MYP0_HORSE
ID MYP0_HORSE Reviewed; 248 AA.
AC Q6WEB5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Blechynden L.M., Akkari P.A., Hilbert B.J., Laing N.G.;
RT "Characterization of the equine MPZ, PMP22 and GJB1 genes and their
RT evaluation as candidate genes for equine idiopathic laryngeal hemiplegia.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Is an adhesion molecule necessary for normal myelination in
CC the peripheral nervous system. It mediates adhesion between adjacent
CC myelin wraps and ultimately drives myelin compaction.
CC {ECO:0000250|UniProtKB:P25189}.
CC -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25189};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25189}.
CC -!- PTM: N-glycosylated; contains sulfate-substituted glycan.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; AY293741; AAQ55549.1; -; mRNA.
DR RefSeq; NP_001075363.1; NM_001081894.2.
DR AlphaFoldDB; Q6WEB5; -.
DR SMR; Q6WEB5; -.
DR STRING; 9796.ENSECAP00000042161; -.
DR PaxDb; Q6WEB5; -.
DR Ensembl; ENSECAT00000060822; ENSECAP00000042161; ENSECAG00000009075.
DR GeneID; 100034024; -.
DR KEGG; ecb:100034024; -.
DR CTD; 4359; -.
DR VGNC; VGNC:20300; MPZ.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_090350_3_1_1; -.
DR InParanoid; Q6WEB5; -.
DR OrthoDB; 1440680at2759; -.
DR Proteomes; UP000002281; Chromosome 5.
DR Bgee; ENSECAG00000009075; Expressed in zone of skin and 16 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043209; C:myelin sheath; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098743; P:cell aggregation; ISS:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
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; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..248
FT /note="Myelin protein P0"
FT /id="PRO_0000249730"
FT TOPO_DOM 30..153
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 154..179
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 180..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 30..143
FT /note="Ig-like V-type"
FT REGION 222..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P10522"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27573"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27573"
FT MOD_RES 233
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P10522"
FT MOD_RES 243
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P10522"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 248 AA; 27485 MW; 68B78C51225AC61E CRC64;
MAPGAPSSSP SPILAALLFS SLVLSPAQAI VVYTDKEVYG AVGSRVTLHC SFWSSEWVSD
DISFTWRYQP EGGRDAISIF HYAKGQPYID EVGTFKERIQ WVGDPQWKDG SIVIHNLDYS
DNGTFTCDVK NPPDIVGKTS QVTLYVFEKV PTRYGVVLGA VIGGVLGVVL LVLLLFYVVR
YCWLRRQAAL QRRLSAMEKG KLHKPGKDTS KRGRQTPVLY AMLDHSRSTK AASEKKAKGL
GESRKDKK
