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Myelin P2 protein (Peripheral myelin protein 2)

 MYP2_HUMAN              Reviewed;         132 AA.
P02689; Q6FHL4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 155.
RecName: Full=Myelin P2 protein;
AltName: Full=Peripheral myelin protein 2;
Name=PMP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1720307; DOI=10.1016/S0006-291X(05)81402-0;
Hayasaka K., Nanao K., Tahara M., Sato W., Takada G., Miura M.,
Uyemura K.;
"Isolation and sequence determination of cDNA encoding P2 protein of
human peripheral myelin.";
Biochem. Biophys. Res. Commun. 181:204-207(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
PubMed=7525873;
Narayanan V., Ripepi B., Jabs E.W., Hawkins A., Griffin C.,
Tennekoon G.;
"Partial structure and mapping of the human myelin P2 protein gene.";
J. Neurochem. 63:2010-2013(1994).
[8]
PROTEIN SEQUENCE OF 2-132, AND ACETYLATION AT SER-2.
PubMed=6183401; DOI=10.1111/j.1471-4159.1982.tb08017.x;
Suzuki M., Kitamura K., Sakamoto Y., Uyemura K.;
"The complete amino acid sequence of human P2 protein.";
J. Neurochem. 39:1759-1762(1982).
[9]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PALMITATE,
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, CIRCULAR
DICHROISM, AND DOMAIN.
PubMed=20421974; DOI=10.1371/journal.pone.0010300;
Majava V., Polverini E., Mazzini A., Nanekar R., Knoll W., Peters J.,
Natali F., Baumgartel P., Kursula I., Kursula P.;
"Structural and functional characterization of human peripheral
nervous system myelin protein P2.";
PLoS ONE 5:E10300-E10300(2010).
[10]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-132.
Structural genomics consortium (SGC);
"Crystal structure of human peripheral myelin protein 2.";
Submitted (AUG-2010) to the PDB data bank.
-!- FUNCTION: May play a role in lipid transport protein in Schwann
cells. May bind cholesterol. {ECO:0000269|PubMed:20421974}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20421974}.
-!- INTERACTION:
O95273:CCNDBP1; NbExp=3; IntAct=EBI-10193858, EBI-748961;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- DOMAIN: Forms a beta-barrel structure that accommodates
hydrophobic ligands in its interior.
{ECO:0000269|PubMed:20421974}.
-!- MISCELLANEOUS: P2 protein and myelin basic protein together
constitute a major fraction of peripheral nervous system myelin
protein.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D16181; BAA03726.1; -; Genomic_DNA.
EMBL; X62167; CAA44096.1; -; mRNA.
EMBL; AK311758; BAG34701.1; -; mRNA.
EMBL; CR541649; CAG46450.1; -; mRNA.
EMBL; CR541738; CAG46538.1; -; mRNA.
EMBL; AC018616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471068; EAW87090.1; -; Genomic_DNA.
EMBL; BC034997; AAH34997.1; -; mRNA.
EMBL; AH004648; AAB32592.2; -; Genomic_DNA.
CCDS; CCDS6229.1; -.
PIR; JT0977; MPHU2.
RefSeq; NP_002668.1; NM_002677.4.
UniGene; Hs.571512; -.
PDB; 2WUT; X-ray; 1.85 A; A=1-132.
PDB; 3NR3; X-ray; 1.95 A; A=3-132.
PDB; 4A1H; X-ray; 2.20 A; A/B/C=1-132.
PDB; 4A1Y; X-ray; 1.20 A; A/B/C/D=1-132.
PDB; 4A8Z; X-ray; 1.80 A; A=1-132.
PDB; 4BVM; X-ray; 0.93 A; A=1-132.
PDB; 4D6A; X-ray; 1.45 A; A=1-132.
PDB; 4D6B; X-ray; 2.12 A; A=1-132.
PDB; 5N4M; X-ray; 1.59 A; A=1-132.
PDB; 5N4P; X-ray; 1.53 A; A=1-132.
PDB; 5N4Q; X-ray; 1.72 A; A=1-132.
PDBsum; 2WUT; -.
PDBsum; 3NR3; -.
PDBsum; 4A1H; -.
PDBsum; 4A1Y; -.
PDBsum; 4A8Z; -.
PDBsum; 4BVM; -.
PDBsum; 4D6A; -.
PDBsum; 4D6B; -.
PDBsum; 5N4M; -.
PDBsum; 5N4P; -.
PDBsum; 5N4Q; -.
ProteinModelPortal; P02689; -.
SMR; P02689; -.
BioGrid; 111388; 7.
IntAct; P02689; 1.
MINT; MINT-5006340; -.
STRING; 9606.ENSP00000256103; -.
ChEMBL; CHEMBL3826864; -.
DrugBank; DB04147; Lauryl Dimethylamine-N-Oxide.
DrugBank; DB04224; Oleic Acid.
DrugBank; DB03796; Palmitic Acid.
DrugBank; DB01915; S-Hydroxycysteine.
iPTMnet; P02689; -.
PhosphoSitePlus; P02689; -.
SwissPalm; P02689; -.
BioMuta; PMP2; -.
DMDM; 127725; -.
MaxQB; P02689; -.
PaxDb; P02689; -.
PeptideAtlas; P02689; -.
PRIDE; P02689; -.
DNASU; 5375; -.
Ensembl; ENST00000256103; ENSP00000256103; ENSG00000147588.
GeneID; 5375; -.
KEGG; hsa:5375; -.
UCSC; uc003ycb.3; human.
CTD; 5375; -.
DisGeNET; 5375; -.
EuPathDB; HostDB:ENSG00000147588.6; -.
GeneCards; PMP2; -.
HGNC; HGNC:9117; PMP2.
MalaCards; PMP2; -.
MIM; 170715; gene.
neXtProt; NX_P02689; -.
OpenTargets; ENSG00000147588; -.
PharmGKB; PA33443; -.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00760000118898; -.
HOGENOM; HOG000004829; -.
HOVERGEN; HBG005633; -.
InParanoid; P02689; -.
OMA; VGNRTKP; -.
OrthoDB; EOG091G0QSV; -.
PhylomeDB; P02689; -.
TreeFam; TF316894; -.
EvolutionaryTrace; P02689; -.
GeneWiki; PMP2; -.
GenomeRNAi; 5375; -.
PRO; PR:P02689; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000147588; -.
CleanEx; HS_PMP2; -.
ExpressionAtlas; P02689; baseline and differential.
Genevisible; P02689; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:InterPro.
GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
GO; GO:0005215; F:transporter activity; IEA:InterPro.
GO; GO:0061024; P:membrane organization; IEA:Ensembl.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
InterPro; IPR031256; Myelin_P2.
PANTHER; PTHR11955; PTHR11955; 1.
PANTHER; PTHR11955:SF64; PTHR11955:SF64; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Lipid-binding;
Phosphoprotein; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6183401}.
CHAIN 2 132 Myelin P2 protein.
/FTId=PRO_0000067388.
REGION 127 129 Fatty acid binding.
BINDING 107 107 Fatty acid.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:6183401}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P55054}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:P55054}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000250|UniProtKB:P55054}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000250|UniProtKB:P55054}.
DISULFID 118 125 {ECO:0000269|PubMed:6183401}.
CONFLICT 25 25 G -> GG (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 99 99 D -> N (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 111 111 N -> D (in Ref. 8; AA sequence).
{ECO:0000305}.
HELIX 3 5 {ECO:0000244|PDB:4BVM}.
STRAND 7 16 {ECO:0000244|PDB:4BVM}.
HELIX 17 23 {ECO:0000244|PDB:4BVM}.
HELIX 28 36 {ECO:0000244|PDB:4BVM}.
STRAND 40 46 {ECO:0000244|PDB:4BVM}.
STRAND 49 55 {ECO:0000244|PDB:4BVM}.
STRAND 61 65 {ECO:0000244|PDB:4BVM}.
STRAND 71 74 {ECO:0000244|PDB:4BVM}.
STRAND 80 88 {ECO:0000244|PDB:4BVM}.
STRAND 91 98 {ECO:0000244|PDB:4BVM}.
STRAND 101 110 {ECO:0000244|PDB:4BVM}.
STRAND 113 120 {ECO:0000244|PDB:4BVM}.
STRAND 123 131 {ECO:0000244|PDB:4BVM}.
SEQUENCE 132 AA; 14909 MW; 3D515D32695899D2 CRC64;
MSNKFLGTWK LVSSENFDDY MKALGVGLAT RKLGNLAKPT VIISKKGDII TIRTESTFKN
TEISFKLGQE FEETTADNRK TKSIVTLQRG SLNQVQRWDG KETTIKRKLV NGKMVAECKM
KGVVCTRIYE KV


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