MYPRB_XENLA
ID MYPRB_XENLA Reviewed; 280 AA.
AC P23290; Q7SZ96;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Myelin proteolipid protein B;
DE Short=PLP-B;
DE AltName: Full=Lipophilin-B;
GN Name=plp1-b; 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] (ISOFORM 1).
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] (ISOFORM 2).
RC TISSUE=Tadpole;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-208.
RX PubMed=1722981; DOI=10.1515/bchm3.1991.372.2.865;
RA Schliess F., Stoffel W.;
RT "Evolution of the myelin integral membrane proteins of the central nervous
RT system.";
RL Biol. Chem. Hoppe-Seyler 372:865-874(1991).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P23290-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23290-2; Sequence=VSP_036602;
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z19523; CAB46194.1; -; mRNA.
DR EMBL; BC053789; AAH53789.1; -; mRNA.
DR EMBL; X61662; CAA43840.1; -; Genomic_DNA.
DR EMBL; X61663; CAA43840.1; JOINED; Genomic_DNA.
DR PIR; S31492; S31492.
DR RefSeq; NP_001079734.1; NM_001086265.2. [P23290-2]
DR AlphaFoldDB; P23290; -.
DR SMR; P23290; -.
DR DNASU; 379423; -.
DR GeneID; 379423; -.
DR KEGG; xla:379423; -.
DR CTD; 379423; -.
DR Xenbase; XB-GENE-6255820; plp1.S.
DR OrthoDB; 914457at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 379423; Expressed in brain and 9 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 Alternative splicing; Cell membrane; Disulfide bond; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..280
FT /note="Myelin proteolipid protein B"
FT /id="PRO_0000159013"
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 VAR_SEQ 256..280
FT /note="LTYMVGASFNYAVLRVTGRSDRSKF -> IHALMCLSANRVYQQRVLEEKGK
FT SQETPQAESSELTDILPETPQRSAENLL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_036602"
FT CONFLICT 70
FT /note="Y -> F (in Ref. 1; CAB46194)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="I -> M (in Ref. 1; CAB46194)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="L -> S (in Ref. 3; CAA43840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 30758 MW; 566CF8A6AFA49C2B CRC64;
MGWHDGCIRC MVGVPFASVI ATVLCFAGVA LFCGCGHEAL SGTEKLIETY FSKNYQEYEY
LIHVINAFQY VIYGIAIFFF LYGILLLAEG FYTTTAIKHI LGEFKPPAMK GGLISTVTGG
PPKGRSTRGR QPVHTIELIC RCLGKWLGHP DKFVGVTYVI TILWILIFAC SAVPVYIYFN
TWVTCQSIAF PGKTTTSVST LCLDARMYGV LPWNAFPGKV CGTSLLAICK TSEFQMTFHL
FIAAFVGAAA TLVALLTYMV GASFNYAVLR VTGRSDRSKF
