MYPR_PONAB
ID MYPR_PONAB Reviewed; 277 AA.
AC Q5R6E6; Q5R4I5; Q5R6Q3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Myelin proteolipid protein;
DE Short=PLP;
DE AltName: Full=Lipophilin;
GN Name=PLP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Myelin membrane {ECO:0000250}. Note=Colocalizes
CC with SIRT2 in internodal regions, at paranodal axoglial junction and
CC Schmidt-Lanterman incisures of myelin sheat. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R6E6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R6E6-2; Sequence=VSP_022981;
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
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DR EMBL; CR860432; CAH92557.1; -; mRNA.
DR EMBL; CR860545; CAH92670.1; -; mRNA.
DR EMBL; CR861263; CAH93331.1; -; mRNA.
DR EMBL; CR926047; CAI29679.1; -; mRNA.
DR RefSeq; NP_001126498.1; NM_001133026.2.
DR RefSeq; NP_001127654.1; NM_001134182.1. [Q5R6E6-2]
DR RefSeq; XP_009233351.1; XM_009235076.1.
DR RefSeq; XP_009233352.1; XM_009235077.1. [Q5R6E6-2]
DR AlphaFoldDB; Q5R6E6; -.
DR SMR; Q5R6E6; -.
DR STRING; 9601.ENSPPYP00000023045; -.
DR PRIDE; Q5R6E6; -.
DR Ensembl; ENSPPYT00000042281; ENSPPYP00000043570; ENSPPYG00000020590. [Q5R6E6-2]
DR GeneID; 100173486; -.
DR GeneID; 100174736; -.
DR KEGG; pon:100173486; -.
DR CTD; 5354; -.
DR eggNOG; KOG4800; Eukaryota.
DR GeneTree; ENSGT00390000006915; -.
DR HOGENOM; CLU_064167_2_1_1; -.
DR InParanoid; Q5R6E6; -.
DR OMA; ENYFARN; -.
DR OrthoDB; 914457at2759; -.
DR TreeFam; TF315162; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043209; C:myelin sheath; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0061564; P:axon development; IEA:Ensembl.
DR GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..277
FT /note="Myelin proteolipid protein"
FT /id="PRO_0000276759"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305"
FT TOPO_DOM 37..63
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305"
FT TOPO_DOM 89..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..177
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305"
FT TOPO_DOM 178..233
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 234..260
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305"
FT TOPO_DOM 261..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:0000250"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 109
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 139
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 141
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 184..228
FT /evidence="ECO:0000250"
FT DISULFID 201..220
FT /evidence="ECO:0000250"
FT VAR_SEQ 117..151
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022981"
FT CONFLICT 9
FT /note="R -> K (in Ref. 1; CAH92557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 30077 MW; 3C2BC973C3061C38 CRC64;
MGLLECCARC LVGAPFASLV ATGLCFFGVA LFCGCGHEAL TGTEKLIETY FSKNYQDYEY
LINVIHAFQY VIYGTASFFF LYGALLLAEG FYTTGAVRQI FGDYKTTICG KGLSATVTGG
QKGRGSRGQH QAHSLERVCH CLGKWLGHPD KFVGITYALT VVWLLVFACS AVPVYIYFNT
WTTCQSIAFP SKTSASIGSL CADARMYGVL PWNAFPGKVC GSNLLSICKT AEFQMTFHLF
IAAFVGAAAT LVSLLTFMIA ATYNFAVLKL MGRGTKF
