MAG_HUMAN
ID MAG_HUMAN Reviewed; 626 AA.
AC P20916; B7Z2E5; F5GYC0; Q15489; Q567S4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Myelin-associated glycoprotein;
DE AltName: Full=Siglec-4a;
DE Flags: Precursor;
GN Name=MAG; Synonyms=GMA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2476987; DOI=10.1016/0006-291x(89)91145-5;
RA Sato S., Fujita N., Kurihara T., Kuwano R., Sakimura K., Takahashi Y.,
RA Miyatake T.;
RT "cDNA cloning and amino acid sequence for human myelin-associated
RT glycoprotein.";
RL Biochem. Biophys. Res. Commun. 163:1473-1480(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=2479762; DOI=10.1002/jnr.490240203;
RA Spagnol G., Williams M., Srinivasan J., Golier J., Bauer D., Lebo R.V.,
RA Latov N.;
RT "Molecular cloning of human myelin-associated glycoprotein.";
RL J. Neurosci. Res. 24:137-142(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-202.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 528-626 (ISOFORM 2), ALTERNATIVE SPLICING,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000312|EMBL:CAA67055.1};
RX PubMed=9495552; DOI=10.1016/s0169-328x(97)00254-4;
RA Miescher G.C., Luetzelschwab R., Erne B., Ferracin F., Huber S.,
RA Steck A.J.;
RT "Reciprocal expression of myelin-associated glycoprotein splice variants in
RT the adult human peripheral and central nervous systems.";
RL Brain Res. Mol. Brain Res. 52:299-306(1997).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=6200494; DOI=10.1016/0165-5728(84)90039-0;
RA Favilla J.T., Frail D.E., Palkovits C.G., Stoner G.L., Braun P.E.,
RA Webster H.D.;
RT "Myelin-associated glycoprotein (MAG) distribution in human central nervous
RT tissue studied immunocytochemically with monoclonal antibody.";
RL J. Neuroimmunol. 6:19-30(1984).
RN [8]
RP GLYCOSYLATION AT ASN-99; ASN-106; ASN-223; ASN-246; ASN-315; ASN-406;
RP ASN-450 AND ASN-454, AND LACK OF GLYCOSYLATION AT ASN-332.
RX PubMed=7505568; DOI=10.1006/bbrc.1993.2501;
RA Burger D., Pidoux L., Steck A.J.;
RT "Identification of the glycosylated sequons of human myelin-associated
RT glycoprotein.";
RL Biochem. Biophys. Res. Commun. 197:457-464(1993).
RN [9]
RP INTERACTION WITH RTN4R.
RX PubMed=19052207; DOI=10.1523/jneurosci.3828-08.2008;
RA Budel S., Padukkavidana T., Liu B.P., Feng Z., Hu F., Johnson S.,
RA Lauren J., Park J.H., McGee A.W., Liao J., Stillman A., Kim J.E.,
RA Yang B.Z., Sodi S., Gelernter J., Zhao H., Hisama F., Arnsten A.F.,
RA Strittmatter S.M.;
RT "Genetic variants of Nogo-66 receptor with possible association to
RT schizophrenia block myelin inhibition of axon growth.";
RL J. Neurosci. 28:13161-13172(2008).
RN [10]
RP INVOLVEMENT IN SPG75, AND VARIANT SPG75 GLY-430.
RX PubMed=24482476; DOI=10.1126/science.1247363;
RA Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
RA Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A.,
RA Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M.,
RA Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G.,
RA Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S.,
RA Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M.,
RA Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J.,
RA Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A.,
RA Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T.,
RA Gleeson J.G.;
RT "Exome sequencing links corticospinal motor neuron disease to common
RT neurodegenerative disorders.";
RL Science 343:506-511(2014).
RN [11]
RP INVOLVEMENT IN SPG75, VARIANT SPG75 ARG-133, CHARACTERIZATION OF VARIANT
RP SPG75 ARG-133, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
RX PubMed=26179919; DOI=10.1093/brain/awv204;
RA Lossos A., Elazar N., Lerer I., Schueler-Furman O., Fellig Y., Glick B.,
RA Zimmerman B.E., Azulay H., Dotan S., Goldberg S., Gomori J.M., Ponger P.,
RA Newman J.P., Marreed H., Steck A.J., Schaeren-Wiemers N., Mor N., Harel M.,
RA Geiger T., Eshed-Eisenbach Y., Meiner V., Peles E.;
RT "Myelin-associated glycoprotein gene mutation causes Pelizaeus-Merzbacher
RT disease-like disorder.";
RL Brain 138:2521-2536(2015).
RN [12]
RP VARIANT SPG75 HIS-118.
RX PubMed=27606346; DOI=10.1002/acn3.329;
RA Roda R.H., FitzGibbon E.J., Boucekkine H., Schindler A.B., Blackstone C.;
RT "Neurologic syndrome associated with homozygous mutation at MAG sialic acid
RT binding site.";
RL Ann. Clin. Transl. Neurol. 3:650-654(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 (By
CC similarity). Not required for initial myelination, but seems to play a
CC role in the maintenance of normal axon myelination. Protects
CC motoneurons against apoptosis, also after injury; protection against
CC apoptosis is probably mediated via interaction with neuronal RTN4R and
CC RTN4RL2. Required to prevent degeneration of myelinated axons in
CC 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. In cerebellar granule cells the
CC inhibition is mediated primarily via binding to neuronal gangliosides.
CC In sensory neurons, inhibition of neurite extension depends only
CC partially on RTN4R, RTN4RL2 and gangliosides. Inhibits axon
CC longitudinal growth (By similarity). Inhibits axon outgrowth by binding
CC to RTN4R (By similarity). Preferentially binds to alpha-2,3-linked
CC sialic acid. Binds ganglioside Gt1b (By similarity).
CC {ECO:0000250|UniProtKB:P07722, ECO:0000250|UniProtKB:P20917}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts (via the
CC first three N-terminal Ig-like domains) with RTN4R and RTN4RL2 (By
CC similarity). Interacts with RTN4R (PubMed:19052207). Interacts with
CC isoform 2 of BSG (By similarity). {ECO:0000250|UniProtKB:P07722,
CC ECO:0000250|UniProtKB:P20917, ECO:0000269|PubMed:19052207}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26179919};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:26179919}.
CC Membrane raft {ECO:0000250|UniProtKB:P07722}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=L-MAG {ECO:0000303|PubMed:9495552};
CC IsoId=P20916-1; Sequence=Displayed;
CC Name=2; Synonyms=S-MAG {ECO:0000303|PubMed:9495552};
CC IsoId=P20916-2; Sequence=VSP_042688;
CC Name=3;
CC IsoId=P20916-3; Sequence=VSP_045843;
CC -!- TISSUE SPECIFICITY: Both isoform 1 and isoform 2 are detected in
CC myelinated structures in the central and peripheral nervous system, in
CC periaxonal myelin and at Schmidt-Lanterman incisures (PubMed:9495552,
CC PubMed:6200494). Detected in optic nerve, in oligodendroglia and in
CC periaxonal myelin sheaths (PubMed:6200494). Detected in compact myelin
CC (at protein level) (PubMed:6200494). Both isoform 1 and isoform 2 are
CC detected in the central and peripheral nervous system (PubMed:9495552).
CC {ECO:0000269|PubMed:6200494, ECO:0000269|PubMed:9495552}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:26179919}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000250|UniProtKB:P07722}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P20917}.
CC -!- DISEASE: Spastic paraplegia 75, autosomal recessive (SPG75)
CC [MIM:616680]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body. SPG75 is characterized
CC by onset in early childhood and is associated with mild to moderate
CC cognitive impairment. {ECO:0000269|PubMed:24482476,
CC ECO:0000269|PubMed:26179919, ECO:0000269|PubMed:27606346}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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_hum_Itlect_271";
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DR EMBL; M29273; AAA59545.1; -; mRNA.
DR EMBL; AK294644; BAH11831.1; -; mRNA.
DR EMBL; AC002132; AAB58805.1; -; Genomic_DNA.
DR EMBL; AD000684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053347; AAH53347.1; -; mRNA.
DR EMBL; BC093045; AAH93045.1; -; mRNA.
DR EMBL; X98405; CAA67055.1; -; mRNA.
DR CCDS; CCDS12455.1; -. [P20916-1]
DR CCDS; CCDS12456.1; -. [P20916-2]
DR CCDS; CCDS56090.1; -. [P20916-3]
DR PIR; A61084; A61084.
DR RefSeq; NP_001186145.1; NM_001199216.1. [P20916-3]
DR RefSeq; NP_002352.1; NM_002361.3. [P20916-1]
DR RefSeq; NP_542167.1; NM_080600.2. [P20916-2]
DR AlphaFoldDB; P20916; -.
DR SMR; P20916; -.
DR BioGRID; 110273; 22.
DR DIP; DIP-58523N; -.
DR IntAct; P20916; 4.
DR STRING; 9606.ENSP00000376048; -.
DR BindingDB; P20916; -.
DR ChEMBL; CHEMBL5807; -.
DR GlyGen; P20916; 9 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P20916; -.
DR PhosphoSitePlus; P20916; -.
DR SwissPalm; P20916; -.
DR BioMuta; MAG; -.
DR DMDM; 126689; -.
DR MassIVE; P20916; -.
DR PaxDb; P20916; -.
DR PeptideAtlas; P20916; -.
DR PRIDE; P20916; -.
DR ProteomicsDB; 24691; -.
DR ProteomicsDB; 53823; -. [P20916-1]
DR ProteomicsDB; 53824; -. [P20916-2]
DR ABCD; P20916; 7 sequenced antibodies.
DR Antibodypedia; 1364; 403 antibodies from 39 providers.
DR DNASU; 4099; -.
DR Ensembl; ENST00000361922.8; ENSP00000355234.4; ENSG00000105695.15. [P20916-2]
DR Ensembl; ENST00000392213.8; ENSP00000376048.2; ENSG00000105695.15. [P20916-1]
DR Ensembl; ENST00000537831.2; ENSP00000440695.1; ENSG00000105695.15. [P20916-3]
DR GeneID; 4099; -.
DR KEGG; hsa:4099; -.
DR MANE-Select; ENST00000392213.8; ENSP00000376048.2; NM_002361.4; NP_002352.1.
DR UCSC; uc002nyx.3; human. [P20916-1]
DR CTD; 4099; -.
DR DisGeNET; 4099; -.
DR GeneCards; MAG; -.
DR HGNC; HGNC:6783; MAG.
DR HPA; ENSG00000105695; Tissue enriched (brain).
DR MalaCards; MAG; -.
DR MIM; 159460; gene.
DR MIM; 616680; phenotype.
DR neXtProt; NX_P20916; -.
DR OpenTargets; ENSG00000105695; -.
DR Orphanet; 459056; Autosomal recessive spastic paraplegia type 75.
DR PharmGKB; PA30541; -.
DR VEuPathDB; HostDB:ENSG00000105695; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT01040000240433; -.
DR HOGENOM; CLU_020480_1_0_1; -.
DR InParanoid; P20916; -.
DR OMA; EIMDITP; -.
DR PhylomeDB; P20916; -.
DR TreeFam; TF332441; -.
DR PathwayCommons; P20916; -.
DR Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; P20916; -.
DR SIGNOR; P20916; -.
DR BioGRID-ORCS; 4099; 17 hits in 1073 CRISPR screens.
DR ChiTaRS; MAG; human.
DR GeneWiki; Myelin-associated_glycoprotein; -.
DR GenomeRNAi; 4099; -.
DR Pharos; P20916; Tchem.
DR PRO; PR:P20916; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P20916; protein.
DR Bgee; ENSG00000105695; Expressed in C1 segment of cervical spinal cord and 144 other tissues.
DR ExpressionAtlas; P20916; baseline and differential.
DR Genevisible; P20916; HS.
DR GO; GO:0043218; C:compact myelin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0097453; C:mesaxon; IEA:Ensembl.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
DR GO; GO:0033270; C:paranode region of axon; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:1905576; F:ganglioside GT1b binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0033691; F:sialic acid binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; IEA:Ensembl.
DR GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
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; 5.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disease variant;
KW Disulfide bond; Glycoprotein; Hereditary spastic paraplegia;
KW Immunoglobulin domain; Lectin; Lipid-binding; Lipoprotein; Membrane;
KW Neurodegeneration; Palmitate; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..19
FT CHAIN 20..626
FT /note="Myelin-associated glycoprotein"
FT /id="PRO_0000014856"
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:0000250|UniProtKB:P07722"
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 582..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 SITE 332
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:7505568"
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 LIPID 531
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P07722"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7505568"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:7505568"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7505568"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7505568"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7505568"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7505568"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7505568"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7505568"
FT DISULFID 37..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 42..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 159..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 261..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 347..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 421..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 432..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045843"
FT VAR_SEQ 574..626
FT /note="ERRLGSERRLLGLRGEPPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRV
FT K -> KEVSTLESH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9495552"
FT /id="VSP_042688"
FT VARIANT 118
FT /note="R -> H (in SPG75; unknown pathological significance;
FT dbSNP:rs762045079)"
FT /evidence="ECO:0000269|PubMed:27606346"
FT /id="VAR_077495"
FT VARIANT 133
FT /note="S -> R (in SPG75; alters proper folding; impairs N-
FT glycosylation; retained in the endoplasmic reticulum;
FT increased proteasome-dependent degradation;
FT dbSNP:rs2301600)"
FT /evidence="ECO:0000269|PubMed:26179919"
FT /id="VAR_076224"
FT VARIANT 202
FT /note="L -> M (in dbSNP:rs11084810)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_059399"
FT VARIANT 430
FT /note="C -> G (in SPG75; unknown pathological significance;
FT dbSNP:rs587777229)"
FT /evidence="ECO:0000269|PubMed:24482476"
FT /id="VAR_076225"
FT CONFLICT 614
FT /note="T -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 69069 MW; ED2D36B24F21CAAA CRC64;
MIFLTALPLF WIMISASRGG HWGAWMPSSI SAFEGTCVSI PCRFDFPDEL RPAVVHGVWY
FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSNVSPE LGGKYYFRGD
LGGYNQYTFS EHSVLDIVNT PNIVVPPEVV AGTEVEVSCM VPDNCPELRP ELSWLGHEGL
GEPAVLGRLR EDEGTWVQVS LLHFVPTREA NGHRLGCQAS FPNTTLQFEG YASMDVKYPP
VIVEMNSSVE AIEGSHVSLL CGADSNPPPL LTWMRDGTVL REAVAESLLL ELEEVTPAED
GVYACLAENA YGQDNRTVGL SVMYAPWKPT VNGTMVAVEG ETVSILCSTQ SNPDPILTIF
KEKQILSTVI YESELQLELP AVSPEDDGEY WCVAENQYGQ RATAFNLSVE FAPVLLLESH
CAAARDTVQC LCVVKSNPEP SVAFELPSRN VTVNESEREF VYSERSGLVL TSILTLRGQA
QAPPRVICTA RNLYGAKSLE LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK
NVTESPSFSA GDNPPVLFSS DFRISGAPEK YESERRLGSE RRLLGLRGEP PELDLSYSHS
DLGKRPTKDS YTLTEELAEY AEIRVK
