MYPR_RABIT
ID MYPR_RABIT Reviewed; 277 AA.
AC P47789;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Myelin proteolipid protein;
DE Short=PLP;
DE AltName: Full=Lipophilin;
GN Name=PLP1; Synonyms=PLP;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PT GLN-37.
RC TISSUE=Brain;
RX PubMed=7525875; DOI=10.1046/j.1471-4159.1994.63062210.x;
RA Tosic M., Dolivo M., Domanska-Janik K., Matthieu J.-M.;
RT "Paralytic tremor (pt): a new allele of the proteolipid protein gene in
RT rabbits.";
RL J. Neurochem. 63:2210-2216(1994).
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 {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 -!- DISEASE: Note=Defects in PLP1 are the cause of paralytic tremor (pt); a
CC sex-linked mutation in rabbit that affects myelination of the CNS.
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
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DR EMBL; S73471; AAB32593.2; -; mRNA.
DR RefSeq; NP_001075797.1; NM_001082328.1.
DR AlphaFoldDB; P47789; -.
DR STRING; 9986.ENSOCUP00000012723; -.
DR GeneID; 100009169; -.
DR KEGG; ocu:100009169; -.
DR CTD; 5354; -.
DR eggNOG; KOG4800; Eukaryota.
DR HOGENOM; CLU_064167_2_1_1; -.
DR InParanoid; P47789; -.
DR OMA; ENYFARN; -.
DR OrthoDB; 914457at2759; -.
DR TreeFam; TF315162; -.
DR Proteomes; UP000001811; Unplaced.
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 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_0000159009"
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 threonine"
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 -> Q (in pt)"
FT /evidence="ECO:0000269|PubMed:7525875"
SQ SEQUENCE 277 AA; 30091 MW; 9C7ECC2393061AE5 CRC64;
MGLLECCARC LVGAPFASLV ATGLCFFGVA LFCGCGHEAL TGTEKLIETY FSKNYQDYEY
LINVIHAFQY VIYGTASFFF LYGALLLAEG FYTTGAVRQI FGDYKTTICG KGLSATVTGG
QKGRGSRGQH QAHSLERVCH CLGKWLGHPD KFVGITYALT VVWLLVFACS AVPVYIYFNT
WTTCQSIAFP SKTSASIGTL CADARMYGVL PWNAFPGKVC GSNLLSICKT AEFQMTFHLF
IAAFVGAAAT LVSLLTFMIA ATYNFAVLKL MGRGTKF
