FA10A_DANRE
ID FA10A_DANRE Reviewed; 126 AA.
AC Q9I8L5; Q8JHE8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Fatty acid-binding protein 10-A, liver basic;
DE Short=Zf-FABP10;
DE Short=Zf-Lb-FABP;
DE AltName: Full=Fatty acid-binding protein, liver;
DE AltName: Full=Liver bile acid-binding protein;
DE Short=L-BABP;
DE Short=z-L-BABP;
DE AltName: Full=Liver-type fatty acid-binding protein;
DE Short=L-FABP;
DE Short=Liver-type FABP;
GN Name=fabp10a; Synonyms=fabp10; ORFNames=zgc:103719, zgc:92741;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11004494; DOI=10.1016/s0167-4781(00)00102-0;
RA Denovan-Wright E.M., Pierce M., Sharma M.K., Wright J.M.;
RT "cDNA sequence and tissue-specific expression of a basic liver-type fatty
RT acid binding protein in adult zebrafish (Danio rerio).";
RL Biochim. Biophys. Acta 1492:227-232(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59, AND TISSUE SPECIFICITY.
RX PubMed=12815620; DOI=10.1002/dvdy.10324;
RA Her G.M., Yeh Y.-H., Wu J.-L.;
RT "435-bp liver regulatory sequence in the liver fatty acid binding protein
RT (L-FABP) gene is sufficient to modulate liver regional expression in
RT transgenic zebrafish.";
RL Dev. Dyn. 227:347-356(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12633865; DOI=10.1016/s0014-5793(03)00157-1;
RA Her G.M., Chiang C.C., Chen W.Y., Wu J.L.;
RT "In vivo studies of liver-type fatty acid binding protein (L-FABP) gene
RT expression in liver of transgenic zebrafish (Danio rerio).";
RL FEBS Lett. 538:125-133(2003).
RN [5]
RP TISSUE SPECIFICITY, AND GENE DUPLICATION.
RX PubMed=16857010; DOI=10.1111/j.1742-4658.2006.05330.x;
RA Sharma M.K., Liu R.Z., Thisse C., Thisse B., Denovan-Wright E.M.,
RA Wright J.M.;
RT "Hierarchical subfunctionalization of fabp1a, fabp1b and fabp10 tissue-
RT specific expression may account for retention of these duplicated genes in
RT the zebrafish (Danio rerio) genome.";
RL FEBS J. 273:3216-3229(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH CHOLATE, AND
RP MUTAGENESIS OF GLY-56 AND CYS-92.
RX PubMed=17670743; DOI=10.1074/jbc.m705399200;
RA Capaldi S., Guariento M., Saccomani G., Fessas D., Perduca M., Monaco H.L.;
RT "A single amino acid mutation in zebrafish (Danio rerio) liver bile acid-
RT binding protein can change the stoichiometry of ligand binding.";
RL J. Biol. Chem. 282:31008-31018(2007).
CC -!- FUNCTION: Binds hydrophobic ligands, such as cholate, in the cytoplasm.
CC May be involved in intracellular lipid transport (By similarity). Binds
CC one cholate per subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the developing embryonic liver from 48
CC hpf. Also expressed in the liver of 5-day-old larvae. In adults,
CC primarily expressed in the liver, with weak expression in the testis
CC and intestine. {ECO:0000269|PubMed:11004494,
CC ECO:0000269|PubMed:12633865, ECO:0000269|PubMed:12815620,
CC ECO:0000269|PubMed:16857010}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior.
CC -!- MISCELLANEOUS: A member of the basic liver-type FABPs, which are only
CC found, thus far, in non-mammalian vertebrates.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
CC -!- CAUTION: PubMed:12633865 reports expression in the ventral endoderm at
CC 36 hpf, whereas PubMed:16857010 does not detect expression this early.
CC The different timings may reflect strain-specific differences.
CC {ECO:0000305}.
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DR EMBL; AF254642; AAF67743.1; -; mRNA.
DR EMBL; BC076219; AAH76219.1; -; mRNA.
DR EMBL; BC081518; AAH81518.1; -; mRNA.
DR EMBL; AF512998; AAM47005.1; -; Genomic_DNA.
DR RefSeq; NP_694492.1; NM_152960.1.
DR PDB; 2QO4; X-ray; 1.50 A; A=1-126.
DR PDB; 2QO5; X-ray; 1.50 A; A=2-126.
DR PDB; 2QO6; X-ray; 1.90 A; A=1-126.
DR PDBsum; 2QO4; -.
DR PDBsum; 2QO5; -.
DR PDBsum; 2QO6; -.
DR AlphaFoldDB; Q9I8L5; -.
DR SMR; Q9I8L5; -.
DR STRING; 7955.ENSDARP00000056094; -.
DR TCDB; 8.A.33.1.4; the fatty acid binding protein (fabp) family.
DR PaxDb; Q9I8L5; -.
DR Ensembl; ENSDART00000056095; ENSDARP00000056094; ENSDARG00000038439.
DR GeneID; 171481; -.
DR KEGG; dre:171481; -.
DR CTD; 171481; -.
DR ZFIN; ZDB-GENE-020318-1; fabp10a.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000164147; -.
DR HOGENOM; CLU_113772_4_1_1; -.
DR InParanoid; Q9I8L5; -.
DR OMA; GKFCHVQ; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; Q9I8L5; -.
DR TreeFam; TF330348; -.
DR EvolutionaryTrace; Q9I8L5; -.
DR PRO; PR:Q9I8L5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000038439; Expressed in liver and 18 other tissues.
DR ExpressionAtlas; Q9I8L5; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032052; F:bile acid binding; IDA:ZFIN.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid-binding; Reference proteome; Transport.
FT CHAIN 1..126
FT /note="Fatty acid-binding protein 10-A, liver basic"
FT /id="PRO_0000312344"
FT BINDING 57
FT /ligand="cholate"
FT /ligand_id="ChEBI:CHEBI:29747"
FT /evidence="ECO:0000269|PubMed:17670743"
FT BINDING 77
FT /ligand="cholate"
FT /ligand_id="ChEBI:CHEBI:29747"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="cholate"
FT /ligand_id="ChEBI:CHEBI:29747"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="cholate"
FT /ligand_id="ChEBI:CHEBI:29747"
FT /evidence="ECO:0000250"
FT MUTAGEN 56
FT /note="G->R: No effect on cholate binding stoichiometry."
FT /evidence="ECO:0000269|PubMed:17670743"
FT MUTAGEN 92
FT /note="C->T: Changes cholate binding stoichiometry so that
FT 2 cholate molecules are bound per subunit."
FT /evidence="ECO:0000269|PubMed:17670743"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:2QO4"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:2QO4"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:2QO4"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:2QO4"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:2QO4"
SQ SEQUENCE 126 AA; 14004 MW; F77419F1F2489814 CRC64;
MAFSGTWQVY AQENYEEFLR AISLPEEVIK LAKDVKPVTE IQQNGSDFTI TSKTPGKTVT
NSFTIGKEAE ITTMDGKKLK CIVKLDGGKL VCRTDRFSHI QEIKAGEMVE TLTVGGTTMI
RKSKKI
