O15540 (FABP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fatty acid-binding protein, brain

Alternative name(s):
Brain lipid-binding protein
Short name=BLBP
Brain-type fatty acid-binding protein
Short name=B-FABP
Fatty acid-binding protein 7
Mammary-derived growth inhibitor related

Gene names

Name:	FABP7
Synonyms:	BLBP, FABPB, MRG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	132 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in brain and other neural tissues.
Domain	Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Sequence similarities	Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Lipid-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation in forebrain Inferred from electronic annotation. Source: Compara epithelial cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Traceable author statement PubMed 9250612. Source: ProtInc nervous system development Traceable author statement Ref.2. Source: ProtInc neurogenesis Inferred from electronic annotation. Source: Compara prepulse inhibition Inferred from electronic annotation. Source: Compara
Cellular_component	cell projection Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	lipid binding Traceable author statement Ref.2. Source: ProtInc transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 132

131

Fatty acid-binding protein, brain

PRO_0000067373

Regions

Region

127 – 129

3

Fatty acid binding

Natural variations

Natural variant

61

1

T → M.
Corresponds to variant rs2279381 [ dbSNP | Ensembl ].

VAR_049012

Experimental info

Sequence conflict

60

1

N → D in BAA23324. Ref.4

Sequence conflict

110

1

K → R in CAG33338. Ref.6

Secondary structure

1

.

.

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132

Helix Strand Turn

Details...

Helix

3 – 5

3

Beta strand

7 – 16

10

Helix

17 – 23

7

Helix

28 – 36

9

Beta strand

40 – 46

7

Beta strand

49 – 55

7

Beta strand

63 – 65

3

Beta strand

71 – 74

4

Turn

76 – 78

3

Beta strand

80 – 88

9

Beta strand

91 – 98

8

Beta strand

101 – 110

10

Beta strand

113 – 120

8

Beta strand

123 – 131

9

Sequences

	Sequence		Length	Mass (Da)
	O15540 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F1E8EE12B9474B97	FASTA	132	14,889
	10 20 30 40 50 60 MVEAFCATWK LTNSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGDKV VIRTLSTFKN 70 80 90 100 110 120 TEISFQLGEE FDETTADDRN CKSVVSLDGD KLVHIQKWDG KETNFVREIK DGKMVMTLTF 130 GDVVAVRHYE KA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human brain-type fatty acid binding protein shows high affinity for omega-3 fatty acids but not for omega-6 fatty acids." Schnuetgen F., Boerchers T., Xhong N., Godbout R., Sacchettini J.C., Spener F. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Isolation and expression of a cDNA for human brain fatty acid-binding protein (B-FABP)." Shimizu F., Watanabe T.K., Shinomiya H., Nakamura Y., Fujiwara T. Biochim. Biophys. Acta 1354:24-28(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Correlation of B-FABP and GFAP expression in malignant glioma." Godbout R., Bisgrove D.A., Shkolny D., Day R.S. III Oncogene 16:1955-1962(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[5]	"Identification and characterization of a novel human tumor suppressor gene with homology to mammary derived growth inhibitor." Shi Y.E., Ni J. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[8]	"The DNA sequence and analysis of human chromosome 6." 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. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[11]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 11-53; 60-79; 83-97 AND 114-127, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[12]	"Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein." Balendiran G.K., Schnuetgen F., Scapin G., Boerchers T., Xhong N., Lim K., Godbout R., Spener F., Sacchettini J.C. J. Biol. Chem. 275:27045-27054(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
[13]	"Solution structure of fatty acid-binding protein from human brain." Rademacher M., Zimmerman A.W., Rueterjans H., Veerkamp J.H., Luecke C. Mol. Cell. Biochem. 239:61-68(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ002962 mRNA. Translation: CAA05773.1.
D88648 mRNA. Translation: BAA23645.1.
U51338 mRNA. Translation: AAB87141.1.
D50373 mRNA. Translation: BAA23324.1.
U81235 mRNA. Translation: AAD00507.1.
CR457057 mRNA. Translation: CAG33338.1.
AK311867 mRNA. Translation: BAG34808.1.
AL645811 Genomic DNA. Translation: CAI15449.1.
CH471051 Genomic DNA. Translation: EAW48167.1.
BC012299 mRNA. Translation: AAH12299.1.

IPI

IPI00215747.

RefSeq

NP_001437.1. NM_001446.3.

UniGene

Hs.26770.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FDQ	X-ray	2.10	A/B	2-132	[»]
1FE3	X-ray	2.80	A	2-132	[»]
1JJX	NMR	-	A	2-132	[»]

ProteinModelPortal

O15540.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000357429.

PTM databases

PhosphoSite

O15540.

2D gel databases

DOSAC-COBS-2DPAGE

O15540.

Proteomic databases

PaxDb

O15540.

PRIDE

O15540.

Protocols and materials databases

DNASU

2173.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368444; ENSP00000357429; ENSG00000164434.

GeneID

2173.

KEGG

hsa:2173.

UCSC

uc003pzf.3. human.

Organism-specific databases

CTD

2173.

GeneCards

GC06P123142.

HGNC

HGNC:3562. FABP7.

HPA

CAB025488.
CAB058697.
HPA028825.

MIM

602965. gene.

neXtProt

NX_O15540.

PharmGKB

PA27963.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG241430.

HOGENOM

HOG000004829.

HOVERGEN

HBG005633.

KO

K08756.

OMA

PTIVISH.

OrthoDB

EOG4P8FKD.

Gene expression databases

ArrayExpress

O15540.

Bgee

O15540.

CleanEx

HS_FABP7.

Genevestigator

O15540.

GermOnline

ENSG00000164434. Homo sapiens.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR00178. FATTYACIDBP.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00214. FABP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00132. Alpha-Linolenic Acid.
DB00154. gamma-Homolinolenic acid.
DB00159. Icosapent.

EvolutionaryTrace

O15540.

GenomeRNAi

2173.

NextBio

8777.

SOURCE

Search...

Entry information

Entry name

FABP7_HUMAN

Accession

Primary (citable) accession number: O15540
Secondary accession number(s): B2R4L1, O14951, Q6IAU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.