ID   GPM6A_BOVIN             Reviewed;         278 AA.
AC   Q0VD07;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=Neuronal membrane glycoprotein M6-a;
DE            Short=M6a;
GN   Name=GPM6A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Brain cortex;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in neuronal differentiation, including
CC       differentiation and migration of neuronal stem cells. Plays a role in
CC       neuronal plasticity and is involved in neurite and filopodia outgrowth,
CC       filopodia motility and probably synapse formation. GPM6A-induced
CC       filopodia formation involves mitogen-activated protein kinase (MAPK)
CC       and Src signaling pathways. May be involved in neuronal NGF-dependent
CC       Ca(2+) influx. May be involved in regulation of endocytosis and
CC       intracellular trafficking of G-protein-coupled receptors (GPCRs); may
CC       enhance internalization and recycling of mu-type opioid receptor (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with OPRM1 (By similarity). Interacts with
CC       palmitoyltransferase ZDHHC17/HIP14; the interaction leads to
CC       palmitoylation of GPM6A (By similarity). {ECO:0000250|UniProtKB:P51674,
CC       ECO:0000250|UniProtKB:Q812E9}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35802};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P35802}. Cell
CC       projection, axon {ECO:0000250|UniProtKB:P35802}. Cell projection,
CC       growth cone {ECO:0000250|UniProtKB:P35802}. Cell projection, dendritic
CC       spine {ECO:0000250|UniProtKB:Q812E9}. Cell projection, filopodium
CC       {ECO:0000250|UniProtKB:Q812E9}. Cell projection, neuron projection
CC       {ECO:0000250|UniProtKB:Q812E9}. Note=Localizes to cholesterol-rich
CC       lipid rafts of the plasma membrane of hippocampal neurons. Localized to
CC       plasma membrane of cell bodies and neurites of hippocampal neurons.
CC       Localized in membrane protrusions (filopodia and spines) of primary
CC       hippocampal neurons (By similarity). Localized to the growth cone edge
CC       membrane of elongating axons (By similarity).
CC       {ECO:0000250|UniProtKB:P35802, ECO:0000250|UniProtKB:Q812E9}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P51674}.
CC   -!- PTM: Palmitoylated by ZDHHC17/HIP14. {ECO:0000250|UniProtKB:P51674}.
CC   -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC       {ECO:0000305}.
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DR   EMBL; BC119902; AAI19903.1; -; mRNA.
DR   RefSeq; NP_001068777.1; NM_001075309.1.
DR   AlphaFoldDB; Q0VD07; -.
DR   STRING; 9913.ENSBTAP00000005543; -.
DR   GlyCosmos; Q0VD07; 2 sites, No reported glycans.
DR   Ensembl; ENSBTAT00000005543.5; ENSBTAP00000005543.5; ENSBTAG00000004231.5.
DR   GeneID; 507389; -.
DR   KEGG; bta:507389; -.
DR   CTD; 2823; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004231; -.
DR   VGNC; VGNC:97275; GPM6A.
DR   GeneTree; ENSGT00390000006915; -.
DR   InParanoid; Q0VD07; -.
DR   OMA; IQDENTH; -.
DR   OrthoDB; 3091734at2759; -.
DR   Proteomes; UP000009136; Chromosome 27.
DR   Bgee; ENSBTAG00000004231; Expressed in occipital lobe and 100 other cell types or tissues.
DR   GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0003407; P:neural retina development; ISS:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR   GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR   GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR   InterPro; IPR001614; Myelin_PLP.
DR   InterPro; IPR018237; Myelin_PLP_CS.
DR   PANTHER; PTHR11683; MYELIN PROTEOLIPID; 1.
DR   PANTHER; PTHR11683:SF4; NEURONAL MEMBRANE GLYCOPROTEIN M6-A; 1.
DR   Pfam; PF01275; Myelin_PLP; 1.
DR   PRINTS; PR00214; MYELINPLP.
DR   SMART; SM00002; PLP; 1.
DR   PROSITE; PS00575; MYELIN_PLP_1; 1.
DR   PROSITE; PS01004; MYELIN_PLP_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Cell projection; Disulfide bond; Glycoprotein;
KW   Lipoprotein; Membrane; Neurogenesis; Palmitate; Phosphoprotein;
KW   Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN           1..278
FT                   /note="Neuronal membrane glycoprotein M6-a"
FT                   /id="PRO_0000283789"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P51674"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35802"
FT   MOD_RES         278
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q812E9"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        174..192
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   278 AA;  31210 MW;  DD0DB598C0E86B5D CRC64;
     MEENMEEGQT QKGCFECCIK CLGGIPYASL IATILLYAGV ALFCGCGHEA LSGTVNILQT
     YFEMARTAGD TLDVFTMIDI FKYVIYGIAA AFFVYGILLM VEGFFTTGAI KDLYGDFKIT
     TCGRCVSAWF IMLTYLFMLA WLGVTAFTSL PVYMYFNLWT ICRNTTLVEG ANLCLDLRQF
     GIVTIGEEKK ICTVSENFLR MCESTELNMT FHLFIVALAG AGAAVIAMVH YLMVLSANWA
     YVKDACRMQK YEDIKSKEEQ ELHDIHSTRS KERLNAYT
//