MYP0_RAT
ID MYP0_RAT Reviewed; 248 AA.
AC P06907;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 172.
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; Synonyms=P0;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2578885; DOI=10.1016/0092-8674(85)90198-9;
RA Lemke G., Axel R.;
RT "Isolation and sequence of a cDNA encoding the major structural protein of
RT peripheral myelin.";
RL Cell 40:501-508(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2483091; DOI=10.1016/0896-6273(88)90211-5;
RA Lemke G., Lamar E., Patterson J.;
RT "Isolation and analysis of the gene encoding peripheral myelin protein
RT zero.";
RL Neuron 1:73-83(1988).
RN [3]
RP PROTEIN SEQUENCE OF 85-96, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-148, SUBUNIT, AND DISULFIDE
RP BOND.
RX PubMed=8816707; DOI=10.1016/s0896-6273(00)80176-2;
RA Shapiro L., Doyle J.P., Hensley P., Colman D.R., Hendrickson W.A.;
RT "Crystal structure of the extracellular domain from P0, the major
RT structural protein of peripheral nerve myelin.";
RL Neuron 17:435-449(1996).
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:0000305|PubMed:8816707}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; K03242; AAA41576.1; -; mRNA.
DR PIR; JQ0622; MPRT0.
DR RefSeq; NP_058723.2; NM_017027.2.
DR PDB; 1NEU; X-ray; 1.90 A; A=30-153.
DR PDBsum; 1NEU; -.
DR AlphaFoldDB; P06907; -.
DR SMR; P06907; -.
DR STRING; 10116.ENSRNOP00000004279; -.
DR GlyGen; P06907; 1 site.
DR iPTMnet; P06907; -.
DR PhosphoSitePlus; P06907; -.
DR PaxDb; P06907; -.
DR PRIDE; P06907; -.
DR GeneID; 24564; -.
DR KEGG; rno:24564; -.
DR UCSC; RGD:3109; rat.
DR CTD; 4359; -.
DR RGD; 3109; Mpz.
DR VEuPathDB; HostDB:ENSRNOG00000003171; -.
DR eggNOG; ENOG502QVJ0; Eukaryota.
DR HOGENOM; CLU_090350_3_1_1; -.
DR InParanoid; P06907; -.
DR OMA; WVGDPHW; -.
DR OrthoDB; 1440680at2759; -.
DR PhylomeDB; P06907; -.
DR TreeFam; TF331728; -.
DR EvolutionaryTrace; P06907; -.
DR PRO; PR:P06907; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003171; Expressed in esophagus and 14 other tissues.
DR Genevisible; P06907; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0043209; C:myelin sheath; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IMP:CACAO.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
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:0045217; P:cell-cell junction maintenance; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
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 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT CHAIN 30..248
FT /note="Myelin protein P0"
FT /id="PRO_0000019302"
FT TOPO_DOM 30..153
FT /note="Extracellular"
FT TRANSMEM 154..179
FT /note="Helical"
FT TOPO_DOM 180..248
FT /note="Cytoplasmic"
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 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27573"
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,
FT ECO:0000269|PubMed:8816707"
FT CONFLICT 43
FT /note="G -> R (in Ref. 1; AAA41576)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1NEU"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1NEU"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1NEU"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:1NEU"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:1NEU"
SQ SEQUENCE 248 AA; 27571 MW; BB703F173466119B CRC64;
MAPGAPSSSP SPILAALLFS SLVLSPTLAI VVYTDREVYG AVGSQVTLHC SFWSSEWVSD
DISFTWRYQP EGGRDAISIF HYAKGQPYID EVGTFKERIQ WVGDPSWKDG SIVIHNLDYS
DNGTFTCDVK NPPDIVGKTS QVTLYVFEKV PTRYGVVLGA VIGGILGVVL LLLLLFYLIR
YCWLRRQAAL QRRLSAMEKG KFHKSSKDSS KRGRQTPVLY AMLDHSRSTK AASEKKSKGL
GESRKDKK
