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Q812E9

- GPM6A_RAT

UniProt

Q812E9 - GPM6A_RAT

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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

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

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei23 – 4321HelicalSequence AnalysisAdd
BLAST
Topological domaini44 – 8441ExtracellularSequence AnalysisAdd
BLAST
Transmembranei85 – 10521HelicalSequence AnalysisAdd
BLAST
Topological domaini106 – 12722CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei128 – 14821HelicalSequence AnalysisAdd
BLAST
Topological domaini149 – 21365Extracellular1 PublicationAdd
BLAST
Transmembranei214 – 23421HelicalSequence AnalysisAdd
BLAST
Topological domaini235 – 27844CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axonal growth cone Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  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
Complete GO annotation...

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.

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

        10         20         30         40         50
MEENMEEGQT QKGCFECCIK CLGGIPYASL IATILLYAGV ALFCGCGHEA
60 70 80 90 100
LSGTVNILQT YFEMARTAGD TLDVFTMIDI FKYVIYGIAA AFFVYGILLM
110 120 130 140 150
VEGFFTTGAI KDLYGDFKIT TCGRCVSAWF IMLTYLFMLA WLGVTAFTSL
160 170 180 190 200
PVYMYFNVWT ICRNTTLVEG ANLCLDLRQF GIVTIGEEKK ICTVSENFLR
210 220 230 240 250
MCESTELNMT FHLFIVALAG AGAAVIAMVH YLMVLSANWA YVKDACRMQK
260 270
YEDIKSKEEQ ELHDIHSTRS KERLNAYT
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:
EMBLi
GenBanki
DDBJi
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]
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:
EMBLi
GenBanki
DDBJi
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 ]
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

« Hide 'large scale' publications
  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 29, 2014
This is version 73 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