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0LRRN5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLRRN5
DescriptionLeucine-rich repeats neuronal protein 5 precursor (glioma amplified on chromosome 1 protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004872 receptor activity (TAS)
0007155 cell adhesion (TAS)
0007165 signal transduction (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 unassigned to SynO:
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents I-set domains.hich are found in several cell adhesion molecules.ncluding vascular (VCAM).ntercellular (ICAM).eural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules.s well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families.ncluding several tyrosine-protein kinase receptors.he hemolymph protein hemolin.he muscle proteins titin.elokin.nd twitchin.he neuronal adhesion molecule axonin-1 .nd the signalling molecule semaphorin 4D that is involved in axonal guidance.mmune function and angiogenesis .
  IPR013098:Immunoglobulin I-set
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents a subtype of the immunoglobulin domain.nd is found in a diverse range of protein families that includes glycoproteins.ibroblast growth factor receptors.ascular endothelial growth factor receptors.nterleukin-6 receptor.nd neural cell adhesion molecules. It also includes proteins that are classified as unassigned proteinase inhibitors belonging to MEROPS inhibitor families I2.17 and I43 .
  IPR003598:Immunoglobulin subtype 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.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
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
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
IPR013098:I-set 
Evalue:-13.7447271347046 
Location:426-514IPR003591:LRR_TYP 
Evalue:-4.39794000867204 
Location:140-163IPR000483:LRRCT 
Evalue:-2.56863617897034 
Location:394-421IPR003591:LRR_TYP 
Evalue:-2.14874165128092 
Location:116-139IPR001611:LRR_1 
Evalue:-1.88605666160583 
Location:311-334IPR000372:LRRNT 
Evalue:-1.35654732351381 
Location:28-73IPR008957:FN_III-like 
Evalue:0 
Location:520-615IPR001611:LEURICHRPT 
Evalue:0 
Location:95-108IPR001611:LRR_1 
Evalue:0.0413926839828491 
Location:262-284IPR001611:LRR_1 
Evalue:0.278753608465195 
Location:214-236IPR001611:LRR_1 
Evalue:0.838849067687988 
Location:238-260IPR001611:LRR_1 
Evalue:0.886490702629089 
Location:166-188
SequencesProtein: LRRN5_HUMAN (713 aa)
mRNA: NM_006338
Local Annotation
Synapse Ontology
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: 1015 residues, 202852927-202855969Exon2: 44 residues, 202918620-202918748Exon3: 13 residues, 202921070-202921104Exon4: 2 residues, -Jump to LRRN5_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2584 203064404-203258586 ~-194K 3738(NFASC)(+)Loci: 3860 202852927-202921104 ~-68K 3737(LRRN5)(-)Link out to UCSC