P27573 (MYP0_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myelin protein P0

Alternative name(s):
Myelin peripheral protein
Short name=MPP
Myelin protein zero

Gene names

Name:	Mpz
Synonyms:	P0

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Creation of an extracellular membrane face which guides the wrapping process and ultimately compacts adjacent lamellae.
Subunit structure	Homodimer and homotetramer By similarity.
Subcellular location	Cell membrane; Single-pass type I membrane protein.
Tissue specificity	Found only in peripheral nervous system Schwann cells.
Post-translational modification	N-glycosylated; contains sulfate-substituted glycan By similarity.
Sequence similarities	Belongs to the myelin P0 protein family. Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Immunoglobulin domain Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell-cell junction maintenance Inferred from mutant phenotype PubMed 11749037. Source: MGI
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Kcnma1	Q08460	4	EBI-1634589,EBI-1633915

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	By similarity
	Chain	30 – 248	219	Myelin protein P0		PRO_0000019301
Regions
	Topological domain	30 – 153	124	Extracellular By similarity
	Transmembrane	154 – 179	26	Helical; By similarity
	Topological domain	180 – 248	69	Cytoplasmic By similarity
	Domain	30 – 143	114	Ig-like V-type
Amino acid modifications
	Modified residue	210	1	Phosphoserine; by PKC By similarity
	Modified residue	216	1	Phosphothreonine Ref.6
	Modified residue	226	1	Phosphoserine Ref.5
	Modified residue	228	1	Phosphoserine Ref.5
	Modified residue	233	1	Phosphoserine; by PKC By similarity
	Modified residue	237	1	Phosphoserine Ref.5
	Modified residue	243	1	Phosphoserine Ref.5 Ref.6
	Glycosylation	122	1	N-linked (GlcNAc...) (complex) Potential
	Disulfide bond	50 ↔ 127		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27573 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 936D66684300CAC9	FASTA	248	27,622
	10 20 30 40 50 60 MAPGAPSSSP SPILAALLFS SLVLSPALAI VVYTDREIYG AVGSQVTLHC SFWSSEWVSD 70 80 90 100 110 120 DISFTWRYQP EGGRDAISIF HYAKGQPYID EVGAFKERIQ WVGDPRWKDG SIVIHNLDYS 130 140 150 160 170 180 DNGTFTCDVK NPPDIVGKTS QVTLYVFEKV PTRYGVVLGA VIGGILGVVL LLLLLFYLIR 190 200 210 220 230 240 YCWLRRQAAL QRRLSAMEKG RFHKSSKDSS KRGRQTPVLY AMLDHSRSTK AASEKKSKGL GESRKDKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence, genomic organization, and chromosomal localization of the mouse peripheral myelin protein zero gene: identification of polymorphic alleles." You K.H., Hsieh C.L., Hayes C., Stahl N., Francke U., Popko B. Genomics 9:751-757(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Inner ear.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Myelin P0 glycoprotein: identification of the site phosphorylated in vitro and in vivo by endogenous protein kinases." Hilmi S., Fournier M., Valeins H., Gandar J.C., Bonnet J. J. Neurochem. 64:902-907(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-226; SER-228; SER-233; SER-237 AND SER-243.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216 AND SER-243, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M62860 , M62857, M62858, M62859 Genomic DNA. Translation: AAA39867.1. AK089180 mRNA. Translation: BAC40781.1. AK157960 mRNA. Translation: BAE34285.1. CH466520 Genomic DNA. Translation: EDL39129.1. CH466520 Genomic DNA. Translation: EDL39131.1. BC139139 mRNA. Translation: AAI39140.1. BC141226 mRNA. Translation: AAI41227.1.
IPI	IPI00117735.
PIR	A54662.
RefSeq	NP_032649.2. NM_008623.4.
UniGene	Mm.9986.
3D structure databases
ProteinModelPortal	P27573.
SMR	P27573. Positions 30-150.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27573. 1 interaction.
STRING	10090.ENSMUSP00000106966.
PTM databases
PhosphoSite	P27573.
Proteomic databases
PRIDE	P27573.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	17528.
KEGG	mmu:17528.
UCSC	uc007dnc.1. mouse.
Organism-specific databases
CTD	4359.
MGI	MGI:103177. Mpz.
Phylogenomic databases
eggNOG	NOG47065.
HOGENOM	HOG000232144.
HOVERGEN	HBG096384.
InParanoid	Q542C9.
KO	K06770.
OrthoDB	EOG4GTKFB.
Gene expression databases
CleanEx	MM_MPZ.
Genevestigator	P27573.
GermOnline	ENSMUSG00000056569. Mus musculus.
Family and domain databases
Gene3D	2.60.40.10. 1 hit.
InterPro	IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR013106. Ig_V-set. IPR003596. Ig_V-set_subgr. IPR019566. Myelin-PO_C. IPR000920. Myelin_P0. IPR019738. Myelin_P0_CS. [Graphical view]
Pfam	PF10570. Myelin-PO_C. 1 hit. PF07686. V-set. 1 hit. [Graphical view]
PRINTS	PR00213. MYELINP0.
SMART	SM00406. IGv. 1 hit. [Graphical view]
PROSITE	PS50835. IG_LIKE. 1 hit. PS00568. MYELIN_P0. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	292144.
SOURCE	Search...

Entry information

Entry name

MYP0_MOUSE

Accession

Primary (citable) accession number: P27573
Secondary accession number(s): Q542C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program