| IED ID | IndEnz0002007165 |
| Enzyme Type ID | protease007165 |
| Protein Name |
Neural cell adhesion molecule L1-like protein Close homolog of L1 Cleaved into: Processed neural cell adhesion molecule L1-like protein |
| Gene Name | CHL1 CALL |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MEPLLLGRGLIVYLMFLLLKFSKAIEIPSSVQQVPTIIKQSKVQVAFPFDEYFQIECEAKGNPEPTFSWTKDGNPFYFTDHRIIPSNNSGTFRIPNEGHISHFQGKYRCFASNKLGIAMSEEIEFIVPSVPKFPKEKIDPLEVEEGDPIVLPCNPPKGLPPLHIYWMNIELEHIEQDERVYMSQKGDLYFANVEEKDSRNDYCCFAAFPRLRTIVQKMPMKLTVNSSNSIKQRKPKLLLPPTESGSESSITILKGEILLLECFAEGLPTPQVDWNKIGGDLPKGRETKENYGKTLKIENVSYQDKGNYRCTASNFLGTATHDFHVIVEEPPRWTKKPQSAVYSTGSNGILLCEAEGEPQPTIKWRVNGSPVDNHPFAGDVVFPREISFTNLQPNHTAVYQCEASNVHGTILANANIDVVDVRPLIQTKDGENYATVVGYSAFLHCEFFASPEAVVSWQKVEEVKPLEGRRYHIYENGTLQINRTTEEDAGSYSCWVENAIGKTAVTANLDIRNATKLRVSPKNPRIPKLHMLELHCESKCDSHLKHSLKLSWSKDGEAFEINGTEDGRIIIDGANLTISNVTLEDQGIYCCSAHTALDSAADITQVTVLDVPDPPENLHLSERQNRSVRLTWEAGADHNSNISEYIVEFEGNKEEPGRWEELTRVQGKKTTVILPLAPFVRYQFRVIAVNEVGRSQPSQPSDHHETPPAAPDRNPQNIRVQASQPKEMIIKWEPLKSMEQNGPGLEYRVTWKPQGAPVEWEEETVTNHTLRVMTPAVYAPYDVKVQAINQLGSGPDPQSVTLYSGEDYPDTAPVIHGVDVINSTLVKVTWSTVPKDRVHGRLKGYQINWWKTKSLLDGRTHPKEVNILRFSGQRNSGMVPSLDAFSEFHLTVLAYNSKGAGPESEPYIFQTPEGVPEQPTFLKVIKVDKDTATLSWGLPKKLNGNLTGYLLQYQIINDTYEIGELNDINITTPSKPSWHLSNLNATTKYKFYLRACTSQGCGKPITEESSTLGEGSKGIGKISGVNLTQKTHPIEVFEPGAEHIVRLMTKNWGDNDSIFQDVIETRGREYAGLYDDISTQGWFIGLMCAIALLTLLLLTVCFVKRNRGGKYSVKEKEDLHPDPEIQSVKDETFGEYSDSDEKPLKGSLRSLNRDMQPTESADSLVEYGEGDHGLFSEDGSFIGAYAGSKEKGSVESNGSSTATFPLRA |
| Enzyme Length | 1208 |
| Uniprot Accession Number | O00533 |
| 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 and 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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (2); Compositional bias (2); Disulfide bond (6); Domain (10); Erroneous initiation (1); Glycosylation (10); Modified residue (3); Motif (2); Natural variant (4); Region (3); 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 | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Soluble forms produced by cleavage/shedding also exist. {ECO:0000250}.; SUBCELLULAR LOCATION: [Processed neural cell adhesion molecule L1-like protein]: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | MOD_RES 1147; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70232; MOD_RES 1160; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70232; MOD_RES 1180; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70232 |
| 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 (By similarity). Cleaved by BACE1 (By similarity). {ECO:0000250|UniProtKB:P70232}.; PTM: N-glycosylated. Contains N-linked oligosaccharides with a sulfated carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc) (By similarity). {ECO:0000250}.; PTM: O-glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11986985; 12721290; 15653271; 15704102; 16597699; 17178404; 17592550; 18046458; 18077678; 19064572; 19509545; 20195357; 20298200; 20379614; 20634891; 21332311; 21408220; 22634495; 22744455; 22909203; 22988240; 23857787; 23906755; 24203666; 24288179; 24512353; 24971532; 25943212; 28178655; 30134821; 30622339; 30943448; 31372722; 32557322; 33326488; 33453020; |
| Motif | MOTIF 555..558; /note=DGEA; MOTIF 1181..1185; /note=FIG[AQ]Y |
| Gene Encoded By | |
| Mass | 135,071 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |