FBP12_HUMAN
ID FBP12_HUMAN Reviewed; 140 AA.
AC A6NFH5; B7SUN0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Fatty acid-binding protein 12;
GN Name=FABP12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Retinoblastoma;
RX PubMed=18786628; DOI=10.1016/j.ygeno.2008.08.003;
RA Liu R.Z., Li X., Godbout R.;
RT "A novel fatty acid-binding protein (FABP) gene resulting from tandem gene
RT duplication in mammals: transcription in rat retina and testis.";
RL Genomics 92:436-445(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-140.
RA Xiao Y.;
RT "Regulation of human fatty acid binding protein.";
RL Patent number WO03050280, 19-JUN-2003.
CC -!- FUNCTION: May play a role in lipid transport. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in a number of retinoblastoma cell lines.
CC {ECO:0000269|PubMed:18786628}.
CC -!- DEVELOPMENTAL STAGE: Not detected in fetal tissues.
CC {ECO:0000269|PubMed:18786628}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; EU733650; ACI03640.1; -; mRNA.
DR EMBL; AC023644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW87093.1; -; Genomic_DNA.
DR EMBL; BC146973; AAI46974.1; -; mRNA.
DR EMBL; BC146981; AAI46982.1; -; mRNA.
DR EMBL; AX785170; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AX785174; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS47882.1; -.
DR RefSeq; NP_001098751.1; NM_001105281.2.
DR RefSeq; XP_006716528.1; XM_006716465.3.
DR RefSeq; XP_011515879.1; XM_011517577.2.
DR AlphaFoldDB; A6NFH5; -.
DR SMR; A6NFH5; -.
DR BioGRID; 571347; 1.
DR STRING; 9606.ENSP00000353650; -.
DR iPTMnet; A6NFH5; -.
DR PhosphoSitePlus; A6NFH5; -.
DR BioMuta; FABP12; -.
DR MassIVE; A6NFH5; -.
DR PaxDb; A6NFH5; -.
DR PeptideAtlas; A6NFH5; -.
DR PRIDE; A6NFH5; -.
DR Antibodypedia; 49988; 69 antibodies from 16 providers.
DR DNASU; 646486; -.
DR Ensembl; ENST00000360464.5; ENSP00000353650.4; ENSG00000197416.5.
DR Ensembl; ENST00000692030.1; ENSP00000510293.1; ENSG00000197416.5.
DR GeneID; 646486; -.
DR KEGG; hsa:646486; -.
DR UCSC; uc011lfp.3; human.
DR CTD; 646486; -.
DR DisGeNET; 646486; -.
DR GeneCards; FABP12; -.
DR HGNC; HGNC:34524; FABP12.
DR HPA; ENSG00000197416; Tissue enriched (retina).
DR MIM; 618923; gene.
DR neXtProt; NX_A6NFH5; -.
DR OpenTargets; ENSG00000197416; -.
DR PharmGKB; PA164719513; -.
DR VEuPathDB; HostDB:ENSG00000197416; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000162398; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; A6NFH5; -.
DR OMA; MVVESSV; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; A6NFH5; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; A6NFH5; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR BioGRID-ORCS; 646486; 7 hits in 1055 CRISPR screens.
DR GenomeRNAi; 646486; -.
DR Pharos; A6NFH5; Tdark.
DR PRO; PR:A6NFH5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; A6NFH5; protein.
DR Bgee; ENSG00000197416; Expressed in left testis and 43 other tissues.
DR ExpressionAtlas; A6NFH5; 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; 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; IPR031261; FABP12.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF76; PTHR11955:SF76; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 2: Evidence at transcript level;
KW Lipid-binding; Reference proteome; Transport.
FT CHAIN 1..140
FT /note="Fatty acid-binding protein 12"
FT /id="PRO_0000342881"
FT BINDING 107
FT /ligand="a fatty acid"
FT /ligand_id="ChEBI:CHEBI:28868"
FT /evidence="ECO:0000250"
FT BINDING 127..129
FT /ligand="a fatty acid"
FT /ligand_id="ChEBI:CHEBI:28868"
FT /evidence="ECO:0000250"
SQ SEQUENCE 140 AA; 15565 MW; 0231973A7A7F260B CRC64;
MIDQLQGTWK SISCENSEDY MKELGIGRAS RKLGRLAKPT VTISTDGDVI TIKTKSIFKN
NEISFKLGEE FEEITPGGHK TKSKVTLDKE SLIQVQDWDG KETTITRKLV DGKMVVESTV
NSVICTRTYE KVSSNSVSNS
