Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 162 (08 May 2019)
Sequence version 1 (01 Apr 1988)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Myelin-associated glycoprotein

Gene

Mag

Organism
Rattus norvegicus (Rat)
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:8995428, PubMed:9298990). Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination. Protects motoneurons against apoptosis, also after injury; protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2. Required to prevent degeneration of myelinated axons in adults; this probably depends on binding to gangliosides on the axon cell membrane (By similarity). 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 primarily via binding to neuronal gangliosides (PubMed:17640868). In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides (PubMed:19367338). Inhibits axon longitudinal growth (PubMed:9298990). Inhibits axon outgrowth by binding to RTN4R (By similarity). Preferentially binds to alpha-2,3-linked sialic acid (PubMed:8995428). Binds ganglioside Gt1b (PubMed:8995428).By similarity4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 GT1bBy similarity1

<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

GO - Biological processi

<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-RNO-193634 Axonal growth inhibition (RHOA activation)
R-RNO-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):
1B2362 Publications
Brain neuron cytoplasmic protein 3
Sialic acid-binding Ig-like lectin 4a
Short name:
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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 1

Organism-specific databases

Rat genome database

More...
RGDi
3035 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 & Seán O’Donoghue; 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

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>Mutagenesisi118R → A or D: Abolishes inhibition of neurite outgrowth from CNS neurons. 1 Publication1
Mutagenesisi118R → A: No effect on inhibition of neurite outgrowth from sensory neurons. 1 Publication1

<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_000001485820 – 626Myelin-associated glycoproteinAdd BLAST607

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 ↔ 1651 Publication
Disulfide bondi42 ↔ 1001 Publication
<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>Glycosylationi99N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi159 ↔ 2171 Publication
Glycosylationi223N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi246N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi261 ↔ 3051 Publication
Glycosylationi315N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi332N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi347 ↔ 3921 Publication
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi421 ↔ 4301 Publication
Disulfide bondi432 ↔ 4881 Publication
Glycosylationi450N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi454N-linked (GlcNAc...) asparagineSequence analysis1
<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 cysteine1 Publication1
<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 residuei545PhosphoserineCombined sources1
Modified residuei547PhosphoserineCombined sources1
Modified residuei549PhosphoserineCombined 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.By similarity
Phosphorylated on tyrosine residues.1 Publication
Ubiquitinated, leading to proteasomal degradation.By similarity

Keywords - PTMi

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

Proteomic databases

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

More...
PaxDbi
P07722

PRoteomics IDEntifications database

More...
PRIDEi
P07722

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07722

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

More...
PhosphoSitePlusi
P07722

<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 myelin (PubMed:17640868). Detected in olfactory bulb and throughout the brain (at protein level) (PubMed:4020419). Detected in brain (PubMed:2432614).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000021023 Expressed in 6 organ(s), highest expression level in brain

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P07722 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P07722 RN

<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 (By similarity).

Interacts (via the first three N-terminal Ig-like domains) with RTN4R and RTN4RL2 (PubMed:19420245).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
248059, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000028544

<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

3D structure databases

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

More...
SMRi
P07722

Database of comparative protein structure models

More...
ModBasei
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 RTN4RL21 PublicationAdd BLAST306
Regioni65 – 67Ganglioside GT1b bindingBy similarity3
Regioni124 – 128Ganglioside GT1b bindingBy similarity5
Regioni577 – 626Required for normal axon myelination in the central nervous systemBy similarityAdd 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).By similarity
The extracellular domain is required to protect against axon degeneration (By similarity). The first three Ig-like domains mediate interaction with RTN4R and RTN4RL2, but are not sufficient to inhibit neurite outgrowth (PubMed:19420245). The two C-terminal extracellular Ig-like C2-type domains are required for inhibition of axon longitudinal growth (PubMed:9298990, PubMed:19420245, PubMed:19367338). Besides, the two C-terminal extracellular Ig-like C2-type domains are required for protection against apoptosis after nerve injury (By similarity).By similarity3 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

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IUGJ Eukaryota
ENOG410XQVV LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182663

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000113464

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07722

KEGG Orthology (KO)

More...
KOi
K06771

Identification of Orthologs from Complete Genome Data

More...
OMAi
CVVKANP

Database of Orthologous Groups

More...
OrthoDBi
415025at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07722

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>. The information is filed in different subsections. The current subsections and their content are listed below:<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 1 potential isoform that is computationally mapped.Show allAlign All

Isoform L-MAG (identifier: P07722-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MIFLTTLPLF WIMISASRGG HWGAWMPSSI SAFEGTCVSI PCRFDFPDEL
60 70 80 90 100
RPAVVHGVWY FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC
110 120 130 140 150
TLLLSTLSPE LGGKYYFRGD LGGYNQYTFS EHSVLDIINT PNIVVPPEVV
160 170 180 190 200
AGTEVEVSCM VPDNCPELRP ELSWLGHEGL GEPTVLGRLR EDEGTWVQVS
210 220 230 240 250
LLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP VIVEMNSSVE
260 270 280 290 300
AIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAESLYL DLEEVTPAED
310 320 330 340 350
GIYACLAENA 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 TSILTLRGQA QAPPRVICTS RNLYGTQSLE
510 520 530 540 550
LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK NVTESPSFSA
560 570 580 590 600
GDNPHVLYSP EFRISGAPDK YESEKRLGSE RRLLGLRGEP PELDLSYSHS
610 620
DLGKRPTKDS YTLTEELAEY AEIRVK
Length:626
Mass (Da):69,353
Last modified:April 1, 1988 - v1
<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:iE97998E280ECD635
GO
Isoform S-MAG (identifier: P07722-2) [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):64,351
Checksum:i2A7A9A9FF76D48C4
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V9B3G3V9B3_RAT
Myelin-associated glycoprotein
Mag rCG_53777
582Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti309 – 310NA → KS (PubMed:6586369).Curated2
Sequence conflicti309 – 310NA → KS (PubMed:4020419).Curated2
Sequence conflicti309 – 310NA → KS (PubMed:6347394).Curated2

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002529574 – 582EKRLGSERR → REVSTRDCH in isoform S-MAG. 1 Publication9
Alternative sequenceiVSP_002530583 – 626Missing in isoform S-MAG. 1 PublicationAdd 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
M14871 mRNA Translation: AAA41556.1
M22357 mRNA Translation: AAA41558.1
M16800 mRNA Translation: AAA41557.1
X05301 mRNA Translation: CAA28920.1
M11721 mRNA Translation: AAA42082.1
M36702 mRNA Translation: AAA40831.1
V01544 Genomic DNA Translation: CAA24786.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A29028 BNRT3

NCBI Reference Sequences

More...
RefSeqi
NP_058886.1, NM_017190.4 [P07722-1]
XP_006228886.1, XM_006228824.3 [P07722-1]
XP_008757360.1, XM_008759138.2 [P07722-1]
XP_017444540.1, XM_017589051.1 [P07722-1]
XP_017444541.1, XM_017589052.1 [P07722-1]
XP_017444542.1, XM_017589053.1 [P07722-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000028544; ENSRNOP00000028544; ENSRNOG00000021023 [P07722-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29409

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:29409

UCSC genome browser

More...
UCSCi
RGD:3035 rat [P07722-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14871 mRNA Translation: AAA41556.1
M22357 mRNA Translation: AAA41558.1
M16800 mRNA Translation: AAA41557.1
X05301 mRNA Translation: CAA28920.1
M11721 mRNA Translation: AAA42082.1
M36702 mRNA Translation: AAA40831.1
V01544 Genomic DNA Translation: CAA24786.1
PIRiA29028 BNRT3
RefSeqiNP_058886.1, NM_017190.4 [P07722-1]
XP_006228886.1, XM_006228824.3 [P07722-1]
XP_008757360.1, XM_008759138.2 [P07722-1]
XP_017444540.1, XM_017589051.1 [P07722-1]
XP_017444541.1, XM_017589052.1 [P07722-1]
XP_017444542.1, XM_017589053.1 [P07722-1]

3D structure databases

SMRiP07722
ModBaseiSearch...

Protein-protein interaction databases

BioGridi248059, 2 interactors
STRINGi10116.ENSRNOP00000028544

PTM databases

iPTMnetiP07722
PhosphoSitePlusiP07722

Proteomic databases

PaxDbiP07722
PRIDEiP07722

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028544; ENSRNOP00000028544; ENSRNOG00000021023 [P07722-1]
GeneIDi29409
KEGGirno:29409
UCSCiRGD:3035 rat [P07722-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4099
RGDi3035 Mag

Phylogenomic databases

eggNOGiENOG410IUGJ Eukaryota
ENOG410XQVV LUCA
GeneTreeiENSGT00950000182663
HOGENOMiHOG000113464
InParanoidiP07722
KOiK06771
OMAiCVVKANP
OrthoDBi415025at2759
PhylomeDBiP07722
TreeFamiTF332441

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P07722

Gene expression databases

BgeeiENSRNOG00000021023 Expressed in 6 organ(s), highest expression level in brain
ExpressionAtlasiP07722 baseline and differential
GenevisibleiP07722 RN

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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_RAT
<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: P07722
Secondary accession number(s): P02685, P07723
<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: July 21, 1986
Last sequence update: April 1, 1988
Last modified: May 8, 2019
This is version 162 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again