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0PGBM_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameHSPG2
DescriptionBasement membrane-specific heparan sulfate proteoglycan core protein precursor (hspg) (perlecan) (plc).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains assigned to SynO:
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains.hich are critical for heparin-binding and cell attachment activity . Laminin alpha4 is distributed in a variety of tissues including peripheral nerves.orsal root ganglion.keletal muscle and capillaries; in the neuromuscular junction.t is required for synaptic specialisation . The structure of the laminin-G domain has been predicted to resemble that of pentraxin .Laminin G domains can vary in their function.nd a variety of binding functions have been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation. Proteins with laminin-G domains include:Laminin.Merosin.Agrin.Neurexins.Vitamin K dependent protein S.Sex steroid binding protein SBP/SHBG.Drosophila proteins Slit.rumbs.at.several proteoglycan precursors.
  IPR001791:Laminin G
InterPro domains unassigned to SynO:
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains.hich are critical for heparin-binding and cell attachment activity . Laminin alpha4 is distributed in a variety of tissues including peripheral nerves.orsal root ganglion.keletal muscle and capillaries; in the neuromuscular junction.t is required for synaptic specialisation . The structure of the laminin-G domain has been predicted to resemble that of pentraxin . Laminin G domains can vary in their function.nd a variety of binding functions have been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation. This entry represents one subtype of laminin G domains.hich is sometimes found in association with thrombospondin-type laminin G domains ().
  IPR012680:Laminin G, subdomain 2
Laminins represent a distinct family of extracellular matrix proteins present only in basement membranes in almost every animal tissue. They are heterotrimeric molecules composed of alpha.eta and gamma subunits (formerly A.1.nd B2.espectively ) and form a cruciform structure consisting of 3 short arms.ach formed by a different chain.nd a long arm composed of all 3 chains . Most of the globular domains of the short arms correspond to one of two different motifs.he 200-residue laminin N-terminal (domain VI) (LN) module and the 250-residue laminin domain IV (L4) module . All alpha chains share a unique C-terminal G domain which consists of five laminin G modules. The laminins can self-assemble.ind to other matrix macromolecules.nd have unique and shared cell interactions mediated by integrins.ystroglycan.nd other receptors. There are at least 14 laminin isoforms that regulate a variety of cellular functions including cell adhesion.igration.roliferation.ignaling and differentiation .The laminin B domain (also known as domain IV) is an extracellular module of unknown function. It is found in a number of different proteins that include.eparan sulphate proteoglycan from basement membrane. laminin-like protein from Caenorhabditis elegans and laminin. Laminin IV domain is not found in short laminin chains (alpha4 or beta3).
  IPR000034:Laminin B
Laminins are the major noncollagenous components of basement membranesthat mediate cell adhesion.rowth migration.nd differentiation. They arecomposed of distinct but related alpha.eta and gamma chains. The threechains form a cross-shaped molecule that consist of a long arm and three shortglobular arms. The long arm consist of a coiled coil structure contributed byall three chains and cross-linked by interchain disulphide bonds.Beside different types of globular domains each subunit contains.n its firsthalf.onsecutive repeats of about 60 amino acids in length that include eightconserved cysteines . The tertiary structure .f this domain isremotely similar in its N-terminal to that of the EGF-like module (see ). It is known as a LE or laminin-type EGF-like domain. Thenumber of copies of the LE domain in the different forms of laminins is highlyvariable; from 3 up to 22 copies have been found.A schematic representation of the topology of the four disulphide bonds inthe LE domain is shown below.In mouse laminin gamma-1 chain.he seventh LE domain has been shown to be theonly one that binds with a high affinity to nidogen . The binding-sites arelocated on the surface within the loops C1-C3 and C5-C6 . Longconsecutive arrays of LE domains in laminins form rod-like elements of limitedflexibility .hich determine the spacing in the formation of lamininnetworks of basement membranes .
  IPR002049:EGF-like, laminin
Low density lipoprotein (LDL) is the major cholesterol-carrying lipoprotein of plasma. The receptor protein binds LDL and transports it into cells by endocytosis. In order to be internalised.he receptor-ligand complex must first cluster into clathrin-coated pits. Seven successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein .The LDL-receptor class A domain contains 6 disulphide-bound cysteines and a highly conserved cluster of negatively charged amino acids.f which many are clustered on one face of the module . A schematic representation of this domain is shown here:In LDL-receptors the class A domains form the binding site for LDL and calcium . The acidic residues between the fourth and sixth cysteines are important for high-affinity binding of positively charged sequences in LDLRs ligands . The repeat has been shown to consist of a beta-hairpin structure followed by a series of beta turns. In the absence of calcium.DL-A domains are unstructured; the bound calcium ion imparts structural integrity.Following these repeats is a 350 residue domain that resembles part of the epidermal growth factor (EGF) precursor .Similar domains have been found (see references in ) in several extracellular and membrane proteins (see examples).Numerous familial hypercholestorolemia mutations of the LDL receptor alter the calcium coordinating residue of LDL-A domains or other crucial scaffolding residues.
  IPR002172:Low density lipoprotein-receptor, class A
SEA is an extracellular domain associated with O-glycosylation .Proteins found to contain SEA-modules include.grin.nterokinase.3 kDa sea urchin (Strongylocentrotus purpuratus) sperm protein.erlecan (heparan sulphate proteoglycan core.ucin 1 and the cell surface antigen.14/A10.nd two functionally uncharacterised.robably extracellular.aenorhabditis elegans proteins. Despite the functional diversity of these adhesive proteins. common denominator seems to be their existence in heavily glycosylated environments. In addition.he better characterised proteins all contain O-glycosidic-linked carbohydrates such as heparan sulphate that contribute considerably to their molecular masses. The common module might regulate or assist binding to neighbouring carbohydrate moieties.Enterokinase.he initiator of intestinal digestion.s a mosaic protease composed of a distinctive assortment of domains .
  IPR000082:SEA
This entry is for immunoglobulin-like domains. Studies indicate that the interactions essential for defining the structure of these beta sandwich proteins are also important in nucleation of folding.nd that proteins containing this fold may share similar folding pathways even though the proteins may have low sequence homology. The fold consists of a beta-sandwich formed of 7 strands in 2 sheets with a Greek-key topology. Some members of the fold have additional strands. The Pfam alignments do not include the first and last strand of the immunoglobulin-like domain.
  IPR013151:Immunoglobulin
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents a subtype of the immunoglobulin domain.nd is found in a diverse range of protein families that includes glycoproteins.ibroblast growth factor receptors.ascular endothelial growth factor receptors.nterleukin-6 receptor.nd neural cell adhesion molecules. It also includes proteins that are classified as unassigned proteinase inhibitors belonging to MEROPS inhibitor families I2.17 and I43 .
  IPR003598:Immunoglobulin subtype 2
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents I-set domains.hich are found in several cell adhesion molecules.ncluding vascular (VCAM).ntercellular (ICAM).eural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules.s well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families.ncluding several tyrosine-protein kinase receptors.he hemolymph protein hemolin.he muscle proteins titin.elokin.nd twitchin.he neuronal adhesion molecule axonin-1 .nd the signalling molecule semaphorin 4D that is involved in axonal guidance.mmune function and angiogenesis .
  IPR013098:Immunoglobulin I-set
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents the V-set domains.hich are Ig-like domains resembling the antibody variable domain. V-set domains are found in diverse protein families.ncluding immunoglobulin light and heavy chains; in several T-cell receptors such as CD2 (Cluster of Differentiation 2).D4.D80.nd CD86; in myelin membrane adhesion molecules; in junction adhesion molecules (JAM); in tyrosine-protein kinase receptors; and in the programmed cell death protein 1 (PD1).
  IPR013106:Immunoglobulin V-set
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases and xylanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . Xylanase and cellobiohydrolase I degrade hemicellulose and cellulose.espectively . There are many Con A-like domains found in proteins involved in cell recognition and adhesion. For example.everal viral and bacterial toxins carry Con A-like domains. Examples include the Clostridium neurotoxins responsible for the neuroparalytic effects of botulism and tetanus . The Pseudomonas exotoxin A. virulence factor which is highly toxic to eukaryotic cells.ausing the arrest of protein synthesis.ontains a Con A-like domain involved in receptor binding . Cholerae neuraminidase can bind to cell surfaces.ossibly through their Con A-like domains.here they function as part of a mucinase complex to degrade the mucin layer of the gastrointestinal tract . The rotaviral outer capsid protein.P4.as a Con A-like sialic acid binding domain.hich functions in cell attachment and membrane penetration . Con A-like domains also play a role in cell recognition in eukaryotes. Proteins containing a Con A-like domain include the sex hormone-binding globulins which transport sex steroids in blood and regulate their access to target tissues .aminins which are large heterotrimeric glycoproteins involved in basement membrane architecture and function .eurexins which are expressed in hundreds of isoforms on the neuronal cell surface.here they may function as cell recognition molecules and sialidases that are found in both microorganisms and animals.nd function in cell adhesion and signal transduction . Other proteins containing a Con A-like domain include pentraxins and calnexins. The pentraxin PTX3 is a TNFalpha-induced.ecreted protein of adipose cells produced during inflammation . The calnexin family of molecular chaperones is conserved among plants.ungi.nd animals. Family members include Calnexin. type-I integral membrane protein in the endoplasmic reticulum which coordinates the processing of newly synthesized N-linked glycoproteins with their productive folding.almegin. type-I membrane protein expressed mainly in the spermatids of the testis.nd calreticulin. soluble ER lumenal paralog .
  IPR008985:Concanavalin A-like lectin/glucanase
The growth factor receptor domain is a cysteine-rich region that is found in a variety of eukaryotic proteins that are involved in the mechanism of signal transduction by receptor tyrosine kinases. Proteins containing the growth factor receptor domain include the insulin-like growth factor-binding proteins (IGFBP) .he type-1 insulin-like growth-factor receptor (IGF-1R) .nd the receptor protein-tyrosine kinase Erbb-3 (ErbB3) . The general structure of the growth factor receptor domain is a disulphide-bound fold containing a beta-hairpin with two adjacent disulphides. IGFBPs control the distribution.unction and activity of insulin-like growth factors (IGFs) IGF-I and IGF-II.hich are key regulators of cell proliferation.ifferentiation and transformation. All IGFBPs share a common domain organization.here the highest conservation is found in the N-terminal Cys-rich IGF-binding domain. The N-terminal domain contains 10-12 conserved cysteine residues. IGF-1R is a member of the tyrosine-kinase receptor superfamily that is involved in both normal growth and development and malignant transformation. The Cys-rich domain is flanked by two L-domains.nd together they contribute to hormone binding and ligand specificity.ven though they do not bind ligand directly. The Cys-rich region is composed of eight disulphide-bonded modules.even of which form a rod-shaped domain. ErbB3 is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. The extracellular region of ErbB3 is made up of two Cys-rich domains and two L-domains.rranged alternately. The two L-domains and the first Cys-rich domain are structurally homologous to those found in IGF-1R. The two Cys-rich domains are extended repeats of seven small disulphide-containing modules. A beta-hairpin loop extends from the first Cys-rich domain to contact the C-terminal portion of the second Cys-rich domain.reating a large pore structure. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009030:Growth factor, receptor
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . This entry differs from () by omitting the xylanases and glycosyl hydrolases.
  IPR013320:Concanavalin A-like lectin/glucanase, subgroup
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR000034:LamB 
Evalue:-63.4685210829577 
Location:1391-1516IPR000034:LamB 
Evalue:-60.2596373105057 
Location:985-1112IPR000034:LamB 
Evalue:-55.2518119729938 
Location:590-717IPR012680:Laminin_G_2 
Evalue:-43.1307678222656 
Location:4234-4364IPR012680:Laminin_G_2 
Evalue:-42.0087738037109 
Location:3957-4085IPR012680:Laminin_G_2 
Evalue:-39.5686378479004 
Location:3692-3828IPR000082:SEA 
Evalue:-25.431798275933 
Location:80-194IPR013098:I-set 
Evalue:-18.3187580108643 
Location:3299-3382IPR002049:Laminin_EGF 
Evalue:-18.2596378326416 
Location:764-811IPR002049:Laminin_EGF 
Evalue:-18.1307678222656 
Location:1159-1206IPR002172:Ldl_recept_a 
Evalue:-16.5686359405518 
Location:323-359IPR002049:Laminin_EGF 
Evalue:-16.4685211181641 
Location:1563-1610IPR013098:I-set 
Evalue:-16.4559326171875 
Location:3212-3295IPR003598:IGc2 
Evalue:-15.9208187539524 
Location:2063-2124IPR002172:Ldl_recept_a 
Evalue:-15.9208183288574 
Location:283-319IPR013098:I-set 
Evalue:-15.8538722991943 
Location:1956-2042IPR013098:I-set 
Evalue:-15.5376024246216 
Location:2437-2520IPR003598:IGc2 
Evalue:-15.4948500216801 
Location:3501-3562IPR002049:Laminin_EGF 
Evalue:-14.6777811050415 
Location:1275-1322IPR002172:Ldl_recept_a 
Evalue:-14.5528421401978 
Location:197-234IPR013098:I-set 
Evalue:-14.3372421264648 
Location:3576-3658IPR003598:IGc2 
Evalue:-14.0457574905607 
Location:2642-2703IPR013098:I-set 
Evalue:-13.958607673645 
Location:1866-1950IPR013098:I-set 
Evalue:-13.5850267410278 
Location:2827-2910IPR002172:Ldl_recept_a 
Evalue:-12.4202165603638 
Location:366-403IPR013098:I-set 
Evalue:-12.1549015045166 
Location:2245-2325IPR013098:I-set 
Evalue:-12 
Location:1677-1763IPR013151:ig 
Evalue:-11.958607673645 
Location:2166-2220IPR003598:IGc2 
Evalue:-11.9208187539524 
Location:419-486IPR013151:ig 
Evalue:-11.7447271347046 
Location:2741-2795IPR003598:IGc2 
Evalue:-11.3565473235138 
Location:2937-2998IPR003598:IGc2 
Evalue:-11.3467874862247 
Location:2546-2607IPR013151:ig 
Evalue:-10.6382722854614 
Location:2355-2409IPR006209:EGF 
Evalue:-10.1739253997803 
Location:3848-3880IPR003598:IGc2 
Evalue:-10.0457574905607 
Location:3125-3192IPR003598:IGc2 
Evalue:-9.92081875395237 
Location:1784-1847IPR013098:I-set 
Evalue:-9.79588031768799 
Location:3022-3108IPR002049:Laminin_EGF 
Evalue:-9.58502674102783 
Location:814-869IPR002049:Laminin_EGF 
Evalue:-8.11350917816162 
Location:1209-1263IPR006209:EGF 
Evalue:-7.92081880569458 
Location:4108-4140IPR013151:ig 
Evalue:-7.76955127716064 
Location:3414-3468IPR002049:Laminin_EGF 
Evalue:-7.23657178878784 
Location:1613-1668IPR002049:Laminin_EGF 
Evalue:-6.35654735565186 
Location:891-921IPR006209:EGF 
Evalue:-6.19381999969482 
Location:4147-4175IPR006209:EGF 
Evalue:-5.50863838195801 
Location:3888-3921IPR009030:Grow_fac_recept 
Evalue:0 
Location:1324-1352IPR013032:EGF_2 
Evalue:0 
Location:731-745IPR013032:EGF_2 
Evalue:0 
Location:1530-1544IPR013032:EGF_2 
Evalue:0 
Location:1126-1140IPR008985:ConA_like_lec_gl 
Evalue:0 
Location:29-35
SequencesProtein: PGBM_HUMAN (4391 aa)
mRNA: NM_005529 X62515
Local Annotation
Synapse Ontology
A neuromuscular junction is the junction of the axon terminal of a motoneuron with the motor end plate, the highly-excitable region of muscle fiber plasma membrane responsible for initiation of action potentials across the muscle's surface.
sdb:0024 neuromuscular junction  (Evidence:keywords,domains)
A typical resting membrane potential for neurons varies from -65 to -90 mV. This potential represents the sum of the equilibrium potentials for each contributing ion.
sdb:0237 resting membrane potentiaion  (Evidence:keywords,domains)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords,domains)
KO assignmentK06255
  Level 3 annotation:
    heparan sulfate proteoglycan 2 (perlecan)
  Level 2 annotation:
    Proteoglycans
    ECM-receptor interaction
    CAM ligands
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 415 residues, 22021324-22022568Exon2: 36 residues, 22022695-22022799Exon3: 30 residues, 22023200-22023284Exon4: 25 residues, 22023385-22023456Exon5: 28 residues, 22023616-22023695Exon6: 27 residues, 22023783-22023859Exon7: 21 residues, 22026942-22026999Exon8: 43 residues, 22027109-22027232Exon9: 59 residues, 22027334-22027506Exon10: 83 residues, 22027914-22028159Exon11: 76 residues, 22028462-22028684Exon12: 35 residues, 22029072-22029171Exon13: 38 residues, 22030061-22030170Exon14: 38 residues, 22030294-22030404Exon15: 35 residues, 22030542-22030642Exon16: 50 residues, 22030731-22030876Exon17: 39 residues, 22031574-22031686Exon18: 41 residues, 22032347-22032464Exon19: 51 residues, 22032546-22032694Exon20: 38 residues, 22032895-22033005Exon21: 91 residues, 22033758-22034025Exon22: 34 residues, 22034619-22034717Exon23: 70 residues, 22035881-22036086Exon24: 89 residues, 22037904-22038165Exon25: 62 residues, 22038450-22038630Exon26: 67 residues, 22038901-22039097Exon27: 63 residues, 22040180-22040365Exon28: 47 residues, 22040618-22040753Exon29: 49 residues, 22041081-22041222Exon30: 49 residues, 22041318-22041460Exon31: 52 residues, 22041849-22042001Exon32: 49 residues, 22042376-22042518Exon33: 52 residues, 22043227-22043379Exon34: 51 residues, 22045187-22045335Exon35: 52 residues, 22045527-22045679Exon36: 48 residues, 22046433-22046572Exon37: 52 residues, 22046768-22046920Exon38: 47 residues, 22047037-22047173Exon39: 52 residues, 22047722-22047874Exon40: 48 residues, 22047972-22048111Exon41: 52 residues, 22049120-22049272Exon42: 47 residues, 22049442-22049578Exon43: 52 residues, 22050625-22050777Exon44: 47 residues, 22050870-22051006Exon45: 50 residues, 22051167-22051313Exon46: 46 residues, 22051779-22051912Exon47: 52 residues, 22051998-22052150Exon48: 52 residues, 22053272-22053423Exon49: 53 residues, 22053690-22053845Exon50: 47 residues, 22053927-22054063Exon51: 49 residues, 22054383-22054526Exon52: 53 residues, 22054602-22054755Exon53: 44 residues, 22054866-22054992Exon54: 62 residues, 22056094-22056275Exon55: 35 residues, 22056364-22056465Exon56: 39 residues, 22058645-22058756Exon57: 58 residues, 22058914-22059082Exon58: 21 residues, 22059256-22059315Exon59: 31 residues, 22060836-22060923Exon60: 44 residues, 22061067-22061195Exon61: 40 residues, 22063179-22063293Exon62: 79 residues, 22063922-22064153Exon63: 29 residues, 22064364-22064445Exon64: 33 residues, 22064796-22064889Exon65: 66 residues, 22071265-22071457Exon66: 49 residues, 22071699-22071840Exon67: 33 residues, 22072076-22072171Exon68: 18 residues, 22072454-22072504Exon69: 31 residues, 22073004-22073091Exon70: 44 residues, 22073485-22073613Exon71: 40 residues, 22073695-22073809Exon72: 39 residues, 22073970-22074082Exon73: 41 residues, 22074708-22074827Exon74: 62 residues, 22074942-22075122Exon75: 61 residues, 22075308-22075485Exon76: 49 residues, 22075591-22075732Exon77: 24 residues, 22077265-22077333Exon78: 21 residues, 22077512-22077571Exon79: 31 residues, 22077656-22077743Exon80: 44 residues, 22078073-22078201Exon81: 51 residues, 22079186-22079334Exon82: 67 residues, 22079442-22079639Exon83: 62 residues, 22079735-22079915Exon84: 56 residues, 22080418-22080582Exon85: 51 residues, 22083607-22083754Exon86: 52 residues, 22083846-22083998Exon87: 50 residues, 22084092-22084237Exon88: 46 residues, 22084399-22084531Exon89: 42 residues, 22086294-22086414Exon90: 87 residues, 22086499-22086754Exon91: 45 residues, 22087017-22087146Exon92: 55 residues, 22089060-22089221Exon93: 21 residues, 22089506-22089565Exon94: 38 residues, 22089664-22089774Exon95: 17 residues, 22095001-22095046Exon96: 47 residues, 22095254-22095390Exon97: 35 residues, 22136234-22136334Exon98: 2 residues, -Jump to PGBM_HUMANExon1: 248 residues, 22021826-22022568Exon2: 36 residues, 22022695-22022799Exon3: 30 residues, 22023200-22023284Exon4: 25 residues, 22023385-22023456Exon5: 28 residues, 22023616-22023695Exon6: 27 residues, 22023783-22023859Exon7: 21 residues, 22026942-22026999Exon8: 43 residues, 22027109-22027232Exon9: 59 residues, 22027334-22027506Exon10: 83 residues, 22027914-22028159Exon11: 76 residues, 22028462-22028684Exon12: 35 residues, 22029072-22029171Exon13: 38 residues, 22030061-22030170Exon14: 38 residues, 22030294-22030404Exon15: 35 residues, 22030542-22030642Exon16: 50 residues, 22030731-22030876Exon17: 39 residues, 22031574-22031686Exon18: 41 residues, 22032347-22032464Exon19: 51 residues, 22032546-22032694Exon20: 38 residues, 22032895-22033005Exon21: 91 residues, 22033758-22034025Exon22: 34 residues, 22034619-22034717Exon23: 70 residues, 22035881-22036086Exon24: 89 residues, 22037904-22038165Exon25: 62 residues, 22038450-22038630Exon26: 67 residues, 22038901-22039097Exon27: 63 residues, 22040180-22040365Exon28: 47 residues, 22040618-22040753Exon29: 49 residues, 22041081-22041222Exon30: 49 residues, 22041318-22041460Exon31: 52 residues, 22041849-22042001Exon32: 49 residues, 22042376-22042518Exon33: 52 residues, 22043227-22043379Exon34: 51 residues, 22045187-22045335Exon35: 52 residues, 22045527-22045679Exon36: 48 residues, 22046433-22046572Exon37: 52 residues, 22046768-22046920Exon38: 47 residues, 22047037-22047173Exon39: 52 residues, 22047722-22047874Exon40: 48 residues, 22047972-22048111Exon41: 52 residues, 22049120-22049272Exon42: 47 residues, 22049442-22049578Exon43: 52 residues, 22050625-22050777Exon44: 47 residues, 22050870-22051006Exon45: 50 residues, 22051167-22051313Exon46: 46 residues, 22051779-22051912Exon47: 52 residues, 22051998-22052150Exon48: 52 residues, 22053272-22053423Exon49: 53 residues, 22053690-22053845Exon50: 47 residues, 22053927-22054063Exon51: 49 residues, 22054383-22054526Exon52: 53 residues, 22054602-22054755Exon53: 44 residues, 22054866-22054992Exon54: 62 residues, 22056094-22056275Exon55: 35 residues, 22056364-22056465Exon56: 39 residues, 22058645-22058756Exon57: 58 residues, 22058914-22059082Exon58: 21 residues, 22059256-22059315Exon59: 31 residues, 22060836-22060923Exon60: 44 residues, 22061067-22061195Exon61: 40 residues, 22063179-22063293Exon62: 79 residues, 22063922-22064153Exon63: 29 residues, 22064364-22064445Exon64: 33 residues, 22064796-22064889Exon65: 66 residues, 22071265-22071457Exon66: 49 residues, 22071699-22071840Exon67: 33 residues, 22072076-22072171Exon68: 18 residues, 22072454-22072504Exon69: 31 residues, 22073004-22073091Exon70: 44 residues, 22073485-22073613Exon71: 40 residues, 22073695-22073809Exon72: 39 residues, 22073970-22074082Exon73: 41 residues, 22074708-22074827Exon74: 62 residues, 22074942-22075122Exon75: 61 residues, 22075308-22075485Exon76: 49 residues, 22075591-22075732Exon77: 24 residues, 22077265-22077333Exon78: 21 residues, 22077512-22077571Exon79: 31 residues, 22077656-22077743Exon80: 44 residues, 22078073-22078201Exon81: 51 residues, 22079186-22079334Exon82: 67 residues, 22079442-22079639Exon83: 62 residues, 22079735-22079915Exon84: 56 residues, 22080418-22080582Exon85: 52 residues, 22083607-22083757Exon86: 52 residues, 22083846-22083998Exon87: 50 residues, 22084092-22084237Exon88: 46 residues, 22084399-22084531Exon89: 42 residues, 22086294-22086414Exon90: 87 residues, 22086499-22086754Exon91: 45 residues, 22087017-22087146Exon92: 55 residues, 22089060-22089221Exon93: 21 residues, 22089506-22089565Exon94: 38 residues, 22089664-22089774Exon95: 17 residues, 22095001-22095046Exon96: 47 residues, 22095254-22095390Exon97: 35 residues, 22136234-22136334Exon98: 2 residues, -Jump to PGBM_HUMAN  
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Loci Cluster (Details)Loci: 2488 22251768-22289571 ~-38K 631(CDC42)(+)Loci: 3778 22021324-22136334 ~-115K 626(HSPG2)(-)Link out to UCSC