MOBP_RAT
ID MOBP_RAT Reviewed; 170 AA.
AC Q63327; Q63328; Q63343; Q63519; Q64266; Q9QZV5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Myelin-associated oligodendrocyte basic protein;
GN Name=Mobp;
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] (ISOFORMS 1 AND 6), FUNCTION, AND ALTERNATIVE
RP SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RX PubMed=7989345; DOI=10.1016/s0021-9258(18)31756-3;
RA Yamamoto Y., Mizuno R., Nishimura T., Ogawa Y., Yoshikawa H., Fujimura H.,
RA Adachi E., Kishimoto T., Yanagihara T., Sakoda S.;
RT "Cloning and expression of myelin-associated oligodendrocytic basic
RT protein. A novel basic protein constituting the central nervous system
RT myelin.";
RL J. Biol. Chem. 269:31725-31730(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 2-15,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=10537049;
RA Gould R.M., Freund C.M., Barbarese E.;
RT "Myelin-associated oligodendrocytic basic protein mRNAs reside at different
RT subcellular locations.";
RL J. Neurochem. 73:1913-1924(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Lewis; TISSUE=Oligodendrocyte;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-98 AND SER-107, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:7989345}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10537049, ECO:0000269|PubMed:8551331}. Note=Present
CC in the major dense line of CNS myelin. Isoform 5 may be differentially
CC localized in the oligodendrocytes or perinuclear region. Isoform 2, 4,
CC 5 and 6 are highly enriched in myelin. Isoform 1 and 3 are not enriched
CC in mylein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=rOPRP1;
CC IsoId=Q63327-1; Sequence=Displayed;
CC Name=2; Synonyms=MOBP169;
CC IsoId=Q63327-2; Sequence=VSP_023951;
CC Name=3; Synonyms=MOBP69;
CC IsoId=Q63327-3; Sequence=VSP_023946, VSP_023947;
CC Name=4; Synonyms=MOBP99;
CC IsoId=Q63327-4; Sequence=VSP_023943, VSP_023950;
CC Name=5; Synonyms=MOBP81-A, MOBP81-B;
CC IsoId=Q63327-5; Sequence=VSP_023944, VSP_023949;
CC Name=6; Synonyms=rOP1, MOBP71;
CC IsoId=Q63327-6; Sequence=VSP_023945, VSP_023948;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in oligodendrocytes, in CNS
CC myelin of the cerebrum and spinal cord. No expression seen in sciatic
CC nerve. {ECO:0000269|PubMed:10537049, ECO:0000269|PubMed:8551331}.
CC -!- DEVELOPMENTAL STAGE: Expression in different brain regions during
CC development is correlated with the progression of myelin formation.
CC Isoform 5 seems to be the most abundant spliced form expressed during
CC development. Expressed at P7 in optic nerve, at this time point, the
CC first compact myelin is formed. At P9 abundantly expressed in the optic
CC nerve. {ECO:0000269|PubMed:8551331}.
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DR EMBL; D28110; BAA05657.1; -; mRNA.
DR EMBL; D28111; BAA05658.1; -; mRNA.
DR EMBL; AF157498; AAD44968.1; -; mRNA.
DR EMBL; X87900; CAA61151.1; -; mRNA.
DR EMBL; X89637; CAA61795.1; -; mRNA.
DR EMBL; X89638; CAA61796.1; -; mRNA.
DR EMBL; X90402; CAA62039.1; -; mRNA.
DR EMBL; BC087694; AAH87694.1; -; mRNA.
DR PIR; B55663; B55663.
DR RefSeq; NP_036852.1; NM_012720.1. [Q63327-5]
DR RefSeq; XP_006244127.1; XM_006244065.3. [Q63327-1]
DR RefSeq; XP_006244129.1; XM_006244067.3. [Q63327-1]
DR RefSeq; XP_008764891.1; XM_008766669.2. [Q63327-1]
DR AlphaFoldDB; Q63327; -.
DR SMR; Q63327; -.
DR BioGRID; 247116; 1.
DR STRING; 10116.ENSRNOP00000025279; -.
DR iPTMnet; Q63327; -.
DR PhosphoSitePlus; Q63327; -.
DR SwissPalm; Q63327; -.
DR PaxDb; Q63327; -.
DR PRIDE; Q63327; -.
DR Ensembl; ENSRNOT00000025279; ENSRNOP00000025279; ENSRNOG00000018700. [Q63327-1]
DR Ensembl; ENSRNOT00000025343; ENSRNOP00000025344; ENSRNOG00000018700. [Q63327-5]
DR Ensembl; ENSRNOT00000104512; ENSRNOP00000080049; ENSRNOG00000018700. [Q63327-4]
DR GeneID; 25037; -.
DR KEGG; rno:25037; -.
DR UCSC; RGD:3101; rat. [Q63327-1]
DR CTD; 4336; -.
DR RGD; 3101; Mobp.
DR eggNOG; ENOG502TDAR; Eukaryota.
DR GeneTree; ENSGT00950000183138; -.
DR HOGENOM; CLU_2855470_0_0_1; -.
DR InParanoid; Q63327; -.
DR OMA; CCAPFSF; -.
DR PhylomeDB; Q63327; -.
DR PRO; PR:Q63327; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000018700; Expressed in cerebellum and 4 other tissues.
DR ExpressionAtlas; Q63327; baseline and differential.
DR Genevisible; Q63327; RN.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:RGD.
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:RGD.
DR GO; GO:0032289; P:central nervous system myelin formation; IEP:RGD.
DR GO; GO:0007399; P:nervous system development; IEP:RGD.
DR InterPro; IPR041282; FYVE_2.
DR Pfam; PF02318; FYVE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..170
FT /note="Myelin-associated oligodendrocyte basic protein"
FT /id="PRO_0000281027"
FT REPEAT 93..101
FT /note="1"
FT REPEAT 105..110
FT /note="2; half-length"
FT REPEAT 111..119
FT /note="3"
FT REGION 69..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..119
FT /note="3 X 9 AA approximate tandem repeats"
FT COMPBIAS 92..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..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:22673903"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 69..99
FT /note="SRRATSPQKPKHQPAASPVVVRAPPAKPKSP -> RIRAYAYILTAHNPVLV
FT IAYIRRSHRSHSFF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8551331"
FT /id="VSP_023943"
FT VAR_SEQ 69..81
FT /note="SRRATSPQKPKHQ -> RLRRRSRSTPRKK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8551331"
FT /id="VSP_023944"
FT VAR_SEQ 69..71
FT /note="SRR -> RTV (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:7989345"
FT /id="VSP_023945"
FT VAR_SEQ 69
FT /note="S -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8551331"
FT /id="VSP_023946"
FT VAR_SEQ 70..170
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8551331"
FT /id="VSP_023947"
FT VAR_SEQ 72..170
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:7989345"
FT /id="VSP_023948"
FT VAR_SEQ 82..170
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8551331"
FT /id="VSP_023949"
FT VAR_SEQ 100..170
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8551331"
FT /id="VSP_023950"
FT VAR_SEQ 170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10537049"
FT /id="VSP_023951"
SQ SEQUENCE 170 AA; 19103 MW; 9B2119B1CACDBEF5 CRC64;
MSQKVAKEGP RLSKNQKFSE HFSIHCCPPF TFLNSKREIV DRKYSICKSG CFYQKKEEDW
ICCACQKTSR RATSPQKPKH QPAASPVVVR APPAKPKSPP RPAKPRSPPI PAKPRSPSRT
ERQPRPRPEV RPPPAKQKPP QKSKQPARSS PLRGPGTSRG GSPTRAPRFW
