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0CSTN1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCLSTN1
DescriptionCalsyntenin-1 precursor.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Cadherins are a family of adhesion molecules that mediate Ca2+-dependent cell-cell adhesion in all solid tissues of the organism which modulate a wide variety of processes including cell polarisation and migration . Cadherin-mediated cell-cell junctions are formed as a result of interaction between extracellular domains of identical cadherins.hich are located on the membranes of the neighbouring cells. The stability of these adhesive junctions is ensured by binding of the intracellular cadherin domain with the actin cytoskeleton. There are a number of different isoforms distributed in a tissue-specific manner in a wide variety of organisms. Cells containing different cadherins tend to segregate in vitro.hile those that contain the same cadherins tend to preferentially aggregate together. This observation is linked to the finding that cadherin expression causes morphological changes involving the positional segregation of cells into layers.uggesting they may play an important role in the sorting of different cell types during morphogenesis.istogenesis and regeneration. They may also be involved in the regulation of tight and gap junctions.nd in the control of intercellular spacing. Cadherins are evolutionary related to the desmogleins which are component of intercellular desmosome junctions involved in the interaction of plaque proteins.Structurally.adherins comprise a number of domains: classically.hese include a signal sequence; a propeptide of around 130 residues; a single transmembrane domain and five tandemly repeated extracellular cadherin domains. of which are cadherin repeats.nd the fifth contains 4 conserved cysteines and a N-terminal cytoplasmic domain . However.roteins are designated as members of the broadly defined cadherin family if they have one or more cadherin repeats. A cadherin repeat is an independently folding sequence of approximately 110 amino acids that contains motifs with the conserved sequences DRE.XNDNAPXF.nd DXD. Crystal structures have revealed that multiple cadherin domains form Ca2+-dependent rod-like structures with a conserved Ca2+-binding pocket at thedomain-domain interface. Cadherins depend on calcium for their function: calcium ions bind to specific residues in each cadherin repeat to ensure its proper folding.o confer rigidity upon the extracellular domain and is essential for cadherin adhesive function and for protection against protease digestion.
  IPR002126:Cadherin
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
IPR002126:CA 
Evalue:-10.3098039199715 
Location:59-162IPR002126:Cadherin 
Evalue:-4.82390880584717 
Location:169-258IPR008985:ConA_like_lec_gl 
Evalue:0 
Location:312-502IPR008985:ConA_like_lec_gl 
Evalue:0 
Location:530-563IPR002126:CADHERIN_1 
Evalue:0 
Location:0-0
SequencesProtein: CSTN1_HUMAN (981 aa)
mRNA: NM_001009566
Local Annotation
Synapse Ontology
Postsynaptic compartment is represented by a patch of plasma membrane containing a packed array of neurotransmitter receptors and by an underlying dense matrix, the postsynaptic density (PSD).
sdb:0005 Postsynaptic compartment  (Evidence:keywords)
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)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 562 residues, 9711666-9713350Exon2: 63 residues, 9713850-9714035Exon3: 47 residues, 9714405-9714541Exon4: 50 residues, 9716045-9716191Exon5: 59 residues, 9716616-9716787Exon6: 77 residues, 9717592-9717819Exon7: 51 residues, 9718111-9718260Exon8: 54 residues, 9718529-9718687Exon9: 21 residues, 9720142-9720199Exon10: 56 residues, 9723738-9723901Exon11: 42 residues, 9726528-9726650Exon12: 85 residues, 9727039-9727288Exon13: 64 residues, 9732105-9732291Exon14: 52 residues, 9732408-9732558Exon15: 71 residues, 9734117-9734326Exon16: 67 residues, 9737758-9737954Exon17: 12 residues, 9739125-9739155Exon18: 43 residues, 9755916-9756039Exon19: 285 residues, 9806287-9807137Exon20: 2 residues, -Jump to CSTN1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3770 9711666-9807137 ~-95K 324(CLSTN1)(-)Loci: 2479 9522144-9565420 ~-43K 318(+)Link out to UCSC