FA1B1_DANRE
ID FA1B1_DANRE Reviewed; 128 AA.
AC Q4VBT1; Q1AMT2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Fatty acid binding protein 1-B.1;
DE AltName: Full=Fatty acid binding protein 1b {ECO:0000303|PubMed:16857010};
DE Short=Zf-FABP1b {ECO:0000303|PubMed:16857010};
GN Name=fabp1b.1;
GN Synonyms=fabp1b {ECO:0000312|EMBL:AAZ08576.1,
GN ECO:0000312|ZFIN:ZDB-GENE-050522-96}; ORFNames=zgc:110431;
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] {ECO:0000305, ECO:0000312|EMBL:AAZ08576.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 [2] {ECO:0000312|EMBL:AAH95259.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH95259.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP INDUCTION.
RX PubMed=19725974; DOI=10.1186/1471-2148-9-219;
RA Karanth S., Lall S.P., Denovan-Wright E.M., Wright J.M.;
RT "Differential transcriptional modulation of duplicated fatty acid-binding
RT protein genes by dietary fatty acids in zebrafish (Danio rerio): evidence
RT for subfunctionalization or neofunctionalization of duplicated genes.";
RL BMC Evol. Biol. 9:219-219(2009).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=19953126; DOI=10.1139/g09-071;
RA Karanth S., Denovan-Wright E.M., Thisse C., Thisse B., Wright J.M.;
RT "Tandem duplication of the fabp1b gene and subsequent divergence of the
RT tissue-specific distribution of fabp1b.1 and fabp1b.2 transcripts in
RT zebrafish (Danio rerio).";
RL Genome 52:985-992(2009).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P07148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07148}.
CC -!- TISSUE SPECIFICITY: Expressed in the yolk syncytial layer (YSL) and
CC subsequently in the intestinal bulb in developing embryos and larvae.
CC In adults, expressed in the intestine. {ECO:0000269|PubMed:16857010,
CC ECO:0000269|PubMed:19953126}.
CC -!- INDUCTION: By a linolenic acid-rich diet.
CC {ECO:0000269|PubMed:19725974}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250|UniProtKB:P07148}.
CC -!- MISCELLANEOUS: The zebrafish genome contains duplicated fabp1b genes
CC (fabp1b.1 and fabp1b.2) which probably arose from a tandem gene
CC duplication event. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000255}.
CC -!- CAUTION: PubMed:16857010 reports that adult expression is restricted to
CC the intestine and absent from the liver, whereas PubMed:19953126
CC detects expression in the liver, intestine, heart, testis, ovary, and
CC gills. {ECO:0000305}.
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DR EMBL; DQ062096; AAZ08576.1; -; mRNA.
DR EMBL; DQ474062; ABF18598.1; -; mRNA.
DR EMBL; BC095259; AAH95259.1; -; mRNA.
DR RefSeq; NP_001019822.1; NM_001024651.2.
DR AlphaFoldDB; Q4VBT1; -.
DR SMR; Q4VBT1; -.
DR STRING; 7955.ENSDARP00000124794; -.
DR PRIDE; Q4VBT1; -.
DR Ensembl; ENSDART00000149528; ENSDARP00000124794; ENSDARG00000059227.
DR GeneID; 554095; -.
DR KEGG; dre:554095; -.
DR CTD; 554095; -.
DR ZFIN; ZDB-GENE-050522-96; fabp1b.1.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155135; -.
DR HOGENOM; CLU_113772_4_2_1; -.
DR InParanoid; Q4VBT1; -.
DR OMA; DTITNTM; -.
DR OrthoDB; 1440574at2759; -.
DR PhylomeDB; Q4VBT1; -.
DR Reactome; R-DRE-163560; Triglyceride catabolism.
DR Reactome; R-DRE-189483; Heme degradation.
DR Reactome; R-DRE-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-DRE-9707564; Cytoprotection by HMOX1.
DR PRO; PR:Q4VBT1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000059227; Expressed in intestine and 16 other tissues.
DR ExpressionAtlas; Q4VBT1; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; ISS:ZFIN.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0033993; P:response to lipid; IDA:ZFIN.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR031276; Lb-FABP.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF96; PTHR11955:SF96; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Lipid-binding; Reference proteome; Transport.
FT CHAIN 1..128
FT /note="Fatty acid binding protein 1-B.1"
FT /id="PRO_0000397923"
FT CONFLICT 16
FT /note="V -> E (in Ref. 1; AAZ08576/ABF18598)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="R -> K (in Ref. 1; AAZ08576/ABF18598)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="I -> T (in Ref. 1; AAZ08576/ABF18598)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="A -> T (in Ref. 1; AAZ08576/ABF18598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 14115 MW; D33DBCC611A09466 CRC64;
MSFTGKYQLE SQEGFVEFMK AVGLPDDMIE KGKDIKSVSE IEENGNQFKV TVTTGSKVLT
NSFTIGQEAD IETLTGERVK TIVNREGNKL KVVLNRITSI TELVDANTLV NTLTLGGLVY
KRISKRVA
