ID   MYP2_RABIT              Reviewed;         132 AA.
AC   P02691;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Myelin P2 protein;
GN   Name=PMP2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2453513; DOI=10.1016/s0021-9258(18)68481-9;
RA   Narayanan V., Barbosa E., Reed R., Tennekoon G.;
RT   "Characterization of a cloned cDNA encoding rabbit myelin P2 protein.";
RL   J. Biol. Chem. 263:8332-8337(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-56, AND ACETYLATION AT SER-2.
RX   PubMed=7356651; DOI=10.1016/s0021-9258(19)86141-0;
RA   Ishaque A., Hofmann T., Rhee S., Eylar E.H.;
RT   "The NH2-terminal region of the P2 protein from rabbit sciatic nerve
RT   myelin.";
RL   J. Biol. Chem. 255:1058-1063(1980).
RN   [3]
RP   PROTEIN SEQUENCE OF 56-132.
RX   PubMed=6172423; DOI=10.1016/s0021-9258(19)68231-1;
RA   Ishaque A., Hofmann T., Eylar E.H.;
RT   "The complete amino acid sequence of the rabbit P2 protein.";
RL   J. Biol. Chem. 257:592-595(1982).
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}.
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   EMBL; J03744; AAA31451.1; -; mRNA.
DR   PIR; A28081; MPRB2.
DR   RefSeq; NP_001075699.1; NM_001082230.1.
DR   AlphaFoldDB; P02691; -.
DR   SMR; P02691; -.
DR   STRING; 9986.ENSOCUP00000023290; -.
DR   iPTMnet; P02691; -.
DR   Ensembl; ENSOCUT00000024328; ENSOCUP00000023290; ENSOCUG00000007445.
DR   GeneID; 100009045; -.
DR   KEGG; ocu:100009045; -.
DR   CTD; 5375; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00940000161845; -.
DR   HOGENOM; CLU_113772_0_0_1; -.
DR   InParanoid; P02691; -.
DR   OMA; CIMGDVI; -.
DR   OrthoDB; 1417203at2759; -.
DR   Proteomes; UP000001811; Chromosome 3.
DR   Bgee; ENSOCUG00000007445; Expressed in autopod skin and 16 other tissues.
DR   ExpressionAtlas; P02691; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043209; C:myelin sheath; IEA:InterPro.
DR   GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR   GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
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   Acetylation; Cytoplasm; Direct protein sequencing; Lipid-binding;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7356651"
FT   CHAIN           2..132
FT                   /note="Myelin P2 protein"
FT                   /id="PRO_0000067390"
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:7356651"
FT   CONFLICT        73
FT                   /note="E -> Q (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="I -> T (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="D -> N (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   132 AA;  14922 MW;  E568B1CF5ADA9A0E CRC64;
     MSNKFLGTWK LVSSENFDDY MKALGVGLAT RKLGNLAKPN VIISKKGDII TIRTESTFKN
     TEISFKLGQE FEETTADNRK TKSIITLERG ALNQVQKWDG KETTIKRKLV DGKMVVECKM
     KGVVCTRIYE KV