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0LRTM1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLRRTM1
DescriptionLeucine-rich repeat transmembrane neuronal protein 1 precursor.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
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.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
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
IPR003591:LRR_TYP 
Evalue:-3.72124639904717 
Location:136-159IPR003591:LRR_TYP 
Evalue:-2.65757731917779 
Location:112-135IPR001611:LRR_1 
Evalue:-1.92081880569458 
Location:186-208IPR003591:LRR_TYP 
Evalue:-1.02227639471115 
Location:160-183IPR000372:LRRNT 
Evalue:-0.397940008672038 
Location:38-70IPR001611:LEURICHRPT 
Evalue:0 
Location:255-268IPR001611:LRR_1 
Evalue:0.380211234092712 
Location:210-232IPR001611:LRR_1 
Evalue:0.518513917922974 
Location:281-302
SequencesProtein: LRTM1_HUMAN (522 aa)
mRNA: NM_178839
Local Annotation
Synapse Ontology
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 504 residues, 80378817-80380326Exon2: 646 residues, 80382580-80384514Exon3: 194 residues, 80384787-80385363Exon4: 2 residues, -Jump to LRTM1_HUMAN  
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