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UniProtKB - P20917 (MAG_MOUSE)

Protein

Myelin-associated glycoprotein

Gene

Mag

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).By similarity13 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei118Ganglioside GT1b1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • ganglioside GT1b binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: MGI
  • sialic acid binding Source: UniProtKB
  • signaling receptor binding Source: MGI
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion
LigandLectin, Lipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-193634 Axonal growth inhibition (RHOA activation)
R-MMU-210991 Basigin interactions

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Myelin-associated glycoprotein
Alternative name(s):
Siglec-4a
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Mag
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:96912 Mag

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini20 – 516ExtracellularSequence analysisAdd BLAST497
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei517 – 536HelicalSequence analysisAdd BLAST20
Topological domaini537 – 626CytoplasmicSequence analysisAdd BLAST90

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

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).7 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi25W → Q: Abolishes C-linked mannosylation. 1 Publication1
Mutagenesisi65Y → A: Decreases ganglioside binding. 1 Publication1
Mutagenesisi118 – 120RGD → KGE: Abolishes protection against axon degeneration. 1 Publication3
Mutagenesisi118R → A: Abolishes ganglioside binding. 1 Publication1
Mutagenesisi127Y → A: Abolishes ganglioside binding. 1 Publication1
Mutagenesisi128T → A: Abolishes ganglioside binding. 1 Publication1
Mutagenesisi406N → Q: Increases homodimerization. 1 Publication1
Mutagenesisi473I → E: Abolishes homodimerization. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1250416

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Add BLAST19
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001485720 – 626Myelin-associated glycoproteinAdd BLAST607

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi22C-linked (Man) tryptophan1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi37 ↔ 165PROSITE-ProRule annotation1 Publication
Disulfide bondi42 ↔ 100PROSITE-ProRule annotation1 Publication
Glycosylationi99N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi159 ↔ 217PROSITE-ProRule annotation1 Publication
Glycosylationi223N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi246N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi261 ↔ 305PROSITE-ProRule annotation1 Publication
Glycosylationi315N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi332N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi347 ↔ 392PROSITE-ProRule annotation1 Publication
Glycosylationi406N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi421 ↔ 430PROSITE-ProRule annotation1 Publication
Disulfide bondi432 ↔ 488PROSITE-ProRule annotation1 Publication
Glycosylationi450N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi454N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi531S-palmitoyl cysteineBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei545PhosphoserineBy similarity1
Modified residuei547PhosphoserineBy similarity1
Modified residuei549PhosphoserineBy similarity1
Modified residuei590PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.2 Publications
Phosphorylated on tyrosine residues.By similarity
Ubiquitinated, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P20917

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P20917

PeptideAtlas

More...PeptideAtlasi		P20917

PRoteomics IDEntifications database

More...PRIDEi		P20917

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P20917

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P20917

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P20917

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in the myelin tract in brain, especially in the corpus callosum and in peripheral nerve (PubMed:7516497, PubMed:9482783, PubMed:24191038). 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).6 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000036634 Expressed in 121 organ(s), highest expression level in ventral horn of spinal cord

CleanEx database of gene expression profiles

More...CleanExi		MM_MAG

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P20917 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P20917 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer and homodimer (PubMed:27922006). Interacts (via the first three N-terminal Ig-like domains) with RTN4R and RTN4RL2 (PubMed:12089450, PubMed:26335717).3 Publications

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		201285, 1 interactor

Protein interaction database and analysis system

More...IntActi		P20917, 4 interactors

Molecular INTeraction database

More...MINTi		P20917

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000041464

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P20917

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1626
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P20917

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P20917

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini22 – 120Ig-like V-typeAdd BLAST99
Domaini139 – 237Ig-like C2-type 1Add BLAST99
Domaini241 – 325Ig-like C2-type 2Add BLAST85
Domaini327 – 412Ig-like C2-type 3Add BLAST86
Domaini413 – 508Ig-like C2-type 4Add BLAST96

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni20 – 325Interaction with RTN4R and RTN4RL2By similarityAdd BLAST306
Regioni65 – 67Ganglioside GT1b binding1 Publication3
Regioni124 – 128Ganglioside GT1b binding1 Publication5
Regioni577 – 626Required for normal axon myelination in the central nervous system1 PublicationAdd BLAST50

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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).1 Publication
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).By similarity2 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410KDW4 Eukaryota
ENOG410XQVV LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153276

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000113464

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG006317

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P20917

KEGG Orthology (KO)

More...KOi		K06771

Identification of Orthologs from Complete Genome Data

More...OMAi		CVVKANP

Database for complete collections of gene phylogenies

More...PhylomeDBi		P20917

TreeFam database of animal gene trees

More...TreeFami		TF332441

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.10, 4 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013162 CD80_C2-set
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08205 C2-set_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00409 IG, 4 hits
SM00408 IGc2, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48726 SSF48726, 4 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50835 IG_LIKE, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform L-MAG (identifier: P20917-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MIFLATLPLF WIMISASRGG HWGAWMPSTI SAFEGTCVSI PCRFDFPDEL 
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RPAVVHGVWY FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC 
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TLLLSTLSPE LGGKYYFRGD LGGYNQYTFS EHSVLDIVNT PNIVVPPEVV 
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AGTEVEVSCM VPDNCPELRP ELSWLGHEGL GEPTVLGRLR EDEGTWVQVS 
       210        220        230        240        250
LLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP VIVEMNSSVE 
       260        270        280        290        300
AIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAKSLYL DLEEVTPGED 
       310        320        330        340        350
GVYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ 
       360        370        380        390        400
SNPDPILTIF KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ 
       410        420        430        440        450
RATAFNLSVE FAPIILLESH CAAARDTVQC LCVVKSNPEP SVAFELPSRN 
       460        470        480        490        500
VTVNETEREF VYSERSGLLL TSILTIRGQA QAPPRVICTS RNLYGTQSLE 
       510        520        530        540        550
LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK NVTESSSFSG 
       560        570        580        590        600
GDNPHVLYSP EFRISGAPDK YESEKRLGSE RRLLGLRGES PELDLSYSHS 
       610        620 
DLGKRPTKDS YTLTEELAEY AEIRVK
Length:626
Mass (Da):69,260
Last modified:July 15, 1998 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9C797BD6B52B6057
GO
Isoform S-MAG (identifier: P20917-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     574-582: EKRLGSERR → REVSTRDCH
     583-626: Missing.

Show »
Length:582
Mass (Da):64,268
Checksum:i892DD384D653FCDC
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WPR1A0A087WPR1_MOUSE
Myelin-associated glycoprotein
Mag
627Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q3ZB60Q3ZB60_MOUSE
Mag protein
Mag
567Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WRD6A0A087WRD6_MOUSE
Myelin-associated glycoprotein
Mag
168Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WPP5A0A087WPP5_MOUSE
Myelin-associated glycoprotein
Mag
64Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002527574 – 582EKRLGSERR → REVSTRDCH in isoform S-MAG. Curated9
Alternative sequenceiVSP_002528583 – 626Missing in isoform S-MAG. CuratedAdd BLAST44

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M31811 mRNA Translation: AAA39487.1
M74793
, M74783, M74784, M74785, M74786, M74787, M74788, M74790, M74791 Genomic DNA Translation: AAA91743.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS21115.1 [P20917-2]

Protein sequence database of the Protein Information Resource

More...PIRi		B33785

NCBI Reference Sequences

More...RefSeqi		NP_001333015.1, NM_001346086.1 [P20917-2]
NP_001333016.1, NM_001346087.1 [P20917-2]
NP_001333017.1, NM_001346088.1 [P20917-2]
NP_034888.1, NM_010758.3 [P20917-2]
XP_011248743.1, XM_011250441.2 [P20917-2]
XP_017177497.1, XM_017322008.1 [P20917-2]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.241355

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000040548; ENSMUSP00000041464; ENSMUSG00000036634 [P20917-2]
ENSMUST00000187137; ENSMUSP00000139564; ENSMUSG00000036634 [P20917-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		17136

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:17136

UCSC genome browser

More...UCSCi		uc009ghb.1 mouse [P20917-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Siglec-4

Functional Glycomics Gateway - Glycan Binding

Siglec-4a [3 Fc Domains]

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31811 mRNA Translation: AAA39487.1
M74793
, M74783, M74784, M74785, M74786, M74787, M74788, M74790, M74791 Genomic DNA Translation: AAA91743.1
CCDSiCCDS21115.1 [P20917-2]
PIRiB33785
RefSeqiNP_001333015.1, NM_001346086.1 [P20917-2]
NP_001333016.1, NM_001346087.1 [P20917-2]
NP_001333017.1, NM_001346088.1 [P20917-2]
NP_034888.1, NM_010758.3 [P20917-2]
XP_011248743.1, XM_011250441.2 [P20917-2]
XP_017177497.1, XM_017322008.1 [P20917-2]
UniGeneiMm.241355

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5LF5X-ray3.80A20-508[»]
5LFRX-ray2.12A/B20-325[»]
5LFUX-ray4.30A20-508[»]
5LFVX-ray2.30A/B20-325[»]
6GZJX-ray1.98B573-626[»]
ProteinModelPortaliP20917
SMRiP20917
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201285, 1 interactor
IntActiP20917, 4 interactors
MINTiP20917
STRINGi10090.ENSMUSP00000041464

Chemistry databases

BindingDBiP20917
ChEMBLiCHEMBL1250416

PTM databases

iPTMnetiP20917
PhosphoSitePlusiP20917
SwissPalmiP20917

Proteomic databases

MaxQBiP20917
PaxDbiP20917
PeptideAtlasiP20917
PRIDEiP20917

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040548; ENSMUSP00000041464; ENSMUSG00000036634 [P20917-2]
ENSMUST00000187137; ENSMUSP00000139564; ENSMUSG00000036634 [P20917-2]
GeneIDi17136
KEGGimmu:17136
UCSCiuc009ghb.1 mouse [P20917-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4099
MGIiMGI:96912 Mag

Phylogenomic databases

eggNOGiENOG410KDW4 Eukaryota
ENOG410XQVV LUCA
GeneTreeiENSGT00940000153276
HOGENOMiHOG000113464
HOVERGENiHBG006317
InParanoidiP20917
KOiK06771
OMAiCVVKANP
PhylomeDBiP20917
TreeFamiTF332441

Enzyme and pathway databases

ReactomeiR-MMU-193634 Axonal growth inhibition (RHOA activation)
R-MMU-210991 Basigin interactions

Miscellaneous databases

Protein Ontology

More...PROi		PR:P20917

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000036634 Expressed in 121 organ(s), highest expression level in ventral horn of spinal cord
CleanExiMM_MAG
ExpressionAtlasiP20917 baseline and differential
GenevisibleiP20917 MM

Family and domain databases

Gene3Di2.60.40.10, 4 hits
InterProiView protein in InterPro
IPR013162 CD80_C2-set
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
PfamiView protein in Pfam
PF08205 C2-set_2, 1 hit
SMARTiView protein in SMART
SM00409 IG, 4 hits
SM00408 IGc2, 2 hits
SUPFAMiSSF48726 SSF48726, 4 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMAG_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P20917
Secondary accession number(s): P16880
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 15, 1998
Last modified: December 5, 2018
This is version 177 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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