ID   MYP0_CHICK              Reviewed;         249 AA.
AC   P37301;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 106.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1690817; DOI=10.1002/jnr.490250119;
RA   Barbu M.;
RT   "Molecular cloning of cDNAs that encode the chicken P0 protein: evidence
RT   for early expression in avians.";
RL   J. Neurosci. Res. 25:143-151(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   -!- 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   -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR   PIR; A61087; A61087.
DR   AlphaFoldDB; P37301; -.
DR   SMR; P37301; -.
DR   IntAct; P37301; 1.
DR   STRING; 9031.ENSGALP00000042850; -.
DR   VEuPathDB; HostDB:geneid_100859605; -.
DR   eggNOG; ENOG502QVJ0; Eukaryota.
DR   InParanoid; P37301; -.
DR   PhylomeDB; P37301; -.
DR   Proteomes; UP000000539; Unplaced.
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:0000250"
FT   CHAIN           30..249
FT                   /note="Myelin protein P0"
FT                   /id="PRO_0000019303"
FT   TOPO_DOM        30..153
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..249
FT                   /note="Cytoplasmic"
FT   DOMAIN          30..143
FT                   /note="Ig-like V-type"
FT   REGION          227..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   249 AA;  27467 MW;  FBD14801FF8A08FB CRC64;
     MALGAIGDGR LLLLLVGLLS ASGPSPTLAI HVYTPREVYG TVGSHVTLSC SFWSSEWISE
     DISYTWHFQA EGSRDSISIF HYGKGQPYID DVGSFKERME WVGNPRRKDG SIVIHNLDYT
     DNGTFTCDVK NPPDIVGKSS QVTLYVLEKV PTRYGVVLGS IIGGVLLLVA LLVAVVYLVR
     FCWLRRQAVL QRRLSAMEKG KLQRSAKDAS KRSRQPPVLY AMLDHSRSAK AAAEKKSKGA
     PGEARKDKK