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Protein

Fatty acid-binding protein, adipocyte

Gene

FABP4

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). Involved in the regulation of intramuscular fat accretion.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, adipocyte
Alternative name(s):
AP2
Adipocyte lipid-binding protein
Short name:
ALBP
Adipocyte-type fatty acid-binding protein
Short name:
A-FABP
Short name:
AFABP
Fatty acid-binding protein 4
Gene namesi
Name:FABP4
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000673682 – 132Fatty acid-binding protein, adipocyteAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylcysteineBy similarity1
Modified residuei13PhosphoserineBy similarity1
Modified residuei20Phosphotyrosine; by Tyr-kinasesBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PeptideAtlasiO97788.
PRIDEiO97788.

Expressioni

Tissue specificityi

Adipose tissue.1 Publication

Interactioni

Subunit structurei

Monomer and homodimer. Interacts with PPARG (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO97788.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni127 – 129Fatty acid bindingBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi22 – 32Nuclear localization signalBy similarityAdd BLAST11

Domaini

Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.By similarity

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG005633.
InParanoidiO97788.
KOiK08753.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR033073. FABP4.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF83. PTHR11955:SF83. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
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.

O97788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN LIITVNGDMI
60 70 80 90 100
TIRSESTFKN TEIAFKLGQE FDEVTADDRK VKSTITLDGG ALVQVQKWDG
110 120 130
KTTTINRKIV DDKLVVECIM KGVTATRIYE RA
Length:132
Mass (Da):14,676
Last modified:January 23, 2007 - v3
Checksum:i653389F3C1ABBAB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16039 Genomic DNA. Translation: CAA75995.1.
AJ416020 mRNA. Translation: CAC95166.1.
EF061460 Genomic DNA. Translation: ABK58143.1.
EF061461 Genomic DNA. Translation: ABK58144.1.
EF061462 Genomic DNA. Translation: ABK58145.1.
EF061463 Genomic DNA. Translation: ABK58146.1.
EF061464 Genomic DNA. Translation: ABK58147.1.
EF061466 Genomic DNA. Translation: ABK58149.1.
EF061467 Genomic DNA. Translation: ABK58150.1.
EF061468 Genomic DNA. Translation: ABK58151.1.
EF061469 Genomic DNA. Translation: ABK58152.1.
EF061470 Genomic DNA. Translation: ABK58153.1.
EF061471 Genomic DNA. Translation: ABK58154.1.
EF061473 Genomic DNA. Translation: ABK58156.1.
EF061474 Genomic DNA. Translation: ABK58157.1.
EF061475 Genomic DNA. Translation: ABK58158.1.
EF061476 Genomic DNA. Translation: ABK58159.1.
EF061477 Genomic DNA. Translation: ABK58160.1.
EF061478 Genomic DNA. Translation: ABK58161.1.
EF061479 Genomic DNA. Translation: ABK58162.1.
EF061480 Genomic DNA. Translation: ABK58163.1.
EF061481 Genomic DNA. Translation: ABK58164.1.
EF061482 Genomic DNA. Translation: ABK58165.1.
RefSeqiNP_001002817.1. NM_001002817.1.
UniGeneiSsc.1089.

Genome annotation databases

GeneIDi399533.
KEGGissc:399533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16039 Genomic DNA. Translation: CAA75995.1.
AJ416020 mRNA. Translation: CAC95166.1.
EF061460 Genomic DNA. Translation: ABK58143.1.
EF061461 Genomic DNA. Translation: ABK58144.1.
EF061462 Genomic DNA. Translation: ABK58145.1.
EF061463 Genomic DNA. Translation: ABK58146.1.
EF061464 Genomic DNA. Translation: ABK58147.1.
EF061466 Genomic DNA. Translation: ABK58149.1.
EF061467 Genomic DNA. Translation: ABK58150.1.
EF061468 Genomic DNA. Translation: ABK58151.1.
EF061469 Genomic DNA. Translation: ABK58152.1.
EF061470 Genomic DNA. Translation: ABK58153.1.
EF061471 Genomic DNA. Translation: ABK58154.1.
EF061473 Genomic DNA. Translation: ABK58156.1.
EF061474 Genomic DNA. Translation: ABK58157.1.
EF061475 Genomic DNA. Translation: ABK58158.1.
EF061476 Genomic DNA. Translation: ABK58159.1.
EF061477 Genomic DNA. Translation: ABK58160.1.
EF061478 Genomic DNA. Translation: ABK58161.1.
EF061479 Genomic DNA. Translation: ABK58162.1.
EF061480 Genomic DNA. Translation: ABK58163.1.
EF061481 Genomic DNA. Translation: ABK58164.1.
EF061482 Genomic DNA. Translation: ABK58165.1.
RefSeqiNP_001002817.1. NM_001002817.1.
UniGeneiSsc.1089.

3D structure databases

ProteinModelPortaliO97788.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PeptideAtlasiO97788.
PRIDEiO97788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi399533.
KEGGissc:399533.

Organism-specific databases

CTDi2167.

Phylogenomic databases

HOVERGENiHBG005633.
InParanoidiO97788.
KOiK08753.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR033073. FABP4.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF83. PTHR11955:SF83. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABP4_PIG
AccessioniPrimary (citable) accession number: O97788
Secondary accession number(s): A0SXU3
, A0SXU5, A0SXV1, A0SXV2, A0SXW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.