MYP0_XENLA
ID MYP0_XENLA Reviewed; 245 AA.
AC A2VD98;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Myelin protein P0;
DE AltName: Full=Myelin peripheral protein;
DE Short=MPP;
DE AltName: Full=Myelin protein zero;
DE Flags: Precursor;
GN Name=mpz;
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 [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Creation of an extracellular membrane face which guides the
CC wrapping process and ultimately compacts adjacent lamellae.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; BC129641; AAI29642.1; -; mRNA.
DR RefSeq; NP_001091356.1; NM_001097887.1.
DR AlphaFoldDB; A2VD98; -.
DR SMR; A2VD98; -.
DR DNASU; 100037196; -.
DR GeneID; 100037196; -.
DR KEGG; xla:100037196; -.
DR CTD; 100037196; -.
DR Xenbase; XB-GENE-876975; mpz.S.
DR OrthoDB; 1440680at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 100037196; Expressed in internal ear and 13 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043209; C:myelin sheath; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR029869; Myelin_P0.
DR InterPro; IPR000920; Myelin_P0-rel.
DR InterPro; IPR019566; MYP0_C.
DR PANTHER; PTHR13869; PTHR13869; 1.
DR PANTHER; PTHR13869:SF7; PTHR13869:SF7; 1.
DR Pfam; PF10570; Myelin-PO_C; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR00213; MYELINP0.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..245
FT /note="Myelin protein P0"
FT /id="PRO_0000376826"
FT TOPO_DOM 29..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..143
FT /note="Ig-like V-type"
FT REGION 199..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 245 AA; 27249 MW; 236169FD508CF8E1 CRC64;
MEPSGLRTPC SLLALVLLSA LVLTPTLAIE VYTDREVYGT AGSRVTLSCS FWSSEWISDD
ISVTWHYQPD HSREMYSIVH FAKGLSSIDA GIFKDRIEWV GSPKWKDASI VVHNLELTDN
GTFTCDVKNP PDVVGKSSYV HLQVQEKGPA RAGLILGIII AVALALVIVV TILILLIRYC
WLRRKARVQR ELSALERGKL HKAKDSSKRS SRQTPILYAM LDQTRGKSSE KKAKGGIGDS
RKDRK
