MOBP_MOUSE
ID MOBP_MOUSE Reviewed; 170 AA.
AC Q9D2P8; O35713; Q792D7; Q792D8; Q9JLY4; Q9JLY5; Q9JLY6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Myelin-associated oligodendrocyte basic protein;
GN Name=Mobp;
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 2).
RC STRAIN=C57BL/6J;
RX PubMed=8551331; DOI=10.1523/jneurosci.16-02-00467.1996;
RA Holz A., Schaeren-Wiemers N., Schaefer C., Pott U., Colello R.J.,
RA Schwab M.E.;
RT "Molecular and developmental characterization of novel cDNAs of the myelin-
RT associated/oligodendrocytic basic protein.";
RL J. Neurosci. 16:467-477(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1; 2;
RP 3; 4 AND 5).
RC STRAIN=129/Sv;
RX PubMed=10328883; DOI=10.1006/mcne.1999.0745;
RA McCallion A.S., Stewart G.J., Montague P., Griffiths I.R., Davies R.W.;
RT "Splicing pattern, transcript start distribution, and DNA sequence of the
RT mouse gene (Mobp) encoding myelin-associated oligodendrocytic basic
RT protein.";
RL Mol. Cell. Neurosci. 13:229-236(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RC STRAIN=CAST/EiJ, and SJL/J;
RA Lee I.Y., Baxter D.H., Qin S., Hood L.E.;
RT "Genomic sequence analysis of laminin receptor loci in mice.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, and Hippocampus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP 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 play a role in compacting or stabilizing the myelin
CC sheath possibly by binding the negatively charged acidic phospholipids
CC of the cytoplasmic membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Note=Present in
CC the major dense line of CNS myelin. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=MOBP170;
CC IsoId=Q9D2P8-1; Sequence=Displayed;
CC Name=2; Synonyms=MOBP81;
CC IsoId=Q9D2P8-2; Sequence=VSP_023936, VSP_023942;
CC Name=3; Synonyms=MOBP73;
CC IsoId=Q9D2P8-3; Sequence=VSP_023937, VSP_023941;
CC Name=4; Synonyms=MOBP69;
CC IsoId=Q9D2P8-4; Sequence=VSP_023938, VSP_023939;
CC Name=5; Synonyms=MOBP74;
CC IsoId=Q9D2P8-5; Sequence=VSP_023940, VSP_023941;
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DR EMBL; U81317; AAB65617.1; -; mRNA.
DR EMBL; AF120475; AAF60192.1; -; Genomic_DNA.
DR EMBL; AF120476; AAF60193.1; -; Genomic_DNA.
DR EMBL; AF120475; AAF60193.1; JOINED; Genomic_DNA.
DR EMBL; AF120475; AAF60194.1; -; Genomic_DNA.
DR EMBL; AF120476; AAF60195.1; -; Genomic_DNA.
DR EMBL; AF120475; AAF60195.1; JOINED; Genomic_DNA.
DR EMBL; AF120477; AAF60196.1; -; Genomic_DNA.
DR EMBL; AF120475; AAF60196.1; JOINED; Genomic_DNA.
DR EMBL; DQ360291; ABC95974.1; -; Genomic_DNA.
DR EMBL; DQ360292; ABC95978.1; -; Genomic_DNA.
DR EMBL; AK013799; BAB28998.1; -; mRNA.
DR EMBL; AK019323; BAB31666.1; -; mRNA.
DR EMBL; AK028057; BAC25727.1; -; mRNA.
DR EMBL; AK083103; BAC38761.1; -; mRNA.
DR EMBL; AK140055; BAE24224.1; -; mRNA.
DR EMBL; BC048492; AAH48492.1; -; mRNA.
DR CCDS; CCDS23626.1; -. [Q9D2P8-1]
DR CCDS; CCDS40808.1; -. [Q9D2P8-2]
DR RefSeq; NP_001034453.1; NM_001039364.2.
DR RefSeq; NP_001034454.1; NM_001039365.2. [Q9D2P8-1]
DR RefSeq; NP_032640.1; NM_008614.2. [Q9D2P8-2]
DR AlphaFoldDB; Q9D2P8; -.
DR SMR; Q9D2P8; -.
DR STRING; 10090.ENSMUSP00000071084; -.
DR iPTMnet; Q9D2P8; -.
DR PhosphoSitePlus; Q9D2P8; -.
DR SwissPalm; Q9D2P8; -.
DR PaxDb; Q9D2P8; -.
DR PeptideAtlas; Q9D2P8; -.
DR PRIDE; Q9D2P8; -.
DR ProteomicsDB; 290270; -. [Q9D2P8-1]
DR ProteomicsDB; 290271; -. [Q9D2P8-2]
DR ProteomicsDB; 290272; -. [Q9D2P8-3]
DR ProteomicsDB; 290273; -. [Q9D2P8-4]
DR ProteomicsDB; 290274; -. [Q9D2P8-5]
DR Antibodypedia; 28962; 198 antibodies from 28 providers.
DR DNASU; 17433; -.
DR Ensembl; ENSMUST00000068698; ENSMUSP00000071084; ENSMUSG00000032517. [Q9D2P8-1]
DR Ensembl; ENSMUST00000093773; ENSMUSP00000091287; ENSMUSG00000032517. [Q9D2P8-2]
DR Ensembl; ENSMUST00000111627; ENSMUSP00000107254; ENSMUSG00000032517. [Q9D2P8-2]
DR Ensembl; ENSMUST00000174193; ENSMUSP00000134410; ENSMUSG00000032517. [Q9D2P8-2]
DR Ensembl; ENSMUST00000214943; ENSMUSP00000149285; ENSMUSG00000032517. [Q9D2P8-2]
DR Ensembl; ENSMUST00000215512; ENSMUSP00000149831; ENSMUSG00000032517. [Q9D2P8-4]
DR GeneID; 17433; -.
DR KEGG; mmu:17433; -.
DR UCSC; uc009scj.1; mouse. [Q9D2P8-1]
DR UCSC; uc009sck.1; mouse. [Q9D2P8-2]
DR CTD; 4336; -.
DR MGI; MGI:108511; Mobp.
DR VEuPathDB; HostDB:ENSMUSG00000032517; -.
DR eggNOG; ENOG502TDAR; Eukaryota.
DR GeneTree; ENSGT00950000183138; -.
DR HOGENOM; CLU_1481517_0_0_1; -.
DR InParanoid; Q9D2P8; -.
DR OMA; CCAPFSF; -.
DR OrthoDB; 492485at2759; -.
DR PhylomeDB; Q9D2P8; -.
DR BioGRID-ORCS; 17433; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Mobp; mouse.
DR PRO; PR:Q9D2P8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D2P8; protein.
DR Bgee; ENSMUSG00000032517; Expressed in cerebellar nuclear complex and 106 other tissues.
DR Genevisible; Q9D2P8; MM.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IDA:MGI.
DR GO; GO:0032289; P:central nervous system myelin formation; IEA:Ensembl.
DR InterPro; IPR041282; FYVE_2.
DR Pfam; PF02318; FYVE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..170
FT /note="Myelin-associated oligodendrocyte basic protein"
FT /id="PRO_0000281026"
FT REPEAT 93..101
FT /note="1"
FT REPEAT 105..110
FT /note="2"
FT REPEAT 111..115
FT /note="3; half-length"
FT REGION 69..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..115
FT /note="3 X 9 AA approximate tandem repeats"
FT COMPBIAS 92..114
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63327"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63327"
FT VAR_SEQ 69..81
FT /note="SRRATSPQRPKHQ -> RLRRRSRSTPRKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8551331"
FT /id="VSP_023936"
FT VAR_SEQ 69..73
FT /note="SRRAT -> RTVRK (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_023937"
FT VAR_SEQ 69
FT /note="S -> R (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_023938"
FT VAR_SEQ 70..170
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_023939"
FT VAR_SEQ 70..73
FT /note="RRAT -> MTFW (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_023940"
FT VAR_SEQ 74..170
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_023941"
FT VAR_SEQ 82..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8551331"
FT /id="VSP_023942"
FT CONFLICT 5
FT /note="M -> V (in Ref. 2; AAF60192/AAF60193/AAF60194/
FT AAF60195/AAF60196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 170 AA; 19197 MW; E3132C958C631BC4 CRC64;
MSQKMAKEGP RLSKNQKFSE HFSIHCCPPF TFLNSKREIV DRKYSICKSG CFYQKKEEDW
ICCACQKTSR RATSPQRPKH QPAASPVVVR APPAKPKSPL MPAKPRSPPR PAKPRSPSRT
ERQPRPRPEV RPPPAKQKPP QKSKQPARSS PLRGPGTSRG GSPTRAPRFW
