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Database: UniProt
Entry: A0A2K5DH38_AOTNA
LinkDB: A0A2K5DH38_AOTNA
Original site: A0A2K5DH38_AOTNA 
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
//
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