ID   MYPR_ONCMY              Reviewed;         258 AA.
AC   P79826;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Myelin proteolipid protein;
DE            Short=PLP;
DE   AltName: Full=DM20;
DE   AltName: Full=Lipophilin;
GN   Name=plp;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=8883944; DOI=10.1016/0169-328x(96)00082-4;
RA   Tang S., Panno J.P., McKeown B.A.;
RT   "Cloning and expression of the proteolipid protein DM20 cDNA from the brain
RT   of the rainbow trout, Oncorhynchus mykiss.";
RL   Brain Res. Mol. Brain Res. 41:134-139(1996).
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. May be involved in neuron and
CC       glial cell differentiation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Central nervous system. Highest levels in spinal
CC       cord and medulla oblongata. {ECO:0000269|PubMed:8883944}.
CC   -!- DEVELOPMENTAL STAGE: First expressed at hatching day, levels rapidly
CC       increase during the early postnatal period reaching a maximum by the
CC       9th week. High levels are maintained in adults.
CC       {ECO:0000269|PubMed:8883944}.
CC   -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC       {ECO:0000305}.
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DR   EMBL; U21686; AAB39006.1; -; mRNA.
DR   RefSeq; NP_001118173.1; NM_001124701.1.
DR   AlphaFoldDB; P79826; -.
DR   GeneID; 100136749; -.
DR   KEGG; omy:100136749; -.
DR   CTD; 3772382; -.
DR   OrthoDB; 914457at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Lipoprotein; Membrane; Palmitate;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..258
FT                   /note="Myelin proteolipid protein"
FT                   /id="PRO_0000159014"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..48
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..82
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..128
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..218
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           18
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           19
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           22
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           121
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           124
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        181..200
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   258 AA;  28782 MW;  5CBEF6DD3882E945 CRC64;
     MFPVRHALLC KALGCYDCCI RCLGAVPYPS LVSTLLCFTG MALFCGCGHE ALAHTEVLVE
     TYFVRNIQDY VILASFIKYF QYVIYGLASF FFLYCILLLA EGFYTTSAVK QTFGEFRSTR
     CGRCLSLTFI IVTYVLAVIW LAVFAFTAIP SSSSLIWHRP ATTSTSWTET TPSINQHGWI
     CMDARQYGLL PWNAMPGKAC GMTLASICKT KEFFVTYDLY IAAFAGAGIA LLALFLYVVA
     TTYNYAVLRF LGRKGLRC