ID A0A3L8T2C4_CHLGU Unreviewed; 149 AA.
AC A0A3L8T2C4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Myelin P2 protein {ECO:0000256|ARBA:ARBA00018567};
GN ORFNames=DV515_00000358 {ECO:0000313|EMBL:RLW13144.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW13144.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW13144.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW13144.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW13144.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW13144.1}.
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DR EMBL; QUSF01000001; RLW13144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8T2C4; -.
DR STRING; 44316.ENSEGOP00005000443; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Transport {ECO:0000256|RuleBase:RU003696}.
FT DOMAIN 7..24
FT /note="Cytosolic fatty-acid binding proteins"
FT /evidence="ECO:0000259|PROSITE:PS00214"
SQ SEQUENCE 149 AA; 16636 MW; 7FE8280294F994EF CRC64;
MCNRFVGTWK LISSENFDDY MKELGVGLAA RKLGGLARPD IIISMKGDIV TIRTESTFKN
TSISFKLGQQ FDETTADDRK VKSVVTLEKG SLVQVQKWNG KETTIKRRLV DGKMVVVSSR
SLYTAKGQPD AAFSTFLSKQ TIKFGLLFE
//
