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Protein

Myelin protein P0

Gene

Mpz

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Creation of an extracellular membrane face which guides the wrapping process and ultimately compacts adjacent lamellae.

GO - Biological processi

  • cell-cell junction maintenance Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Myelin protein P0
Alternative name(s):
Myelin peripheral protein
Short name:
MPP
Myelin protein zero
Gene namesi
Name:Mpz
Synonyms:P0
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:103177. Mpz.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 153124ExtracellularBy similarityAdd
BLAST
Transmembranei154 – 17926HelicalBy similarityAdd
BLAST
Topological domaini180 – 24869CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929By similarityAdd
BLAST
Chaini30 – 248219Myelin protein P0PRO_0000019301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 127PROSITE-ProRule annotation
Glycosylationi122 – 1221N-linked (GlcNAc...) (complex)Sequence Analysis
Modified residuei210 – 2101Phosphoserine; by PKCBy similarity
Modified residuei226 – 2261Phosphoserine1 Publication
Modified residuei228 – 2281Phosphoserine1 Publication
Modified residuei233 – 2331Phosphoserine; by PKCBy similarity
Modified residuei237 – 2371Phosphoserine1 Publication
Modified residuei243 – 2431Phosphoserine1 Publication

Post-translational modificationi

N-glycosylated; contains sulfate-substituted glycan.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP27573.

PTM databases

PhosphoSiteiP27573.

Expressioni

Tissue specificityi

Found only in peripheral nervous system Schwann cells.

Gene expression databases

CleanExiMM_MPZ.
GenevisibleiP27573. MM.

Interactioni

Subunit structurei

Homodimer and homotetramer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Kcnma1Q084604EBI-1634589,EBI-1633915

Protein-protein interaction databases

BioGridi201482. 1 interaction.
IntActiP27573. 1 interaction.
STRINGi10090.ENSMUSP00000066701.

Structurei

3D structure databases

ProteinModelPortaliP27573.
SMRiP27573. Positions 30-150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 143114Ig-like V-typeAdd
BLAST

Sequence similaritiesi

Belongs to the myelin P0 protein family.Curated

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47065.
HOGENOMiHOG000232144.
HOVERGENiHBG096384.
InParanoidiP27573.
KOiK06770.
PhylomeDBiP27573.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
IPR019566. Myelin-PO_C.
IPR000920. Myelin_P0-rel.
IPR019738. Myelin_P0_CS.
IPR029869. P0.
[Graphical view]
PANTHERiPTHR13869. PTHR13869. 1 hit.
PTHR13869:SF7. PTHR13869:SF7. 1 hit.
PfamiPF10570. Myelin-PO_C. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR00213. MYELINP0.
SMARTiSM00406. IGv. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00568. MYELIN_P0. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27573-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPGAPSSSP SPILAALLFS SLVLSPALAI VVYTDREIYG AVGSQVTLHC
60 70 80 90 100
SFWSSEWVSD DISFTWRYQP EGGRDAISIF HYAKGQPYID EVGAFKERIQ
110 120 130 140 150
WVGDPRWKDG SIVIHNLDYS DNGTFTCDVK NPPDIVGKTS QVTLYVFEKV
160 170 180 190 200
PTRYGVVLGA VIGGILGVVL LLLLLFYLIR YCWLRRQAAL QRRLSAMEKG
210 220 230 240
RFHKSSKDSS KRGRQTPVLY AMLDHSRSTK AASEKKSKGL GESRKDKK
Length:248
Mass (Da):27,622
Last modified:August 1, 1992 - v1
Checksum:i936D66684300CAC9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15479.1.
PIRiA54662.
RefSeqiNP_032649.2. NM_008623.4.
UniGeneiMm.9986.

Genome annotation databases

GeneIDi17528.
KEGGimmu:17528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15479.1.
PIRiA54662.
RefSeqiNP_032649.2. NM_008623.4.
UniGeneiMm.9986.

3D structure databases

ProteinModelPortaliP27573.
SMRiP27573. Positions 30-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201482. 1 interaction.
IntActiP27573. 1 interaction.
STRINGi10090.ENSMUSP00000066701.

PTM databases

PhosphoSiteiP27573.

Proteomic databases

PRIDEiP27573.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi17528.
KEGGimmu:17528.

Organism-specific databases

CTDi4359.
MGIiMGI:103177. Mpz.

Phylogenomic databases

eggNOGiNOG47065.
HOGENOMiHOG000232144.
HOVERGENiHBG096384.
InParanoidiP27573.
KOiK06770.
PhylomeDBiP27573.

Miscellaneous databases

NextBioi292144.
PROiP27573.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MPZ.
GenevisibleiP27573. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
IPR019566. Myelin-PO_C.
IPR000920. Myelin_P0-rel.
IPR019738. Myelin_P0_CS.
IPR029869. P0.
[Graphical view]
PANTHERiPTHR13869. PTHR13869. 1 hit.
PTHR13869:SF7. PTHR13869:SF7. 1 hit.
PfamiPF10570. Myelin-PO_C. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR00213. MYELINP0.
SMARTiSM00406. IGv. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00568. MYELIN_P0. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiMYP0_MOUSE
AccessioniPrimary (citable) accession number: P27573
Secondary accession number(s): Q542C9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 22, 2015
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.