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basement membrane-specific heparan sulfate proteoglycan core protein; HSPG; perlecan; PLC (HSPG2)

Function: - integral component of basement membranes - responsible for the fixed negative electrostatic charge of basement membrane - role in the charge-selective ultrafiltration properties of basement membrane - serves as an attachment substrate for cells N-glycosylated & O-glycosylated - purified perlecan has a strong tendency to aggregate in dimers or stellate structures - interacts with other basement membrane components such as laminin, prolargin & collagen typ-4 - interacts with COL13A1, FGFBP1 & VWA1 Structure: - contains three heparan sulfate chains - contains 4 EGF-like domains - contains 22 Ig-like C2-type domain (immunoglobulin-like) - contains 11 laminin EGF-like domains - contains 3 laminin G-like domains - contains 3 laminin IV type A domains - contains 4 LDL-receptor class A domains - contains 1 SEA domain Compartment: - secreted, extracellular space - extracellular matrix, basement membrane Expression: found in the basement membranes Pathology: - defects in HSPG2 are the cause of a) Schwartz-Jampel syndrome b) dyssegmental dysplasia Silverman-Handmaker type

Related

HSPG2 gene

General

matrix protein proteoglycan core protein

Properties

SIZE: entity length = 4391 aa MW = 469 kD COMPARTMENT: extracellular matrix MOTIF: signal sequence {1-21} Ser glycosylation site {S65} Ser glycosylation site {S71} Ser glycosylation site {S76} SEA domain {80-194} MOTIF: N-glycosylation site {N89} LDL-receptor class A {198-404} (4) MOTIF: cysteine residue {C199} MODIFICATION: cysteine residue {C212} cysteine residue {C206} MODIFICATION: cysteine residue {C225} cysteine residue {C212} MODIFICATION: cysteine residue {C199} cysteine residue {C219} MODIFICATION: cysteine residue {C234} cysteine residue {C225} MODIFICATION: cysteine residue {C206} cysteine residue {C234} MODIFICATION: cysteine residue {C219} immunoglobulin superfamily domain {405-3662} (22) EGF domain {521-4176} (15) MOTIF: cysteine residue {C814} MODIFICATION: cysteine residue {C829} cysteine residue {C816} MODIFICATION: cysteine residue {C839} cysteine residue {C829} MODIFICATION: cysteine residue {C814} cysteine residue {C839} MODIFICATION: cysteine residue {C816} cysteine residue {C842} MODIFICATION: cysteine residue {C851} cysteine residue {C851} MODIFICATION: cysteine residue {C842} cysteine residue {C854} MODIFICATION: cysteine residue {C869} cysteine residue {C869} MODIFICATION: cysteine residue {C854} Laminin IV type A {538-1529} (3) MOTIF: N-glycosylation site {N554} Laminin G-like {3663-4389} (3) MOTIF: N-glycosylation site {N3780} cysteine residue {C3819} MODIFICATION: cysteine residue {C3845} N-glycosylation site {N3836} cysteine residue {C3845} MODIFICATION: cysteine residue {C3819} Ser glycosylation site {S4179}

Database Correlations

OMIM correlations UniProt P98160 PFAM correlations Entrez Gene 3339 Kegg hsa:3339

References

  1. UniProt :accession P98160
  2. Atlas of Genetics & Cytogenetics in Oncology & Haematology http://atlasgeneticsoncology.org//genes/HSPG2ID40890ch1p36.html
  3. Wikipedia; Note: perlecan entry http://en.wikipedia.org/wiki/perlecan
  4. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=HSPG2
  5. Ruoslahti E, Yamaguchi Y. Proteoglycans as modulators of growth factor activities. Cell. 1991 Mar 8;64(5):867-9. Review. PMID: 2001586
  6. Noonan DM, Fulle A, Valente P, Cai S, Horigan E, Sasaki M, Yamada Y, Hassell JR. The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule. J Biol Chem. 1991 Dec 5;266(34):22939-47. PMID: 1744087