ID A0A2K5DH38_AOTNA Unreviewed; 127 AA.
AC A0A2K5DH38;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Fatty acid-binding protein, liver {ECO:0000256|ARBA:ARBA00013460, ECO:0000256|RuleBase:RU369022};
DE Short=L-FABP {ECO:0000256|RuleBase:RU369022};
DE AltName: Full=Liver-type fatty acid-binding protein {ECO:0000256|RuleBase:RU369022};
GN Name=FABP1 {ECO:0000313|Ensembl:ENSANAP00000020249.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000020249.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000020249.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Binds free fatty acids and their coenzyme A derivatives,
CC bilirubin, and some other small molecules in the cytoplasm. May be
CC involved in intracellular lipid transport.
CC {ECO:0000256|RuleBase:RU369022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369022}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000256|RuleBase:RU369022}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000256|ARBA:ARBA00008390,
CC ECO:0000256|RuleBase:RU369022}.
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DR RefSeq; XP_012328400.1; XM_012472977.1.
DR AlphaFoldDB; A0A2K5DH38; -.
DR STRING; 37293.ENSANAP00000020249; -.
DR Ensembl; ENSANAT00000038124.1; ENSANAP00000020249.1; ENSANAG00000027916.1.
DR GeneID; 105731272; -.
DR CTD; 2168; -.
DR GeneTree; ENSGT00940000155135; -.
DR OMA; DTITNTM; -.
DR OrthoDB; 3015340at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016209; F:antioxidant activity; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0005504; F:fatty acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; IEA:UniProtKB-UniRule.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR CDD; cd19444; FABP1; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR PANTHER; PTHR11955; FATTY ACID BINDING PROTEIN; 1.
DR PANTHER; PTHR11955:SF96; FATTY ACID-BINDING PROTEIN, LIVER; 1.
DR Pfam; PF14651; Lipocalin_7; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00214; FABP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU369022};
KW Lipid-binding {ECO:0000256|RuleBase:RU369022};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU369022}.
FT DOMAIN 5..22
FT /note="Cytosolic fatty-acid binding proteins"
FT /evidence="ECO:0000259|PROSITE:PS00214"
SQ SEQUENCE 127 AA; 14174 MW; 78629FCBF9A13C04 CRC64;
MNFTGKYQLQ SQENFEPFMK AIGLPDEIIQ KGKDIKGVSE IVQNGKHFKL TITAGSKVIN
NEFTLGEECE LETMSGEKVK AVVQMEGDNK LVTTFKNIKS VTELNGDIIT STMTLGDIVF
KRISKRI
//