The domain within your query sequence starts at position 11 and ends at position 566; the E-value for the Glypican domain shown below is 3.1e-199.

LLHLCPGLGPGHGSEAKVVRSCAETRQVLGARGYSLNLIPPSLISGEHLQVCPQEYTCCS
SETEQKLIRDAEVTFRGLVEDSGSFLIHTLAARHRKFNEFFREMLSISQHSLAQLFSHSY
GRLYSQHAVIFNSLFSGLRDYYEKSGEGLDDTLADFWAQLLERAFPLLHPQYSFPPDFLL
CLTRLTSTADGSLQPFGDSPRRLRLQISRALVAARALVQGLETGRNVVSEALKVPVLEGC
RQALMRLIGCPLCRGVPSLMPCRGFCLNVAHGCLSSRGLEPEWGGYLDGLLLLAEKLQGP
FSFELAAESIGVKISEGLMHLQENSVKVSAKVFQECGTPHPVQSRSRRAPAPREEASRSW
RASAEEERPTTAAGTNLHRLVWELRERLSRVRGFWAGLPVTVCGDSRMAADLSQETAPCW
TGVGRGRYMSPVVVGSLNEQLHNPELDTSSPDVPTRRRRLHLRAATARMKAAALGQDLDM
HDADEDASGSGGGQQYADDWKAGAVPVVPPARPPRPPRPPRRDGLGVRGGSGSARYNQGR
SRNLGSSVGLHTPLVL

Glypican

Glypican
PFAM accession number:PF01153
Interpro abstract (IPR001863):

Glypicans [ (PUBMED:8589707) (PUBMED:7657705) ] are a family of heparan sulphate proteoglycans which are anchored to cell membranes by a glycosylphosphatidylinositol (GPI) linkage. Six members (GPC1-6) are known in vertebrates [ (PUBMED:11474185) ]. The main function of glypicans is to regulate several signaling pathways, including those of Wnts, Hedgehogs, fibroblast growth factors and bone morphogenetic proteins (BMPs) [ (PUBMED:18505598) (PUBMED:24412155) ].

Structurally, these proteins consist of three separate domains:

  • A signal sequence;
  • An extracellular domain of about 500 residues that contains 12 conserved cysteines probably involved in disulphide bonds and which also contains the sites of attachment of the heparan sulphate glycosaminoglycan side chains;
  • A C-terminal hydrophobic region which is post-translationally removed after formation of the GPI-anchor.
GO process:regulation of signal transduction (GO:0009966)
GO component:anchored component of plasma membrane (GO:0046658), collagen-containing extracellular matrix (GO:0062023)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Glypican