
 - Morus nigra (black mulberry) mornigaG and mornigaM.
 - Ipomoea batatas (sweet potato) ipomoelin (IPO).
 - Musa acuminata (banana) lectin BanLec.
 - Helianthus tuberosus (Jerusalem artichoke) Heltuba.
 - Griffithsia sp. griffithsin.
 - Mammalian  zymogen  granule  membrane protein 16 (ZG16) and zymogen granule
   protein 16 homolog B (ZG16b).

The profile we developed covers the entire jacalin-type lectin domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: March 2015 / First entry.

[ 1] Raval S., Gowda S.B., Singh D.D., Chandra N.R.
     "A database analysis of jacalin-like lectins:
     sequence-structure-function relationships."
     Glycobiology 14:1247-1263(2004).
     PubMed=15329359; DOI=10.1093/glycob/cwh140
[ 2] Rabijns A., Barre A., Van Damme E.J.M., Peumans W.J., De Ranter C.J.,
     Rouge P.
     "Structural analysis of the jacalin-related lectin MornigaM from the
     black mulberry (Morus nigra) in complex with mannose."
     FEBS J. 272:3725-3732(2005).
     PubMed=16008570; DOI=10.1111/j.1742-4658.2005.04801.x
[ 3] Gallego del Sol F., Nagano C., Cavada B.S., Calvete J.J.
     "The first crystal structure of a Mimosoideae lectin reveals a novel
     quaternary arrangement of a widespread domain."
     J. Mol. Biol. 353:574-583(2005).
     PubMed=16185708; DOI=10.1016/j.jmb.2005.08.055
[ 4] Kanagawa M., Satoh T., Ikeda A., Nakano Y., Yagi H., Kato K.,
     Kojima-Aikawa K., Yamaguchi Y.
     "Crystal structures of human secretory proteins ZG16p and ZG16b reveal
     a Jacalin-related beta-prism fold."
     Biochem. Biophys. Res. Commun. 404:201-205(2011).
     PubMed=21110947; DOI=10.1016/j.bbrc.2010.11.093
[ 5] Chang W.-C., Liu K.-L., Hsu F.-C., Jeng S.-T., Cheng Y.-S.
     "Ipomoelin, a jacalin-related lectin with a compact tetrameric
     association and versatile carbohydrate binding properties regulated by
     its N terminus."
     PLoS ONE 7:E40618-E40618(2012).
     PubMed=22808208; DOI=10.1371/journal.pone.0040618

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