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Protein

Fatty acid-binding protein 2, liver

Gene
N/A
Organism
Ambystoma mexicanum (Axolotl)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity). The specificity of axolotl L-FABP differs from that of LB-FABP. Binds 2 ligands per protein molecule.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211Cholate 11 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 2, liver
Alternative name(s):
Liver basic FABP
Short name:
LB-FABP
Liver-type fatty acid-binding protein
Short name:
L-FABP
OrganismiAmbystoma mexicanum (Axolotl)
Taxonomic identifieri8296 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaCaudataSalamandroideaAmbystomatidaeAmbystoma

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 2, liverPRO_0000067344Add
BLAST

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Helixi15 – 228Combined sources
Helixi26 – 327Combined sources
Beta strandi38 – 5316Combined sources
Beta strandi58 – 647Combined sources
Beta strandi69 – 724Combined sources
Helixi74 – 763Combined sources
Beta strandi78 – 814Combined sources
Beta strandi84 – 863Combined sources
Beta strandi89 – 935Combined sources
Beta strandi95 – 10410Combined 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
2FT9X-ray2.50A2-126[»]
2FTBX-ray2.00A2-126[»]
ProteinModelPortaliP81400.
SMRiP81400. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81400.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 563Cholate 1 binding
Regioni99 – 1013Cholate 2 binding

Domaini

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

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG005633.

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.

P81400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFNGTWQVY SQENYEAFLR AVGLPEDIIN VAKDINPIIE IQQNGDNFVV
60 70 80 90 100
TSKTPNQSVT NSFTIGKEAE ITSMGGKKIK CTVVLEGGKL VSKTDQFSHI
110 120
QEVKGNEMVE TLTVGGATLI RRSKRV
Length:126
Mass (Da):13,875
Last modified:January 23, 2007 - v2
Checksum:i130A84C12D0EB1AF
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FT9X-ray2.50A2-126[»]
2FTBX-ray2.00A2-126[»]
ProteinModelPortaliP81400.
SMRiP81400. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005633.

Miscellaneous databases

EvolutionaryTraceiP81400.

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. "Isolation, amino acid sequence determination and binding properties of two fatty-acid-binding proteins from axolotl (Ambistoma mexicanum) liver. Evolutionary relationship."
    Di Pietro S.M., Veerkamp J.H., Santome J.A.
    Eur. J. Biochem. 259:127-134(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-126.
    Tissue: Liver.
  2. "Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic and oleic acid."
    Capaldi S., Guariento M., Perduca M., Di Pietro S.M., Santome J.A., Monaco H.L.
    Proteins 64:79-88(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CHOLATE AND OLEATE.

Entry informationi

Entry nameiFABP2_AMBME
AccessioniPrimary (citable) accession number: P81400
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 77 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, Direct protein sequencing

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.