Fabp1

Functionⁱ

Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (By similarity). Binds cholesterol (PubMed:25732850). Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity).By similarity1 Publication

Miscellaneous

There are three fractions of Z-protein: DE-I, DE-II and DE-III. DE-I is virtually lipid free, DE-II binds palmitic, stearic, oleic, linoleic and arachidonic acids and DE-III binds mainly arachidonic acid.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	31	Fatty acid 11 Publication	1
Binding siteⁱ	39	Fatty acid 21 Publication	1
Binding siteⁱ	122	Fatty acid 21 Publication	1

GO - Molecular functionⁱ

antioxidant activity Source: Ensembl
bile acid binding
Source: RGD
Inferred from mutant phenotypeⁱ
- 12479568
chromatin binding Source: Ensembl
drug binding
Source: RGD
Inferred from physical interactionⁱ
- 1939124
fatty acid binding
Source: RGD
Inferred from direct assayⁱ
- 3478711
long-chain fatty acid transporter activity
Source: RGD
Inferred from mutant phenotypeⁱ
- 15035630
lysophospholipid transporter activity
Source: RGD
Inferred by curatorⁱ
- 12479568
phospholipid binding
Source: RGD
Inferred from mutant phenotypeⁱ
- 12479568

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to hydrogen peroxide Source: Ensembl
cellular response to hypoxia Source: Ensembl
intestinal absorption
Source: RGD
Inferred from direct assayⁱ
- 10666570
long-chain fatty acid transport
Source: RGD
Inferred from mutant phenotypeⁱ
- 15035630
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
positive regulation of fatty acid beta-oxidation
Source: RGD
Inferred from direct assayⁱ
- 16262600
positive regulation of hydrolase activity
Source: RGD
Inferred from direct assayⁱ
- 16262600

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Transport
Ligand	Lipid-binding

Enzyme and pathway databases

Reactomeⁱ	R-RNO-163560 Triglyceride catabolism R-RNO-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)

Reactomeⁱ

R-RNO-163560 Triglyceride catabolism
R-RNO-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)

Chemistry databases

SwissLipidsⁱ	SLP:000001517

SwissLipidsⁱ

SLP:000001517

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Fatty acid-binding protein, liver Alternative name(s): Fatty acid-binding protein 1 Liver-type fatty acid-binding protein Short name: L-FABP Squalene- and sterol-carrier protein Short name: SCP Z-protein p14
Gene namesⁱ	Name:Fabp1
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 4

Organism-specific databases

Rat genome database More...RGDⁱ	2590 Fabp1

RGDⁱ

2590 Fabp1

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL5738
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2531

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000067337	1 – 127	Fatty acid-binding protein, liverAdd BLAST		127

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionine2 Publications	1
Modified residueⁱ	11	PhosphoserineCombined sources	1
Modified residueⁱ	31	N6-succinyllysineBy similarity	1
Modified residueⁱ	36	N6-succinyllysineBy similarity	1
Modified residueⁱ	39	PhosphoserineCombined sources	1
Modified residueⁱ	46	N6-succinyllysineBy similarity	1
Modified residueⁱ	51	PhosphothreonineBy similarity	1
Modified residueⁱ	56	PhosphoserineCombined sources	1
Modified residueⁱ	57	N6-succinyllysineBy similarity	1
Modified residueⁱ	78	N6-succinyllysineBy similarity	1
Modified residueⁱ	84	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	84	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	90	N6-succinyllysineBy similarity	1
Modified residueⁱ	100	PhosphoserineBy similarity	1
Cross-linkⁱ	105 ↔ 106	Isoaspartyl glycine isopeptide (Asn-Gly); alternate
Modified residueⁱ	105	Deamidated asparagine; alternate1 Publication	1
Modified residueⁱ	121	N6-succinyllysineBy similarity	1

Post-translational modificationⁱ

Deamidation and transpeptidation at the beta carboxyl of Asn-105 forms an isoaspartyl residue found in an isoform of the DE-III fraction. This rearrangement gives rise to an extra negative charge carried by the acid form.1 Publication

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein

Proteomic databases

PaxDbⁱ	P02692
PRIDEⁱ	P02692

PTM databases

CarbonylDBⁱ	P02692
iPTMnetⁱ	P02692
PhosphoSitePlusⁱ	P02692

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSRNOG00000006675 Expressed in 8 organ(s), highest expression level in liver
Genevisibleⁱ	P02692 RN

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Hnf4a	P22449	3	EBI-1209448,EBI-5261592

With

Entry

#Exp.

IntAct

Notes

Hnf4a

P22449

3

EBI-1209448,EBI-5261592

Protein-protein interaction databases

IntActⁱ	P02692, 2 interactors
Molecular INTeraction database More...MINTⁱ	P02692
STRINGⁱ	10116.ENSRNOP00000008841

Chemistry databases

BindingDBⁱ	P02692

BindingDBⁱ

P02692

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 14	Combined sources	10
Helixⁱ	15 – 21	Combined sources	7
Helixⁱ	26 – 32	Combined sources	7
Beta strandⁱ	38 – 44	Combined sources	7
Beta strandⁱ	47 – 54	Combined sources	8
Beta strandⁱ	57 – 64	Combined sources	8
Beta strandⁱ	67 – 72	Combined sources	6
Beta strandⁱ	74 – 76	Combined sources	3
Beta strandⁱ	78 – 82	Combined sources	5
Beta strandⁱ	84 – 86	Combined sources	3
Turnⁱ	87 – 89	Combined sources	3
Beta strandⁱ	90 – 95	Combined sources	6
Beta strandⁱ	98 – 105	Combined sources	8
Beta strandⁱ	108 – 115	Combined sources	8
Beta strandⁱ	118 – 127	Combined sources	10

Show more details

3D structure databases

ProteinModelPortalⁱ	P02692
SMRⁱ	P02692
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P02692

EvolutionaryTraceⁱ

P02692

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	54 – 56	Fatty acid 1 binding		3

Domainⁱ

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

Sequence similaritiesⁱ

Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.Curated

Phylogenomic databases

eggNOGⁱ	KOG4015 Eukaryota ENOG4111US8 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000012034
HOGENOMⁱ	HOG000004830
HOVERGENⁱ	HBG005633
InParanoidⁱ	P02692
KEGG Orthology (KO) More...KOⁱ	K08750
OMAⁱ	FTLGEEC
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G16BV
PhylomeDBⁱ	P02692
TreeFamⁱ	TF330348

Family and domain databases

Gene3Dⁱ	2.40.128.20, 1 hit
InterProⁱ	View protein in InterPro IPR012674 Calycin IPR000463 Fatty_acid-bd IPR031259 ILBP IPR031276 Lb-FABP
PANTHERⁱ	PTHR11955 PTHR11955, 1 hit PTHR11955:SF96 PTHR11955:SF96, 1 hit
PRINTSⁱ	PR00178 FATTYACIDBP
SUPFAMⁱ	SSF50814 SSF50814, 1 hit
PROSITEⁱ	View protein in PROSITE PS00214 FABP, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P02692-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNFSGKYQVQ SQENFEPFMK AMGLPEDLIQ KGKDIKGVSE IVHEGKKVKL 
        60         70         80         90        100
TITYGSKVIH NEFTLGEECE LETMTGEKVK AVVKMEGDNK MVTTFKGIKS 
       110        120 
VTEFNGDTIT NTMTLGDIVY KRVSKRI

Length:127

Mass (Da):14,273

Last modified:August 13, 1987 - v1

Checksum:ⁱ08C7F59A99FE0D3A

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	V01235 mRNA Translation: CAA24545.1 M13501 Genomic DNA Translation: AAA41140.1 M35991 mRNA Translation: AAA41135.1 S55929 Other DNA Translation: AAB19788.1 BC086947 mRNA Translation: AAH86947.1 M17899 mRNA Translation: AAA41134.1 M10951 mRNA Translation: AAA42119.1
PIRⁱ	A92416 FZRTL I52354 I52850 I55238
NCBI Reference Sequences More...RefSeqⁱ	NP_036688.1, NM_012556.2
UniGeneⁱ	Rn.36412

Genome annotation databases

Ensemblⁱ	ENSRNOT00000008840; ENSRNOP00000008841; ENSRNOG00000006675
GeneIDⁱ	24360
KEGGⁱ	rno:24360
UCSC genome browser More...UCSCⁱ	RGD:2590 rat

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P02692	Fatty acid-binding protein, liver		MOUSE		127	UniRef90_P02692
UPI00006832AA		RAT		128
UPI0004ED309C		NANGA		127
UPI000A30A858		MUSPA		127
UPI000A315199		MUSCR		127
+2

Protein	Similar proteins		Species	Score	Length	Source
P02692	Fatty acid-binding protein, liver		MOUSE		127	UniRef50_P02692
Fatty acid-binding protein, liver (Fragment)		HETGA		111
fatty acid-binding protein, liver		PHYCD		127
fatty acid-binding protein, liver		DELLE		127
Fatty acid-binding protein, liver (Fragment)		ESCRO		127
+24

Entry informationⁱ

Entry nameⁱ	FABPL_RAT
Accessionⁱ	P02692Primary (citable) accession number: P02692
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	August 13, 1987
	Last modified:	September 12, 2018
	This is version 173 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

UniParc

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UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P02692 (FABPL_RAT)

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Fatty acid-binding protein, liver

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Other locations

Cytosol

Nucleus

Peroxisome

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ