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Protein

Extracellular fatty acid-binding protein

Gene

EXFABP

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

Functioni

Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei104Catecholate-type ferric siderophore1
Binding sitei123Catecholate-type ferric siderophore1
Binding sitei134Catecholate-type ferric siderophore1

GO - Molecular functioni

  • arachidonic acid binding Source: AgBase
  • fatty acid binding Source: AgBase
  • fatty acid transporter activity Source: AgBase
  • linoleic acid binding Source: AgBase
  • oleic acid binding Source: AgBase
  • stearic acid binding Source: AgBase

GO - Biological processi

  • acute-phase response Source: AgBase
  • apoptotic process Source: AgBase
  • cell differentiation Source: AgBase
  • cell proliferation Source: AgBase
  • cellular lipid metabolic process Source: AgBase
  • cellular response to linoleic acid Source: AgBase
  • chondrocyte differentiation Source: AgBase
  • defense response to bacterium Source: UniProtKB-KW
  • embryo development ending in birth or egg hatching Source: AgBase
  • fatty acid homeostasis Source: AgBase
  • fatty acid transport Source: AgBase
  • heart development Source: AgBase
  • inflammatory response Source: AgBase
  • innate immune response Source: UniProtKB-KW
  • long-chain fatty acid transport Source: AgBase
  • muscle fiber development Source: AgBase
  • negative regulation of apoptotic process Source: AgBase
  • positive regulation of cell proliferation Source: AgBase
  • positive regulation of chondrocyte differentiation Source: AgBase
  • positive regulation of myoblast differentiation Source: AgBase
  • positive regulation of myotube differentiation Source: AgBase
  • response to corticosterone Source: AgBase
  • response to cytokine Source: AgBase
  • response to drug Source: AgBase
  • response to linoleic acid Source: AgBase
  • response to lipopolysaccharide Source: AgBase
  • response to toxic substance Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Biological processi

Immunity, Innate immunity, Transport

Keywords - Ligandi

Iron

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular fatty acid-binding protein
Short name:
Ex-FABP
Alternative name(s):
Protein Ch21
Quiescence-specific protein
p20K
Gene namesi
Name:EXFABP
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • cell Source: AgBase
  • extracellular space Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000001795821 – 178Extracellular fatty acid-binding proteinAdd BLAST158

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21Blocked amino end (Ala)1
Disulfide bondi80 ↔ 1731 Publication

Post-translational modificationi

Does not seem to be glycosylated.

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Preferentially synthesized in nonproliferating cells.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 40Combined sources9
Helixi44 – 49Combined sources6
Helixi50 – 52Combined sources3
Beta strandi56 – 63Combined sources8
Turni64 – 66Combined sources3
Beta strandi67 – 74Combined sources8
Beta strandi81 – 88Combined sources8
Beta strandi91 – 94Combined sources4
Beta strandi96 – 99Combined sources4
Turni100 – 103Combined sources4
Beta strandi104 – 111Combined sources8
Beta strandi113 – 125Combined sources13
Beta strandi128 – 141Combined sources14
Helixi144 – 155Combined sources12
Turni156 – 158Combined sources3
Helixi161 – 163Combined sources3
Beta strandi164 – 166Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SAOX-ray1.80A/B23-178[»]
ProteinModelPortaliP21760.
SMRiP21760.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG096019.
InParanoidiP21760.
PhylomeDBiP21760.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21760-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTLALSLAL ALLCLLHTEA AATVPDRSEV AGKWYIVALA SNTDFFLREK
60 70 80 90 100
GKMKMVMARI SFLGEDELEV SYAAPSPKGC RKWETTFKKT SDDGELYYSE
110 120 130 140 150
EAEKTVEVLD TDYKSYAVIF ATRVKDGRTL HMMRLYSRSR EVSPTAMAIF
160 170
RKLARERNYT DEMVAVLPSQ EECSVDEV
Length:178
Mass (Da):20,201
Last modified:April 16, 2002 - v2
Checksum:i0DDBDC33C1A0C6B8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4L → S in AAA48677 (PubMed:1737754).Curated1
Sequence conflicti27R → S (PubMed:1737754).Curated1
Sequence conflicti27R → S (PubMed:2229062).Curated1
Sequence conflicti45F → S (PubMed:1737754).Curated1
Sequence conflicti45F → S (PubMed:2229062).Curated1
Sequence conflicti62F → S in AAA53371 (PubMed:2498647).Curated1
Sequence conflicti96L → V in AAA53371 (PubMed:2498647).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25784 mRNA. Translation: AAA53371.1.
M55644 mRNA. Translation: AAA48677.1.
AF121346 Genomic DNA. Translation: AAD23569.1.
AY545055 Genomic DNA. Translation: AAT73770.1.
X61199 mRNA. No translation available.
PIRiA30230.
RefSeqiNP_990753.1. NM_205422.1.
UniGeneiGga.739.

Genome annotation databases

GeneIDi396393.
KEGGigga:396393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25784 mRNA. Translation: AAA53371.1.
M55644 mRNA. Translation: AAA48677.1.
AF121346 Genomic DNA. Translation: AAD23569.1.
AY545055 Genomic DNA. Translation: AAT73770.1.
X61199 mRNA. No translation available.
PIRiA30230.
RefSeqiNP_990753.1. NM_205422.1.
UniGeneiGga.739.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SAOX-ray1.80A/B23-178[»]
ProteinModelPortaliP21760.
SMRiP21760.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396393.
KEGGigga:396393.

Organism-specific databases

CTDi389812.

Phylogenomic databases

HOVERGENiHBG096019.
InParanoidiP21760.
PhylomeDBiP21760.

Miscellaneous databases

PROiP21760.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEXFAB_CHICK
AccessioniPrimary (citable) accession number: P21760
Secondary accession number(s): P21928, Q6E6M8, Q9PWN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: April 16, 2002
Last modified: November 2, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Developmentally regulated in chick embryo.

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.