MYPR_CANLF
ID MYPR_CANLF Reviewed; 277 AA.
AC P23294;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Myelin proteolipid protein;
DE Short=PLP;
DE AltName: Full=Lipophilin;
GN Name=PLP1; Synonyms=PLP;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-37.
RX PubMed=1723945; DOI=10.1242/dev.110.2.529;
RA Nadon N.L., Duncan I.D., Hudson L.D.;
RT "A point mutation in the proteolipid protein gene of the 'shaking pup'
RT interrupts oligodendrocyte development.";
RL Development 110:529-537(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 {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Myelin membrane. Note=Colocalizes with SIRT2 in
CC internodal regions, at paranodal axoglial junction and Schmidt-
CC Lanterman incisures of myelin sheat. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in PLP1 are the cause of 'shaking pup' disease; a
CC dysmyelinating disease.
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
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DR EMBL; X55317; CAA39025.1; -; Genomic_DNA.
DR PIR; A43548; A43548.
DR RefSeq; NP_001013856.1; NM_001013834.2.
DR AlphaFoldDB; P23294; -.
DR STRING; 9615.ENSCAFP00000065483; -.
DR PRIDE; P23294; -.
DR Ensembl; ENSCAFT00030039698; ENSCAFP00030034642; ENSCAFG00030021594.
DR Ensembl; ENSCAFT00040039507; ENSCAFP00040034471; ENSCAFG00040021257.
DR Ensembl; ENSCAFT00845042032; ENSCAFP00845032966; ENSCAFG00845023800.
DR GeneID; 481002; -.
DR KEGG; cfa:481002; -.
DR CTD; 5354; -.
DR VEuPathDB; HostDB:ENSCAFG00845023800; -.
DR GeneTree; ENSGT00390000006915; -.
DR InParanoid; P23294; -.
DR OrthoDB; 914457at2759; -.
DR Proteomes; UP000002254; Chromosome X.
DR Bgee; ENSCAFG00000017811; Expressed in prefrontal cortex and 43 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043209; C:myelin sheath; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0061564; P:axon development; IBA:GO_Central.
DR GO; GO:0022010; P:central nervous system myelination; IBA:GO_Central.
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:0031175; P:neuron projection development; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell membrane; Disease variant; 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_0000159004"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..178
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..268
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 LIPID 199
FT /note="O-palmitoyl serine"
FT /evidence="ECO:0000250"
FT DISULFID 184..228
FT /evidence="ECO:0000250"
FT DISULFID 201..220
FT /evidence="ECO:0000250"
FT VARIANT 37
FT /note="H -> P (in shaking pup)"
FT /evidence="ECO:0000269|PubMed:1723945"
SQ 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
