Detail Information for IndEnz0002006589
IED ID IndEnz0002006589
Enzyme Type ID protease006589
Protein Name Neural cell adhesion molecule L1-like protein
Cell adhesion molecule with homology to L1CAM
Chl1-like protein
Close homolog of L1

Cleaved into: Processed neural cell adhesion molecule L1-like protein
Gene Name Chl1 Call
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MMELPLCGRGLILSLIFLLLKLSAAEIPLSVQQVPTIVKQSYVQVAFPFDEYFQIECEAKGNPEPIFSWTKDDKPFDLSDPRIIAANNSGTFKIPNEGHISHFQGKYRCFASNRLGTAVSEEIEFIVPGVPKFPKEKIEPIDVEEGDSIVLPCNPPKGLPPLHIYWMNIELEHIEQDERVYMSQRGDLYFANVEENDSRNDYCCFAAFPKLRTIVQKMPMKLTVNSSNSIKQRKPKLLLPPAQMGSLSAKTVLKGDTLLLECFAEGLPTPHIQWSKPGSELPEGRATIEVHEKTLKIENISYQDRGNYRCTANNLLGKASHDFHVTVEEPPRWKKKPQSAVYSTGSSGILLCEAEGEPQPTIKWRLNGLPIEKHPFPGDFMFPREISFTNLLPNHTGVYQCEASNIHGTILANANIDVIDVIPLIKTKNEENYATVVGYSAFLHCEYFASPKATVVWEVADETHPLEGDRYHTHENGTLEIYRTTEEDAGSYSCWVDNAMGKAVITANLDIRNATKLRVSPKNPRIPKSHVLELYCESQCDSHLKHSLKLSWSKDGEAFEMNGTEDGRIVIDGAYLTISNITAEDQGVYSCSAQTSLDSTSEKTQVTVLGVPDPPGNLHLSERQNRSVRLSWEAGDDHNSKISEYIVEFEGNREEPGKWEELTRVQGEETDVVLSLAPYVRYQFRVTAVNEVGRSHASLPSDHHETPPAAPDKNPQNIRVQASQPKEMIIKWEPLKSMEQNGPGLEYKVSWKPQGAPEEWEEEIVTNHTLRVMTPTVYAPYDVKVQAINQLGSSPDPQPVTLYSGEDYPSTAPVIQRVDVMNSTLVKVTWSSIPKETVHGLLRGYQINWWKTKSLLDGRTHPKEVNILRFSGQRNSGMVPSLDPFSEFHLTVLAYNSKGAGPESEPYIFQTPEGVPEQPSFLKVIKVDKDTATLSWGLPKKLNGNLTGYLLQYQIINDTYELGELNEINVTTPSKSSWHLSNLNSTTKYKFYLRACTSRGCGKPISEEGATLGEGSKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETRGREYAGLYDDISTQGWFIGLMCAIALLTLILLTICFVKRNRGGKYSVKEKEDLHPDPEVQSAKDETFGEYSDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNEDGSFIGAYTGAKEKGSVESNGSSTATFPLRA
Enzyme Length 1209
Uniprot Accession Number P70232
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons as well as in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane. {ECO:0000269|PubMed:10022583, ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:12391163, ECO:0000269|PubMed:12721290, ECO:0000269|PubMed:12812975, ECO:0000269|PubMed:14659567, ECO:0000269|PubMed:14761956, ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:16623841}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (3); Chain (2); Compositional bias (1); Disulfide bond (6); Domain (10); Frameshift (1); Glycosylation (10); Modified residue (3); Motif (2); Mutagenesis (2); Region (2); Sequence conflict (5); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Cell adhesion;Cell membrane;Developmental protein;Differentiation;Disulfide bond;Extracellular matrix;Glycoprotein;Immunoglobulin domain;Membrane;Neurogenesis;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix
Interact With Q9JMB8; P18052
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=Soluble forms produced by cleavage/shedding also exist.; SUBCELLULAR LOCATION: [Processed neural cell adhesion molecule L1-like protein]: Secreted, extracellular space, extracellular matrix.
Modified Residue MOD_RES 1148; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1161; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1181; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079
Post Translational Modification PTM: Cleavage by metalloprotease ADAM8 in the extracellular part generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is inhibited by metalloprotease inhibitors. In brain extracts, these two soluble forms are also present and are dramatically reduced in mice lacking ADAM8 (PubMed:14761956). Cleaved by BACE1 (PubMed:29325091). {ECO:0000269|PubMed:14761956, ECO:0000269|PubMed:29325091}.; PTM: N-glycosylated. Contains N-linked oligosaccharides with a sulfated carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc). {ECO:0000269|PubMed:8921253}.; PTM: O-glycosylated. {ECO:0000269|PubMed:8921253}.
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10662501; 12466851; 12605410; 12973829; 15533325; 15880726; 16602821; 16615898; 16701205; 17126027; 17178404; 17611275; 17995939; 18046458; 18077678; 18447583; 18588951; 19074023; 19226508; 19262122; 19303029; 19672967; 19819308; 19877281; 20151419; 20576928; 20711454; 20933598; 21677750; 22008794; 22097715; 22473292; 22579729; 22692213; 22696295; 22789544; 22988240; 23949217; 24027281; 24411736; 24559674; 24952961; 25007825; 25355214; 25775569; 25826454; 26285062; 26299962; 26527397; 27178982; 27346367; 28583411; 28630165; 28647594; 28839197; 29099309; 29127326; 29775614; 29881335; 31073041; 31152445; 31182634; 31300520; 32052901; 32184019; 32553152; 32557322; 32640308; 33240104; 34170322;
Motif MOTIF 555..558; /note=DGEA; MOTIF 1182..1186; /note=FIG[AQ]Y
Gene Encoded By
Mass 135,074
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda