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Database: UniProt
Entry: A0A2K5Z091_MANLE
LinkDB: A0A2K5Z091_MANLE
Original site: A0A2K5Z091_MANLE 
ID   A0A2K5Z091_MANLE        Unreviewed;       132 AA.
AC   A0A2K5Z091;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Myelin P2 protein {ECO:0000256|ARBA:ARBA00018567};
GN   Name=PMP2 {ECO:0000313|Ensembl:ENSMLEP00000021215.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000021215.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000021215.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: May play a role in lipid transport protein in Schwann cells.
CC       May bind cholesterol. {ECO:0000256|ARBA:ARBA00025662}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000256|ARBA:ARBA00008390,
CC       ECO:0000256|RuleBase:RU003696}.
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DR   RefSeq; XP_011845160.1; XM_011989770.1.
DR   AlphaFoldDB; A0A2K5Z091; -.
DR   STRING; 9568.ENSMLEP00000021215; -.
DR   Ensembl; ENSMLET00000044715.1; ENSMLEP00000021215.1; ENSMLEG00000034823.1.
DR   GeneID; 105546535; -.
DR   KEGG; mleu:105546535; -.
DR   CTD; 5375; -.
DR   GeneTree; ENSGT00940000160445; -.
DR   OMA; YITIRTE; -.
DR   OrthoDB; 46617at2759; -.
DR   Proteomes; UP000233140; Unplaced.
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; IEA:Ensembl.
DR   GO; GO:0005504; F:fatty acid binding; IEA:Ensembl.
DR   GO; GO:0061024; P:membrane organization; IEA:Ensembl.
DR   CDD; cd19469; FABP8; 1.
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; FATTY ACID BINDING PROTEIN; 1.
DR   PANTHER; PTHR11955:SF64; MYELIN P2 PROTEIN; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003696}.
FT   DOMAIN          7..24
FT                   /note="Cytosolic fatty-acid binding proteins"
FT                   /evidence="ECO:0000259|PROSITE:PS00214"
SQ   SEQUENCE   132 AA;  14907 MW;  D0E60B98DFEE3364 CRC64;
     MSNKFLGTWK LVSSENFDDY MKALGVGLAT RKLGNLAKPT VIISKKGDIL TIRTESTFKN
     TEISFKLGQE FEETTADNRK AKSIVTLQRG SLNQVQRWDG KETTIKRKLV NGKMVVECKM
     KGVVCTRIYE KV
//
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