ID   MYPR_TAEGU              Reviewed;         277 AA.
AC   P47790;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Myelin proteolipid protein;
DE            Short=PLP;
DE   AltName: Full=Lipophilin;
GN   Name=PLP1; Synonyms=PLP;
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7528351; DOI=10.1007/bf00968717;
RA   Campagnoni C.W., Kampf K., Mason B., Handley V.W., Campagnoni A.T.;
RT   "Isolation and characterization of a cDNA encoding the zebra finch myelin
RT   proteolipid protein.";
RL   Neurochem. Res. 19:1061-1065(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}.
CC   -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC       {ECO:0000305}.
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DR   EMBL; S75729; AAB32825.2; -; mRNA.
DR   PIR; I51270; I51270.
DR   RefSeq; NP_001070171.1; NM_001076703.1.
DR   AlphaFoldDB; P47790; -.
DR   STRING; 59729.ENSTGUP00000028740; -.
DR   PRIDE; P47790; -.
DR   Ensembl; ENSTGUT00000025770; ENSTGUP00000028740; ENSTGUG00000006519.
DR   GeneID; 100220245; -.
DR   KEGG; tgu:100220245; -.
DR   CTD; 5354; -.
DR   GeneTree; ENSGT00390000006915; -.
DR   InParanoid; P47790; -.
DR   OrthoDB; 914457at2759; -.
DR   Proteomes; UP000007754; Chromosome 4A.
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   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..277
FT                   /note="Myelin proteolipid protein"
FT                   /id="PRO_0000159011"
FT   TOPO_DOM        2..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   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"
SQ   SEQUENCE   277 AA;  30228 MW;  95E9DCEF25C20D6A CRC64;
     MGLLECCARC LIGAPFASLV ATGLCFFGVA LFCGCGHEAL TGTEQLIETY FSKNYQDYEF
     LIDVIHGFQY FIYGTAAFFF LYGALLLAEG FYTTGAVRQI FGDYRTTICG KGLSATVTGG
     PKGRGARGPQ RAHSWQRVCH CLGKWLGHPD KFVGITYVLT IIWLLVFACS AVPVYIYFNT
     WTTCQSIGNP TKTSASIGTL CADARMYGIL PWNAFPGKVC GSNLLSICKT SEFQMTFHLF
     IAAFVGAAAT LVSLVTFIIA TTYNFAVLRL MGRGTKF