ID U3I073_ANAPP Unreviewed; 127 AA.
AC U3I073;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Fatty acid-binding protein, liver {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:ENSAPLP00000000643.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000000643.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000000643.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000000643.1}
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 AlphaFoldDB; U3I073; -.
DR STRING; 8840.ENSAPLP00000000643; -.
DR Ensembl; ENSAPLT00000001213.2; ENSAPLP00000000643.1; ENSAPLG00000001196.2.
DR GeneTree; ENSGT00940000155135; -.
DR HOGENOM; CLU_113772_4_2_1; -.
DR OMA; DTITNTM; -.
DR Proteomes; UP000016666; Chromosome 4.
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:UP000016666};
KW Transport {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; 14097 MW; 67E879447835F852 CRC64;
MSFTGKYELQ SQENFEPFMK ALGLPDDQIQ KGKDMKSISE IVQDGNKFKV TVTTGSKVLS
NEFTIGEECE MELLTGEKAK TVVNMEGNNK LVANLKGLKS VTELNGDTIT HTMTMGDLTM
KRVSKRI
//
