MYP0_HETFR
ID MYP0_HETFR Reviewed; 246 AA.
AC P20938;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 99.
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 Heterodontus francisci (Horn shark) (Cestracion francisci).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Heterodontoidea; Heterodontiformes;
OC Heterodontidae; Heterodontus.
OX NCBI_TaxID=7792;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2478717; DOI=10.1007/bf02100113;
RA Saavedra R.A., Fors L., Aebersold R.H., Arden B., Horvath S., Sanders J.,
RA Hood L.;
RT "The myelin proteins of the shark brain are similar to the myelin proteins
RT of the mammalian peripheral nervous system.";
RL J. Mol. Evol. 29:149-156(1989).
CC -!- FUNCTION: Creation of an extracellular membrane face which guides the
CC wrapping process and ultimately compacts adjacent lamellae.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Found only in peripheral nervous system Schwann
CC cells.
CC -!- PTM: N-glycan is sulfated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; X16714; CAB37865.1; -; mRNA.
DR PIR; A32999; A32999.
DR AlphaFoldDB; P20938; -.
DR SMR; P20938; -.
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; IPR019738; Myelin_P0_CS.
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.
DR PROSITE; PS00568; MYELIN_P0; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..246
FT /note="Myelin protein P0"
FT /id="PRO_0000019304"
FT TOPO_DOM 28..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..143
FT /note="Ig-like V-type"
FT REGION 200..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 48..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 246 AA; 27335 MW; A776A9ED9D430FA0 CRC64;
MFRDLKPAYL FCCSVLYAFS VLRPSQGISV STHHNLHKTV GSDVTLYCGF WSNEYVSDLT
TLSWRFRPDN SRDIISIFHY GNGVPYIEKW GQFRGRVEWV GDISKHDGSI VIRNLDYIDN
GTFTCDVKNP PDVVGTSSDV HLTVYDKIPP VGAGVVSGAI IGTFLGIILL IVGGLYLFRY
IVRRRARSET SFLQRRRSAA ERGKVSGKAG TVSKGPVLYA TLDQSKSGKG ASEKKSKLSE
SKRDKK
