MYP0_BOVIN
ID MYP0_BOVIN Reviewed; 248 AA.
AC P10522; Q05B76;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 151.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 29-248, AND GLYCOSYLATION AT ASN-122.
RC TISSUE=Brain;
RX PubMed=2435734; DOI=10.1016/s0021-9258(18)61334-1;
RA Sakamoto Y., Kitamura K., Yoshimura K., Nishijima T., Uyemura K.;
RT "Complete amino acid sequence of PO protein in bovine peripheral nerve
RT myelin.";
RL J. Biol. Chem. 262:4208-4214(1987).
RN [3]
RP PHOSPHORYLATION AT SER-210; SER-233 AND SER-243.
RX PubMed=1700069; DOI=10.1111/j.1471-4159.1990.tb05783.x;
RA Suzuki M., Sakamoto Y., Kitamura K., Fukunaga K., Yamamoto H., Miyamoto E.,
RA Uyemura K.;
RT "Phosphorylation of P0 glycoprotein in peripheral nerve myelin.";
RL J. Neurochem. 55:1966-1971(1990).
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 -!- TISSUE SPECIFICITY: Found only in peripheral nervous system Schwann
CC cells.
CC -!- PTM: N-glycosylated; contains sulfate-substituted glycan.
CC {ECO:0000269|PubMed:2435734}.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; BC122659; AAI22660.1; -; mRNA.
DR PIR; A29128; A29128.
DR RefSeq; NP_001072975.1; NM_001079507.2.
DR RefSeq; NP_001303288.1; NM_001316359.1.
DR AlphaFoldDB; P10522; -.
DR SMR; P10522; -.
DR STRING; 9913.ENSBTAP00000045141; -.
DR GlyConnect; 427; 22 N-Linked glycans (1 site).
DR iPTMnet; P10522; -.
DR PaxDb; P10522; -.
DR Ensembl; ENSBTAT00000048021; ENSBTAP00000045141; ENSBTAG00000033835.
DR GeneID; 539462; -.
DR KEGG; bta:539462; -.
DR CTD; 4359; -.
DR VEuPathDB; HostDB:ENSBTAG00000033835; -.
DR VGNC; VGNC:31591; MPZ.
DR eggNOG; ENOG502QVJ0; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_090350_3_1_1; -.
DR InParanoid; P10522; -.
DR OMA; WVGDPHW; -.
DR OrthoDB; 1440680at2759; -.
DR TreeFam; TF331728; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000033835; Expressed in pigment epithelium of eye and 75 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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:2435734"
FT CHAIN 29..248
FT /note="Myelin protein P0"
FT /id="PRO_0000159002"
FT TOPO_DOM 29..155
FT /note="Extracellular"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..248
FT /note="Cytoplasmic"
FT DOMAIN 30..143
FT /note="Ig-like V-type"
FT REGION 224..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:0000269|PubMed:1700069"
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:0000269|PubMed:1700069"
FT MOD_RES 243
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:1700069"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:2435734"
FT /id="CAR_000221"
FT DISULFID 50..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 248 AA; 27452 MW; 29177235A76647E4 CRC64;
MAPGAPSSSP SPILAALLFS SLVLSPVQAI VVYTDKEVHG AVGSQVTLYC SFWSSEWVSD
DLSFTWRYQP EGGRDAISIF HYAKGQPYID EVGTFKERIQ WVGDPHRKDG SIVIHNLDYG
DNGTFTCDVK NPPDIVGKTS QVTLYVFEKV PTRYGVVLGA VIGGVLGVVL LALLLFYLIR
YCWLRRQAAL QRRLSAMEKG KLHKTAKDAS KRGRQTPVLY AMLDHSRSTK AASEKKTKGL
GESRKDKK
