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Myelin-associated glycoprotein (Siglec-4a)

 MAG_MOUSE               Reviewed;         626 AA.
P20917; P16880;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
25-OCT-2017, entry version 169.
RecName: Full=Myelin-associated glycoprotein;
AltName: Full=Siglec-4a;
Flags: Precursor;
Name=Mag;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE (ISOFORMS L-MAG AND S-MAG).
PubMed=2482022; DOI=10.1016/0006-291X(89)92724-1;
Fujita N., Sato S., Kurihara T., Kuwano R., Sakimura K., Inuzuka T.,
Takahashi Y., Miyatake T.;
"cDNA cloning of mouse myelin-associated glycoprotein: a novel
alternative splicing pattern.";
Biochem. Biophys. Res. Commun. 165:1162-1169(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM S-MAG).
TISSUE=Brain;
PubMed=1712586; DOI=10.1016/0006-291X(91)91811-P;
Nakano R., Fujita N., Sato S., Inuzuka T., Sakimura K., Ishiguro H.,
Mishina M., Miyatake T.;
"Structure of mouse myelin-associated glycoprotein gene.";
Biochem. Biophys. Res. Commun. 178:282-290(1991).
[3]
PROTEIN SEQUENCE OF 78-88 AND 466-477, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
TISSUE SPECIFICITY.
PubMed=2474006; DOI=10.1002/cne.902840310;
Bartsch U., Kirchhoff F., Schachner M.;
"Immunohistological localization of the adhesion molecules L1, N-CAM,
and MAG in the developing and adult optic nerve of mice.";
J. Comp. Neurol. 284:451-462(1989).
[5]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
PubMed=1716323; DOI=10.1002/jnr.490290202;
Pedraza L., Frey A.B., Hempstead B.L., Colman D.R., Salzer J.L.;
"Differential expression of MAG isoforms during development.";
J. Neurosci. Res. 29:141-148(1991).
[6]
FUNCTION, SIALIC ACID-BINDING, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=7533044; DOI=10.1016/S0960-9822(00)00220-7;
Kelm S., Pelz A., Schauer R., Filbin M.T., Tang S., de Bellard M.E.,
Schnaar R.L., Mahoney J.A., Hartnell A., Bradfield P., Crocker P.R.;
"Sialoadhesin, myelin-associated glycoprotein and CD22 define a new
family of sialic acid-dependent adhesion molecules of the
immunoglobulin superfamily.";
Curr. Biol. 4:965-972(1994).
[7]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=7516497; DOI=10.1038/369747a0;
Li C., Tropak M.B., Gerlai R., Clapoff S., Abramow-Newerly W.,
Trapp B., Peterson A., Roder J.;
"Myelination in the absence of myelin-associated glycoprotein.";
Nature 369:747-750(1994).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9262180; DOI=10.1016/S0006-8993(97)00484-8;
Bartsch S., Montag D., Schachner M., Bartsch U.;
"Increased number of unmyelinated axons in optic nerves of adult mice
deficient in the myelin-associated glycoprotein (MAG).";
Brain Res. 762:231-234(1997).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9482781;
Yin X., Crawford T.O., Griffin J.W., Tu P.-H., Lee V.M., Li C.,
Roder J., Trapp B.D.;
"Myelin-associated glycoprotein is a myelin signal that modulates the
caliber of myelinated axons.";
J. Neurosci. 18:1953-1962(1998).
[10]
FUNCTION (ISOFORM L-MAG), TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
TOPOLOGY, AND DOMAIN.
PubMed=9482783;
Fujita N., Kemper A., Dupree J., Nakayasu H., Bartsch U.,
Schachner M., Maeda N., Suzuki K., Popko B.;
"The cytoplasmic domain of the large myelin-associated glycoprotein
isoform is needed for proper CNS but not peripheral nervous system
myelination.";
J. Neurosci. 18:1970-1978(1998).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9469574;
DOI=10.1002/(SICI)1097-4547(19980115)51:2<210::AID-JNR9>3.0.CO;2-G;
Li C., Trapp B., Ludwin S., Peterson A., Roder J.;
"Myelin associated glycoprotein modulates glia-axon contact in vivo.";
J. Neurosci. Res. 51:210-217(1998).
[12]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10625334;
DOI=10.1002/(SICI)1098-1136(20000115)29:2<154::AID-GLIA9>3.0.CO;2-3;
Schachner M., Bartsch U.;
"Multiple functions of the myelin-associated glycoprotein MAG (siglec-
4a) in formation and maintenance of myelin.";
Glia 29:154-165(2000).
[13]
FUNCTION, AND INTERACTION WITH RTN4R.
PubMed=12089450; DOI=10.1126/science.1073031;
Liu B.P., Fournier A., GrandPre T., Strittmatter S.M.;
"Myelin-associated glycoprotein as a functional ligand for the Nogo-66
receptor.";
Science 297:1190-1193(2002).
[14]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15953602; DOI=10.1016/j.expneurol.2005.04.017;
Pan B., Fromholt S.E., Hess E.J., Crawford T.O., Griffin J.W.,
Sheikh K.A., Schnaar R.L.;
"Myelin-associated glycoprotein and complementary axonal ligands,
gangliosides, mediate axon stability in the CNS and PNS:
neuropathology and behavioral deficits in single- and double-null
mice.";
Exp. Neurol. 195:208-217(2005).
[15]
FUNCTION.
PubMed=17640868; DOI=10.1074/jbc.M704055200;
Mehta N.R., Lopez P.H., Vyas A.A., Schnaar R.L.;
"Gangliosides and Nogo receptors independently mediate myelin-
associated glycoprotein inhibition of neurite outgrowth in different
nerve cells.";
J. Biol. Chem. 282:27875-27886(2007).
[16]
DISRUPTION PHENOTYPE, FUNCTION, DOMAIN, AND MUTAGENESIS OF
118-ARG--ASP-120.
PubMed=19158290; DOI=10.1523/JNEUROSCI.5204-08.2009;
Nguyen T., Mehta N.R., Conant K., Kim K.J., Jones M., Calabresi P.A.,
Melli G., Hoke A., Schnaar R.L., Ming G.L., Song H., Keswani S.C.,
Griffin J.W.;
"Axonal protective effects of the myelin-associated glycoprotein.";
J. Neurosci. 29:630-637(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
DISRUPTION PHENOTYPE, FUNCTION, DOMAIN, AND INTERACTION WITH RTN4R AND
RTN4RL2.
PubMed=26335717; DOI=10.1038/cddis.2015.228;
Palandri A., Salvador V.R., Wojnacki J., Vivinetto A.L., Schnaar R.L.,
Lopez P.H.;
"Myelin-associated glycoprotein modulates apoptosis of motoneurons
during early postnatal development via NgR/p75(NTR) receptor-mediated
activation of RhoA signaling pathways.";
Cell Death Dis. 6:E1876-E1876(2015).
[19]
X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 20-325, X-RAY
CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 20-508 IN COMPLEX WITH
N-ACETYLNEURAMINYL-N-ACETYLLACTOSAMINE, FUNCTION, DISULFIDE BONDS,
GLYCOSYLATION AT TRP-22; ASN-99; ASN-223; ASN-246; ASN-315; ASN-332;
ASN-406; ASN-450 AND ASN-454, IDENTIFICATION BY MASS SPECTROMETRY,
SUBUNIT, AND MUTAGENESIS OF TRP-25; TYR-65; ARG-118; TYR-127; THR-128;
ASN-406 AND ILE-473.
PubMed=27922006; DOI=10.1038/ncomms13584;
Pronker M.F., Lemstra S., Snijder J., Heck A.J., Thies-Weesie D.M.,
Pasterkamp R.J., Janssen B.J.;
"Structural basis of myelin-associated glycoprotein adhesion and
signalling.";
Nat. Commun. 7:13584-13584(2016).
-!- 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:7533044, PubMed:12089450, PubMed:27922006). Not required
for initial myelination, but seems to play a role in the
maintenance of normal axon myelination (PubMed:7516497,
PubMed:9262180, PubMed:9482781, PubMed:9482783, PubMed:9469574,
PubMed:10625334). 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:19158290, PubMed:27922006, PubMed:12089450). 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:7533044, PubMed:27922006). 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}.
-!- SUBUNIT: Monomer and homodimer (PubMed:27922006). Interacts (via
the first three N-terminal Ig-like domains) with RTN4R and RTN4RL2
(PubMed:12089450, PubMed:26335717). {ECO:0000269|PubMed:12089450,
ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:27922006}.
-!- SUBCELLULAR LOCATION: Cell membrane {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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=L-MAG;
IsoId=P20917-1; Sequence=Displayed;
Name=S-MAG;
IsoId=P20917-2; Sequence=VSP_002527, VSP_002528;
-!- TISSUE SPECIFICITY: Detected in the myelin tract in brain,
especially in the corpus callosum and in peripheral nerve
(PubMed:7516497, PubMed:9482783). Expressed by myelinating glial
cells in the central and peripheral nervous system
(PubMed:10625334). Detected in oligodendrocyte processes before
formation of compact myelin (PubMed:2474006, PubMed:10625334).
Restricted to the periaxonal space after myelination
(PubMed:10625334). Isoform S-MAG is the predominant isoform in CNS
and PNS of the adult (at protein level) (PubMed:1716323).
{ECO:0000269|PubMed:10625334, ECO:0000269|PubMed:1716323,
ECO:0000269|PubMed:2474006, ECO:0000269|PubMed:7516497,
ECO:0000269|PubMed:9482783}.
-!- DEVELOPMENTAL STAGE: In CNS isoform L-MAG is the major form
synthesized early in development, and it persists as a significant
proportion of the MAG present in the adult. In the PNS isoform L-
MAG is expressed at modest levels during development; it is absent
in the adult. {ECO:0000269|PubMed:1716323}.
-!- DOMAIN: The C-terminal cytoplasmic region found only in isoform L-
MAG is required for normal myelination in the central nervous
system (CNS), but is apparently not required for normal
myelination in the peripheral nervous system (PNS).
{ECO:0000269|PubMed:9482783}.
-!- DOMAIN: The extracellular domain is required to protect against
axon degeneration (PubMed:19158290, PubMed:26335717). The first
three Ig-like domains mediate interaction with RTN4R and RTN4RL2,
but are not sufficient to inhibit neurite outgrowth (By
similarity). The two C-terminal extracellular Ig-like C2-type
domains are required for inhibition of axon longitudinal growth.
Besides, the two C-terminal extracellular Ig-like C2-type domains
are required for protection against apoptosis after nerve injury
(PubMed:26335717). {ECO:0000250|UniProtKB:P07722,
ECO:0000269|PubMed:19158290, ECO:0000269|PubMed:26335717}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:1716323,
ECO:0000269|PubMed:27922006}.
-!- PTM: Phosphorylated on tyrosine residues.
{ECO:0000250|UniProtKB:P07722}.
-!- DISRUPTION PHENOTYPE: Mutant mice appear normal, excepting subtle
defects in motor coordination and a slight intention tremor
(PubMed:7516497). They have similar numbers of motoneurons as
wild-type at birth, but display an important loss of motoneurons
during the first week after birth (PubMed:26335717).Five month old
mutant mice display a decreased ability to remain on a rotating
cylinder (PubMed:15953602). Contrary to wild-type, about 40% of
mutant mice have severe episodes of whole-body tremor, both during
movement and when resting (PubMed:15953602). The myelination in
brain and around peripheral nerves appears grossly normal in young
animals, but the periaxonal cytoplasmic collar is often missing in
optic nerve (PubMed:7516497, PubMed:9262180, PubMed:9482781,
PubMed:9469574). When present, the cytoplasm of the periaxonal
collar has generally a disorganized aspect (PubMed:7516497).
Mutant mice have an increased percentage of unmyelinated axons in
optic nerve (PubMed:9262180, PubMed:9469574). Besides, a small
proportion of nerves from mutant mice display redundant
myelination, and also rare cases of multiple myelination, where
axons are surrounded by two or more compact myelin sheets
(PubMed:9469574). Sciatic nerves from over three month old mutant
mice show signs of Wallerian degeneration, with redundant myelin,
degeneration of myelinated fibers, and an apparent decrease in the
diameter of myelinated axons (PubMed:9482781, PubMed:15953602).
The distances between neurofilaments in myelinated axons from over
3 month old mice are shorter than normal (PubMed:9482781,
PubMed:15953602). With increasing age, mutant mice display
progressive axon degeneration in the spinal cord and sciatic
nerve, resulting in a decrease of 28% in the number of spinal cord
axons after 15 months (PubMed:19158290). Mutant mice display
increased motoneuron apoptosis after injury (PubMed:26335717).
Likewise, they display strongly increased axon degeneration after
treatment with the neurotoxin acrylamide (PubMed:19158290). Mutant
mice display much more severe axon loss in response to
experimental autoimmune encephalitis (PubMed:19158290).
{ECO:0000269|PubMed:15953602, ECO:0000269|PubMed:19158290,
ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:7516497,
ECO:0000269|PubMed:9262180, ECO:0000269|PubMed:9469574,
ECO:0000269|PubMed:9482781}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC
(sialic acid binding Ig-like lectin) family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Siglec-4;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_196";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Siglec-4a [3 Fc Domains];
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_00003";
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EMBL; M31811; AAA39487.1; -; mRNA.
EMBL; M74793; AAA91743.1; -; Genomic_DNA.
EMBL; M74783; AAA91743.1; JOINED; Genomic_DNA.
EMBL; M74784; AAA91743.1; JOINED; Genomic_DNA.
EMBL; M74785; AAA91743.1; JOINED; Genomic_DNA.
EMBL; M74786; AAA91743.1; JOINED; Genomic_DNA.
EMBL; M74787; AAA91743.1; JOINED; Genomic_DNA.
EMBL; M74788; AAA91743.1; JOINED; Genomic_DNA.
EMBL; M74790; AAA91743.1; JOINED; Genomic_DNA.
EMBL; M74791; AAA91743.1; JOINED; Genomic_DNA.
CCDS; CCDS21115.1; -. [P20917-2]
PIR; B33785; B33785.
RefSeq; NP_001333015.1; NM_001346086.1. [P20917-2]
RefSeq; NP_001333016.1; NM_001346087.1. [P20917-2]
RefSeq; NP_001333017.1; NM_001346088.1. [P20917-2]
RefSeq; NP_034888.1; NM_010758.3. [P20917-2]
RefSeq; XP_011248743.1; XM_011250441.2. [P20917-2]
RefSeq; XP_017177497.1; XM_017322008.1. [P20917-2]
UniGene; Mm.241355; -.
PDB; 5LF5; X-ray; 3.80 A; A=20-508.
PDB; 5LFR; X-ray; 2.12 A; A/B=20-325.
PDB; 5LFU; X-ray; 4.30 A; A=20-508.
PDB; 5LFV; X-ray; 2.30 A; A/B=20-325.
PDBsum; 5LF5; -.
PDBsum; 5LFR; -.
PDBsum; 5LFU; -.
PDBsum; 5LFV; -.
ProteinModelPortal; P20917; -.
SMR; P20917; -.
BioGrid; 201285; 1.
IntAct; P20917; 4.
MINT; MINT-202735; -.
STRING; 10090.ENSMUSP00000041464; -.
BindingDB; P20917; -.
ChEMBL; CHEMBL1250416; -.
iPTMnet; P20917; -.
PhosphoSitePlus; P20917; -.
SwissPalm; P20917; -.
MaxQB; P20917; -.
PaxDb; P20917; -.
PeptideAtlas; P20917; -.
PRIDE; P20917; -.
Ensembl; ENSMUST00000040548; ENSMUSP00000041464; ENSMUSG00000036634. [P20917-2]
Ensembl; ENSMUST00000187137; ENSMUSP00000139564; ENSMUSG00000036634. [P20917-2]
GeneID; 17136; -.
KEGG; mmu:17136; -.
UCSC; uc009ghb.1; mouse. [P20917-2]
CTD; 4099; -.
MGI; MGI:96912; Mag.
eggNOG; ENOG410KDW4; Eukaryota.
eggNOG; ENOG410XQVV; LUCA.
GeneTree; ENSGT00760000119139; -.
HOGENOM; HOG000113464; -.
HOVERGEN; HBG006317; -.
InParanoid; P20917; -.
KO; K06771; -.
PhylomeDB; P20917; -.
TreeFam; TF332441; -.
Reactome; R-MMU-193634; Axonal growth inhibition (RHOA activation).
Reactome; R-MMU-210991; Basigin interactions.
PRO; PR:P20917; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000036634; -.
CleanEx; MM_MAG; -.
ExpressionAtlas; P20917; baseline and differential.
Genevisible; P20917; MM.
GO; GO:0043218; C:compact myelin; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0097453; C:mesaxon; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:1905576; F:ganglioside GT1b binding; IMP:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0033691; F:sialic acid binding; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0022010; P:central nervous system myelination; IMP:UniProtKB.
GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:0031643; P:positive regulation of myelination; IMP:CACAO.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF08205; C2-set_2; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Lectin; Lipid-binding;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 19
CHAIN 20 626 Myelin-associated glycoprotein.
/FTId=PRO_0000014857.
TOPO_DOM 20 516 Extracellular. {ECO:0000255}.
TRANSMEM 517 536 Helical. {ECO:0000255}.
TOPO_DOM 537 626 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 120 Ig-like V-type.
DOMAIN 139 237 Ig-like C2-type 1.
DOMAIN 241 325 Ig-like C2-type 2.
DOMAIN 327 412 Ig-like C2-type 3.
DOMAIN 413 508 Ig-like C2-type 4.
REGION 20 325 Interaction with RTN4R and RTN4RL2.
{ECO:0000250|UniProtKB:P07722}.
REGION 65 67 Ganglioside GT1b binding.
{ECO:0000269|PubMed:27922006}.
REGION 124 128 Ganglioside GT1b binding.
{ECO:0000269|PubMed:27922006}.
REGION 577 626 Required for normal axon myelination in
the central nervous system.
{ECO:0000269|PubMed:9482783}.
BINDING 118 118 Ganglioside GT1b.
{ECO:0000269|PubMed:27922006}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000250|UniProtKB:P07722}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000250|UniProtKB:P07722}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000250|UniProtKB:P07722}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
LIPID 531 531 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P07722}.
CARBOHYD 22 22 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:27922006}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27922006}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27922006}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27922006}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27922006}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27922006}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27922006}.
CARBOHYD 450 450 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27922006}.
CARBOHYD 454 454 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27922006}.
DISULFID 37 165 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:27922006}.
DISULFID 42 100 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:27922006}.
DISULFID 159 217 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:27922006}.
DISULFID 261 305 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:27922006}.
DISULFID 347 392 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:27922006}.
DISULFID 421 430 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:27922006}.
DISULFID 432 488 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:27922006}.
VAR_SEQ 574 582 EKRLGSERR -> REVSTRDCH (in isoform S-
MAG). {ECO:0000305}.
/FTId=VSP_002527.
VAR_SEQ 583 626 Missing (in isoform S-MAG).
{ECO:0000305}.
/FTId=VSP_002528.
MUTAGEN 25 25 W->Q: Abolishes C-linked mannosylation.
{ECO:0000269|PubMed:27922006}.
MUTAGEN 65 65 Y->A: Decreases ganglioside binding.
{ECO:0000269|PubMed:27922006}.
MUTAGEN 118 120 RGD->KGE: Abolishes protection against
axon degeneration.
{ECO:0000269|PubMed:19158290}.
MUTAGEN 118 118 R->A: Abolishes ganglioside binding.
{ECO:0000269|PubMed:27922006}.
MUTAGEN 127 127 Y->A: Abolishes ganglioside binding.
{ECO:0000269|PubMed:27922006}.
MUTAGEN 128 128 T->A: Abolishes ganglioside binding.
{ECO:0000269|PubMed:27922006}.
MUTAGEN 406 406 N->Q: Increases homodimerization.
{ECO:0000269|PubMed:27922006}.
MUTAGEN 473 473 I->E: Abolishes homodimerization.
{ECO:0000269|PubMed:27922006}.
STRAND 22 25 {ECO:0000244|PDB:5LFR}.
STRAND 28 33 {ECO:0000244|PDB:5LFR}.
STRAND 38 40 {ECO:0000244|PDB:5LFR}.
STRAND 43 45 {ECO:0000244|PDB:5LFR}.
HELIX 48 50 {ECO:0000244|PDB:5LFV}.
STRAND 56 62 {ECO:0000244|PDB:5LFR}.
STRAND 72 75 {ECO:0000244|PDB:5LFR}.
TURN 76 78 {ECO:0000244|PDB:5LFR}.
HELIX 83 85 {ECO:0000244|PDB:5LFR}.
TURN 86 88 {ECO:0000244|PDB:5LFR}.
STRAND 89 91 {ECO:0000244|PDB:5LFR}.
HELIX 95 97 {ECO:0000244|PDB:5LFR}.
STRAND 102 104 {ECO:0000244|PDB:5LFR}.
HELIX 109 111 {ECO:0000244|PDB:5LFR}.
STRAND 113 120 {ECO:0000244|PDB:5LFR}.
STRAND 126 128 {ECO:0000244|PDB:5LFR}.
STRAND 133 140 {ECO:0000244|PDB:5LFR}.
STRAND 142 144 {ECO:0000244|PDB:5LFR}.
STRAND 155 162 {ECO:0000244|PDB:5LFR}.
STRAND 171 176 {ECO:0000244|PDB:5LFR}.
HELIX 178 180 {ECO:0000244|PDB:5LFR}.
STRAND 184 190 {ECO:0000244|PDB:5LFR}.
HELIX 192 194 {ECO:0000244|PDB:5LFR}.
STRAND 196 204 {ECO:0000244|PDB:5LFR}.
HELIX 208 210 {ECO:0000244|PDB:5LFR}.
STRAND 214 220 {ECO:0000244|PDB:5LFR}.
STRAND 227 233 {ECO:0000244|PDB:5LFR}.
STRAND 236 245 {ECO:0000244|PDB:5LFR}.
STRAND 248 252 {ECO:0000244|PDB:5LFR}.
STRAND 257 267 {ECO:0000244|PDB:5LFR}.
STRAND 270 275 {ECO:0000244|PDB:5LFR}.
STRAND 278 292 {ECO:0000244|PDB:5LFR}.
HELIX 297 299 {ECO:0000244|PDB:5LFR}.
STRAND 301 309 {ECO:0000244|PDB:5LFR}.
STRAND 312 324 {ECO:0000244|PDB:5LFR}.
SEQUENCE 626 AA; 69260 MW; 9C797BD6B52B6057 CRC64;
MIFLATLPLF WIMISASRGG HWGAWMPSTI SAFEGTCVSI PCRFDFPDEL RPAVVHGVWY
FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSTLSPE LGGKYYFRGD
LGGYNQYTFS EHSVLDIVNT PNIVVPPEVV AGTEVEVSCM VPDNCPELRP ELSWLGHEGL
GEPTVLGRLR EDEGTWVQVS LLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP
VIVEMNSSVE AIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAKSLYL DLEEVTPGED
GVYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ SNPDPILTIF
KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ RATAFNLSVE FAPIILLESH
CAAARDTVQC LCVVKSNPEP SVAFELPSRN VTVNETEREF VYSERSGLLL TSILTIRGQA
QAPPRVICTS RNLYGTQSLE LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK
NVTESSSFSG GDNPHVLYSP EFRISGAPDK YESEKRLGSE RRLLGLRGES PELDLSYSHS
DLGKRPTKDS YTLTEELAEY AEIRVK


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