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0CNTP4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCNTNAP4
DescriptionContactin-associated protein-like 4 precursor (cell recognition molecule caspr4).
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:
Blood coagulation factors V and VIII contain a C-terminal.wice repeated.omain of about 150 amino acids.hich is called F5/8 type C.A58C.r C1/C2-like domain. In the slime mold cell adhesion protein discoidin. relateddomain.amed discoidin I-like domain.LD.r DS.as been found which sharesa common C-terminal region of about 110 amino acids with the FA58C domain.utwhose N-terminal 40 amino acids are much less conserved. Similar domains havebeen detected in other extracellular and membrane proteins In coagulation factors V and VIII the repeated domains compose part of alarger functional domain which promotes binding to anionic phospholipids onthe surface of platelets and endothelial cells . The C-terminal domain ofthe second FA58C repeat (C2) of coagulation factor VIII has been shown to beresponsible for phosphatidylserine-binding and essential for activity .It forms an amphipathic alpha-helix.hich binds to the membrane .FA58C contains two conserved cysteines in most proteins.hich link theextremities of the domain by a disulphide bond . A further disulphidebond is located near the C-terminal of the second FA58C domain in MFGM .
  IPR000421:Coagulation factor 5/8 type, C-terminal
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
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
Fibrinogen plays key roles in both blood clotting and platelet aggregation. During blood clot formation.he conversion of soluble fibrinogen to insoluble fibrin is triggered by thrombin.esulting in the polymerisation of fibrin.hich forms a soft clot; this is then converted to a hard clot by factor XIIIA.hich further cross-links fibrin molecules. Platelet aggregation involves the binding of the platelet protein receptor integrin alpha(IIb)-beta(3) to the C-terminal domain of the fibrinogen gamma chain.ediating a range of adhesive reactions that include adhesion.latelet aggregation and fibrin clot retraction .Fibrinogen occurs as a dimer.here each monomer is composed of three non-identical chains.lpha.eta and gamma.inked together by several disulphide bonds . The N-terminals of all six chains come together to form the centre of the molecule.rom which the monomers extend in opposite directions as coiled coils.ollowed by C-terminal globular domains. The C-terminal globular domains are referred to as the D regions.hile the coiled-coil and N-terminal central region are referred to as the E region. During clot formation.he N-terminal alpha and beta chains are cleaved.nabling them to bind to the C-terminal gamma and beta chains.espectively.f adjacent molecules.ausing the proteins to polymerise .This entry represents the C-terminal globular domains (D region) of the alpha.eta and gamma chains. These domains are related to domains in other proteins: in the sea cucumber fibrogen-like FreP-A and FreP-B proteins; in the C-terminus of Drosophila scabrous protein that is involved in the regulation of neurogenesis.ossibly through the inhibition of R8 cell differentiation; and in ficolin proteins.hich display lectin activity towards N-acetylglucosamine through their fibrogen-like domains .
  IPR002181:Fibrinogen, alpha/beta/gamma chain, C-terminal globular
Proteins containing a galactose-binding domain-like fold can be found in several different protein families.n both eukaryotes and prokaryotes. The common function of these domains is to bind to specific ligands.uch as cell-surface-attached carbohydrate substrates for galactose oxidase and sialidase .hospholipids on the outer side of the mammalian cell membrane for coagulation factor Va .embrane-anchored ephrin for the Eph family of receptor tyrosine kinases .nd a complex of broken single-stranded DNA and DNA polymerase beta for XRCC1 . The structure of the galactose-binding domain-like members consists of a beta-sandwich.n which the strands making up the sheets exhibit a jellyroll fold. There is a high degree of similarity in the beta-sandwich and in the loops between different family members.espite an often low level of sequence similarity.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008979:Galactose-binding like
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
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
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
IPR000421:F5_F8_type_C 
Evalue:-38.4948501586914 
Location:43-174IPR012680:Laminin_G_2 
Evalue:-35.3872146606445 
Location:821-940IPR012680:Laminin_G_2 
Evalue:-32.3767509460449 
Location:212-341IPR012680:Laminin_G_2 
Evalue:-28.9208183288574 
Location:398-524IPR012680:Laminin_G_2 
Evalue:-22.0969104766846 
Location:1046-1176IPR006209:EGF 
Evalue:-6.35654735565186 
Location:553-585IPR006209:EGF 
Evalue:-2.74472761154175 
Location:962-996IPR002181:FBG 
Evalue:-0.0177287669604316 
Location:589-769IPR008985:ConA_like_lec_gl 
Evalue:0 
Location:22-31IPR013032:EGF_1 
Evalue:0 
Location:0-0
SequencesProtein: CNTP4_HUMAN (1308 aa)
mRNA: NM_033401
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:domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 115 residues, 74907577-74907921Exon2: 66 residues, 74946715-74946909Exon3: 51 residues, 75018849-75018997Exon4: 70 residues, 75039409-75039613Exon5: 63 residues, 75040164-75040349Exon6: 50 residues, 75041112-75041256Exon7: 89 residues, 75043905-75044167Exon8: 52 residues, 75053353-75053503Exon9: 59 residues, 75058749-75058921Exon10: 37 residues, 75067336-75067443Exon11: 42 residues, 75070816-75070936Exon12: 68 residues, 75081083-75081281Exon13: 54 residues, 75086307-75086464Exon14: 44 residues, 75089964-75090092Exon15: 59 residues, 75112537-75112708Exon16: 75 residues, 75113436-75113655Exon17: 82 residues, 75126942-75127182Exon18: 77 residues, 75129513-75129738Exon19: 46 residues, 75131116-75131250Exon20: 31 residues, 75132100-75132188Exon21: 75 residues, 75144680-75144899Exon22: 26 residues, 75145233-75145305Exon23: 193 residues, 75149887-75150461Exon24: 2 residues, -Jump to CNTP4_HUMAN  
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