IED ID | IndEnz0005000986 |
Enzyme Type ID | lipase000986 |
Protein Name |
Neuroligin-1 Neuroligin I |
Gene Name | Nlgn1 |
Organism | Rattus norvegicus (Rat) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
Enzyme Sequence | MALPRCMWPNYVWRAMMACVVHRGSGAPLTLCLLGCLLQTFHVLSQKLDDVDPLVTTNFGKIRGIKKELNNEILGPVIQFLGVPYAAPPTGEHRFQPPEPPSPWSDIRNATQFAPVCPQNIIDGRLPEVMLPVWFTNNLDVVSSYVQDQSEDCLYLNIYVPTEDVKRISKECARKPGKKICRKGDIRDSGGPKPVMVYIHGGSYMEGTGNLYDGSVLASYGNVIVITVNYRLGVLGFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFGGDPLRITVFGSGAGGSCVNLLTLSHYSEGNRWSNSTKGLFQRAIAQSGTALSSWAVSFQPAKYARILATKVGCNVSDTVELVECLQKKPYKELVDQDVQPARYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGLKFVENIVDSDDGVSASDFDFAVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRHNPETRRKTLLALFTDHQWVAPAVATADLHSNFGSPTYFYAFYHHCQTDQVPAWADAAHGDEVPYVLGIPMIGPTELFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVAWTRYSQKDQLYLHIGLKPRVKEHYRANKVNLWLELVPHLHNLNDISQYTSTTTKVPSTDITLRPTRKNSTPVTSAFPTAKQDDPKQQPSPFSVDQRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHDVHRRCSPQRTTTNDLTHAPEEEIMSLQMKHTDLDHECESIHPHEVVLRTACPPDYTLAMRRSPDDVPLMTPNTITMIPNTIPGIQPLHTFNTFTGGQNNTLPHPHPHPHSHSTTRV |
Enzyme Length | 843 |
Uniprot Accession Number | Q62765 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep (By similarity). The protein is involved in nervous system development. {ECO:0000250|UniProtKB:Q99K10, ECO:0000269|PubMed:15620359, ECO:0000269|PubMed:9325340}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (2); Beta strand (26); Chain (1); Disulfide bond (4); Glycosylation (6); Helix (28); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (6) |
Keywords | 3D-structure;Alternative splicing;Biological rhythms;Cell adhesion;Cell junction;Cell membrane;Direct protein sequencing;Disulfide bond;Glycoprotein;Membrane;Reference proteome;Secreted;Signal;Synapse;Transmembrane;Transmembrane helix |
Interact With | P97924-5; F1M0Z1; Q63373-3 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, synapse, postsynaptic density {ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:19914352, ECO:0000269|PubMed:9927700}. Cell junction, synapse, synaptic cleft {ECO:0000269|PubMed:9927700}. Cell junction, synapse, synaptic cell membrane {ECO:0000269|PubMed:9927700}. Note=Enriched in synaptic plasma membranes and clustered in synaptic clefts and postsynaptic densities. Colocalized with DLG4/PSD-95 and GRIN1/NMDAR1. {ECO:0000269|PubMed:19914352, ECO:0000269|PubMed:9927700}. |
Modified Residue | |
Post Translational Modification | PTM: The N-terminus is blocked. |
Signal Peptide | SIGNAL 1..45; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 3BIW; 3BIX; 3VKF; |
Mapped Pubmed ID | 10892652; 12141453; 12930820; 14522992; 15519238; 15681343; 15797875; 16298368; 17237775; 17582332; 18579781; 19098102; 19105974; 19450252; 19628693; 19730411; 19816407; 20176955; 20534458; 20543817; 20739565; 21056983; 21532576; 21911064; 21940442; 22539981; 22671294; 22750515; 22840401; 23083734; 23426688; 24860089; 25157101; 25428619; 26325471; 27423632; 28194405; 28875935; 29592780; 30049666; 30790215; 31801062; 32915137; 34353896; 9278515; |
Motif | |
Gene Encoded By | |
Mass | 94,294 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |