GPM6B_RAT
ID GPM6B_RAT Reviewed; 265 AA.
AC Q9JJK1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Neuronal membrane glycoprotein M6-b;
DE Short=M6b;
DE AltName: Full=Rhombencephalic expression protein-29 kDa;
DE Short=Rhombex-29;
GN Name=Gpm6b; Synonyms=M6b, rhombex-29;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INDUCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=11002282;
RX DOI=10.1002/1097-4547(20001001)62:1<1::aid-jnr1>3.0.co;2-k;
RA Shimokawa N., Miura M.;
RT "Rhombex-29, a novel gene of the PLP/DM20-M6 family cloned from rat medulla
RT oblongata by differential display.";
RL J. Neurosci. Res. 62:1-8(2000).
RN [2]
RP INTERACTION WITH SERT.
RX PubMed=18581270; DOI=10.1007/s12031-008-9092-4;
RA Fjorback A.W., Muller H.K., Wiborg O.;
RT "Membrane glycoprotein M6B interacts with the human serotonin
RT transporter.";
RL J. Mol. Neurosci. 37:191-200(2009).
CC -!- FUNCTION: May be involved in neural development. Involved in regulation
CC of osteoblast function and bone formation. Involved in matrix vesicle
CC release by osteoblasts; this function seems to involve maintenance of
CC the actin cytoskeleton. May be involved in cellular trafficking of SERT
CC and thereby in regulation of serotonin uptake.
CC -!- SUBUNIT: Interacts with SERT. {ECO:0000269|PubMed:18581270}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:11002282}.
CC Note=Colocalizes with SERT at the plasma membrane.
CC -!- TISSUE SPECIFICITY: Highly expressed in the ventral medullary surface,
CC moderately in the cerebral cortex and cerebellum, poorly in lung and
CC kidney, and not at all in heart, skeletal muscle, liver, stomach or
CC stomach. {ECO:0000269|PubMed:11002282}.
CC -!- DEVELOPMENTAL STAGE: In the developing brain, expression begins by at
CC least embryonic day 20, increases gradually through postnatal day 2 and
CC day 50 and decreases by postnatal day 300.
CC {ECO:0000269|PubMed:11002282}.
CC -!- INDUCTION: By hypercapnic stimulation (CO2 inhalation) in ventral
CC medullary surface neurons but not in the cerebral cortex.
CC {ECO:0000269|PubMed:11002282}.
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
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DR EMBL; AB036421; BAA98020.1; -; mRNA.
DR RefSeq; NP_620201.1; NM_138846.1.
DR AlphaFoldDB; Q9JJK1; -.
DR BioGRID; 251339; 2.
DR IntAct; Q9JJK1; 1.
DR STRING; 10116.ENSRNOP00000006777; -.
DR GlyGen; Q9JJK1; 2 sites.
DR PhosphoSitePlus; Q9JJK1; -.
DR SwissPalm; Q9JJK1; -.
DR PaxDb; Q9JJK1; -.
DR PRIDE; Q9JJK1; -.
DR GeneID; 192179; -.
DR KEGG; rno:192179; -.
DR UCSC; RGD:620580; rat.
DR CTD; 2824; -.
DR RGD; 620580; Gpm6b.
DR eggNOG; KOG4800; Eukaryota.
DR InParanoid; Q9JJK1; -.
DR OrthoDB; 914457at2759; -.
DR PhylomeDB; Q9JJK1; -.
DR PRO; PR:Q9JJK1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0085029; P:extracellular matrix assembly; ISS:UniProtKB.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0051612; P:negative regulation of serotonin uptake; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion 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 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Differentiation; Glycoprotein;
KW Membrane; Neurogenesis; Osteogenesis; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..265
FT /note="Neuronal membrane glycoprotein M6-b"
FT /id="PRO_0000418017"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35803"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 265 AA; 28973 MW; 81BA7690D70C1333 CRC64;
MKPAMETAAE ENTEQSQERK GCFECCIKCL GGVPYASLVA TILCFSGVAL FCGCGHVALA
GTVAILEQHF STNTSDHALL SEVIQLMQYV IYGIASFFFL YGIILLAEGF YTTSAVKELH
GEFKTTACGR CISGMFVFLT YVLGVAWLGV FGFSAVPVFM FYNIWSTCEV IKSPQSNGTS
GVEQICVDVR QYGIIPWNAF PGKICGSALE NICNTNEFYM SYHLFIVACA GAGATVIALL
IYMMATTYNY AVLKFKSRED CCPKF
