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Myelin proteolipid protein (PLP) (Lipophilin)

 MYPR_CANLF              Reviewed;         277 AA.
P23294;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 95.
RecName: Full=Myelin proteolipid protein;
Short=PLP;
AltName: Full=Lipophilin;
Name=PLP1; Synonyms=PLP;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-37.
PubMed=1723945;
Nadon N.L., Duncan I.D., Hudson L.D.;
"A point mutation in the proteolipid protein gene of the 'shaking pup'
interrupts oligodendrocyte development.";
Development 110:529-537(1990).
-!- FUNCTION: This is the major myelin protein from the central
nervous system. It plays an important role in the formation or
maintenance of the multilamellar structure of myelin.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Myelin membrane. Note=Colocalizes
with SIRT2 in internodal regions, at paranodal axoglial junction
and Schmidt-Lanterman incisures of myelin sheat. {ECO:0000250}.
-!- DISEASE: Note=Defects in PLP1 are the cause of 'shaking pup'
disease; a dysmyelinating disease.
-!- SIMILARITY: Belongs to the myelin proteolipid protein family.
{ECO:0000305}.
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EMBL; X55317; CAA39025.1; -; Genomic_DNA.
PIR; A43548; A43548.
RefSeq; NP_001013856.1; NM_001013834.2.
PRIDE; P23294; -.
GeneID; 481002; -.
KEGG; cfa:481002; -.
CTD; 5354; -.
HOVERGEN; HBG000096; -.
InParanoid; P23294; -.
KO; K17271; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043209; C:myelin sheath; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
InterPro; IPR001614; Myelin_PLP.
InterPro; IPR018237; Myelin_PLP_CS.
PANTHER; PTHR11683; PTHR11683; 1.
Pfam; PF01275; Myelin_PLP; 1.
PRINTS; PR00214; MYELINPLP.
SMART; SM00002; PLP; 1.
PROSITE; PS00575; MYELIN_PLP_1; 1.
PROSITE; PS01004; MYELIN_PLP_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disease mutation; Disulfide bond;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 277 Myelin proteolipid protein.
/FTId=PRO_0000159004.
TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.
TRANSMEM 11 36 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 37 59 Extracellular. {ECO:0000255}.
TRANSMEM 60 88 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 89 151 Cytoplasmic. {ECO:0000255}.
TRANSMEM 152 178 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 179 238 Extracellular. {ECO:0000255}.
TRANSMEM 239 268 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 269 277 Cytoplasmic. {ECO:0000255}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:P60203}.
MOD_RES 116 116 Phosphothreonine.
{ECO:0000250|UniProtKB:P60203}.
MOD_RES 118 118 Phosphothreonine.
{ECO:0000250|UniProtKB:P60203}.
LIPID 6 6 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 7 7 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 10 10 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 109 109 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 139 139 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 141 141 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 199 199 O-palmitoyl serine. {ECO:0000250}.
DISULFID 184 228 {ECO:0000250}.
DISULFID 201 220 {ECO:0000250}.
VARIANT 37 37 H -> P (in shaking pup).
{ECO:0000269|PubMed:1723945}.
SEQUENCE 277 AA; 30091 MW; 6C2BD673CB1A7AE3 CRC64;
MGLLECCARC LVGAPFASLV ATGLCFFGVA LFCGCGHEAL TGTEKLIETY FSKNYQDYEY
LINVIHAFQY VIYGTASFFF LYGALLLAEG FYTTGAVRQI FGDYKTTICG KGLSATVTGG
QKGRGSRGQH QAHSLERVCH CLGKWLGHPD KFVGITYALT IVWLLVFACS AVPVYIYFNT
WTTCQSIAFP SKTSASIGSL CADARMYGVL PWNAFPGKVC GSNLLSICKT AEFQMTFHLF
IAAFVGAAAT LVSLLTFMIA ATYNFAVLKL MGRGTKF


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