MAG_MOUSE
ID MAG_MOUSE Reviewed; 627 AA.
AC P20917; A0A087WPR1; P16880;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Myelin-associated glycoprotein;
DE AltName: Full=Siglec-4a;
DE Flags: Precursor;
GN Name=Mag;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L-MAG AND S-MAG).
RX PubMed=2482022; DOI=10.1016/0006-291x(89)92724-1;
RA Fujita N., Sato S., Kurihara T., Kuwano R., Sakimura K., Inuzuka T.,
RA Takahashi Y., Miyatake T.;
RT "cDNA cloning of mouse myelin-associated glycoprotein: a novel alternative
RT splicing pattern.";
RL Biochem. Biophys. Res. Commun. 165:1162-1169(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM S-MAG).
RC TISSUE=Brain;
RX PubMed=1712586; DOI=10.1016/0006-291x(91)91811-p;
RA Nakano R., Fujita N., Sato S., Inuzuka T., Sakimura K., Ishiguro H.,
RA Mishina M., Miyatake T.;
RT "Structure of mouse myelin-associated glycoprotein gene.";
RL Biochem. Biophys. Res. Commun. 178:282-290(1991).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PROTEIN SEQUENCE OF 78-88 AND 466-477, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=2474006; DOI=10.1002/cne.902840310;
RA Bartsch U., Kirchhoff F., Schachner M.;
RT "Immunohistological localization of the adhesion molecules L1, N-CAM, and
RT MAG in the developing and adult optic nerve of mice.";
RL J. Comp. Neurol. 284:451-462(1989).
RN [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=1716323; DOI=10.1002/jnr.490290202;
RA Pedraza L., Frey A.B., Hempstead B.L., Colman D.R., Salzer J.L.;
RT "Differential expression of MAG isoforms during development.";
RL J. Neurosci. Res. 29:141-148(1991).
RN [7]
RP FUNCTION, SIALIC ACID-BINDING, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=7533044; DOI=10.1016/s0960-9822(00)00220-7;
RA Kelm S., Pelz A., Schauer R., Filbin M.T., Tang S., de Bellard M.E.,
RA Schnaar R.L., Mahoney J.A., Hartnell A., Bradfield P., Crocker P.R.;
RT "Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family
RT of sialic acid-dependent adhesion molecules of the immunoglobulin
RT superfamily.";
RL Curr. Biol. 4:965-972(1994).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7516497; DOI=10.1038/369747a0;
RA Li C., Tropak M.B., Gerlai R., Clapoff S., Abramow-Newerly W., Trapp B.,
RA Peterson A., Roder J.;
RT "Myelination in the absence of myelin-associated glycoprotein.";
RL Nature 369:747-750(1994).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9262180; DOI=10.1016/s0006-8993(97)00484-8;
RA Bartsch S., Montag D., Schachner M., Bartsch U.;
RT "Increased number of unmyelinated axons in optic nerves of adult mice
RT deficient in the myelin-associated glycoprotein (MAG).";
RL Brain Res. 762:231-234(1997).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9482781; DOI=10.1523/jneurosci.18-06-01953.1998;
RA Yin X., Crawford T.O., Griffin J.W., Tu P.-H., Lee V.M., Li C., Roder J.,
RA Trapp B.D.;
RT "Myelin-associated glycoprotein is a myelin signal that modulates the
RT caliber of myelinated axons.";
RL J. Neurosci. 18:1953-1962(1998).
RN [11]
RP FUNCTION (ISOFORM L-MAG), TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND DOMAIN.
RX PubMed=9482783; DOI=10.1523/jneurosci.18-06-01970.1998;
RA Fujita N., Kemper A., Dupree J., Nakayasu H., Bartsch U., Schachner M.,
RA Maeda N., Suzuki K., Popko B.;
RT "The cytoplasmic domain of the large myelin-associated glycoprotein isoform
RT is needed for proper CNS but not peripheral nervous system myelination.";
RL J. Neurosci. 18:1970-1978(1998).
RN [12]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9469574;
RX DOI=10.1002/(sici)1097-4547(19980115)51:2<210::aid-jnr9>3.0.co;2-g;
RA Li C., Trapp B., Ludwin S., Peterson A., Roder J.;
RT "Myelin associated glycoprotein modulates glia-axon contact in vivo.";
RL J. Neurosci. Res. 51:210-217(1998).
RN [13]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10625334;
RX DOI=10.1002/(sici)1098-1136(20000115)29:2<154::aid-glia9>3.0.co;2-3;
RA Schachner M., Bartsch U.;
RT "Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a)
RT in formation and maintenance of myelin.";
RL Glia 29:154-165(2000).
RN [14]
RP FUNCTION, AND INTERACTION WITH RTN4R.
RX PubMed=12089450; DOI=10.1126/science.1073031;
RA Liu B.P., Fournier A., GrandPre T., Strittmatter S.M.;
RT "Myelin-associated glycoprotein as a functional ligand for the Nogo-66
RT receptor.";
RL Science 297:1190-1193(2002).
RN [15]
RP INTERACTION WITH BSG.
RX PubMed=12558975; DOI=10.1046/j.1471-4159.2003.01537.x;
RA Heller M., von der Ohe M., Kleene R., Mohajeri M.H., Schachner M.;
RT "The immunoglobulin-superfamily molecule basigin is a binding protein for
RT oligomannosidic carbohydrates: an anti-idiotypic approach.";
RL J. Neurochem. 84:557-565(2003).
RN [16]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15953602; DOI=10.1016/j.expneurol.2005.04.017;
RA Pan B., Fromholt S.E., Hess E.J., Crawford T.O., Griffin J.W., Sheikh K.A.,
RA Schnaar R.L.;
RT "Myelin-associated glycoprotein and complementary axonal ligands,
RT gangliosides, mediate axon stability in the CNS and PNS: neuropathology and
RT behavioral deficits in single- and double-null mice.";
RL Exp. Neurol. 195:208-217(2005).
RN [17]
RP FUNCTION.
RX PubMed=17640868; DOI=10.1074/jbc.m704055200;
RA Mehta N.R., Lopez P.H., Vyas A.A., Schnaar R.L.;
RT "Gangliosides and Nogo receptors independently mediate myelin-associated
RT glycoprotein inhibition of neurite outgrowth in different nerve cells.";
RL J. Biol. Chem. 282:27875-27886(2007).
RN [18]
RP DISRUPTION PHENOTYPE, FUNCTION, DOMAIN, AND MUTAGENESIS OF
RP 118-ARG--ASP-120.
RX PubMed=19158290; DOI=10.1523/jneurosci.5204-08.2009;
RA Nguyen T., Mehta N.R., Conant K., Kim K.J., Jones M., Calabresi P.A.,
RA Melli G., Hoke A., Schnaar R.L., Ming G.L., Song H., Keswani S.C.,
RA Griffin J.W.;
RT "Axonal protective effects of the myelin-associated glycoprotein.";
RL J. Neurosci. 29:630-637(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [20]
RP TISSUE SPECIFICITY, AND UBIQUITINATION.
RX PubMed=24191038; DOI=10.1073/pnas.1318501110;
RA Shin D., Lin S.T., Fu Y.H., Ptacek L.J.;
RT "Very large G protein-coupled receptor 1 regulates myelin-associated
RT glycoprotein via Galphas/Galphaq-mediated protein kinases A/C.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19101-19106(2013).
RN [21]
RP DISRUPTION PHENOTYPE, FUNCTION, DOMAIN, AND INTERACTION WITH RTN4R AND
RP RTN4RL2.
RX PubMed=26335717; DOI=10.1038/cddis.2015.228;
RA Palandri A., Salvador V.R., Wojnacki J., Vivinetto A.L., Schnaar R.L.,
RA Lopez P.H.;
RT "Myelin-associated glycoprotein modulates apoptosis of motoneurons during
RT early postnatal development via NgR/p75(NTR) receptor-mediated activation
RT of RhoA signaling pathways.";
RL Cell Death Dis. 6:E1876-E1876(2015).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 20-325, X-RAY CRYSTALLOGRAPHY
RP (3.80 ANGSTROMS) OF 20-508 IN COMPLEX WITH
RP N-ACETYLNEURAMINYL-N-ACETYLLACTOSAMINE, FUNCTION, DISULFIDE BONDS,
RP GLYCOSYLATION AT TRP-22; ASN-99; ASN-223; ASN-246; ASN-315; ASN-332;
RP ASN-406; ASN-450 AND ASN-454, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT,
RP AND MUTAGENESIS OF TRP-25; TYR-65; ARG-118; TYR-127; THR-128; ASN-406 AND
RP ILE-473.
RX PubMed=27922006; DOI=10.1038/ncomms13584;
RA Pronker M.F., Lemstra S., Snijder J., Heck A.J., Thies-Weesie D.M.,
RA Pasterkamp R.J., Janssen B.J.;
RT "Structural basis of myelin-associated glycoprotein adhesion and
RT signalling.";
RL Nat. Commun. 7:13584-13584(2016).
CC -!- FUNCTION: Adhesion molecule that mediates interactions between
CC myelinating cells and neurons by binding to neuronal sialic acid-
CC containing gangliosides and to the glycoproteins RTN4R and RTN4RL2
CC (PubMed:7533044, PubMed:12089450, PubMed:27922006). Not required for
CC initial myelination, but seems to play a role in the maintenance of
CC normal axon myelination (PubMed:7516497, PubMed:9262180,
CC PubMed:9482781, PubMed:9482783, PubMed:9469574, PubMed:10625334).
CC Protects motoneurons against apoptosis, also after injury; protection
CC against apoptosis is probably mediated via interaction with neuronal
CC RTN4R and RTN4RL2 (PubMed:26335717). Required to prevent degeneration
CC of myelinated axons in adults; this probably depends on binding to
CC gangliosides on the axon cell membrane (PubMed:15953602,
CC PubMed:19158290). Negative regulator of neurite outgrowth that inhibits
CC axon longitudinal growth (PubMed:19158290, PubMed:27922006,
CC PubMed:12089450). Negative regulator of neurite outgrowth; in dorsal
CC root ganglion neurons the inhibition is mediated primarily via binding
CC to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to
CC neuronal gangliosides (PubMed:17640868). In cerebellar granule cells
CC the inhibition is mediated via binding to neuronal gangliosides
CC (PubMed:17640868). In sensory neurons, inhibition of neurite extension
CC depends only partially on RTN4R, RTN4RL2 and gangliosides (By
CC similarity). Inhibits axon outgrowth by binding to RTN4R
CC (PubMed:12089450). Preferentially binds to alpha-2,3-linked sialic acid
CC (PubMed:7533044, PubMed:27922006). Binds ganglioside Gt1b
CC (PubMed:27922006). {ECO:0000250|UniProtKB:P07722,
CC ECO:0000269|PubMed:10625334, ECO:0000269|PubMed:12089450,
CC ECO:0000269|PubMed:15953602, ECO:0000269|PubMed:17640868,
CC ECO:0000269|PubMed:19158290, ECO:0000269|PubMed:26335717,
CC ECO:0000269|PubMed:27922006, ECO:0000269|PubMed:7516497,
CC ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9262180,
CC ECO:0000269|PubMed:9469574, ECO:0000269|PubMed:9482781,
CC ECO:0000269|PubMed:9482783}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:27922006). Interacts (via the
CC first three N-terminal Ig-like domains) with RTN4R and RTN4RL2
CC (PubMed:12089450, PubMed:26335717). Interacts with isoform 2 of BSG
CC (PubMed:12558975). {ECO:0000269|PubMed:12089450,
CC ECO:0000269|PubMed:12558975, ECO:0000269|PubMed:26335717,
CC ECO:0000269|PubMed:27922006}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7533044,
CC ECO:0000269|PubMed:9482783}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9482783}. Membrane raft
CC {ECO:0000250|UniProtKB:P07722}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=L-MAG;
CC IsoId=P20917-1; Sequence=Displayed;
CC Name=S-MAG;
CC IsoId=P20917-2; Sequence=VSP_002527, VSP_002528;
CC -!- TISSUE SPECIFICITY: Detected in the myelin tract in brain, especially
CC in the corpus callosum and in peripheral nerve (PubMed:7516497,
CC PubMed:9482783, PubMed:24191038). Expressed by myelinating glial cells
CC in the central and peripheral nervous system (PubMed:10625334).
CC Detected in oligodendrocyte processes before formation of compact
CC myelin (PubMed:2474006, PubMed:10625334). Restricted to the periaxonal
CC space after myelination (PubMed:10625334). Isoform S-MAG is the
CC predominant isoform in CNS and PNS of the adult (at protein level)
CC (PubMed:1716323). {ECO:0000269|PubMed:10625334,
CC ECO:0000269|PubMed:1716323, ECO:0000269|PubMed:24191038,
CC ECO:0000269|PubMed:2474006, ECO:0000269|PubMed:7516497,
CC ECO:0000269|PubMed:9482783}.
CC -!- DEVELOPMENTAL STAGE: In CNS isoform L-MAG is the major form synthesized
CC early in development, and it persists as a significant proportion of
CC the MAG present in the adult. In the PNS isoform L-MAG is expressed at
CC modest levels during development; it is absent in the adult.
CC {ECO:0000269|PubMed:1716323}.
CC -!- DOMAIN: The C-terminal cytoplasmic region found only in isoform L-MAG
CC is required for normal myelination in the central nervous system (CNS),
CC but is apparently not required for normal myelination in the peripheral
CC nervous system (PNS). {ECO:0000269|PubMed:9482783}.
CC -!- DOMAIN: The extracellular domain is required to protect against axon
CC degeneration (PubMed:19158290, PubMed:26335717). The first three Ig-
CC like domains mediate interaction with RTN4R and RTN4RL2, but are not
CC sufficient to inhibit neurite outgrowth (By similarity). The two C-
CC terminal extracellular Ig-like C2-type domains are required for
CC inhibition of axon longitudinal growth. Besides, the two C-terminal
CC extracellular Ig-like C2-type domains are required for protection
CC against apoptosis after nerve injury (PubMed:26335717).
CC {ECO:0000250|UniProtKB:P07722, ECO:0000269|PubMed:19158290,
CC ECO:0000269|PubMed:26335717}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:1716323,
CC ECO:0000269|PubMed:27922006}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000250|UniProtKB:P07722}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC {ECO:0000269|PubMed:24191038}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice appear normal, excepting subtle
CC defects in motor coordination and a slight intention tremor
CC (PubMed:7516497). They have similar numbers of motoneurons as wild-type
CC at birth, but display an important loss of motoneurons during the first
CC week after birth (PubMed:26335717).Five month old mutant mice display a
CC decreased ability to remain on a rotating cylinder (PubMed:15953602).
CC Contrary to wild-type, about 40% of mutant mice have severe episodes of
CC whole-body tremor, both during movement and when resting
CC (PubMed:15953602). The myelination in brain and around peripheral
CC nerves appears grossly normal in young animals, but the periaxonal
CC cytoplasmic collar is often missing in optic nerve (PubMed:7516497,
CC PubMed:9262180, PubMed:9482781, PubMed:9469574). When present, the
CC cytoplasm of the periaxonal collar has generally a disorganized aspect
CC (PubMed:7516497). Mutant mice have an increased percentage of
CC unmyelinated axons in optic nerve (PubMed:9262180, PubMed:9469574).
CC Besides, a small proportion of nerves from mutant mice display
CC redundant myelination, and also rare cases of multiple myelination,
CC where axons are surrounded by two or more compact myelin sheets
CC (PubMed:9469574). Sciatic nerves from over three month old mutant mice
CC show signs of Wallerian degeneration, with redundant myelin,
CC degeneration of myelinated fibers, and an apparent decrease in the
CC diameter of myelinated axons (PubMed:9482781, PubMed:15953602). The
CC distances between neurofilaments in myelinated axons from over 3 month
CC old mice are shorter than normal (PubMed:9482781, PubMed:15953602).
CC With increasing age, mutant mice display progressive axon degeneration
CC in the spinal cord and sciatic nerve, resulting in a decrease of 28% in
CC the number of spinal cord axons after 15 months (PubMed:19158290).
CC Mutant mice display increased motoneuron apoptosis after injury
CC (PubMed:26335717). Likewise, they display strongly increased axon
CC degeneration after treatment with the neurotoxin acrylamide
CC (PubMed:19158290). Mutant mice display much more severe axon loss in
CC response to experimental autoimmune encephalitis (PubMed:19158290).
CC {ECO:0000269|PubMed:15953602, ECO:0000269|PubMed:19158290,
CC ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:7516497,
CC ECO:0000269|PubMed:9262180, ECO:0000269|PubMed:9469574,
CC ECO:0000269|PubMed:9482781}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-4;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_196";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-4a [3 Fc Domains];
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_00003";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M31811; AAA39487.1; -; mRNA.
DR EMBL; M74793; AAA91743.1; -; Genomic_DNA.
DR EMBL; M74783; AAA91743.1; JOINED; Genomic_DNA.
DR EMBL; M74784; AAA91743.1; JOINED; Genomic_DNA.
DR EMBL; M74785; AAA91743.1; JOINED; Genomic_DNA.
DR EMBL; M74786; AAA91743.1; JOINED; Genomic_DNA.
DR EMBL; M74787; AAA91743.1; JOINED; Genomic_DNA.
DR EMBL; M74788; AAA91743.1; JOINED; Genomic_DNA.
DR EMBL; M74790; AAA91743.1; JOINED; Genomic_DNA.
DR EMBL; M74791; AAA91743.1; JOINED; Genomic_DNA.
DR EMBL; AC165340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS21115.1; -. [P20917-2]
DR CCDS; CCDS90207.1; -. [P20917-1]
DR PIR; B33785; B33785.
DR RefSeq; NP_001333013.1; NM_001346084.1. [P20917-1]
DR RefSeq; NP_001333014.1; NM_001346085.1. [P20917-1]
DR RefSeq; NP_001333015.1; NM_001346086.1. [P20917-2]
DR RefSeq; NP_001333016.1; NM_001346087.1. [P20917-2]
DR RefSeq; NP_001333017.1; NM_001346088.1. [P20917-2]
DR RefSeq; NP_034888.1; NM_010758.3. [P20917-2]
DR RefSeq; XP_006539653.1; XM_006539590.2.
DR RefSeq; XP_006539654.1; XM_006539591.3.
DR RefSeq; XP_011248740.1; XM_011250438.2.
DR RefSeq; XP_011248741.1; XM_011250439.2. [P20917-1]
DR RefSeq; XP_011248742.1; XM_011250440.2. [P20917-1]
DR RefSeq; XP_011248743.1; XM_011250441.2.
DR RefSeq; XP_017177496.1; XM_017322007.1. [P20917-1]
DR RefSeq; XP_017177497.1; XM_017322008.1.
DR PDB; 5LF5; X-ray; 3.80 A; A=20-508.
DR PDB; 5LFR; X-ray; 2.12 A; A/B=20-325.
DR PDB; 5LFU; X-ray; 4.30 A; A=20-508.
DR PDB; 5LFV; X-ray; 2.30 A; A/B=20-325.
DR PDB; 6GZJ; X-ray; 1.98 A; B=573-627.
DR PDB; 6GZL; X-ray; 1.95 A; B=605-621.
DR PDBsum; 5LF5; -.
DR PDBsum; 5LFR; -.
DR PDBsum; 5LFU; -.
DR PDBsum; 5LFV; -.
DR PDBsum; 6GZJ; -.
DR PDBsum; 6GZL; -.
DR AlphaFoldDB; P20917; -.
DR SASBDB; P20917; -.
DR SMR; P20917; -.
DR BioGRID; 201285; 7.
DR IntAct; P20917; 2.
DR MINT; P20917; -.
DR STRING; 10090.ENSMUSP00000139881; -.
DR ChEMBL; CHEMBL1250416; -.
DR UniLectin; P20917; -.
DR GlyConnect; 2446; 2 N-Linked glycans (1 site). [P20917-2]
DR GlyConnect; 2519; 13 N-Linked glycans (1 site).
DR GlyGen; P20917; 9 sites, 13 N-linked glycans (1 site).
DR iPTMnet; P20917; -.
DR PhosphoSitePlus; P20917; -.
DR SwissPalm; P20917; -.
DR MaxQB; P20917; -.
DR PaxDb; P20917; -.
DR PeptideAtlas; P20917; -.
DR PRIDE; P20917; -.
DR ProteomicsDB; 287299; -. [P20917-1]
DR ProteomicsDB; 287300; -. [P20917-2]
DR ProteomicsDB; 312561; -.
DR ABCD; P20917; 19 sequenced antibodies.
DR Antibodypedia; 1364; 403 antibodies from 39 providers.
DR DNASU; 17136; -.
DR Ensembl; ENSMUST00000040548; ENSMUSP00000041464; ENSMUSG00000036634. [P20917-2]
DR Ensembl; ENSMUST00000187137; ENSMUSP00000139564; ENSMUSG00000036634. [P20917-2]
DR Ensembl; ENSMUST00000191081; ENSMUSP00000139881; ENSMUSG00000036634. [P20917-1]
DR GeneID; 17136; -.
DR KEGG; mmu:17136; -.
DR UCSC; uc009ghb.1; mouse. [P20917-2]
DR CTD; 4099; -.
DR MGI; MGI:96912; Mag.
DR VEuPathDB; HostDB:ENSMUSG00000036634; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT01040000240433; -.
DR HOGENOM; CLU_020480_1_0_1; -.
DR InParanoid; P20917; -.
DR OMA; EIMDITP; -.
DR OrthoDB; 415025at2759; -.
DR PhylomeDB; P20917; -.
DR TreeFam; TF332441; -.
DR Reactome; R-MMU-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-MMU-210991; Basigin interactions.
DR BioGRID-ORCS; 17136; 1 hit in 73 CRISPR screens.
DR PRO; PR:P20917; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P20917; protein.
DR Bgee; ENSMUSG00000036634; Expressed in cerebellar nuclear complex and 108 other tissues.
DR ExpressionAtlas; P20917; baseline and differential.
DR Genevisible; P20917; MM.
DR GO; GO:0043218; C:compact myelin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0097453; C:mesaxon; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IDA:MGI.
DR GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:1905576; F:ganglioside GT1b binding; IMP:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0033691; F:sialic acid binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031103; P:axon regeneration; IGI:MGI.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0032289; P:central nervous system myelin formation; IGI:MGI.
DR GO; GO:0022010; P:central nervous system myelination; IMP:UniProtKB.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISO:MGI.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:CACAO.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF08205; C2-set_2; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Lectin; Lipid-binding; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..19
FT CHAIN 20..627
FT /note="Myelin-associated glycoprotein"
FT /id="PRO_0000014857"
FT TOPO_DOM 20..516
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..120
FT /note="Ig-like V-type"
FT DOMAIN 139..237
FT /note="Ig-like C2-type 1"
FT DOMAIN 241..325
FT /note="Ig-like C2-type 2"
FT DOMAIN 327..412
FT /note="Ig-like C2-type 3"
FT DOMAIN 413..508
FT /note="Ig-like C2-type 4"
FT REGION 20..325
FT /note="Interaction with RTN4R and RTN4RL2"
FT /evidence="ECO:0000250|UniProtKB:P07722"
FT REGION 578..627
FT /note="Required for normal axon myelination in the central
FT nervous system"
FT /evidence="ECO:0000269|PubMed:9482783"
FT BINDING 65..67
FT /ligand="ganglioside GT1b (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:78452"
FT /evidence="ECO:0000269|PubMed:27922006"
FT BINDING 118
FT /ligand="ganglioside GT1b (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:78452"
FT /evidence="ECO:0000269|PubMed:27922006"
FT BINDING 124..128
FT /ligand="ganglioside GT1b (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:78452"
FT /evidence="ECO:0000269|PubMed:27922006"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07722"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07722"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07722"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 531
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P07722"
FT CARBOHYD 22
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:27922006"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27922006"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27922006"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27922006"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27922006"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27922006"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27922006"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27922006"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27922006"
FT DISULFID 37..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27922006"
FT DISULFID 42..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27922006"
FT DISULFID 159..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27922006"
FT DISULFID 261..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27922006"
FT DISULFID 347..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27922006"
FT DISULFID 421..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27922006"
FT DISULFID 432..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:27922006"
FT VAR_SEQ 574..582
FT /note="EKQRLGSER -> REVSTRDCH (in isoform S-MAG)"
FT /evidence="ECO:0000305"
FT /id="VSP_002527"
FT VAR_SEQ 583..627
FT /note="Missing (in isoform S-MAG)"
FT /evidence="ECO:0000305"
FT /id="VSP_002528"
FT MUTAGEN 25
FT /note="W->Q: Abolishes C-linked mannosylation."
FT /evidence="ECO:0000269|PubMed:27922006"
FT MUTAGEN 65
FT /note="Y->A: Decreases ganglioside binding."
FT /evidence="ECO:0000269|PubMed:27922006"
FT MUTAGEN 118..120
FT /note="RGD->KGE: Abolishes protection against axon
FT degeneration."
FT /evidence="ECO:0000269|PubMed:19158290"
FT MUTAGEN 118
FT /note="R->A: Abolishes ganglioside binding."
FT /evidence="ECO:0000269|PubMed:27922006"
FT MUTAGEN 127
FT /note="Y->A: Abolishes ganglioside binding."
FT /evidence="ECO:0000269|PubMed:27922006"
FT MUTAGEN 128
FT /note="T->A: Abolishes ganglioside binding."
FT /evidence="ECO:0000269|PubMed:27922006"
FT MUTAGEN 406
FT /note="N->Q: Increases homodimerization."
FT /evidence="ECO:0000269|PubMed:27922006"
FT MUTAGEN 473
FT /note="I->E: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:27922006"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5LFR"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5LFV"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:5LFR"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:5LFR"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5LFR"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5LFR"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5LFR"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:5LFR"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:5LFR"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:5LFR"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 257..267
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 278..292
FT /evidence="ECO:0007829|PDB:5LFR"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 312..324
FT /evidence="ECO:0007829|PDB:5LFR"
FT STRAND 608..614
FT /evidence="ECO:0007829|PDB:6GZL"
SQ SEQUENCE 627 AA; 69388 MW; 54E7D53096010905 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 YESEKQRLGS ERRLLGLRGE SPELDLSYSH
SDLGKRPTKD SYTLTEELAE YAEIRVK
