MYPR_BOVIN
ID MYPR_BOVIN Reviewed; 277 AA.
AC P04116; A2VDT3; Q3ZBU4; Q9TSH8;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Myelin proteolipid protein;
DE Short=PLP;
DE AltName: Full=Lipophilin;
GN Name=PLP1; Synonyms=PLP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9800346;
RA Pfeiffer I., Baumgartner B.G., Kriegesman B., Brenig B.;
RT "A polymorphic microsatellite in intron 2 of the bovine proteolipid protein
RT (PLP) gene.";
RL Anim. Genet. 29:410-411(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus, and Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-277.
RX PubMed=6195969; DOI=10.1016/0003-9861(83)90334-x;
RA Lees M.B., Chao B.H., Lin L.-F.H., Samiullah M., Laursen R.A.;
RT "Amino acid sequence of bovine white matter proteolipid.";
RL Arch. Biochem. Biophys. 226:643-656(1983).
RN [4]
RP PROTEIN SEQUENCE OF 2-277, AND PALMITOYLATION AT THR-199.
RX PubMed=6642431; DOI=10.1515/bchm2.1983.364.2.1455;
RA Stoffel W., Hillen H., Schroeder W., Deutzmann R.;
RT "The primary structure of bovine brain myelin lipophilin (proteolipid
RT apoprotein).";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:1455-1466(1983).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-277.
RX PubMed=3840591; DOI=10.1093/nar/13.20.7413;
RA Naismith A.L., Hoffman-Chudzik E., Tsui L.-C., Riordan J.R.;
RT "Study of the expression of myelin proteolipid protein (lipophilin) using a
RT cloned complementary DNA.";
RL Nucleic Acids Res. 13:7413-7425(1985).
RN [6]
RP DISULFIDE BOND.
RX PubMed=2473918; DOI=10.1016/0014-5793(89)80744-6;
RA Shaw S.Y., Laursen R.A., Lees M.B.;
RT "Identification of thiol groups and a disulfide crosslink site in bovine
RT myelin proteolipid protein.";
RL FEBS Lett. 250:306-310(1989).
RN [7]
RP DISULFIDE BONDS, PALMITOYLATION AT CYS-6; CYS-7; CYS-10; CYS-109; CYS-139
RP AND CYS-141, AND TOPOLOGY.
RX PubMed=1281423; DOI=10.1021/bi00164a002;
RA Weimbs T., Stoffel W.;
RT "Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-
RT bonded, and fatty acid thioester-linked cysteine residues and implications
RT for the membrane topology of PLP.";
RL Biochemistry 31:12289-12296(1992).
RN [8]
RP PALMITOYLATION AT CYS-109.
RX PubMed=1695508; DOI=10.1016/0006-291x(90)91284-y;
RA Bizzozero O.A., Good L.K., Evans J.C.;
RT "Cysteine-108 is an acylation site in myelin proteolipid protein.";
RL Biochem. Biophys. Res. Commun. 170:375-382(1990).
RN [9]
RP TOPOLOGY.
RX PubMed=6206491; DOI=10.1073/pnas.81.16.5012;
RA Stoffel W., Hillen H., Giersiefen H.;
RT "Structure and molecular arrangement of proteolipid protein of central
RT nervous system myelin.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5012-5016(1984).
RN [10]
RP TOPOLOGY.
RX PubMed=1711121; DOI=10.1007/bf01868534;
RA Popot J.-L., Pham-Dinh D., Dautigny A.;
RT "Major myelin proteolipid: the 4-alpha-helix topology.";
RL J. Membr. Biol. 120:233-246(1991).
RN [11]
RP PROTEIN SEQUENCE OF 2-32, AND DEVELOPMENTAL STAGE.
RX PubMed=1700073; DOI=10.1111/j.1471-4159.1990.tb05798.x;
RA Schindler P., Luu B., Sorokine O., Trifilieff E., van Dorsselaer A.;
RT "Developmental study of proteolipids in bovine brain: a novel proteolipid
RT and DM-20 appear before proteolipid protein (PLP) during myelination.";
RL J. Neurochem. 55:2079-2085(1990).
CC -!- FUNCTION: This is the major myelin protein from the central nervous
CC system. It plays an important role in the formation or maintenance of
CC the multilamellar structure of myelin.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Myelin membrane {ECO:0000250}. Note=Colocalizes with SIRT2 in
CC internodal regions, at paranodal axoglial junction and Schmidt-
CC Lanterman incisures of myelin sheat. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04116-1; Sequence=Displayed;
CC Name=DM-20;
CC IsoId=P04116-2; Sequence=VSP_003324;
CC -!- DEVELOPMENTAL STAGE: The DM-20 protein is the major proteolipid
CC component in fetal brain. With the appearance of white matter (27-30
CC weeks of gestation), levels of DM-20 begin to increase significantly
CC and then, dramatically, from weeks 31-40 reaching maximum levels in
CC adulthood. In contrast, PLP is not detected until weeks 31-35 after
CC which levels greatly increase and it becomes the major proteolipid in
CC adults. {ECO:0000269|PubMed:1700073}.
CC -!- PTM: Palmitoylated; contains four to five bound palmitate, probably
CC attached in a non-stoichiometric manner. {ECO:0000269|PubMed:1281423,
CC ECO:0000269|PubMed:1695508, ECO:0000269|PubMed:6642431}.
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
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DR EMBL; AJ009913; CAA08909.1; -; Genomic_DNA.
DR EMBL; BC103102; AAI03103.1; -; mRNA.
DR EMBL; BC133388; AAI33389.1; -; mRNA.
DR EMBL; X03098; CAA26884.1; -; mRNA.
DR PIR; A25289; MPBOPL.
DR RefSeq; NP_776574.2; NM_174149.4. [P04116-1]
DR RefSeq; XP_005227899.1; XM_005227842.2. [P04116-2]
DR AlphaFoldDB; P04116; -.
DR STRING; 9913.ENSBTAP00000009171; -.
DR SwissPalm; P04116; -.
DR PaxDb; P04116; -.
DR PRIDE; P04116; -.
DR Ensembl; ENSBTAT00000009171; ENSBTAP00000009171; ENSBTAG00000006977. [P04116-1]
DR GeneID; 281410; -.
DR KEGG; bta:281410; -.
DR CTD; 5354; -.
DR VEuPathDB; HostDB:ENSBTAG00000006977; -.
DR eggNOG; KOG4800; Eukaryota.
DR GeneTree; ENSGT00390000006915; -.
DR HOGENOM; CLU_064167_2_1_1; -.
DR InParanoid; P04116; -.
DR OMA; ENYFARN; -.
DR OrthoDB; 914457at2759; -.
DR TreeFam; TF315162; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000006977; Expressed in floor plate of diencephalon and 84 other tissues.
DR ExpressionAtlas; P04116; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043209; C:myelin sheath; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
DR GO; GO:0014002; P:astrocyte development; ISS:AgBase.
DR GO; GO:0061564; P:axon development; ISS:AgBase.
DR GO; GO:0008366; P:axon ensheathment; ISS:AgBase.
DR GO; GO:0048469; P:cell maturation; ISS:AgBase.
DR GO; GO:0022010; P:central nervous system myelination; ISS:AgBase.
DR GO; GO:0006954; P:inflammatory response; ISS:AgBase.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISS:AgBase.
DR GO; GO:0042552; P:myelination; ISS:AgBase.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
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 Disulfide bond; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1700073,
FT ECO:0000269|PubMed:6195969, ECO:0000269|PubMed:6642431"
FT CHAIN 2..277
FT /note="Myelin proteolipid protein"
FT /id="PRO_0000159003"
FT TOPO_DOM 2..10
FT /note="Cytoplasmic"
FT TRANSMEM 11..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..59
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 60..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..151
FT /note="Cytoplasmic"
FT TRANSMEM 152..178
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..238
FT /note="Extracellular"
FT TRANSMEM 239..268
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60203"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60203"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60203"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:1281423"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:1281423"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:1281423"
FT LIPID 109
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:1281423,
FT ECO:0000269|PubMed:1695508"
FT LIPID 139
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:1281423"
FT LIPID 141
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:1281423"
FT LIPID 199
FT /note="O-palmitoyl threonine"
FT /evidence="ECO:0000269|PubMed:6642431"
FT DISULFID 184..228
FT DISULFID 201..220
FT VAR_SEQ 117..151
FT /note="Missing (in isoform DM-20)"
FT /evidence="ECO:0000305"
FT /id="VSP_003324"
FT CONFLICT 89
FT /note="E -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="L -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 30015 MW; 9B09CB53E4016DE5 CRC64;
MGLLECCARC LVGAPFASLV ATGLCFFGVA LFCGCGHEAL TGTEKLIETY FSKNYQDYEY
LINVIHAFQY VIYGTASFFF LYGALLLAEG FYTTGAVRQI FGDYKTTICG KGLSATVTGG
QKGRGSRGQH QAHSLERVCH CLGKWLGHPD KFVGITYALT VVWLLVFACS AVPVYIYFNT
WTTCQSIAAP SKTSASIGTL CADARMYGVL PWNAFPGKVC GSNLLSICKT AEFQMTFHLF
IAAFVGAAAT LVSLLTFMIA ATYNFAVLKL MGRGTKF
