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Q812E9

- GPM6A_RAT

UniProt

Q812E9 - GPM6A_RAT

Protein

Neuronal membrane glycoprotein M6-a

Gene

Gpm6a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Involved in neuronal differentiation, including differentiation and migration of neuronal stem cells By similarity. Plays a role in neuronal plasticity and is involved in neurite and filopodia outgrowth, filopodia motility and probably synapse formation. Gpm6a-induced filopodia formation involves mitogen-activated protein kinase (MAPK) and Src signaling pathways. May be involved in neuronal NGF-dependent Ca2+ influx. May be involved in regulation of endocytosis and intracellular trafficking of G-protein-coupled receptors (GPCRs); enhances internalization and recycling of mu-type opioid receptor.By similarity6 Publications

    GO - Molecular functioni

    1. calcium channel activity Source: RGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. calcium ion transmembrane transport Source: GOC
    2. neural retina development Source: UniProtKB
    3. neuron migration Source: UniProtKB
    4. neuron projection morphogenesis Source: UniProtKB
    5. positive regulation of filopodium assembly Source: UniProtKB
    6. stem cell differentiation Source: UniProtKB
    7. synapse assembly Source: UniProtKB

    Keywords - Biological processi

    Neurogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuronal membrane glycoprotein M6-a
    Short name:
    M6a
    Gene namesi
    Name:Gpm6a
    Synonyms:m6a
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 16

    Organism-specific databases

    RGDi631368. Gpm6a.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Cell projectionaxon By similarity. Cell projectiondendritic spine. Cell projectionfilopodium
    Note: Localizes to cholesterol-rich lipid rafts of the plasma membrane of hippocampal neurons. Localized to plasma membrane of cell bodies and neurites of hippocampal neurons. Localized in membrane protrusions (filopodia and spines) of primary hippocampal neurons. Localized to the growth cone edge membrane of elongating axons By similarity.By similarity

    GO - Cellular componenti

    1. axonal growth cone Source: UniProtKB
    2. dendritic spine Source: UniProtKB-SubCell
    3. filopodium Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. neuronal cell body Source: UniProtKB
    6. neuron projection Source: UniProtKB
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101T → A: Reduces motility of Gpm6a-induced filopodia; when associated with A-256, A-267 and A-268. 1 Publication
    Mutagenesisi162 – 1621C → A: Abolishess cell surface expression. 1 Publication
    Mutagenesisi174 – 1741C → A: Impairs Gpm6a-induced filopodium formation. 1 Publication
    Mutagenesisi174 – 1741C → A: Impairs synaptic density in primary hippocampal neurons; when associated with A-192. 1 Publication
    Mutagenesisi192 – 1921C → A: Impairs Gpm6a-induced filopodium formation. 1 Publication
    Mutagenesisi192 – 1921C → A: Impairs synaptic density in primary hippocampal neurons; when associated with A-174. 1 Publication
    Mutagenesisi202 – 2021C → A: Abolishess cell surface expression. 1 Publication
    Mutagenesisi256 – 2561S → A: Reduces motility of Gpm6a-induced filopodia; when associated with A-10, A-267 and A-268. 1 Publication
    Mutagenesisi267 – 2671S → A: Reduces motility of Gpm6a-induced filopodia; when associated with A-10, A-256 and A-268. 1 Publication
    Mutagenesisi268 – 2681T → A: Reduces motility of Gpm6a-induced filopodia; when associated with A-10, A-256 and A-267. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 278278Neuronal membrane glycoprotein M6-aPRO_0000418016Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi174 ↔ 1921 Publication
    Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ812E9.
    PRIDEiQ812E9.

    PTM databases

    PhosphoSiteiQ812E9.

    Expressioni

    Tissue specificityi

    Expressed in hippocampus (at protein level). Isoform 1 is the predominant isoform expressed in brain, specifically in hippocampus. Isoform 2 is expressed at low levels in brain and kidney.2 Publications

    Inductioni

    Isoform 1 is down-regulated by chronic stress in dentate gyrus granule neurons and CA3 pyramidal neurons whereas isoform 2 is up-regulated in the medial prefrontal cortex.1 Publication

    Gene expression databases

    GenevestigatoriQ812E9.

    Interactioni

    Subunit structurei

    Interacts with OPRM1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Oprm1P335357EBI-6113756,EBI-4392569

    Protein-protein interaction databases

    IntActiQ812E9. 1 interaction.
    STRINGi10116.ENSRNOP00000014312.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini44 – 8441ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini106 – 12722CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini149 – 21365Extracellular1 PublicationAdd
    BLAST
    Topological domaini235 – 27844CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei23 – 4321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei85 – 10521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei128 – 14821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei214 – 23421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the myelin proteolipid protein family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG322245.
    GeneTreeiENSGT00390000006915.
    HOGENOMiHOG000231338.
    HOVERGENiHBG000096.
    InParanoidiQ812E9.
    OMAiEEKKVCT.
    OrthoDBiEOG7X3QRG.
    PhylomeDBiQ812E9.
    TreeFamiTF315162.

    Family and domain databases

    InterProiIPR001614. Myelin_PLP.
    IPR018237. Myelin_PLP_CS.
    [Graphical view]
    PANTHERiPTHR11683. PTHR11683. 1 hit.
    PfamiPF01275. Myelin_PLP. 1 hit.
    [Graphical view]
    PRINTSiPR00214. MYELINPLP.
    SMARTiSM00002. PLP. 1 hit.
    [Graphical view]
    PROSITEiPS00575. MYELIN_PLP_1. 1 hit.
    PS01004. MYELIN_PLP_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q812E9-1) [UniParc]FASTAAdd to Basket

    Also known as: Ib

    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.

    « Hide

    MEENMEEGQT QKGCFECCIK CLGGIPYASL IATILLYAGV ALFCGCGHEA    50
    LSGTVNILQT YFEMARTAGD TLDVFTMIDI FKYVIYGIAA AFFVYGILLM 100
    VEGFFTTGAI KDLYGDFKIT TCGRCVSAWF IMLTYLFMLA WLGVTAFTSL 150
    PVYMYFNVWT ICRNTTLVEG ANLCLDLRQF GIVTIGEEKK ICTVSENFLR 200
    MCESTELNMT FHLFIVALAG AGAAVIAMVH YLMVLSANWA YVKDACRMQK 250
    YEDIKSKEEQ ELHDIHSTRS KERLNAYT 278
    Length:278
    Mass (Da):31,196
    Last modified:June 1, 2003 - v1
    Checksum:iD2EDAF98C0E8715D
    GO
    Isoform 2 (identifier: Q812E9-2) [UniParc]FASTAAdd to Basket

    Also known as: Ia

    The sequence of this isoform differs from the canonical sequence as follows:
         1-12: MEENMEEGQTQK → M

    Show »
    Length:267
    Mass (Da):29,891
    Checksum:i9B3D31D6AFADF061
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1212MEENM…GQTQK → M in isoform 2. 1 PublicationVSP_043957Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB089242 mRNA. Translation: BAC56699.1.
    CH473995 Genomic DNA. Translation: EDL78956.1.
    BC088862 mRNA. Translation: AAH88862.1.
    DV216104 mRNA. No translation available.
    RefSeqiNP_835206.1. NM_178105.2. [Q812E9-1]
    XP_006253156.1. XM_006253094.1. [Q812E9-2]
    UniGeneiRn.34370.

    Genome annotation databases

    EnsembliENSRNOT00000014312; ENSRNOP00000014312; ENSRNOG00000010731. [Q812E9-1]
    GeneIDi306439.
    KEGGirno:306439.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB089242 mRNA. Translation: BAC56699.1 .
    CH473995 Genomic DNA. Translation: EDL78956.1 .
    BC088862 mRNA. Translation: AAH88862.1 .
    DV216104 mRNA. No translation available.
    RefSeqi NP_835206.1. NM_178105.2. [Q812E9-1 ]
    XP_006253156.1. XM_006253094.1. [Q812E9-2 ]
    UniGenei Rn.34370.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q812E9. 1 interaction.
    STRINGi 10116.ENSRNOP00000014312.

    PTM databases

    PhosphoSitei Q812E9.

    Proteomic databases

    PaxDbi Q812E9.
    PRIDEi Q812E9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000014312 ; ENSRNOP00000014312 ; ENSRNOG00000010731 . [Q812E9-1 ]
    GeneIDi 306439.
    KEGGi rno:306439.

    Organism-specific databases

    CTDi 2823.
    RGDi 631368. Gpm6a.

    Phylogenomic databases

    eggNOGi NOG322245.
    GeneTreei ENSGT00390000006915.
    HOGENOMi HOG000231338.
    HOVERGENi HBG000096.
    InParanoidi Q812E9.
    OMAi EEKKVCT.
    OrthoDBi EOG7X3QRG.
    PhylomeDBi Q812E9.
    TreeFami TF315162.

    Miscellaneous databases

    NextBioi 656030.
    PROi Q812E9.

    Gene expression databases

    Genevestigatori Q812E9.

    Family and domain databases

    InterProi IPR001614. Myelin_PLP.
    IPR018237. Myelin_PLP_CS.
    [Graphical view ]
    PANTHERi PTHR11683. PTHR11683. 1 hit.
    Pfami PF01275. Myelin_PLP. 1 hit.
    [Graphical view ]
    PRINTSi PR00214. MYELINPLP.
    SMARTi SM00002. PLP. 1 hit.
    [Graphical view ]
    PROSITEi PS00575. MYELIN_PLP_1. 1 hit.
    PS01004. MYELIN_PLP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "M6a acts as a nerve growth factor-gated Ca(2+) channel in neuronal differentiation."
      Mukobata S., Hibino T., Sugiyama A., Urano Y., Inatomi A., Kanai Y., Endo H., Tashiro F.
      Biochem. Biophys. Res. Commun. 297:722-728(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Gene expression profile of the rat eye iridocorneal angle: NEIBank expressed sequence tag analysis."
      Ahmed F., Torrado M., Zinovieva R.D., Senatorov V.V., Wistow G., Tomarev S.I.
      Invest. Ophthalmol. Vis. Sci. 45:3081-3090(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-188 (ISOFORM 2).
    5. "The stress-regulated protein M6a is a key modulator for neurite outgrowth and filopodium/spine formation."
      Alfonso J., Fernandez M.E., Cooper B., Flugge G., Frasch A.C.
      Proc. Natl. Acad. Sci. U.S.A. 102:17196-17201(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    6. "Membrane glycoprotein M6a interacts with the micro-opioid receptor and facilitates receptor endocytosis and recycling."
      Wu D.F., Koch T., Liang Y.J., Stumm R., Schulz S., Schroder H., Hollt V.
      J. Biol. Chem. 282:22239-22247(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH OPRM1.
    7. "Cysteine residues in the large extracellular loop (EC2) are essential for the function of the stress-regulated glycoprotein M6a."
      Fuchsova B., Fernandez M.E., Alfonso J., Frasch A.C.
      J. Biol. Chem. 284:32075-32088(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TOPOLOGY, DISULFIDE BOND, MUTAGENESIS OF CYS-162; CYS-174; CYS-192 AND CYS-202.
    8. "Expression of the axonal membrane glycoprotein M6a is regulated by chronic stress."
      Cooper B., Fuchs E., Flugge G.
      PLoS ONE 4:E3659-E3659(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION.
    9. "Filopodial protrusions induced by glycoprotein M6a exhibit high motility and aids synapse formation."
      Brocco M.A., Fernandez M.E., Frasch A.C.
      Eur. J. Neurosci. 31:195-202(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF THR-10; SER-256; SER-267 AND THR-268.
    10. "Neuronal glycoprotein M6a induces filopodia formation via association with cholesterol-rich lipid rafts."
      Scorticati C., Formoso K., Frasch A.C.
      J. Neurochem. 119:521-531(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiGPM6A_RAT
    AccessioniPrimary (citable) accession number: Q812E9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2012
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3