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Protein

Fatty acid-binding protein, liver

Gene

FABP1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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. Binds 2 molecules of cholate per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Cholate 11 Publication
Binding sitei57 – 571Cholate 11 Publication
Binding sitei77 – 771Cholate 21 Publication
Binding sitei99 – 991Cholate 21 Publication
Binding sitei101 – 1011Cholate 21 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, liver
Alternative name(s):
Fatty acid-binding protein 1
Liver basic FABP
Short name:
LB-FABP
Liver bile acid-binding protein
Short name:
L-BABP
Liver-type fatty acid-binding protein
Short name:
L-FABP
Gene namesi
Name:FABP1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 126125Fatty acid-binding protein, liverPRO_0000067338Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP80226.

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000006574.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Helixi15 – 217Combined sources
Beta strandi22 – 243Combined sources
Helixi26 – 327Combined sources
Beta strandi38 – 447Combined sources
Beta strandi47 – 537Combined sources
Beta strandi58 – 647Combined sources
Beta strandi69 – 724Combined sources
Turni74 – 763Combined sources
Beta strandi78 – 814Combined sources
Beta strandi84 – 863Combined sources
Beta strandi89 – 946Combined sources
Beta strandi97 – 1048Combined sources
Beta strandi107 – 1148Combined sources
Beta strandi117 – 1259Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVGNMR-A2-126[»]
1TVQX-ray2.00A2-126[»]
1TW4X-ray2.00A/B2-126[»]
1ZRYNMR-A2-126[»]
2JN3NMR-A2-126[»]
2K62NMR-A2-126[»]
2LFONMR-A2-126[»]
ProteinModelPortaliP80226.
SMRiP80226. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80226.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
HOGENOMiHOG000004830.
HOVERGENiHBG005633.
InParanoidiP80226.
OrthoDBiEOG7HB5C9.
PhylomeDBiP80226.
TreeFamiTF330348.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR031276. Lb-FABP.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF67. PTHR11955:SF67. 1 hit.
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80226-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFSGTWQVY AQENYEEFLK ALALPEDLIK MARDIKPIVE IQQKGDDFVV
60 70 80 90 100
TSKTPRQTVT NSFTLGKEAD ITTMDGKKLK CTVHLANGKL VTKSEKFSHE
110 120
QEVKGNEMVE TITFGGVTLI RRSKRV
Length:126
Mass (Da):14,210
Last modified:January 23, 2007 - v2
Checksum:i537022389AC431FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921T → C in AAK58094 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF380998 mRNA. Translation: AAK58094.1.
RefSeqiNP_989965.1. NM_204634.1.
UniGeneiGga.40.

Genome annotation databases

GeneIDi395345.
KEGGigga:395345.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF380998 mRNA. Translation: AAK58094.1.
RefSeqiNP_989965.1. NM_204634.1.
UniGeneiGga.40.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVGNMR-A2-126[»]
1TVQX-ray2.00A2-126[»]
1TW4X-ray2.00A/B2-126[»]
1ZRYNMR-A2-126[»]
2JN3NMR-A2-126[»]
2K62NMR-A2-126[»]
2LFONMR-A2-126[»]
ProteinModelPortaliP80226.
SMRiP80226. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000006574.

Proteomic databases

PaxDbiP80226.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395345.
KEGGigga:395345.

Organism-specific databases

CTDi395345.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
HOGENOMiHOG000004830.
HOVERGENiHBG005633.
InParanoidiP80226.
OrthoDBiEOG7HB5C9.
PhylomeDBiP80226.
TreeFamiTF330348.

Miscellaneous databases

EvolutionaryTraceiP80226.
NextBioi20815430.
PROiP80226.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR031276. Lb-FABP.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF67. PTHR11955:SF67. 1 hit.
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Regulation of gene expression of two liver type fatty acid binding proteins in chicken."
    Murai A., Kusumoto K., Okumura J.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: White leghorn.
    Tissue: Liver.
  2. "The primary structure of a basic (pI 9.0) fatty acid-binding protein from liver of Gallus domesticus."
    Ceciliani F., Monaco H.L., Ronchi S., Faotto L., Spadon P.
    Comp. Biochem. Physiol. 109B:261-271(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-126, ACETYLATION AT ALA-2.
    Tissue: Liver.
  3. "Crystal structure of chicken liver basic fatty acid-binding protein at 2.7 A resolution."
    Scapin G., Spadon P., Mammi M., Zanotti G., Monaco H.L.
    Mol. Cell. Biochem. 98:95-99(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  4. "Solution structure of chicken liver basic fatty acid binding protein."
    Vasile F., Ragona L., Catalano M., Zetta L., Perduca M., Monaco H.L., Molinari H.
    J. Biomol. NMR 25:157-160(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  5. "Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid."
    Nichesola D., Perduca M., Capaldi S., Carrizo M.E., Righetti P.G., Monaco H.L.
    Biochemistry 43:14072-14079(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CHOLATE.
  6. "NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid-binding protein."
    Ragona L., Catalano M., Luppi M., Cicero D., Eliseo T., Foote J., Fogolari F., Zetta L., Molinari H.
    J. Biol. Chem. 281:9697-9709(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiFABPL_CHICK
AccessioniPrimary (citable) accession number: P80226
Secondary accession number(s): Q90WB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.