SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0SLIT2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSLIT2
DescriptionSlit homolog 2 protein precursor (slit-2) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005576 extracellular region (IEP)
0005102 receptor binding (TAS)
0008347 glial cell migration (IMP)
0050929 induction of negative chemotaxis (IDA)
0007509 mesoderm migration (IMP)
0008045 motor axon guidance (TAS)
0007399 neurogenesis (TAS)
0008038 neuron recognition (TAS)
0007608 perception of smell (TAS)
0050772 positive regulation of axonogenesis (TAS)
0001657 ureteric bud development (IMP)

Warning: fopen(/home/kongl/syndb/www/temp/612833852.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
schematic display of those terms with internal associations, click the node and browse the corresponding GO term
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
Leucine-rich repeats (LRR.ee ) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape . LRRs occur in proteins ranging from viruses to eukaryotes.nd appear to provide a structural framework for the formation of protein-protein interactions . Proteins containing LRRs include tyrosine kinase receptors.ell-adhesion molecules.irulence factors.nd extracellular matrix-binding glycoproteins.nd are involved in a variety of biological processes.ncluding signal transduction.ell adhesion.NA repair.ecombination.ranscription.NA processing.isease resistance.poptosis and the immune response.LRRs are often flanked by cysteine-rich domains: an N-terminal LRR domain and a C-terminal LRR domain (). This entry represents the N-terminal LRR domain.
  IPR000372:Leucine-rich repeat, cysteine-rich flanking region, N-terminal
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
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown .o be present in a large number of membrane-bound and extracellular.ostly animal.roteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains . Calcium-binding may be crucial for numerous protein-protein interactions.For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. The first.hird and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) . A conserved aromatic residue.s well as the second conserved negative residue.re thought to be involved in stabilizing the calcium-binding site.As in non-calcium binding EGF-like domains.here are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes .
  IPR001881:EGF-like calcium-binding
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
Four recent crystal structures of growth factors--nerve growth factor.ransforming growth factor-beta.latelet-derived growth factor.nd human chorionic gonadotropin--from four separate superfamilies revealed that these proteins are structurally related and share a common overall topology . These proteins have very little sequence homology.ut they all have an unusual arrangement of six cysteines linked to form a "cystine-knot" conformation. The active forms of these proteins are dimers.ither homo- or heterodimers . Because of their shape.here appears to be an intrinsic requirement for the cystine-knot growth factors to form dimers. This extra level of organization increases the variety of structures built around this simple structural motif .
  IPR006207:Cystine knot, C-terminal
Leucine-rich repeats (LRR.ee ) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape . LRRs occur in proteins ranging from viruses to eukaryotes.nd appear to provide a structural framework for the formation of protein-protein interactions . Proteins containing LRRs include tyrosine kinase receptors.ell-adhesion molecules.irulence factors.nd extracellular matrix-binding glycoproteins.nd are involved in a variety of biological processes.ncluding signal transduction.ell adhesion.NA repair.ecombination.ranscription.NA processing.isease resistance.poptosis.nd the immune response.LRRs are often flanked by cysteine-rich domains: an N-terminal LRR domain () and a C-terminal LRR domain. This entry represents the C-terminal LRR domain.
  IPR000483:Cysteine-rich flanking region, C-terminal
Leucine-rich repeats (LRRs) are relatively short motifs (22-28 residues in length) found in a variety of cytoplasmic.embrane and extracellular proteins . Although these proteins are associated with widely different functions. common property involves protein-protein interaction. Little is known about the 3D structure of LRRs.lthough it is believed that they can form amphipathic structures with hydrophobic surfaces capable of interacting with membranes . In vitro studies of a synthetic LRR from Drosophila Toll protein have indicated that the peptides form gels by adopting beta-sheet structures that form extended filaments. These results are consistent with the idea that LRRs mediate protein-protein interactions and cellular adhesion . Other functions of LRR-containing proteins include.or example.inding to enzymes and vascular repair . The 3-D structure of ribonuclease inhibitor. protein containing 15 LRRs.as been determined .evealing LRRs to be a new class of alpha/beta fold. LRRs form elongated non-globular structures and are often flanked by cysteine rich domains.
  IPR003591:Leucine-rich repeat, typical subtype
Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape . LRRs occur in proteins ranging from viruses to eukaryotes.nd appear to provide a structural framework for the formation of protein-protein interactions . Proteins containing LRRs include tyrosine kinase receptors.ell-adhesion molecules.irulence factors.nd extracellular matrix-binding glycoproteins.nd are involved in a variety of biological processes.ncluding signal transduction.ell adhesion.NA repair.ecombination.ranscription.NA processing.isease resistance.poptosis.nd the immune response.Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is.owever.ow clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins.haracterized by different lengths and consensus sequences of the repeats.ave been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL).orresponding to the ß-strand and adjacent loop regions.re conserved in LRR proteins.hereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences.ach of the variable parts contains two half-turns at both ends and a "linear" segment (as the chain follows a linear path overall).sually formed by a helix.n the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with alpha-helix.hus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions . Molecular modeling suggests that the conserved pattern LxxLxL.hich is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats .
  IPR001611:Leucine-rich repeat
G-protein-coupled receptors.PCRs.onstitute a vast protein family that encompasses a wide range of functions (including various autocrine.aracrine and endocrine processes). They show considerable diversity at the sequence level.n the basis of which they can be separated into distinct groups. We use the term clan to describe the GPCRs.s they embrace a group of families for which there are indications of evolutionary relationship.ut between which there is no statistically significant similarity in sequence . The currently known clan members include the rhodopsin-like GPCRs.he secretin-like GPCRs.he cAMP receptors.he fungal mating pheromone receptors.nd the metabotropic glutamate receptor family. There is a specialized database for GPCRs: http://www.gpcr.org/7tm/. The rhodopsin-like GPCRs themselves represent a widespread protein family that includes hormone.eurotransmitter and light receptors.ll of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character.he amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7transmembrane (TM) helices .The gonadotrophins (luteinising hormone.horiogonadotrophin.ollicle-stimulating hormone) and thyroid-stimulating hormone are heterotrimericglycoproteins composed of a common alpha-subunit and distinct beta-subunits. The carbohydrate moiety of the glycoproteins has an essential role inreceptor recognition. The receptors share close sequence similarity.ndare characterised by large extracellular domains believed to be involvedin hormone binding via leucine-rich repeats (LRR) . Modelling of thisportion of the receptors suggests that they contain three-dimensionalstructures similar to that of porcine ribonuclease inhibitor .FSH is released from the anterior pituitary under the influence ofgonadotrophin-releasing hormone and oestrogens.nd from the placenta duringpregnancy. In females.t acts on the ovaries.romoting developmentof follicles and is the principal hormone regulating secretion ofoestrogens. In males.t is responsible for the integrity of theseminiferous tubules and acts on Sertoli cells to support gametogenesis.FSH is used clinically to treat infertility in females and for some typesof spermatogenesis in males. The receptor is found in ovary and testis.ts predominant effector pathway being via activation of adenylyl cyclasethrough G proteins .
  IPR002272:Follicle-stimulating hormone 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 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
This EGF-like domain resembles the follistatin-N-terminal domain.nd is distinct from the kazal-like sequence. Follistatin binds to activin and is a specific inhibotor of the biosynthesis and secretion of pituitary follicle stimulating hormone. This domain is also found in prespore vesicle protein and agrin.
  IPR003645:Follistatin-like, N-terminal
IPR001791:LamG 
Evalue:-39.1426675035687 
Location:1180-1316IPR000483:LRRCT 
Evalue:-12.4202164033832 
Location:859-908IPR006209:EGF 
Evalue:-10.1938199996948 
Location:1080-1111IPR006209:EGF 
Evalue:-9.13076782226562 
Location:1040-1073IPR006209:EGF 
Evalue:-8.95860767364502 
Location:1002-1033IPR000483:LRRCT 
Evalue:-8.45593195564972 
Location:209-258IPR006209:EGF 
Evalue:-8.43179798126221 
Location:1125-1156IPR006209:EGF 
Evalue:-8.30103015899658 
Location:961-995IPR000372:LRRNT 
Evalue:-8.18045606445813 
Location:27-59IPR006209:EGF 
Evalue:-7.85387182235718 
Location:922-954IPR000372:LRRNT 
Evalue:-7.72124624252319 
Location:272-299IPR000372:LRRNT 
Evalue:-7.45593214035034 
Location:505-532IPR000372:LRRNT 
Evalue:-7.38721614328026 
Location:726-758IPR006209:EGF 
Evalue:-6.25181198120117 
Location:1336-1367IPR000483:LRRCT 
Evalue:-5.72124639904717 
Location:430-479IPR000483:LRRCT 
Evalue:-5.32790214206428 
Location:664-713IPR006209:EGF 
Evalue:-4.92081880569458 
Location:1416-1447IPR006207:CT 
Evalue:-3.50863830616573 
Location:1459-1528IPR003591:LRR_TYP 
Evalue:-3.24412514432751 
Location:800-823IPR001611:LRR_1 
Evalue:-3.16115093231201 
Location:325-347IPR003591:LRR_TYP 
Evalue:-3.11350927482752 
Location:824-847IPR003591:LRR_TYP 
Evalue:-2.85387196432176 
Location:557-580IPR006210:EGF 
Evalue:-2.42021640338319 
Location:1374-1407IPR001611:LRR_1 
Evalue:-2.08092188835144 
Location:349-371IPR001611:LRR_1 
Evalue:-1.72124636173248 
Location:176-198IPR003591:LRR_TYP 
Evalue:-1.60205999132796 
Location:78-101IPR001611:LRR_1 
Evalue:-1.56863617897034 
Location:631-653IPR001611:LRR_1 
Evalue:-1.53760194778442 
Location:397-419IPR001611:LRR_1 
Evalue:0.0791812464594841 
Location:152-174IPR001611:LRR_1 
Evalue:0.0791812464594841 
Location:607-629IPR001611:LRR_1 
Evalue:0.176091253757477 
Location:128-150IPR001611:LRR_1 
Evalue:0.556302487850189 
Location:104-124IPR001611:LRR_1 
Evalue:0.819543957710266 
Location:373-395IPR001611:LRR_1 
Evalue:0.913813829421997 
Location:301-323
SequencesProtein: SLIT2_HUMAN (1529 aa)
mRNA: NM_004787
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords,domains)
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 process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords,domains)
The recognition of molecules at the central nervous system midline choice point by an axon growth cone; this choice point determines whether the growth cone will cross the midline.
sdb:0069 axon midline choice point recognition  (Evidence:keywords,domains)
KO assignmentK06839
  Level 3 annotation:
    slit homolog 2 (Drosophila)
  Level 2 annotation:
    CAM ligands
    Axon guidance
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 128 residues, 19864332-19864715Exon2: 26 residues, 19867392-19867464Exon3: 26 residues, 19868588-19868660Exon4: 26 residues, 19879530-19879602Exon5: 26 residues, 20078472-20078544Exon6: 26 residues, 20091436-20091508Exon7: 26 residues, 20096920-20096992Exon8: 56 residues, 20099539-20099703Exon9: 48 residues, 20102481-20102620Exon10: 26 residues, 20121215-20121287Exon11: 26 residues, 20121786-20121858Exon12: 26 residues, 20130102-20130174Exon13: 50 residues, 20134480-20134624Exon14: 56 residues, 20134734-20134898Exon15: 10 residues, 20135869-20135893Exon16: 52 residues, 20139669-20139820Exon17: 27 residues, 20142704-20142779Exon18: 50 residues, 20144292-20144436Exon19: 50 residues, 20150161-20150305Exon20: 57 residues, 20152173-20152340Exon21: 46 residues, 20153214-20153347Exon22: 25 residues, 20156751-20156820Exon23: 26 residues, 20159208-20159280Exon24: 26 residues, 20159777-20159849Exon25: 26 residues, 20161547-20161619Exon26: 56 residues, 20164525-20164689Exon27: 43 residues, 20177982-20178107Exon28: 34 residues, 20178238-20178336Exon29: 48 residues, 20179585-20179725Exon30: 33 residues, 20200364-20200458Exon31: 48 residues, 20206417-20206555Exon32: 82 residues, 20207135-20207376Exon33: 45 residues, 20208985-20209116Exon34: 53 residues, 20220733-20220888Exon35: 98 residues, 20227630-20227919Exon36: 72 residues, 20228159-20228371Exon37: 134 residues, 20229488-20229886Exon38: 2 residues, -Jump to SLIT2_HUMAN  
Tune and view alternative isoforms