The domain within your query sequence starts at position 9 and ends at position 553; the E-value for the Glypican domain shown below is 2.5e-238.

LLCTLAALSASLLAAELKSKSCSEVRRLYVSKGFNKNDAPLYEINGDHLKICPQDYTCCS
QEMEEKYSLQSKDDFKTVVSEQCNHLQAIFASRYKKFDEFFKELLENAEKSLNDMFVKTY
GHLYMQNSELFKDLFVELKRYYVAGNVNLEEMLNDFWARLLERMFRLVNSQYHFTDEYLE
CVSKYTEQLKPFGDVPRKLKLQVTRAFVAARTFAQGLAVARDVVSKVSVVNPTAQCTHAL
LKMIYCSHCRGLVTVKPCYNYCSNIMRGCLANQGDLDFEWNNFIDAMLMVAERLEGPFNI
ESVMDPIDVKISDAIMNMQDNSVQVSQKVFQGCGPPKPLPAGRISRSISESAFSARFRPY
HPEQRPTTAAGTSLDRLVTDVKEKLKQAKKFWSSLPSTVCNDERMAAGNENEDDCWNGKG
KSRYLFAVTGNGLANQGNNPEVQVDTSKPDILILRQIMALRVMTSKMKNAYNGNDVDFFD
ISDESSGEGSGSGCEYQQCPSEFEYNATDHSGKSANEKADSAGGAHAEAKPYLLAALCIL
FLAVQ

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:collagen-containing extracellular matrix (GO:0062023), anchored component of plasma membrane (GO:0046658)

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