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Fatty acid-binding protein, brain (Brain lipid-binding protein) (BLBP) (Brain-type fatty acid-binding protein) (B-FABP) (Fatty acid-binding protein 7)

 FABP7_MOUSE             Reviewed;         132 AA.
P51880; Q4FJK4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 143.
RecName: Full=Fatty acid-binding protein, brain;
AltName: Full=Brain lipid-binding protein;
Short=BLBP;
AltName: Full=Brain-type fatty acid-binding protein;
Short=B-FABP;
AltName: Full=Fatty acid-binding protein 7;
Name=Fabp7; Synonyms=Blbp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ICR X Swiss Webster; TISSUE=Liver;
PubMed=7956838;
Kurtz A., Zimmer A., Schnuetgen F., Bruening G., Spener F.,
Mueller T.;
"The expression pattern of a novel gene encoding brain-fatty acid
binding protein correlates with neuronal and glial cell development.";
Development 120:2637-2649(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8161459; DOI=10.1016/0896-6273(94)90341-7;
Feng L., Hatten M.E., Heintz N.;
"Brain lipid-binding protein (BLBP): a novel signaling system in the
developing mammalian CNS.";
Neuron 12:895-908(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain, and Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-10.
PubMed=8722323; DOI=10.1515/bchm3.1996.377.3.211;
Schnutgen F., Borchers T., Muller T., Spener F.;
"Heterologous expression and characterisation of mouse brain fatty
acid binding protein.";
Biol. Chem. Hoppe-Seyler 377:211-215(1996).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: B-FABP could be involved in the transport of a so far
unknown hydrophobic ligand with potential morphogenic activity
during CNS development. It is required for the establishment of
the radial glial fiber system in developing brain, a system that
is necessary for the migration of immature neurons to establish
cortical layers.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in brain and other neural tissues.
-!- DOMAIN: Forms a beta-barrel structure that accommodates
hydrophobic ligands in its interior. {ECO:0000250}.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
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EMBL; U04827; AAA81904.1; -; Genomic_DNA.
EMBL; S69799; AAB30595.1; -; mRNA.
EMBL; AK002955; BAB22478.1; -; mRNA.
EMBL; AK021271; BAB32356.1; -; mRNA.
EMBL; CT010401; CAJ18607.1; -; mRNA.
EMBL; BC055280; AAH55280.1; -; mRNA.
EMBL; BC057090; AAH57090.1; -; mRNA.
CCDS; CCDS23856.1; -.
PIR; I48923; I48923.
RefSeq; NP_067247.1; NM_021272.3.
UniGene; Mm.3644; -.
ProteinModelPortal; P51880; -.
SMR; P51880; -.
STRING; 10090.ENSMUSP00000020024; -.
iPTMnet; P51880; -.
PhosphoSitePlus; P51880; -.
MaxQB; P51880; -.
PaxDb; P51880; -.
PeptideAtlas; P51880; -.
PRIDE; P51880; -.
Ensembl; ENSMUST00000020024; ENSMUSP00000020024; ENSMUSG00000019874.
GeneID; 12140; -.
KEGG; mmu:12140; -.
UCSC; uc007fct.1; mouse.
CTD; 2173; -.
MGI; MGI:101916; Fabp7.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00760000118898; -.
HOGENOM; HOG000004829; -.
HOVERGEN; HBG005633; -.
InParanoid; P51880; -.
KO; K08756; -.
OMA; ICRREFV; -.
PhylomeDB; P51880; -.
TreeFam; TF316894; -.
Reactome; R-MMU-163560; Triglyceride catabolism.
PRO; PR:P51880; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000019874; Expressed in 248 organ(s), highest expression level in olfactory bulb.
CleanEx; MM_FABP7; -.
ExpressionAtlas; P51880; baseline and differential.
Genevisible; P51880; MM.
GO; GO:0044297; C:cell body; IDA:MGI.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005504; F:fatty acid binding; TAS:BHF-UCL.
GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI.
GO; GO:0050673; P:epithelial cell proliferation; ISO:MGI.
GO; GO:0022008; P:neurogenesis; IMP:MGI.
GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
GO; GO:0001964; P:startle response; IMP:MGI.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11955; PTHR11955; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
Lipid-binding; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q09139}.
CHAIN 2 132 Fatty acid-binding protein, brain.
/FTId=PRO_0000067374.
REGION 127 129 Fatty acid binding. {ECO:0000250}.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000250|UniProtKB:Q09139}.
SEQUENCE 132 AA; 14893 MW; 13D8970E7D8D9C57 CRC64;
MVDAFCATWK LTDSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGGKV VIRTQCTFKN
TEINFQLGEE FEETSIDDRN CKSVVRLDGD KLIHVQKWDG KETNCTREIK DGKMVVTLTF
GDIVAVRCYE KA


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