ID   MYP2_PIG                Reviewed;         132 AA.
AC   P86412;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Myelin P2 protein {ECO:0000303|PubMed:20512566};
GN   Name=PMP2 {ECO:0000250|UniProtKB:P02690};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15679890; DOI=10.1186/1741-7007-3-2;
RA   Jorgensen F.G., Hobolth A., Hornshoj H., Bendixen C., Fredholm M.,
RA   Schierup M.H.;
RT   "Comparative analysis of protein coding sequences from human, mouse and the
RT   domesticated pig.";
RL   BMC Biol. 3:2-2(2005).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-132, MASS SPECTROMETRY, AND ACETYLATION AT SER-2.
RX   PubMed=20512566; DOI=10.1007/s00216-010-3762-0;
RA   Maddalo G., Shariatgorji M., Adams C.M., Fung E., Nilsson U., Zubarev R.A.,
RA   Sedzik J., Ilag L.L.;
RT   "Porcine P2 myelin protein primary structure and bound fatty acids
RT   determined by mass spectrometry.";
RL   Anal. Bioanal. Chem. 397:1903-1910(2010).
CC   -!- FUNCTION: May play a role in lipid transport protein in Schwann cells.
CC       May bind cholesterol (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior. {ECO:0000250|UniProtKB:P02690}.
CC   -!- MASS SPECTROMETRY: Mass=14823.85; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:20512566};
CC   -!- MISCELLANEOUS: P2 protein and myelin basic protein together constitute
CC       a major fraction of peripheral nervous system myelin protein.
CC       {ECO:0000250|UniProtKB:P02690}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000255}.
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DR   EMBL; AY610482; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001171994.1; NM_001185065.1.
DR   RefSeq; XP_005663059.1; XM_005663002.2.
DR   RefSeq; XP_013852106.1; XM_013996652.1.
DR   AlphaFoldDB; P86412; -.
DR   SMR; P86412; -.
DR   STRING; 9823.ENSSSCP00000006563; -.
DR   iPTMnet; P86412; -.
DR   PaxDb; P86412; -.
DR   PeptideAtlas; P86412; -.
DR   PRIDE; P86412; -.
DR   Ensembl; ENSSSCT00005025890; ENSSSCP00005015686; ENSSSCG00005016443.
DR   Ensembl; ENSSSCT00070032947; ENSSSCP00070027510; ENSSSCG00070016714.
DR   Ensembl; ENSSSCT00070032958; ENSSSCP00070027521; ENSSSCG00070016714.
DR   GeneID; 100151890; -.
DR   KEGG; ssc:100151890; -.
DR   CTD; 5375; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   HOGENOM; CLU_113772_0_0_1; -.
DR   InParanoid; P86412; -.
DR   OMA; CIMGDVI; -.
DR   OrthoDB; 1417203at2759; -.
DR   TreeFam; TF316894; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 4.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043209; C:myelin sheath; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR   GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
DR   GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR   GO; GO:0061024; P:membrane organization; IEA:Ensembl.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR031259; ILBP.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   InterPro; IPR031256; Myelin_P2.
DR   PANTHER; PTHR11955; PTHR11955; 1.
DR   PANTHER; PTHR11955:SF64; PTHR11955:SF64; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Lipid-binding; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:20512566"
FT   CHAIN           2..132
FT                   /note="Myelin P2 protein"
FT                   /evidence="ECO:0000269|PubMed:20512566"
FT                   /id="PRO_0000397217"
FT   BINDING         107
FT                   /ligand="(9Z)-octadecenoate"
FT                   /ligand_id="ChEBI:CHEBI:30823"
FT                   /evidence="ECO:0000250|UniProtKB:P02690"
FT   BINDING         107
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:P02689"
FT   BINDING         127..129
FT                   /ligand="(9Z)-octadecenoate"
FT                   /ligand_id="ChEBI:CHEBI:30823"
FT                   /evidence="ECO:0000250|UniProtKB:P02690"
FT   BINDING         127..129
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:P02689"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:20512566"
FT   DISULFID        118..125
FT                   /evidence="ECO:0000250|UniProtKB:P02690"
SQ   SEQUENCE   132 AA;  14922 MW;  6D489CF058438932 CRC64;
     MSNKFLGTWK LVSSENFDDY MKALGVGLAT RKLGNLAKPR VIISKKGDII TIRTESTFKN
     TEISFKLGQE FEETTADNRK AKSVVTLARG SLNQVQKWDG KETTIKRKLV DGKMVVECKM
     KDVVCTRIYE KV