P02689 (MYP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myelin P2 protein

Alternative name(s):
Peripheral myelin protein 2

Gene names

Name:

PMP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	132 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	May play a role in lipid transport protein in Schwann cells. May bind cholesterol. Ref.9
Subunit structure	Monomer. Ref.9
Subcellular location	Cytoplasm By similarity.
Domain	Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. Ref.9
Miscellaneous	P2 protein and myelin basic protein together constitute a major fraction of peripheral nervous system myelin protein.
Sequence similarities	Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm
Ligand	Lipid-binding
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	membrane organization Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cholesterol binding Inferred from direct assay Ref.9. Source: UniProtKB fatty acid binding Inferred from direct assay Ref.9. Source: UniProtKB transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 132

131

Myelin P2 protein

PRO_0000067388

Regions

Region

127 – 129

3

Fatty acid binding

Sites

Binding site

107

1

Fatty acid

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.8

Disulfide bond

118 ↔ 125

Ref.8

Experimental info

Sequence conflict

25

1

G → GG AA sequence Ref.8

Sequence conflict

99

1

D → N AA sequence Ref.8

Sequence conflict

111

1

N → D AA sequence Ref.8

Secondary structure

1

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132

Helix Strand Turn

Details...

Helix

3 – 5

3

Beta strand

7 – 16

10

Helix

17 – 24

8

Helix

28 – 36

9

Beta strand

40 – 46

7

Beta strand

49 – 56

8

Beta strand

59 – 65

7

Beta strand

71 – 74

4

Beta strand

80 – 88

9

Beta strand

91 – 98

8

Beta strand

101 – 110

10

Beta strand

113 – 120

8

Beta strand

123 – 131

9

Sequences

	Sequence		Length	Mass (Da)
	P02689 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3D515D32695899D2	FASTA	132	14,909
	10 20 30 40 50 60 MSNKFLGTWK LVSSENFDDY MKALGVGLAT RKLGNLAKPT VIISKKGDII TIRTESTFKN 70 80 90 100 110 120 TEISFKLGQE FEETTADNRK TKSIVTLQRG SLNQVQRWDG KETTIKRKLV NGKMVAECKM 130 KGVVCTRIYE KV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequence determination of cDNA encoding P2 protein of human peripheral myelin." Hayasaka K., Nanao K., Tahara M., Sato W., Takada G., Miura M., Uyemura K. Biochem. Biophys. Res. Commun. 181:204-207(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"DNA sequence and analysis of human chromosome 8." 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. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Testis.
[7]	"Partial structure and mapping of the human myelin P2 protein gene." Narayanan V., Ripepi B., Jabs E.W., Hawkins A., Griffin C., Tennekoon G. J. Neurochem. 63:2010-2013(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
[8]	"The complete amino acid sequence of human P2 protein." Suzuki M., Kitamura K., Sakamoto Y., Uyemura K. J. Neurochem. 39:1759-1762(1982) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-132, ACETYLATION AT SER-2.
[9]	"Structural and functional characterization of human peripheral nervous system myelin protein P2." Majava V., Polverini E., Mazzini A., Nanekar R., Knoll W., Peters J., Natali F., Baumgartel P., Kursula I., Kursula P. PLoS ONE 5:E10300-E10300(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PALMITATE, FUNCTION, MASS SPECTROMETRY, SUBUNIT, CIRCULAR DICHROISM, DOMAIN.
[10]	"Crystal structure of human peripheral myelin protein 2." Structural genomics consortium (SGC) Submitted (AUG-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-132.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D16181 Genomic DNA. Translation: BAA03726.1.
X62167 mRNA. Translation: CAA44096.1.
AK311758 mRNA. Translation: BAG34701.1.
CR541649 mRNA. Translation: CAG46450.1.
CR541738 mRNA. Translation: CAG46538.1.
AC018616 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW87090.1.
BC034997 mRNA. Translation: AAH34997.1.
AH004648 Genomic DNA. Translation: AAB32592.2.

IPI

IPI00219533.

PIR

MPHU2. JT0977.

RefSeq

NP_002668.1. NM_002677.3.

UniGene

Hs.571512.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WUT	X-ray	1.85	A	1-132	[»]
3NR3	X-ray	1.95	A	3-132	[»]
4A1H	X-ray	2.20	A/B/C	1-132	[»]
4A1Y	X-ray	1.20	A/B/C/D	1-132	[»]
4A8Z	X-ray	1.80	A	1-132	[»]

ProteinModelPortal

P02689.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000256103.

PTM databases

PhosphoSite

P02689.

Polymorphism databases

DMDM

127725.

Proteomic databases

PaxDb

P02689.

PRIDE

P02689.

Protocols and materials databases

DNASU

5375.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256103; ENSP00000256103; ENSG00000147588.

GeneID

5375.

KEGG

hsa:5375.

UCSC

uc003ycb.1. human.

Organism-specific databases

CTD

5375.

GeneCards

GC08M082352.

HGNC

HGNC:9117. PMP2.

MIM

170715. gene.

neXtProt

NX_P02689.

PharmGKB

PA33443.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG322298.

HOGENOM

HOG000004829.

HOVERGEN

HBG005633.

InParanoid

P02689.

OMA

RTESAFK.

OrthoDB

EOG4QC16R.

PhylomeDB

P02689.

Gene expression databases

ArrayExpress

P02689.

Bgee

P02689.

CleanEx

HS_PMP2.

Genevestigator

P02689.

GermOnline

ENSG00000147588. Homo sapiens.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR00178. FATTYACIDBP.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00214. FABP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02689.

GenomeRNAi

5375.

NextBio

20852.

SOURCE

Search...

Entry information

Entry name

MYP2_HUMAN

Accession

Primary (citable) accession number: P02689
Secondary accession number(s): Q6FHL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.