MAG_RAT
ID MAG_RAT Reviewed; 626 AA.
AC P07722; P02685; P07723;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Myelin-associated glycoprotein;
DE AltName: Full=1B236 {ECO:0000303|PubMed:2438699, ECO:0000303|PubMed:4020419};
DE AltName: Full=Brain neuron cytoplasmic protein 3;
DE AltName: Full=Sialic acid-binding Ig-like lectin 4a;
DE Short=Siglec-4a;
DE Flags: Precursor;
GN Name=Mag;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L-MAG AND S-MAG).
RX PubMed=2438699; DOI=10.1073/pnas.84.12.4337;
RA Lai C., Brow M.A., Nave K.-A., Noronha A.B., Quarles R.H., Bloom F.E.,
RA Milner R.J., Sutcliffe J.G.;
RT "Two forms of 1B236/myelin-associated glycoprotein, a cell adhesion
RT molecule for postnatal neural development, are produced by alternative
RT splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4337-4341(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-MAG), PARTIAL PROTEIN SEQUENCE, AND
RP TISSUE SPECIFICITY.
RX PubMed=2432614; DOI=10.1073/pnas.84.2.600;
RA Arquint M., Roder J., Chia L.S., Down J., Wilkinson D., Bayley H.,
RA Braun P., Dunn R.;
RT "Molecular cloning and primary structure of myelin-associated
RT glycoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:600-604(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-MAG).
RX PubMed=2435742; DOI=10.1083/jcb.104.4.957;
RA Salzer J.L., Holmes W.P., Colman D.R.;
RT "The amino acid sequences of the myelin-associated glycoproteins: homology
RT to the immunoglobulin gene superfamily.";
RL J. Cell Biol. 104:957-965(1987).
RN [4]
RP PROTEIN SEQUENCE OF 76-98; 459-477 AND 492-508, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 309-626 (ISOFORM L-MAG).
RX PubMed=6586369; DOI=10.1101/sqb.1983.048.01.052;
RA Sutcliffe J.G., Milner R.J., Bloom F.E.;
RT "Cellular localization and function of the proteins encoded by brain-
RT specific mRNAs.";
RL Cold Spring Harb. Symp. Quant. Biol. 48:477-484(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 309-626 (ISOFORM L-MAG), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=4020419; DOI=10.1523/jneurosci.05-07-01781.1985;
RA Bloom F.E., Battenberg E.L.F., Milner R.J., Sutcliffe J.G.;
RT "Immunocytochemical mapping of 1B236, a brain-specific neuronal polypeptide
RT deduced from the sequence of a cloned mRNA.";
RL J. Neurosci. 5:1781-1802(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 309-626 (ISOFORM L-MAG).
RX PubMed=6347394; DOI=10.1016/0092-8674(83)90010-7;
RA Sutcliffe J.G., Milner R.J., Shinnick T.M., Bloom F.E.;
RT "Identifying the protein products of brain-specific genes with antibodies
RT to chemically synthesized peptides.";
RL Cell 33:671-682(1983).
RN [8]
RP DISULFIDE BONDS, PALMITOYLATION AT CYS-531, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1703542; DOI=10.1083/jcb.111.6.2651;
RA Pedraza L., Owens G.C., Green L.A.D., Salzer J.L.;
RT "The myelin-associated glycoproteins: membrane disposition, evidence of a
RT novel disulfide linkage between immunoglobulin-like domains, and
RT posttranslational palmitylation.";
RL J. Cell Biol. 111:2651-2661(1990).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8995428; DOI=10.1074/jbc.272.2.1248;
RA Collins B.E., Yang L.J., Mukhopadhyay G., Filbin M.T., Kiso M.,
RA Hasegawa A., Schnaar R.L.;
RT "Sialic acid specificity of myelin-associated glycoprotein binding.";
RL J. Biol. Chem. 272:1248-1255(1997).
RN [10]
RP FUNCTION, MUTAGENESIS OF ARG-118, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP DOMAIN.
RX PubMed=9298990; DOI=10.1083/jcb.138.6.1355;
RA Tang S., Shen Y.J., DeBellard M.E., Mukhopadhyay G., Salzer J.L.,
RA Crocker P.R., Filbin M.T.;
RT "Myelin-associated glycoprotein interacts with neurons via a sialic acid
RT binding site at ARG118 and a distinct neurite inhibition site.";
RL J. Cell Biol. 138:1355-1366(1997).
RN [11]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND PHOSPHORYLATION.
RX PubMed=16998591; DOI=10.1017/s1740925x04000067;
RA Marta C.B., Taylor C.M., Cheng S., Quarles R.H., Bansal R., Pfeiffer S.E.;
RT "Myelin associated glycoprotein cross-linking triggers its partitioning
RT into lipid rafts, specific signaling events and cytoskeletal rearrangements
RT in oligodendrocytes.";
RL Neuron Glia Biol. 1:35-46(2004).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [13]
RP FUNCTION.
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 [14]
RP INTERACTION WITH RTN4R AND RTN4RL2, AND DOMAIN.
RX PubMed=19420245; DOI=10.1523/jneurosci.4935-08.2009;
RA Robak L.A., Venkatesh K., Lee H., Raiker S.J., Duan Y., Lee-Osbourne J.,
RA Hofer T., Mage R.G., Rader C., Giger R.J.;
RT "Molecular basis of the interactions of the Nogo-66 receptor and its
RT homolog NgR2 with myelin-associated glycoprotein: development of NgROMNI-
RT Fc, a novel antagonist of CNS myelin inhibition.";
RL J. Neurosci. 29:5768-5783(2009).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ARG-118.
RX PubMed=19367338; DOI=10.1371/journal.pone.0005218;
RA Woerter V., Schweigreiter R., Kinzel B., Mueller M., Barske C., Boeck G.,
RA Frentzel S., Bandtlow C.E.;
RT "Inhibitory activity of myelin-associated glycoprotein on sensory neurons
RT is largely independent of NgR1 and NgR2 and resides within Ig-Like domains
RT 4 and 5.";
RL PLoS ONE 4:E5218-E5218(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545; SER-547 AND SER-549, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:8995428, PubMed:9298990). Not required for initial myelination,
CC but seems to play a role in the maintenance of normal axon myelination.
CC Protects motoneurons against apoptosis, also after injury; protection
CC against apoptosis is probably mediated via interaction with neuronal
CC RTN4R and RTN4RL2. Required to prevent degeneration of myelinated axons
CC in adults; this probably depends on binding to gangliosides on the axon
CC cell membrane (By similarity). Negative regulator of neurite outgrowth;
CC in dorsal root ganglion neurons the inhibition is mediated primarily
CC via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via
CC binding to neuronal gangliosides (PubMed:17640868). In cerebellar
CC granule cells the inhibition is mediated primarily via binding to
CC neuronal gangliosides (PubMed:17640868). In sensory neurons, inhibition
CC of neurite extension depends only partially on RTN4R, RTN4RL2 and
CC gangliosides (PubMed:19367338). Inhibits axon longitudinal growth
CC (PubMed:9298990). Inhibits axon outgrowth by binding to RTN4R (By
CC similarity). Preferentially binds to alpha-2,3-linked sialic acid
CC (PubMed:8995428). Binds ganglioside Gt1b (PubMed:8995428).
CC {ECO:0000250|UniProtKB:P20917, ECO:0000269|PubMed:17640868,
CC ECO:0000269|PubMed:19367338, ECO:0000269|PubMed:8995428,
CC ECO:0000269|PubMed:9298990}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts (via the
CC first three N-terminal Ig-like domains) with RTN4R and RTN4RL2
CC (PubMed:19420245). Interacts with isoform 2 of BSG (By similarity).
CC {ECO:0000250|UniProtKB:P20917, ECO:0000269|PubMed:19420245}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16998591,
CC ECO:0000269|PubMed:19367338, ECO:0000269|PubMed:8995428,
CC ECO:0000269|PubMed:9298990}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16998591, ECO:0000269|PubMed:19367338,
CC ECO:0000269|PubMed:9298990}. Membrane raft
CC {ECO:0000269|PubMed:16998591}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=L-MAG;
CC IsoId=P07722-1; Sequence=Displayed;
CC Name=S-MAG;
CC IsoId=P07722-2; Sequence=VSP_002529, VSP_002530;
CC -!- TISSUE SPECIFICITY: Detected in myelin (PubMed:17640868). Detected in
CC olfactory bulb and throughout the brain (at protein level)
CC (PubMed:4020419). Detected in brain (PubMed:2432614).
CC {ECO:0000269|PubMed:2432614, ECO:0000269|PubMed:4020419}.
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:0000250|UniProtKB:P20917}.
CC -!- DOMAIN: The extracellular domain is required to protect against axon
CC degeneration (By similarity). The first three Ig-like domains mediate
CC interaction with RTN4R and RTN4RL2, but are not sufficient to inhibit
CC neurite outgrowth (PubMed:19420245). The two C-terminal extracellular
CC Ig-like C2-type domains are required for inhibition of axon
CC longitudinal growth (PubMed:9298990, PubMed:19420245, PubMed:19367338).
CC Besides, the two C-terminal extracellular Ig-like C2-type domains are
CC required for protection against apoptosis after nerve injury (By
CC similarity). {ECO:0000250|UniProtKB:P20917,
CC ECO:0000269|PubMed:19367338, ECO:0000269|PubMed:19420245,
CC ECO:0000269|PubMed:9298990}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20916}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:16998591}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P20917}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
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DR EMBL; M14871; AAA41556.1; -; mRNA.
DR EMBL; M22357; AAA41558.1; -; mRNA.
DR EMBL; M16800; AAA41557.1; -; mRNA.
DR EMBL; X05301; CAA28920.1; -; mRNA.
DR EMBL; M11721; AAA42082.1; -; mRNA.
DR EMBL; M36702; AAA40831.1; -; mRNA.
DR EMBL; V01544; CAA24786.1; -; Genomic_DNA.
DR PIR; A29028; BNRT3.
DR RefSeq; NP_058886.1; NM_017190.4. [P07722-1]
DR RefSeq; XP_006228886.1; XM_006228824.3. [P07722-1]
DR RefSeq; XP_008757360.1; XM_008759138.2. [P07722-1]
DR RefSeq; XP_017444540.1; XM_017589051.1. [P07722-1]
DR RefSeq; XP_017444541.1; XM_017589052.1. [P07722-1]
DR RefSeq; XP_017444542.1; XM_017589053.1. [P07722-1]
DR AlphaFoldDB; P07722; -.
DR SMR; P07722; -.
DR BioGRID; 248059; 3.
DR IntAct; P07722; 2.
DR MINT; P07722; -.
DR STRING; 10116.ENSRNOP00000028544; -.
DR GlyGen; P07722; 8 sites.
DR iPTMnet; P07722; -.
DR PhosphoSitePlus; P07722; -.
DR PaxDb; P07722; -.
DR PRIDE; P07722; -.
DR Ensembl; ENSRNOT00000028544; ENSRNOP00000028544; ENSRNOG00000021023. [P07722-1]
DR GeneID; 29409; -.
DR KEGG; rno:29409; -.
DR UCSC; RGD:3035; rat. [P07722-1]
DR CTD; 4099; -.
DR RGD; 3035; Mag.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT01040000240433; -.
DR HOGENOM; CLU_020480_1_0_1; -.
DR InParanoid; P07722; -.
DR OMA; EIMDITP; -.
DR OrthoDB; 415025at2759; -.
DR PhylomeDB; P07722; -.
DR TreeFam; TF332441; -.
DR Reactome; R-RNO-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-RNO-210991; Basigin interactions.
DR PRO; PR:P07722; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021023; Expressed in cerebellum and 8 other tissues.
DR ExpressionAtlas; P07722; baseline and differential.
DR Genevisible; P07722; RN.
DR GO; GO:0043218; C:compact myelin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0097453; C:mesaxon; IDA:RGD.
DR GO; GO:0043209; C:myelin sheath; ISO:RGD.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IDA:RGD.
DR GO; GO:0033270; C:paranode region of axon; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:1905576; F:ganglioside GT1b binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0033691; F:sialic acid binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0031103; P:axon regeneration; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0032289; P:central nervous system myelin formation; ISO:RGD.
DR GO; GO:0022010; P:central nervous system myelination; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:RGD.
DR GO; GO:0007399; P:nervous system development; IEP:RGD.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; IDA:RGD.
DR GO; GO:0031643; P:positive regulation of myelination; ISO:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
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 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..626
FT /note="Myelin-associated glycoprotein"
FT /id="PRO_0000014858"
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..626
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:0000269|PubMed:19420245"
FT REGION 577..626
FT /note="Required for normal axon myelination in the central
FT nervous system"
FT /evidence="ECO:0000250|UniProtKB:P20917"
FT REGION 581..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65..67
FT /ligand="ganglioside GT1b (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:78452"
FT /evidence="ECO:0000250|UniProtKB:P20917"
FT BINDING 118
FT /ligand="ganglioside GT1b (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:78452"
FT /evidence="ECO:0000250|UniProtKB:P20917"
FT BINDING 124..128
FT /ligand="ganglioside GT1b (d18:1(4E))"
FT /ligand_id="ChEBI:CHEBI:78452"
FT /evidence="ECO:0000250|UniProtKB:P20917"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 531
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:1703542"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..165
FT /evidence="ECO:0000305|PubMed:1703542"
FT DISULFID 42..100
FT /evidence="ECO:0000305|PubMed:1703542"
FT DISULFID 159..217
FT /evidence="ECO:0000305|PubMed:1703542"
FT DISULFID 261..305
FT /evidence="ECO:0000305|PubMed:1703542"
FT DISULFID 347..392
FT /evidence="ECO:0000305|PubMed:1703542"
FT DISULFID 421..430
FT /evidence="ECO:0000305|PubMed:1703542"
FT DISULFID 432..488
FT /evidence="ECO:0000305|PubMed:1703542"
FT VAR_SEQ 574..582
FT /note="EKRLGSERR -> REVSTRDCH (in isoform S-MAG)"
FT /evidence="ECO:0000303|PubMed:2438699"
FT /id="VSP_002529"
FT VAR_SEQ 583..626
FT /note="Missing (in isoform S-MAG)"
FT /evidence="ECO:0000303|PubMed:2438699"
FT /id="VSP_002530"
FT MUTAGEN 118
FT /note="R->A,D: Abolishes inhibition of neurite outgrowth
FT from CNS neurons."
FT /evidence="ECO:0000269|PubMed:9298990"
FT MUTAGEN 118
FT /note="R->A: No effect on inhibition of neurite outgrowth
FT from sensory neurons."
FT /evidence="ECO:0000269|PubMed:19367338"
FT CONFLICT 309..310
FT /note="NA -> KS (in Ref. 5, 6 and 7)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 69353 MW; E97998E280ECD635 CRC64;
MIFLTTLPLF WIMISASRGG HWGAWMPSSI SAFEGTCVSI PCRFDFPDEL RPAVVHGVWY
FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSTLSPE LGGKYYFRGD
LGGYNQYTFS EHSVLDIINT PNIVVPPEVV AGTEVEVSCM VPDNCPELRP ELSWLGHEGL
GEPTVLGRLR EDEGTWVQVS LLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP
VIVEMNSSVE AIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAESLYL DLEEVTPAED
GIYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ SNPDPILTIF
KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ RATAFNLSVE FAPIILLESH
CAAARDTVQC LCVVKSNPEP SVAFELPSRN VTVNETEREF VYSERSGLLL TSILTLRGQA
QAPPRVICTS RNLYGTQSLE LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK
NVTESPSFSA GDNPHVLYSP EFRISGAPDK YESEKRLGSE RRLLGLRGEP PELDLSYSHS
DLGKRPTKDS YTLTEELAEY AEIRVK
