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Fatty acid-binding protein 10-A, liver basic (Zf-FABP10) (Zf-Lb-FABP) (Fatty acid-binding protein, liver) (Liver bile acid-binding protein) (L-BABP) (z-L-BABP) (Liver-type fatty acid-binding protein) (L-FABP) (Liver-type FABP)

 FA10A_DANRE             Reviewed;         126 AA.
Q9I8L5; Q8JHE8;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 116.
RecName: Full=Fatty acid-binding protein 10-A, liver basic;
Short=Zf-FABP10;
Short=Zf-Lb-FABP;
AltName: Full=Fatty acid-binding protein, liver;
AltName: Full=Liver bile acid-binding protein;
Short=L-BABP;
Short=z-L-BABP;
AltName: Full=Liver-type fatty acid-binding protein;
Short=L-FABP;
Short=Liver-type FABP;
Name=fabp10a; Synonyms=fabp10; ORFNames=zgc:103719, zgc:92741;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=11004494; DOI=10.1016/S0167-4781(00)00102-0;
Denovan-Wright E.M., Pierce M., Sharma M.K., Wright J.M.;
"cDNA sequence and tissue-specific expression of a basic liver-type
fatty acid binding protein in adult zebrafish (Danio rerio).";
Biochim. Biophys. Acta 1492:227-232(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59, AND TISSUE SPECIFICITY.
PubMed=12815620; DOI=10.1002/dvdy.10324;
Her G.M., Yeh Y.-H., Wu J.-L.;
"435-bp liver regulatory sequence in the liver fatty acid binding
protein (L-FABP) gene is sufficient to modulate liver regional
expression in transgenic zebrafish.";
Dev. Dyn. 227:347-356(2003).
[4]
TISSUE SPECIFICITY.
PubMed=12633865; DOI=10.1016/S0014-5793(03)00157-1;
Her G.M., Chiang C.C., Chen W.Y., Wu J.L.;
"In vivo studies of liver-type fatty acid binding protein (L-FABP)
gene expression in liver of transgenic zebrafish (Danio rerio).";
FEBS Lett. 538:125-133(2003).
[5]
TISSUE SPECIFICITY, AND GENE DUPLICATION.
PubMed=16857010; DOI=10.1111/j.1742-4658.2006.05330.x;
Sharma M.K., Liu R.Z., Thisse C., Thisse B., Denovan-Wright E.M.,
Wright J.M.;
"Hierarchical subfunctionalization of fabp1a, fabp1b and fabp10
tissue-specific expression may account for retention of these
duplicated genes in the zebrafish (Danio rerio) genome.";
FEBS J. 273:3216-3229(2006).
[6]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH CHOLATE, AND
MUTAGENESIS OF GLY-56 AND CYS-92.
PubMed=17670743; DOI=10.1074/jbc.M705399200;
Capaldi S., Guariento M., Saccomani G., Fessas D., Perduca M.,
Monaco H.L.;
"A single amino acid mutation in zebrafish (Danio rerio) liver bile
acid-binding protein can change the stoichiometry of ligand binding.";
J. Biol. Chem. 282:31008-31018(2007).
-!- FUNCTION: Binds hydrophobic ligands, such as cholate, in the
cytoplasm. May be involved in intracellular lipid transport (By
similarity). Binds one cholate per subunit. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the developing embryonic liver
from 48 hpf. Also expressed in the liver of 5-day-old larvae. In
adults, primarily expressed in the liver, with weak expression in
the testis and intestine. {ECO:0000269|PubMed:11004494,
ECO:0000269|PubMed:12633865, ECO:0000269|PubMed:12815620,
ECO:0000269|PubMed:16857010}.
-!- DOMAIN: Forms a beta-barrel structure that accommodates
hydrophobic ligands in its interior.
-!- MISCELLANEOUS: A member of the basic liver-type FABPs, which are
only found, thus far, in non-mammalian vertebrates.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
-!- CAUTION: PubMed:12633865 reports expression in the ventral
endoderm at 36 hpf, whereas PubMed:16857010 does not detect
expression this early. The different timings may reflect strain-
specific differences. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF254642; AAF67743.1; -; mRNA.
EMBL; BC076219; AAH76219.1; -; mRNA.
EMBL; BC081518; AAH81518.1; -; mRNA.
EMBL; AF512998; AAM47005.1; -; Genomic_DNA.
RefSeq; NP_694492.1; NM_152960.1.
UniGene; Dr.104721; -.
PDB; 2QO4; X-ray; 1.50 A; A=1-126.
PDB; 2QO5; X-ray; 1.50 A; A=2-126.
PDB; 2QO6; X-ray; 1.90 A; A=1-126.
PDBsum; 2QO4; -.
PDBsum; 2QO5; -.
PDBsum; 2QO6; -.
ProteinModelPortal; Q9I8L5; -.
SMR; Q9I8L5; -.
STRING; 7955.ENSDARP00000056094; -.
TCDB; 8.A.33.1.4; the fatty acid binding protein (fabp) family.
PaxDb; Q9I8L5; -.
Ensembl; ENSDART00000056095; ENSDARP00000056094; ENSDARG00000038439.
GeneID; 171481; -.
KEGG; dre:171481; -.
CTD; 171481; -.
ZFIN; ZDB-GENE-020318-1; fabp10a.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00390000012034; -.
HOVERGEN; HBG005633; -.
InParanoid; Q9I8L5; -.
OMA; WQVYAQE; -.
OrthoDB; EOG091G16BV; -.
PhylomeDB; Q9I8L5; -.
TreeFam; TF330348; -.
EvolutionaryTrace; Q9I8L5; -.
PRO; PR:Q9I8L5; -.
Proteomes; UP000000437; Chromosome 16.
Bgee; ENSDARG00000038439; -.
ExpressionAtlas; Q9I8L5; baseline and differential.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0032052; F:bile acid binding; IDA:ZFIN.
GO; GO:0005215; F:transporter activity; IEA:InterPro.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
PANTHER; PTHR11955; PTHR11955; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Lipid-binding;
Reference proteome; Transport.
CHAIN 1 126 Fatty acid-binding protein 10-A, liver
basic.
/FTId=PRO_0000312344.
BINDING 57 57 Cholate. {ECO:0000269|PubMed:17670743}.
BINDING 77 77 Cholate. {ECO:0000250}.
BINDING 99 99 Cholate. {ECO:0000250}.
BINDING 101 101 Cholate. {ECO:0000250}.
MUTAGEN 56 56 G->R: No effect on cholate binding
stoichiometry.
{ECO:0000269|PubMed:17670743}.
MUTAGEN 92 92 C->T: Changes cholate binding
stoichiometry so that 2 cholate molecules
are bound per subunit.
{ECO:0000269|PubMed:17670743}.
STRAND 5 14 {ECO:0000244|PDB:2QO4}.
HELIX 15 21 {ECO:0000244|PDB:2QO4}.
HELIX 26 31 {ECO:0000244|PDB:2QO4}.
TURN 32 34 {ECO:0000244|PDB:2QO4}.
STRAND 38 44 {ECO:0000244|PDB:2QO4}.
STRAND 47 54 {ECO:0000244|PDB:2QO4}.
STRAND 57 64 {ECO:0000244|PDB:2QO4}.
STRAND 67 72 {ECO:0000244|PDB:2QO4}.
STRAND 78 82 {ECO:0000244|PDB:2QO4}.
STRAND 84 86 {ECO:0000244|PDB:2QO4}.
STRAND 89 93 {ECO:0000244|PDB:2QO4}.
STRAND 98 104 {ECO:0000244|PDB:2QO4}.
STRAND 107 114 {ECO:0000244|PDB:2QO4}.
STRAND 117 125 {ECO:0000244|PDB:2QO4}.
SEQUENCE 126 AA; 14004 MW; F77419F1F2489814 CRC64;
MAFSGTWQVY AQENYEEFLR AISLPEEVIK LAKDVKPVTE IQQNGSDFTI TSKTPGKTVT
NSFTIGKEAE ITTMDGKKLK CIVKLDGGKL VCRTDRFSHI QEIKAGEMVE TLTVGGTTMI
RKSKKI


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