Gldn
entrez
235379
canonical
uniprot
Q8BMF8
canonical
ensembl
ENSMUSG00000046167
resolver
ensp
ENSMUSP00000056080
resolver
enst
ENSMUST00000056740
resolver
genesymbol
Gldn
resolver
genesymbol_syn
Crgl2
resolver
uniprot
Q80ZC5
resolver
uniprot_entry
GLDN_MOUSE
resolver
uniprot_sec
Q80ZC5
resolver
amino_acid_sequence
MTRAAERGQGATGWGLRGALVAIALLSALNAAGTVFVLCQWRGLSAALRALEAQRGREQREDSALRAFLAELSRAPGRVPEPSQDPMSAARNKRSHNGEPASHIRAESQDMMMMMTYSMVPIRVMIDLCNSTQGICLTGPPGPPGPPGAGGLPGHNGSDGQPGLQGPKGEKGAIGKRGKMGLPGATGNPGEKGEKGDAGELGLPGNEGPPGQKGDKGDKGDVSNDVLLTGAKGDQGPPGPPGPPGPPGPPGSRRSKGPRPPNVFNSQCPGETCVIPNDDTLVGRADEKANERHSPQTESMITSIGNPAQVLKVRETFGTWMRESANKSDDRIWVTEHFSGIMVKEFKDLPALLNSSFTLLHLPHYFHGCGHAVYNNSLYYHKGGSNTIVRFEFGKETPQTLKLENALYFDRKYLFANSKTYFNIAVDEKGIWIIYASSVDGSSILVAQLDERTFSVTQHINTTYPKSKAGNAFIARGILYVTDTKDTRVTFAFDLLGGKQINANFDFRMSQSVLAMLSYNMRDQHLYSWEDGHLMLYPVQFLSAASSQR
uniprot
proteins
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 (PubMed:20188654). 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 (PubMed:20188654). Required, together with NRCAM, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier (PubMed:24719088). {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}.
uniprot
proteins
mass_dalton
59137
uniprot
proteins
mutagenesis
MUTAGEN 91; /note="R->A: Abolishes furin-mediated cleavage and shedding of ectodomain."; /evidence="ECO:0000269|PubMed:17293346"; MUTAGEN 278..279; /note="DD->AA: Abolishes BMP1-mediated cleavage of ectodomain release of olfactomedin-like domain."; /evidence="ECO:0000269|PubMed:17293346
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:17293346}.; PTM: Proteolytic processing by a furin-like protease causes shedding of the ectodomain. Further cleavage by BMP1 releases the olfactomedin-like domain. {ECO:0000269|PubMed:17293346}.
uniprot
proteins
pubmed
12642876
uniprot
proteins
pubmed
16039564
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17293346
uniprot
proteins
pubmed
20188654
uniprot
proteins
pubmed
23897819
uniprot
proteins
pubmed
24719088
uniprot
proteins
pubmed
26121352
uniprot
proteins
sequence_length
549
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17293346}; Single-pass type II membrane protein {ECO:0000305|PubMed:17293346}. Cell projection, axon {ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654}. Note=Localizes to the nodes of Ranvier (PubMed:17293346, PubMed:20188654). Detected at immature heminodes (By similarity). {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654}.; SUBCELLULAR LOCATION: [Gliomedin shedded ectodomain]: Secreted {ECO:0000269|PubMed:17293346}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q80WL1}. Note=Proteolytic processing gives rise to a soluble extracellular domain that is secreted (PubMed:17293346). The gliomedin shedded ectodomain localizes to the nodes of Ranvier (By similarity). {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:17293346}.
uniprot
proteins
transmembrane_region
TRANSMEM 18..38; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins