Mag
entrez
17136
canonical
uniprot
P20917
canonical
ensembl
ENSMUSG00000036634
resolver
ensp
ENSMUSP00000139564
resolver
ensp
ENSMUSP00000139881
resolver
ensp
ENSMUSP00000140526
resolver
ensp
ENSMUSP00000164215
resolver
ensp
ENSMUSP00000164217
resolver
ensp
ENSMUSP00000164219
resolver
ensp
ENSMUSP00000164220
resolver
ensp
ENSMUSP00000164237
resolver
ensp
ENSMUSP00000164240
resolver
ensp
ENSMUSP00000164242
resolver
ensp
ENSMUSP00000164247
resolver
ensp
ENSMUSP00000164248
resolver
ensp
ENSMUSP00000164249
resolver
enst
ENSMUST00000188569
resolver
genesymbol
Mag
resolver
uniprot
A0A087WPR1
resolver
uniprot
A0A087WR94
resolver
uniprot
P16880
resolver
uniprot
Q3ZB60
resolver
uniprot_entry
A0A087WR94_MOUSE
resolver
uniprot_entry
MAG_MOUSE
resolver
uniprot_entry
Q3ZB60_MOUSE
resolver
uniprot_sec
A0A087WPR1
resolver
uniprot_sec
P16880
resolver
amino_acid_sequence
MIFLATLPLFWIMISASRGGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGEDGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIFKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQAQAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKKNVTESSSFSGGDNPHVLYSPEFRISGAPDKYESEKQRLGSERRLLGLRGESPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRVK
uniprot
proteins
function
FUNCTION: Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid-containing gangliosides and to the glycoproteins RTN4R and RTN4RL2 (PubMed:12089450, PubMed:27922006, PubMed:7533044). Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination (PubMed:10625334, PubMed:7516497, PubMed:9262180, PubMed:9469574, PubMed:9482781, PubMed:9482783). Protects motoneurons against apoptosis, also after injury; protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2 (PubMed:26335717). Required to prevent degeneration of myelinated axons in adults; this probably depends on binding to gangliosides on the axon cell membrane (PubMed:15953602, PubMed:19158290). Negative regulator of neurite outgrowth that inhibits axon longitudinal growth (PubMed:12089450, PubMed:19158290, PubMed:27922006). Negative regulator of neurite outgrowth; in dorsal root ganglion neurons the inhibition is mediated primarily via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to neuronal gangliosides (PubMed:17640868). In cerebellar granule cells the inhibition is mediated via binding to neuronal gangliosides (PubMed:17640868). In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides (By similarity). Inhibits axon outgrowth by binding to RTN4R (PubMed:12089450). Preferentially binds to alpha-2,3-linked sialic acid (PubMed:27922006, PubMed:7533044). Binds ganglioside Gt1b (PubMed:27922006). {ECO:0000250|UniProtKB:P07722, ECO:0000269|PubMed:10625334, ECO:0000269|PubMed:12089450, ECO:0000269|PubMed:15953602, ECO:0000269|PubMed:17640868, ECO:0000269|PubMed:19158290, ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:27922006, ECO:0000269|PubMed:7516497, ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9262180, ECO:0000269|PubMed:9469574, ECO:0000269|PubMed:9482781, ECO:0000269|PubMed:9482783}.
uniprot
proteins
mass_dalton
69388
uniprot
proteins
mutagenesis
MUTAGEN 25; /note="W->Q: Abolishes C-linked mannosylation."; /evidence="ECO:0000269|PubMed:27922006"; MUTAGEN 65; /note="Y->A: Decreases ganglioside binding."; /evidence="ECO:0000269|PubMed:27922006"; MUTAGEN 118..120; /note="RGD->KGE: Abolishes protection against axon degeneration."; /evidence="ECO:0000269|PubMed:19158290"; MUTAGEN 118; /note="R->A: Abolishes ganglioside binding."; /evidence="ECO:0000269|PubMed:27922006"; MUTAGEN 127; /note="Y->A: Abolishes ganglioside binding."; /evidence="ECO:0000269|PubMed:27922006"; MUTAGEN 128; /note="T->A: Abolishes ganglioside binding."; /evidence="ECO:0000269|PubMed:27922006"; MUTAGEN 406; /note="N->Q: Increases homodimerization."; /evidence="ECO:0000269|PubMed:27922006"; MUTAGEN 473; /note="I->E: Abolishes homodimerization."; /evidence="ECO:0000269|PubMed:27922006
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:1716323, ECO:0000269|PubMed:27922006}.; PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:P07722}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000269|PubMed:24191038}.
uniprot
proteins
protein_family
Immunoglobulin superfamily
uniprot
proteins
protein_family
SIGLEC (sialic acid binding Ig-like lectin) family
uniprot
proteins
pubmed
10625334
uniprot
proteins
pubmed
12089450
uniprot
proteins
pubmed
12558975
uniprot
proteins
pubmed
15953602
uniprot
proteins
pubmed
1712586
uniprot
proteins
pubmed
1716323
uniprot
proteins
pubmed
17640868
uniprot
proteins
pubmed
19158290
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24191038
uniprot
proteins
pubmed
2474006
uniprot
proteins
pubmed
2482022
uniprot
proteins
pubmed
26335717
uniprot
proteins
pubmed
27922006
uniprot
proteins
pubmed
39327467
uniprot
proteins
pubmed
7516497
uniprot
proteins
pubmed
7533044
uniprot
proteins
pubmed
9262180
uniprot
proteins
pubmed
9469574
uniprot
proteins
pubmed
9482781
uniprot
proteins
pubmed
9482783
uniprot
proteins
sequence_length
627
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:39327467, ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9482783}; Single-pass type I membrane protein {ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9482783}. Membrane raft {ECO:0000250|UniProtKB:P07722}.
uniprot
proteins
transmembrane_region
TRANSMEM 517..536; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins