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P27573 (MYP0_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myelin protein P0
Alternative name(s):
Myelin peripheral protein
Short name=MPP
Myelin protein zero
Gene names
Name:Mpz
Synonyms:P0
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kcnma1Q084604EBI-1634589,EBI-1633915

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 By similarity
Chain30 – 248219Myelin protein P0
PRO_0000019301

Regions

Topological domain30 – 153124Extracellular By similarity
Transmembrane154 – 17926Helical; By similarity
Topological domain180 – 24869Cytoplasmic By similarity
Domain30 – 143114Ig-like V-type

Amino acid modifications

Modified residue2101Phosphoserine; by PKC By similarity
Modified residue2261Phosphoserine Ref.5
Modified residue2281Phosphoserine Ref.5
Modified residue2331Phosphoserine; by PKC By similarity
Modified residue2371Phosphoserine Ref.5
Modified residue2431Phosphoserine Ref.5
Glycosylation1221N-linked (GlcNAc...) (complex) Potential
Disulfide bond50 ↔ 127 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27573 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 936D66684300CAC9

FASTA24827,622
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62860 expand/collapse EMBL AC list , 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.
CCDSCCDS15479.1.
PIRA54662.
RefSeqNP_032649.2. NM_008623.4.
UniGeneMm.9986.

3D structure databases

ProteinModelPortalP27573.
SMRP27573. Positions 30-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP27573. 1 interaction.
STRING10090.ENSMUSP00000106966.

PTM databases

PhosphoSiteP27573.

Proteomic databases

PRIDEP27573.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID17528.
KEGGmmu:17528.

Organism-specific databases

CTD4359.
MGIMGI:103177. Mpz.

Phylogenomic databases

eggNOGNOG47065.
HOGENOMHOG000232144.
HOVERGENHBG096384.
InParanoidQ542C9.
KOK06770.
PhylomeDBP27573.

Gene expression databases

CleanExMM_MPZ.
GenevestigatorP27573.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. 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]
PfamPF10570. Myelin-PO_C. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSPR00213. MYELINP0.
SMARTSM00406. IGv. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS00568. MYELIN_P0. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio292144.
PROP27573.
SOURCESearch...

Entry information

Entry nameMYP0_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot