MYP0_MOUSE
ID MYP0_MOUSE Reviewed; 248 AA.
AC P27573; Q542C9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 160.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1709914; DOI=10.1016/0888-7543(91)90370-t;
RA You K.H., Hsieh C.L., Hayes C., Stahl N., Francke U., Popko B.;
RT "DNA sequence, genomic organization, and chromosomal localization of the
RT mouse peripheral myelin protein zero gene: identification of polymorphic
RT alleles.";
RL Genomics 9:751-757(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION AT SER-226; SER-228; SER-233; SER-237 AND SER-243.
RX PubMed=7530295; DOI=10.1046/j.1471-4159.1995.64020902.x;
RA Hilmi S., Fournier M., Valeins H., Gandar J.C., Bonnet J.;
RT "Myelin P0 glycoprotein: identification of the site phosphorylated in vitro
RT and in vivo by endogenous protein kinases.";
RL J. Neurochem. 64:902-907(1995).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=10068633; DOI=10.1242/dev.126.7.1397;
RA Zorick T.S., Syroid D.E., Brown A., Gridley T., Lemke G.;
RT "Krox-20 controls SCIP expression, cell cycle exit and susceptibility to
RT apoptosis in developing myelinating Schwann cells.";
RL Development 126:1397-1406(1999).
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 -!- INTERACTION:
CC P27573; Q08460: Kcnma1; NbExp=4; IntAct=EBI-1634589, EBI-1633915;
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 -!- DEVELOPMENTAL STAGE: Expressed in the sciatic nerves at postnatal days
CC P6 to P12. {ECO:0000269|PubMed:10068633}.
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; M62860; AAA39867.1; -; Genomic_DNA.
DR EMBL; M62857; AAA39867.1; JOINED; Genomic_DNA.
DR EMBL; M62858; AAA39867.1; JOINED; Genomic_DNA.
DR EMBL; M62859; AAA39867.1; JOINED; Genomic_DNA.
DR EMBL; AK089180; BAC40781.1; -; mRNA.
DR EMBL; AK157960; BAE34285.1; -; mRNA.
DR EMBL; CH466520; EDL39129.1; -; Genomic_DNA.
DR EMBL; CH466520; EDL39131.1; -; Genomic_DNA.
DR EMBL; BC139139; AAI39140.1; -; mRNA.
DR EMBL; BC141226; AAI41227.1; -; mRNA.
DR CCDS; CCDS15479.1; -.
DR PIR; A54662; A54662.
DR RefSeq; NP_001302428.1; NM_001315499.1.
DR RefSeq; NP_001302429.1; NM_001315500.1.
DR RefSeq; NP_032649.2; NM_008623.5.
DR AlphaFoldDB; P27573; -.
DR SMR; P27573; -.
DR BioGRID; 201482; 1.
DR DIP; DIP-51664N; -.
DR IntAct; P27573; 2.
DR STRING; 10090.ENSMUSP00000066701; -.
DR GlyGen; P27573; 1 site.
DR iPTMnet; P27573; -.
DR PhosphoSitePlus; P27573; -.
DR MaxQB; P27573; -.
DR PaxDb; P27573; -.
DR PRIDE; P27573; -.
DR ProteomicsDB; 287537; -.
DR ABCD; P27573; 22 sequenced antibodies.
DR DNASU; 17528; -.
DR GeneID; 17528; -.
DR KEGG; mmu:17528; -.
DR CTD; 4359; -.
DR MGI; MGI:103177; Mpz.
DR eggNOG; ENOG502QVJ0; Eukaryota.
DR InParanoid; P27573; -.
DR OrthoDB; 1440680at2759; -.
DR PhylomeDB; P27573; -.
DR BioGRID-ORCS; 17528; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Mpz; mouse.
DR PRO; PR:P27573; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P27573; protein.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
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; 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..248
FT /note="Myelin protein P0"
FT /id="PRO_0000019301"
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:0000269|PubMed:7530295"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7530295"
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:0000269|PubMed:7530295"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7530295"
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; 27622 MW; 936D66684300CAC9 CRC64;
MAPGAPSSSP SPILAALLFS SLVLSPALAI VVYTDREIYG AVGSQVTLHC SFWSSEWVSD
DISFTWRYQP EGGRDAISIF HYAKGQPYID EVGAFKERIQ WVGDPRWKDG SIVIHNLDYS
DNGTFTCDVK NPPDIVGKTS QVTLYVFEKV PTRYGVVLGA VIGGILGVVL LLLLLFYLIR
YCWLRRQAAL QRRLSAMEKG RFHKSSKDSS KRGRQTPVLY AMLDHSRSTK AASEKKSKGL
GESRKDKK
