GPM6A_PONAB
ID GPM6A_PONAB Reviewed; 278 AA.
AC Q5R9Q3; Q5R463; Q5R6L6; Q5RDM1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Neuronal membrane glycoprotein M6-a;
DE Short=M6a;
GN Name=GPM6A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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);
CC enhances 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R9Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R9Q3-2; Sequence=VSP_016538;
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; CR857883; CAH90136.1; -; mRNA.
DR EMBL; CR858982; CAH91177.1; -; mRNA.
DR EMBL; CR859330; CAH91507.1; -; mRNA.
DR EMBL; CR860472; CAH92594.1; -; mRNA.
DR EMBL; CR861395; CAH93453.1; -; mRNA.
DR RefSeq; NP_001125689.1; NM_001132217.1. [Q5R9Q3-1]
DR RefSeq; NP_001128932.1; NM_001135460.1. [Q5R9Q3-2]
DR AlphaFoldDB; Q5R9Q3; -.
DR STRING; 9601.ENSPPYP00000016996; -.
DR Ensembl; ENSPPYT00000017685; ENSPPYP00000016996; ENSPPYG00000015214. [Q5R9Q3-2]
DR Ensembl; ENSPPYT00000046194; ENSPPYP00000039649; ENSPPYG00000015214. [Q5R9Q3-1]
DR GeneID; 100172611; -.
DR GeneID; 100189889; -.
DR KEGG; pon:100172611; -.
DR CTD; 2823; -.
DR eggNOG; KOG4800; Eukaryota.
DR GeneTree; ENSGT00390000006915; -.
DR HOGENOM; CLU_064167_2_0_1; -.
DR InParanoid; Q5R9Q3; -.
DR OrthoDB; 914457at2759; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
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; PTHR11683; 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; Alternative splicing; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Lipoprotein; Membrane; Neurogenesis;
KW Palmitate; Phosphoprotein; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..278
FT /note="Neuronal membrane glycoprotein M6-a"
FT /id="PRO_0000159020"
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"
FT VAR_SEQ 1..12
FT /note="MEENMEEGQTQK -> M (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016538"
FT CONFLICT 81
FT /note="F -> L (in Ref. 1; CAH92594)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="M -> T (in Ref. 1; CAH92594)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="T -> P (in Ref. 1; CAH93453)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="E -> G (in Ref. 1; CAH93453)"
FT /evidence="ECO:0000305"
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
