ID   MYP2_HORSE              Reviewed;         132 AA.
AC   P0C6G6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Myelin P2 protein;
GN   Name=PMP2;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=16041071; DOI=10.1107/s0907444905014162;
RA   Hunter D.J., Macmaster R., Roszak A.W., Riboldi-Tunnicliffe A.,
RA   Griffiths I.R., Freer A.A.;
RT   "Structure of myelin P2 protein from equine spinal cord.";
RL   Acta Crystallogr. D 61:1067-1071(2005).
CC   -!- FUNCTION: May play a role in lipid transport protein in Schwann cells.
CC       May bind cholesterol. {ECO:0000269|PubMed:16041071}.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16041071}.
CC   -!- TISSUE SPECIFICITY: Detected in spinal cord (at protein level).
CC       {ECO:0000269|PubMed:16041071}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior.
CC   -!- MASS SPECTROMETRY: Mass=14761; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16041071};
CC   -!- MISCELLANEOUS: P2 protein and myelin basic protein together constitute
CC       a major fraction of peripheral nervous system myelin protein.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   PDB; 1YIV; X-ray; 2.10 A; A=2-130.
DR   PDBsum; 1YIV; -.
DR   AlphaFoldDB; P0C6G6; -.
DR   SMR; P0C6G6; -.
DR   InParanoid; P0C6G6; -.
DR   EvolutionaryTrace; P0C6G6; -.
DR   Proteomes; UP000002281; Unplaced.
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:0005504; F:fatty acid binding; IBA:GO_Central.
DR   GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR   GO; GO:0061024; P:membrane organization; IEA:InterPro.
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   3D-structure; Acetylation; Cytoplasm; Disulfide bond; Lipid-binding;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02690"
FT   CHAIN           2..132
FT                   /note="Myelin P2 protein"
FT                   /id="PRO_0000323733"
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:0000250|UniProtKB:P02690"
FT   DISULFID        118..125
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          7..16
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   HELIX           17..23
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   HELIX           28..36
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          40..46
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          80..87
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          89..98
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          101..110
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          113..120
FT                   /evidence="ECO:0007829|PDB:1YIV"
FT   STRAND          123..132
FT                   /evidence="ECO:0007829|PDB:1YIV"
SQ   SEQUENCE   132 AA;  14492 MW;  3600ADB1F99DB4FD CRC64;
     MSNKFLGTWK LTSSENFDEY MKALGVGLGT RSLGNLAGPT VIISKSGDVI TIRTESGFKN
     TEISFKLGQE FEETTADNRK TKSTVTLAGG KLNQVQKWNG NETTIKRELV DGKMVVECSM
     ASVVCTRIYE QV