FABP7_MOUSE
ID FABP7_MOUSE Reviewed; 132 AA.
AC P51880; Q4FJK4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Fatty acid-binding protein, brain;
DE AltName: Full=Brain lipid-binding protein;
DE Short=BLBP;
DE AltName: Full=Brain-type fatty acid-binding protein;
DE Short=B-FABP;
DE AltName: Full=Fatty acid-binding protein 7;
GN Name=Fabp7; Synonyms=Blbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ICR X Swiss Webster; TISSUE=Liver;
RX PubMed=7956838; DOI=10.1242/dev.120.9.2637;
RA Kurtz A., Zimmer A., Schnuetgen F., Bruening G., Spener F., Mueller T.;
RT "The expression pattern of a novel gene encoding brain-fatty acid binding
RT protein correlates with neuronal and glial cell development.";
RL Development 120:2637-2649(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8161459; DOI=10.1016/0896-6273(94)90341-7;
RA Feng L., Hatten M.E., Heintz N.;
RT "Brain lipid-binding protein (BLBP): a novel signaling system in the
RT developing mammalian CNS.";
RL Neuron 12:895-908(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP PROTEIN SEQUENCE OF 2-10.
RX PubMed=8722323; DOI=10.1515/bchm3.1996.377.3.211;
RA Schnutgen F., Borchers T., Muller T., Spener F.;
RT "Heterologous expression and characterisation of mouse brain fatty acid
RT binding protein.";
RL Biol. Chem. Hoppe-Seyler 377:211-215(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: B-FABP could be involved in the transport of a so far unknown
CC hydrophobic ligand with potential morphogenic activity during CNS
CC development. It is required for the establishment of the radial glial
CC fiber system in developing brain, a system that is necessary for the
CC migration of immature neurons to establish cortical layers.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in brain and other neural tissues.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; U04827; AAA81904.1; -; Genomic_DNA.
DR EMBL; S69799; AAB30595.1; -; mRNA.
DR EMBL; AK002955; BAB22478.1; -; mRNA.
DR EMBL; AK021271; BAB32356.1; -; mRNA.
DR EMBL; CT010401; CAJ18607.1; -; mRNA.
DR EMBL; BC055280; AAH55280.1; -; mRNA.
DR EMBL; BC057090; AAH57090.1; -; mRNA.
DR CCDS; CCDS23856.1; -.
DR PIR; I48923; I48923.
DR RefSeq; NP_067247.1; NM_021272.3.
DR AlphaFoldDB; P51880; -.
DR SMR; P51880; -.
DR STRING; 10090.ENSMUSP00000020024; -.
DR iPTMnet; P51880; -.
DR PhosphoSitePlus; P51880; -.
DR MaxQB; P51880; -.
DR PaxDb; P51880; -.
DR PeptideAtlas; P51880; -.
DR PRIDE; P51880; -.
DR ProteomicsDB; 275845; -.
DR Antibodypedia; 19513; 607 antibodies from 41 providers.
DR DNASU; 12140; -.
DR Ensembl; ENSMUST00000020024; ENSMUSP00000020024; ENSMUSG00000019874.
DR GeneID; 12140; -.
DR KEGG; mmu:12140; -.
DR UCSC; uc007fct.1; mouse.
DR CTD; 2173; -.
DR MGI; MGI:101916; Fabp7.
DR VEuPathDB; HostDB:ENSMUSG00000019874; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000156713; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P51880; -.
DR OMA; KDDKMVM; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P51880; -.
DR TreeFam; TF316894; -.
DR Reactome; R-MMU-163560; Triglyceride catabolism.
DR BioGRID-ORCS; 12140; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Fabp7; mouse.
DR PRO; PR:P51880; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P51880; protein.
DR Bgee; ENSMUSG00000019874; Expressed in olfactory bulb and 207 other tissues.
DR ExpressionAtlas; P51880; baseline and differential.
DR Genevisible; P51880; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR GO; GO:0001964; P:startle response; IMP:MGI.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Lipid-binding;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q09139"
FT CHAIN 2..132
FT /note="Fatty acid-binding protein, brain"
FT /id="PRO_0000067374"
FT BINDING 127..129
FT /ligand="a fatty acid"
FT /ligand_id="ChEBI:CHEBI:28868"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:Q09139"
SQ SEQUENCE 132 AA; 14893 MW; 13D8970E7D8D9C57 CRC64;
MVDAFCATWK LTDSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGGKV VIRTQCTFKN
TEINFQLGEE FEETSIDDRN CKSVVRLDGD KLIHVQKWDG KETNCTREIK DGKMVVTLTF
GDIVAVRCYE KA
