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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) (Mammary-derived growth inhibitor related)

 FABP7_HUMAN             Reviewed;         132 AA.
O15540; B2R4L1; O14951; Q6IAU7; Q9H047;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 160.
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;
AltName: Full=Mammary-derived growth inhibitor related;
Name=FABP7; Synonyms=BLBP, FABPB, MRG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Schnuetgen F., Boerchers T., Xhong N., Godbout R., Sacchettini J.C.,
Spener F.;
"Human brain-type fatty acid binding protein shows high affinity for
omega-3 fatty acids but not for omega-6 fatty acids.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9375786; DOI=10.1016/S0167-4781(97)00115-2;
Shimizu F., Watanabe T.K., Shinomiya H., Nakamura Y., Fujiwara T.;
"Isolation and expression of a cDNA for human brain fatty acid-binding
protein (B-FABP).";
Biochim. Biophys. Acta 1354:24-28(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Retina;
PubMed=9591779; DOI=10.1038/sj.onc.1201740;
Godbout R., Bisgrove D.A., Shkolny D., Day R.S. III;
"Correlation of B-FABP and GFAP expression in malignant glioma.";
Oncogene 16:1955-1962(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S.,
Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M.,
Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E.,
Hirai Y.;
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Shi Y.E., Ni J.;
"Identification and characterization of a novel human tumor suppressor
gene with homology to mammary derived growth inhibitor.";
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary gland;
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).
[12]
PROTEIN SEQUENCE OF 11-53; 60-79; 83-97 AND 114-127, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[13]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
PubMed=10854433;
Balendiran G.K., Schnuetgen F., Scapin G., Boerchers T., Xhong N.,
Lim K., Godbout R., Spener F., Sacchettini J.C.;
"Crystal structure and thermodynamic analysis of human brain fatty
acid-binding protein.";
J. Biol. Chem. 275:27045-27054(2000).
[14]
STRUCTURE BY NMR.
PubMed=12479569; DOI=10.1023/A:1020566909213;
Rademacher M., Zimmerman A.W., Rueterjans H., Veerkamp J.H.,
Luecke C.;
"Solution structure of fatty acid-binding protein from human brain.";
Mol. Cell. Biochem. 239:61-68(2002).
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O15540-1; Sequence=Displayed;
Name=2;
IsoId=O15540-2; Sequence=VSP_055490;
-!- TISSUE SPECIFICITY: Expressed in brain and other neural tissues.
-!- DOMAIN: Forms a beta-barrel structure that accommodates the
hydrophobic ligand in its interior.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
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EMBL; AJ002962; CAA05773.1; -; mRNA.
EMBL; D88648; BAA23645.1; -; mRNA.
EMBL; U51338; AAB87141.1; -; mRNA.
EMBL; D50373; BAA23324.1; -; mRNA.
EMBL; U81235; AAD00507.1; -; mRNA.
EMBL; CR457057; CAG33338.1; -; mRNA.
EMBL; AK289836; BAF82525.1; -; mRNA.
EMBL; AK311867; BAG34808.1; -; mRNA.
EMBL; AL512688; CAC21646.1; -; mRNA.
EMBL; AL645811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48166.1; -; Genomic_DNA.
EMBL; CH471051; EAW48167.1; -; Genomic_DNA.
EMBL; BC012299; AAH12299.1; -; mRNA.
CCDS; CCDS5127.1; -. [O15540-1]
CCDS; CCDS83121.1; -. [O15540-2]
RefSeq; NP_001305968.1; NM_001319039.1. [O15540-2]
RefSeq; NP_001437.1; NM_001446.4. [O15540-1]
UniGene; Hs.26770; -.
PDB; 1FDQ; X-ray; 2.10 A; A/B=2-132.
PDB; 1FE3; X-ray; 2.80 A; A=2-132.
PDB; 1JJX; NMR; -; A=2-132.
PDB; 5URA; X-ray; 1.85 A; A/B/C/D=1-132.
PDBsum; 1FDQ; -.
PDBsum; 1FE3; -.
PDBsum; 1JJX; -.
PDBsum; 5URA; -.
ProteinModelPortal; O15540; -.
SMR; O15540; -.
BioGrid; 108471; 10.
IntAct; O15540; 1.
STRING; 9606.ENSP00000357429; -.
ChEMBL; CHEMBL3826863; -.
DrugBank; DB00132; Alpha-Linolenic Acid.
DrugBank; DB00154; Dihomo-gamma-linolenic acid.
DrugBank; DB00159; Icosapent.
DrugBank; DB04224; Oleic Acid.
SwissLipids; SLP:000000498; -.
iPTMnet; O15540; -.
PhosphoSitePlus; O15540; -.
BioMuta; FABP7; -.
DOSAC-COBS-2DPAGE; O15540; -.
EPD; O15540; -.
PaxDb; O15540; -.
PeptideAtlas; O15540; -.
PRIDE; O15540; -.
ProteomicsDB; 48748; -.
DNASU; 2173; -.
Ensembl; ENST00000356535; ENSP00000348931; ENSG00000164434. [O15540-2]
Ensembl; ENST00000368444; ENSP00000357429; ENSG00000164434. [O15540-1]
GeneID; 2173; -.
KEGG; hsa:2173; -.
UCSC; uc003pzd.4; human. [O15540-1]
CTD; 2173; -.
DisGeNET; 2173; -.
EuPathDB; HostDB:ENSG00000164434.11; -.
GeneCards; FABP7; -.
HGNC; HGNC:3562; FABP7.
HPA; CAB025488; -.
HPA; CAB058697; -.
HPA; HPA028825; -.
MIM; 602965; gene.
neXtProt; NX_O15540; -.
OpenTargets; ENSG00000164434; -.
PharmGKB; PA27963; -.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00760000118898; -.
HOGENOM; HOG000004829; -.
HOVERGEN; HBG005633; -.
InParanoid; O15540; -.
KO; K08756; -.
OMA; VCTRIYK; -.
OrthoDB; EOG091G0QSV; -.
PhylomeDB; O15540; -.
TreeFam; TF316894; -.
Reactome; R-HSA-163560; Triglyceride catabolism.
Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
SIGNOR; O15540; -.
ChiTaRS; FABP7; human.
EvolutionaryTrace; O15540; -.
GeneWiki; FABP7; -.
GenomeRNAi; 2173; -.
PRO; PR:O15540; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000164434; -.
CleanEx; HS_FABP7; -.
Genevisible; O15540; HS.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0042995; C:cell projection; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0008289; F:lipid binding; TAS:ProtInc.
GO; GO:0021846; P:cell proliferation in forebrain; IEA:Ensembl.
GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
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;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Lipid-binding; Polymorphism;
Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q09139}.
CHAIN 2 132 Fatty acid-binding protein, brain.
/FTId=PRO_0000067373.
REGION 127 129 Fatty acid binding.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000250|UniProtKB:Q09139}.
VAR_SEQ 117 132 TLTFGDVVAVRHYEKA -> VSNDNSPFFLVFFSSPHTSHL
LPSSSLLLPFFLLPSFFNNTSLARFFNYM (in isoform
2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_055490.
VARIANT 61 61 T -> M (in dbSNP:rs2279381).
/FTId=VAR_049012.
CONFLICT 60 60 N -> D (in Ref. 4; BAA23324).
{ECO:0000305}.
CONFLICT 110 110 K -> R (in Ref. 6; CAG33338).
{ECO:0000305}.
HELIX 3 5 {ECO:0000244|PDB:1FDQ}.
STRAND 7 16 {ECO:0000244|PDB:5URA}.
HELIX 17 24 {ECO:0000244|PDB:5URA}.
HELIX 28 36 {ECO:0000244|PDB:5URA}.
STRAND 40 46 {ECO:0000244|PDB:5URA}.
STRAND 49 55 {ECO:0000244|PDB:5URA}.
STRAND 61 65 {ECO:0000244|PDB:5URA}.
STRAND 71 74 {ECO:0000244|PDB:5URA}.
TURN 76 78 {ECO:0000244|PDB:1JJX}.
STRAND 80 88 {ECO:0000244|PDB:5URA}.
STRAND 91 98 {ECO:0000244|PDB:5URA}.
STRAND 101 110 {ECO:0000244|PDB:5URA}.
STRAND 113 120 {ECO:0000244|PDB:5URA}.
STRAND 123 131 {ECO:0000244|PDB:5URA}.
SEQUENCE 132 AA; 14889 MW; F1E8EE12B9474B97 CRC64;
MVEAFCATWK LTNSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGDKV VIRTLSTFKN
TEISFQLGEE FDETTADDRN CKSVVSLDGD KLVHIQKWDG KETNFVREIK DGKMVMTLTF
GDVVAVRHYE KA


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E0344b ELISA kit Bos taurus,Bovine,Differentiation-associated lipid-binding protein LP2,E-FABP,Epidermal-type fatty acid-binding protein,FABP5,Fatty acid-binding protein 5,Fatty acid-binding protein, epider 96T
E0344m ELISA kit E-FABP,Epidermal-type fatty acid-binding protein,Fabp5,Fabpe,Fatty acid-binding protein 5,Fatty acid-binding protein, epidermal,Keratinocyte lipid-binding protein,Klbp,Mal1,Mouse,Mus muscul 96T
U0344m CLIA E-FABP,Epidermal-type fatty acid-binding protein,Fabp5,Fabpe,Fatty acid-binding protein 5,Fatty acid-binding protein, epidermal,Keratinocyte lipid-binding protein,Klbp,Mal1,Mouse,Mus musculus,PA- 96T
E0344m ELISA E-FABP,Epidermal-type fatty acid-binding protein,Fabp5,Fabpe,Fatty acid-binding protein 5,Fatty acid-binding protein, epidermal,Keratinocyte lipid-binding protein,Klbp,Mal1,Mouse,Mus musculus,PA 96T
E0184m ELISA 3T3-L1 lipid-binding protein,Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Ap2,Fabp4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipoc 96T


 

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