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0LAMA1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLAMA1
DescriptionLaminin alpha-1 chain precursor (laminin a chain).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005606 laminin-1 (NAS)
0005608 laminin-3 (NAS)
0007155 cell adhesion (NAS)
0016477 cell migration (NAS)
0007275 development (NAS)

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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:
Laminin is a large molecular weight glycoprotein present only in basement membranes in almost every animal tissue. Laminin is thought to mediate the attachment.igration and organisation of cells into tissues during embryonic development by interacting with other extracellular matrix components . Each laminin is a heterotrimer assembled from alpha.eta and gamma chain subunits.ecreted and incorporated into cell-associated extracellular matrices . Basement membrane assembly is a cooperative process in which laminins polymerize through their N-terminal domain (LN or domain VI) and anchor to the cell surface through their G domains. Netrins may also associate with this network through heterotypic LN domain interactions . This leads to cell signaling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin. This LN domain dependent self-assembly is considered to be crucial for the integrity of basement membranes.s highlighted by genetic forms of muscular dystrophy containing the deletion of the LN module from the alpha 2 laminin chain . The laminin N-terminal domain is found in all laminin and netrin subunits except laminin alpha 3A.lpha 4 and gamma 2.
  IPR008211:Laminin, N-terminal
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 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.hich includes a large number of extracellular proteins. The C-terminus of 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 has been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each has 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 ().
  IPR012679:Laminin G, subdomain 1
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
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
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
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
IPR008211:Laminin_N 
Evalue:-172.05061340332 
Location:22-268IPR009254:Laminin_I 
Evalue:-105.130767822266 
Location:1567-1831IPR000034:Laminin_B 
Evalue:-84.3372421264648 
Location:1218-1360IPR000034:Laminin_B 
Evalue:-82.0362091064453 
Location:568-707IPR010307:Laminin_II 
Evalue:-55.1079063415527 
Location:2011-2145IPR012679:Laminin_G_1 
Evalue:-54.8538703918457 
Location:2514-2658IPR012679:Laminin_G_1 
Evalue:-53.1487426757813 
Location:2743-2872IPR012679:Laminin_G_1 
Evalue:-47.5376014709473 
Location:2920-3051IPR001791:LamG 
Evalue:-37.4559319556497 
Location:2325-2466IPR012679:Laminin_G_1 
Evalue:-31.9208183288574 
Location:2146-2283IPR002049:Laminin_EGF 
Evalue:-21.075719833374 
Location:902-948IPR002049:Laminin_EGF 
Evalue:-19.0087738037109 
Location:1090-1147IPR002049:Laminin_EGF 
Evalue:-18.6382713317871 
Location:849-899IPR002049:Laminin_EGF 
Evalue:-18.6197891235352 
Location:742-788IPR002049:Laminin_EGF 
Evalue:-18.3979396820068 
Location:397-451IPR002049:Laminin_EGF 
Evalue:-18.1079063415527 
Location:454-500IPR002049:Laminin_EGF 
Evalue:-17.8239078521729 
Location:791-846IPR002049:Laminin_EGF 
Evalue:-16 
Location:1403-1449IPR002049:Laminin_EGF 
Evalue:-15.7447271347046 
Location:951-995IPR002049:Laminin_EGF 
Evalue:-15.0705814361572 
Location:998-1041IPR002049:Laminin_EGF 
Evalue:-14.8860569000244 
Location:1509-1553IPR002049:Laminin_EGF 
Evalue:-14.8538722991943 
Location:1044-1087IPR002049:Laminin_EGF 
Evalue:-13.8860569000244 
Location:1452-1506IPR002049:EGF_Lam 
Evalue:-8.03151705144606 
Location:327-394IPR002049:EGF_Lam 
Evalue:-4.03151705144606 
Location:270-324IPR002049:Laminin_EGF 
Evalue:-3.18045616149902 
Location:708-729IPR002049:Laminin_EGF 
Evalue:-2.95860719680786 
Location:1362-1382IPR008985:ConA_like_lec_gl 
Evalue:0 
Location:3059-3071
SequencesProtein: LAMA1_HUMAN (3075 aa)
mRNA: NM_005559
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 assignmentK05637
  Level 3 annotation:
    laminin, alpha 1
  Level 2 annotation:
    ECM-receptor interaction
    CAM ligands
    Focal adhesion
    Prion disease
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 118 residues, 6931887-6932238Exon2: 76 residues, 6933178-6933401Exon3: 46 residues, 6937161-6937295Exon4: 53 residues, 6938401-6938555Exon5: 55 residues, 6939099-6939258Exon6: 65 residues, 6940780-6940970Exon7: 39 residues, 6945351-6945464Exon8: 45 residues, 6946634-6946764Exon9: 64 residues, 6948475-6948661Exon10: 52 residues, 6949339-6949491Exon11: 60 residues, 6951584-6951758Exon12: 40 residues, 6951943-6952058Exon13: 49 residues, 6954660-6954802Exon14: 50 residues, 6955286-6955431Exon15: 52 residues, 6956145-6956296Exon16: 43 residues, 6961855-6961980Exon17: 52 residues, 6963055-6963206Exon18: 46 residues, 6964901-6965035Exon19: 50 residues, 6965935-6966079Exon20: 53 residues, 6967725-6967880Exon21: 63 residues, 6968194-6968377Exon22: 41 residues, 6970519-6970636Exon23: 33 residues, 6972495-6972589Exon24: 47 residues, 6973097-6973233Exon25: 56 residues, 6975235-6975399Exon26: 41 residues, 6975525-6975642Exon27: 72 residues, 6976135-6976346Exon28: 55 residues, 6982559-6982719Exon29: 39 residues, 6983639-6983751Exon30: 32 residues, 6985355-6985445Exon31: 49 residues, 6987740-6987883Exon32: 66 residues, 6989443-6989637Exon33: 31 residues, 6989909-6989996Exon34: 42 residues, 6992262-6992384Exon35: 48 residues, 6997137-6997275Exon36: 42 residues, 6998486-6998607Exon37: 44 residues, 6999237-6999365Exon38: 64 residues, 7000198-7000384Exon39: 62 residues, 7001298-7001478Exon40: 50 residues, 7001993-7002137Exon41: 81 residues, 7003813-7004050Exon42: 47 residues, 7005720-7005857Exon43: 62 residues, 7006489-7006670Exon44: 37 residues, 7007276-7007383Exon45: 72 residues, 7013162-7013374Exon46: 31 residues, 7014378-7014465Exon47: 44 residues, 7015977-7016105Exon48: 39 residues, 7022064-7022175Exon49: 39 residues, 7022982-7023094Exon50: 72 residues, 7024477-7024689Exon51: 36 residues, 7025985-7026087Exon52: 60 residues, 7027576-7027750Exon53: 49 residues, 7028808-7028949Exon54: 55 residues, 7030074-7030235Exon55: 37 residues, 7032143-7032249Exon56: 61 residues, 7033225-7033404Exon57: 41 residues, 7034720-7034838Exon58: 32 residues, 7036276-7036366Exon59: 62 residues, 7039076-7039256Exon60: 83 residues, 7040692-7040935Exon61: 39 residues, 7069973-7070086Exon62: 59 residues, 7070285-7070456Exon63: 53 residues, 7107658-7107813Exon64: 2 residues, -Jump to LAMA1_HUMANExon1: 1013 residues, 6943728-6946764Exon2: 64 residues, 6948475-6948661Exon3: 452 residues, 6949339-6950691Exon4: 2 residues, -Jump to Q8IXG5_HUMAN  
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