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0LAMA3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLAMA3
DescriptionLaminin alpha-3 chain precursor (epiligrin 170 kda subunit) (e170) (nicein alpha subunit).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005604 basement membrane (TAS)
0005198 structural molecule activity (NAS)
0008544 epidermis development (TAS)

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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 glycoproteins that are major constituents of the basement membrane of cells. Laminins are trimeric molecules; laminin-1 is an alpha1 beta1 gamma1 trimer. It has been suggested that the domains I and II from laminin A.1 and B2 may come together to form a triple helical coiled-coil structure . Binding to cells via a high affinity receptor.aminin is thought to mediate the attachment.igration and organisation of cells into tissues during embryonic development by interacting with other extracellular matrix components.
  IPR009254:Laminin I
It has been suggested that the domains I and II from laminin A.1 and B2 may come together to form a triple helical coiled-coil structure .
  IPR010307:Laminin II
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 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
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
IPR009254:Laminin_I 
Evalue:-102.585029602051 
Location:226-485IPR010307:Laminin_II 
Evalue:-50.1426658630371 
Location:668-796IPR012680:Laminin_G_2 
Evalue:-33.5376014709473 
Location:1566-1691IPR012680:Laminin_G_2 
Evalue:-32.8239097595215 
Location:1396-1516IPR001791:LamG 
Evalue:-20.568636235841 
Location:998-1126IPR012680:Laminin_G_2 
Evalue:-16.5528411865234 
Location:1177-1284IPR002049:Laminin_EGF 
Evalue:-14.8860569000244 
Location:67-111IPR002049:Laminin_EGF 
Evalue:-10.2291479110718 
Location:114-164IPR008985:ConA_like_lec_gl 
Evalue:0 
Location:15-23
SequencesProtein: LAMA3_HUMAN (1713 aa)
mRNA: L34155 NM_000227
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 assignmentK06240
  Level 3 annotation:
    laminin, alpha 3
  Level 2 annotation:
    ECM-receptor interaction
    CAM ligands
    Focal adhesion
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 59 residues, 19707003-19707177Exon2: 40 residues, 19710255-19710369Exon3: 38 residues, 19715897-19716007Exon4: 29 residues, 19718734-19718815Exon5: 37 residues, 19723972-19724079Exon6: 19 residues, 19728259-19728310Exon7: 52 residues, 19728868-19729020Exon8: 39 residues, 19732699-19732810Exon9: 39 residues, 19732915-19733027Exon10: 58 residues, 19733249-19733417Exon11: 67 residues, 19735088-19735285Exon12: 41 residues, 19736970-19737087Exon13: 53 residues, 19737894-19738049Exon14: 49 residues, 19738514-19738656Exon15: 36 residues, 19739483-19739586Exon16: 41 residues, 19741511-19741628Exon17: 62 residues, 19741717-19741897Exon18: 49 residues, 19743114-19743257Exon19: 59 residues, 19746672-19746843Exon20: 52 residues, 19748371-19748523Exon21: 56 residues, 19748659-19748822Exon22: 46 residues, 19749250-19749384Exon23: 50 residues, 19750512-19750657Exon24: 42 residues, 19754896-19755016Exon25: 46 residues, 19755413-19755547Exon26: 41 residues, 19762084-19762202Exon27: 49 residues, 19762586-19762727Exon28: 48 residues, 19765023-19765163Exon29: 46 residues, 19766121-19766253Exon30: 53 residues, 19767743-19767897Exon31: 56 residues, 19773184-19773348Exon32: 63 residues, 19777749-19777933Exon33: 49 residues, 19780105-19780246Exon34: 55 residues, 19783726-19783886Exon35: 45 residues, 19783990-19784121Exon36: 33 residues, 19785645-19785739Exon37: 42 residues, 19786951-19787071Exon38: 189 residues, 19788464-19789025Exon39: 2 residues, -Jump to LAMA3_HUMANExon1: 47 residues, 19707039-19707177Exon2: 40 residues, 19710255-19710369Exon3: 38 residues, 19715897-19716007Exon4: 29 residues, 19718734-19718815Exon5: 37 residues, 19723972-19724079Exon6: 19 residues, 19728259-19728310Exon7: 52 residues, 19728868-19729020Exon8: 39 residues, 19732699-19732810Exon9: 39 residues, 19732915-19733027Exon10: 58 residues, 19733249-19733417Exon11: 67 residues, 19735088-19735285Exon12: 41 residues, 19736970-19737087Exon13: 53 residues, 19737894-19738049Exon14: 49 residues, 19738514-19738656Exon15: 36 residues, 19739483-19739586Exon16: 41 residues, 19741511-19741628Exon17: 62 residues, 19741717-19741897Exon18: 49 residues, 19743114-19743257Exon19: 59 residues, 19746672-19746843Exon20: 52 residues, 19748371-19748523Exon21: 56 residues, 19748659-19748822Exon22: 46 residues, 19749250-19749384Exon23: 50 residues, 19750512-19750657Exon24: 42 residues, 19754896-19755016Exon25: 46 residues, 19755413-19755547Exon26: 41 residues, 19762084-19762202Exon27: 49 residues, 19762586-19762727Exon28: 48 residues, 19765023-19765163Exon29: 46 residues, 19766121-19766253Exon30: 53 residues, 19767743-19767897Exon31: 56 residues, 19773184-19773348Exon32: 63 residues, 19777749-19777933Exon33: 49 residues, 19780105-19780246Exon34: 55 residues, 19783726-19783886Exon35: 45 residues, 19783990-19784121Exon36: 33 residues, 19785645-19785739Exon37: 42 residues, 19786951-19787071Exon38: 147 residues, 19788464-19788901Exon39: 2 residues, -Jump to LAMA3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3059 19707003-19789025 ~-82K 17131(LAMA3)(+)Loci: 4333 19365462-19420426 ~-55K 17127(NPC1)(-)Link out to UCSC