ID B5X785_SALSA Unreviewed; 127 AA.
AC B5X785;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=FABPL {ECO:0000313|EMBL:ACI66705.1};
GN Synonyms=fabpl {ECO:0000313|RefSeq:NP_001134229.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI66705.1};
RN [1] {ECO:0000313|EMBL:ACI66705.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Head kidney {ECO:0000313|EMBL:ACI66705.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI66705.1, ECO:0000313|RefSeq:NP_001134229.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Head kidney {ECO:0000313|EMBL:ACI66705.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACI66705.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Head kidney {ECO:0000313|EMBL:ACI66705.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001134229.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 EMBL; BT046904; ACI66705.1; -; mRNA.
DR RefSeq; NP_001134229.1; NM_001140757.1.
DR STRING; 8030.ENSSSAP00000077361; -.
DR PaxDb; 8030-ENSSSAP00000077361; -.
DR GeneID; 100195728; -.
DR KEGG; sasa:100195728; -.
DR CTD; 100195728; -.
DR OrthoDB; 3015340at2759; -.
DR Proteomes; UP000087266; Chromosome ssa24.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005504; F:fatty acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015908; P:fatty acid transport; IEA:UniProtKB-UniRule.
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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU369022};
KW Lipid-binding {ECO:0000256|RuleBase:RU369022};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
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; 14143 MW; 914C545C10977AAF CRC64;
MSFSGKYQME THENFESFME AIGLPDELIQ EGKDIKSISE IEETGDHFKV TVTTGTKILT
NSFTIGQETE LEPPTGEKVN SVVTREGNKL MAFLNGIEYV TELTDANTLV NTLTLPGISY
KKTSKRM
//
