GPM6B_MOUSE
ID GPM6B_MOUSE Reviewed; 328 AA.
AC P35803; A2AEG4; Q8R3J6; Q99L14; Q9D4F5; Q9JHG9; Q9JHI1; Q9JHK2; Q9JI62;
AC Q9JI63; Q9JI64; Q9JI65;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Neuronal membrane glycoprotein M6-b;
DE Short=M6b;
GN Name=Gpm6b; Synonyms=M6b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
RC TISSUE=Brain;
RX PubMed=8398137; DOI=10.1016/0896-6273(93)90147-j;
RA Yan Y., Lagenaur C., Narayanan V.;
RT "Molecular cloning of M6: identification of a PLP/DM20 gene family.";
RL Neuron 11:423-431(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8),
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11749036; DOI=10.1006/mcne.2001.1044;
RA Werner H., Dimou L., Klugmann M., Pfeiffer S., Nave K.A.;
RT "Multiple splice isoforms of proteolipid M6B in neurons and
RT oligodendrocytes.";
RL Mol. Cell. Neurosci. 18:593-605(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 158-164; 231-243; 299-306 AND 320-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318; SER-320 AND SER-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 {ECO:0000269|PubMed:18581270}.
CC -!- SUBUNIT: Interacts with SERT. {ECO:0000269|PubMed:18581270}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC membrane. Note=Colocalizes with SERT at the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=Alpha-beta-TMD-omega;
CC IsoId=P35803-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha-beta-TMD-psi;
CC IsoId=P35803-2; Sequence=VSP_007324, VSP_007325;
CC Name=3; Synonyms=TMD-omega;
CC IsoId=P35803-3; Sequence=VSP_007318;
CC Name=4; Synonyms=Alpha-TMD-psi;
CC IsoId=P35803-4; Sequence=VSP_007320, VSP_007324, VSP_007325;
CC Name=5; Synonyms=TMD-psi;
CC IsoId=P35803-5; Sequence=VSP_007318, VSP_007324, VSP_007325;
CC Name=6; Synonyms=Alpha-beta-gamma;
CC IsoId=P35803-6; Sequence=VSP_007322, VSP_007323;
CC Name=7; Synonyms=Alpha-gamma;
CC IsoId=P35803-7; Sequence=VSP_007319, VSP_007321;
CC Name=8; Synonyms=Alpha-TMD-omega;
CC IsoId=P35803-8; Sequence=VSP_007320;
CC -!- TISSUE SPECIFICITY: Widely expressed. In the brain, expressed in
CC neurons and oligodendrocytes. {ECO:0000269|PubMed:11749036}.
CC -!- DEVELOPMENTAL STAGE: First detected in presumptive postmitotic neurons
CC in the developing neural tube at embryonic day 9.
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
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DR EMBL; S65737; AAB28351.1; -; mRNA.
DR EMBL; AF254869; AAF87987.1; -; mRNA.
DR EMBL; AF254870; AAF87988.1; -; mRNA.
DR EMBL; AF254871; AAF87989.1; -; mRNA.
DR EMBL; AF254872; AAF87990.1; -; mRNA.
DR EMBL; AF254873; AAF87991.1; -; mRNA.
DR EMBL; AF254874; AAF87992.1; -; mRNA.
DR EMBL; AF254875; AAF87993.1; -; mRNA.
DR EMBL; AF254876; AAF87994.1; -; mRNA.
DR EMBL; AF254877; AAF87995.1; -; mRNA.
DR EMBL; AF254878; AAF87996.1; -; mRNA.
DR EMBL; AF254879; AAF87997.1; -; mRNA.
DR EMBL; AK016567; BAB30309.1; -; mRNA.
DR EMBL; AL671905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003912; AAH03912.1; -; mRNA.
DR EMBL; BC025165; AAH25165.1; -; mRNA.
DR CCDS; CCDS30526.1; -. [P35803-3]
DR CCDS; CCDS53243.1; -. [P35803-5]
DR CCDS; CCDS53244.1; -. [P35803-2]
DR CCDS; CCDS53245.1; -. [P35803-1]
DR CCDS; CCDS53246.1; -. [P35803-4]
DR CCDS; CCDS53247.1; -. [P35803-8]
DR RefSeq; NP_001171426.1; NM_001177955.1.
DR RefSeq; NP_001171427.1; NM_001177956.1.
DR RefSeq; NP_001171428.1; NM_001177957.1.
DR RefSeq; NP_001171429.1; NM_001177958.1. [P35803-8]
DR RefSeq; NP_001171430.1; NM_001177959.1. [P35803-4]
DR RefSeq; NP_001171431.1; NM_001177960.1. [P35803-4]
DR RefSeq; NP_001171432.1; NM_001177961.1. [P35803-5]
DR RefSeq; NP_001171433.1; NM_001177962.1. [P35803-5]
DR RefSeq; NP_075611.1; NM_023122.3. [P35803-3]
DR AlphaFoldDB; P35803; -.
DR BioGRID; 200024; 2.
DR IntAct; P35803; 2.
DR MINT; P35803; -.
DR STRING; 10090.ENSMUSP00000107848; -.
DR TCDB; 9.B.38.1.3; the myelin proteolipid protein (mplp) family.
DR GlyConnect; 2551; 1 N-Linked glycan (1 site).
DR GlyGen; P35803; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P35803; -.
DR PhosphoSitePlus; P35803; -.
DR SwissPalm; P35803; -.
DR MaxQB; P35803; -.
DR PaxDb; P35803; -.
DR PeptideAtlas; P35803; -.
DR PRIDE; P35803; -.
DR ProteomicsDB; 271145; -. [P35803-1]
DR ProteomicsDB; 271146; -. [P35803-2]
DR ProteomicsDB; 271147; -. [P35803-3]
DR ProteomicsDB; 271148; -. [P35803-4]
DR ProteomicsDB; 271149; -. [P35803-5]
DR ProteomicsDB; 271150; -. [P35803-6]
DR ProteomicsDB; 271151; -. [P35803-7]
DR ProteomicsDB; 271152; -. [P35803-8]
DR Antibodypedia; 484; 148 antibodies from 24 providers.
DR DNASU; 14758; -.
DR Ensembl; ENSMUST00000060210; ENSMUSP00000060442; ENSMUSG00000031342. [P35803-3]
DR Ensembl; ENSMUST00000112224; ENSMUSP00000107843; ENSMUSG00000031342. [P35803-4]
DR Ensembl; ENSMUST00000112226; ENSMUSP00000107845; ENSMUSG00000031342. [P35803-4]
DR Ensembl; ENSMUST00000112228; ENSMUSP00000107847; ENSMUSG00000031342. [P35803-8]
DR Ensembl; ENSMUST00000112233; ENSMUSP00000107852; ENSMUSG00000031342. [P35803-5]
DR Ensembl; ENSMUST00000112235; ENSMUSP00000107854; ENSMUSG00000031342. [P35803-5]
DR Ensembl; ENSMUST00000143263; ENSMUSP00000135378; ENSMUSG00000031342. [P35803-7]
DR GeneID; 14758; -.
DR KEGG; mmu:14758; -.
DR UCSC; uc009uwg.2; mouse. [P35803-3]
DR UCSC; uc009uwm.2; mouse. [P35803-4]
DR CTD; 2824; -.
DR MGI; MGI:107672; Gpm6b.
DR VEuPathDB; HostDB:ENSMUSG00000031342; -.
DR eggNOG; KOG4800; Eukaryota.
DR GeneTree; ENSGT00390000006915; -.
DR HOGENOM; CLU_064167_2_0_1; -.
DR InParanoid; P35803; -.
DR OMA; CMARVPY; -.
DR OrthoDB; 914457at2759; -.
DR PhylomeDB; P35803; -.
DR BioGRID-ORCS; 14758; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gpm6b; mouse.
DR PRO; PR:P35803; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P35803; protein.
DR Bgee; ENSMUSG00000031342; Expressed in cerebellum lobe and 259 other tissues.
DR ExpressionAtlas; P35803; baseline and differential.
DR Genevisible; P35803; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0085029; P:extracellular matrix assembly; ISS:UniProtKB.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0051612; P:negative regulation of serotonin uptake; IDA: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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW Glycoprotein; Membrane; Osteogenesis; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..328
FT /note="Neuronal membrane glycoprotein M6-b"
FT /id="PRO_0000159022"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 2..60
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11749036,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_007318"
FT VAR_SEQ 21..60
FT /note="Missing (in isoform 4 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:11749036,
FT ECO:0000303|PubMed:8398137"
FT /id="VSP_007320"
FT VAR_SEQ 21..49
FT /note="VNSRAEMEIGRYHWMYPGSKNHQYRPVPN -> GSKNAKHLAKAGIANRFRM
FT PHLSLGRWDC (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:11749036"
FT /id="VSP_007319"
FT VAR_SEQ 50..328
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:11749036"
FT /id="VSP_007321"
FT VAR_SEQ 62..89
FT /note="CFECCIKCLGGVPYASLVATILCFSGVA -> SKNAKHLAKAGIANRFRMPH
FT LSLGRWDC (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11749036"
FT /id="VSP_007322"
FT VAR_SEQ 90..328
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11749036"
FT /id="VSP_007323"
FT VAR_SEQ 280..305
FT /note="IHFLMILSSNWAYLKDASKMQAYQDI -> LIYMMATTYNYAVLKFKSREDC
FT CTKF (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11749036,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007324"
FT VAR_SEQ 306..328
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11749036,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007325"
FT CONFLICT 288
FT /note="S -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 36210 MW; 88BE3C67DF024B33 CRC64;
MKPAMETAAE ENTEQSQERK VNSRAEMEIG RYHWMYPGSK NHQYRPVPNL GDRAGPLSSP
GCFECCIKCL GGVPYASLVA TILCFSGVAL FCGCGHVALA GTVAILEQHF STNTSDHALL
SEVIQLMQYV IYGIASFFFL YGIILLAEGF YTTSAVKELH GEFKTTACGR CISGMFVFLT
YVLGVAWLGV FGFSAVPVFM FYNIWSTCEV IKSPQSNGTS GVEQICVDVR QYGIIPWNAF
PGKICGSALE NICNTNEFYM SYHLFIVACA GAGATVIALI HFLMILSSNW AYLKDASKMQ
AYQDIKAKEE QELQDIQSRS KEQLNSYT
