IED ID | IndEnz0002018494 |
Enzyme Type ID | protease018494 |
Protein Name |
Gliomedin Cleaved into: Gliomedin shedded ectodomain |
Gene Name | GLDN COLM UNQ9339/PRO34011 |
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 | MARGAEGGRGDAGWGLRGALAAVALLSALNAAGTVFALCQWRGLSSALRALEAQRGREQREDSALRSFLAELSRAPRGASAPPQDPASSARNKRSHSGEPAPHIRAESHDMLMMMTYSMVPIRVMVDLCNSTKGICLTGPSGPPGPPGAGGLPGHNGLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGDVSNDVLLAGAKGDQGPPGPPGPPGPPGPPGPPGSRRAKGPRQPSMFNGQCPGETCAIPNDDTLVGKADEKASEHHSPQAESMITSIGNPVQVLKVTETFGTWIRESANKSDDRIWVTEHFSGIMVKEFKDQPSLLNGSYTFIHLPYYFHGCGHVVYNNSLYYHKGGSNTLVRFEFGQETSQTLKLENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERTFSVVQHVNTTYPKSKAGNAFIARGILYVTDTKDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWEDGHLMLYPVQFLSTTLNQ |
Enzyme Length | 551 |
Uniprot Accession Number | Q6ZMI3 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Ligand for NRCAM and NFASC/neurofascin that plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Mediates interaction between Schwann cell microvilli and axons via its interactions with NRCAM and NFASC. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with NRCAM, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier. {ECO:0000250|UniProtKB:Q8BMF8}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (1); Beta strand (21); Chain (2); Compositional bias (1); Domain (3); Glycosylation (5); Helix (3); Natural variant (5); Region (2); Sequence conflict (1); Site (2); Topological domain (2); Transmembrane (1); Turn (5) |
Keywords | 3D-structure;Alternative splicing;Cell membrane;Cell projection;Collagen;Developmental protein;Differentiation;Disease variant;Extracellular matrix;Glycoprotein;Membrane;Neurogenesis;Reference proteome;Repeat;Secreted;Signal-anchor;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:27616481}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q80WL1}. Cell projection, axon {ECO:0000250|UniProtKB:Q80WL1}. Note=Detected at the nodes of Ranvier. Detected at immature heminodes. {ECO:0000250|UniProtKB:Q80WL1}.; SUBCELLULAR LOCATION: [Gliomedin shedded ectodomain]: Secreted {ECO:0000250|UniProtKB:Q80WL1}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q80WL1}. Note=Proteolytic processing gives rise to a soluble extracellular domain that is secreted. The gliomedin shedded ectodomain localizes to the nodes of Ranvier. {ECO:0000250|UniProtKB:Q80WL1}. |
Modified Residue | |
Post Translational Modification | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BMF8}.; PTM: Proteolytic proccessing by a furin-like protease causes shedding of the ectodomain. Further cleavage by BMP1 releases the olfactomedin-like domain. {ECO:0000250|UniProtKB:Q8BMF8}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 5YBY; |
Mapped Pubmed ID | 22009740; 22462667; 28726266; 32812332; |
Motif | |
Gene Encoded By | |
Mass | 58,957 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |