ID   MYPRA_XENLA             Reviewed;         280 AA.
AC   P35801; Q566G3;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Myelin proteolipid protein A;
DE            Short=PLP-A;
DE   AltName: Full=Lipophilin-A;
GN   Name=plp1-a; Synonyms=plp1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Kiefer B., Schneider A., Nave K.-A.;
RT   "Molecular cloning of two genes for proteolipid protein from Xenopus
RT   laevis.";
RL   Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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; Z19522; CAA79582.1; -; mRNA.
DR   EMBL; BC093560; AAH93560.1; -; mRNA.
DR   PIR; S31491; S31491.
DR   RefSeq; NP_001082268.1; NM_001088799.1.
DR   AlphaFoldDB; P35801; -.
DR   SMR; P35801; -.
DR   PRIDE; P35801; -.
DR   DNASU; 398334; -.
DR   GeneID; 398334; -.
DR   KEGG; xla:398334; -.
DR   CTD; 398334; -.
DR   Xenbase; XB-GENE-1008585; plp1.L.
DR   OMA; ENYFARN; -.
DR   OrthoDB; 914457at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 398334; Expressed in brain and 10 other tissues.
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   CHAIN           1..280
FT                   /note="Myelin proteolipid protein A"
FT                   /id="PRO_0000159012"
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..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..179
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..269
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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           140
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           142
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        185..229
FT                   /evidence="ECO:0000250"
FT   DISULFID        202..221
FT                   /evidence="ECO:0000250"
FT   CONFLICT        205
FT                   /note="A -> R (in Ref. 1; CAA79582)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   280 AA;  30716 MW;  C17D456BF31E820A CRC64;
     MGWHDGCIRC MVGVPFASVI ATVLCFAGVA LFCGCGHEAL SGTEKLIETY FSKNYQEYEY
     LIHVINAFQY VIYGIAIFFF LFGILLLAEG FYTTTAIKHI LGEFKPPAIK GGLISTVTGG
     TPKGRSTRGR QPVHTIELIC RCLGKWLGHP DKFVGVTYII TILWILIFAC SAVPVYIYFN
     TWVTCQSIAF PGKTTTSVST LCSDARMYGV LPWNAFPGKV CGTSLLAICK TSEFQMTFHL
     FIAAFVGAAA TLVALLTYMV GASFNYAVLR VTGRSDRSKF