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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041Catecholate-type ferric siderophore
Binding sitei123 – 1231Catecholate-type ferric siderophore
Binding sitei134 – 1341Catecholate-type ferric siderophore

GO - Molecular functioni

  • arachidonic 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
  • cellular lipid metabolic process Source: AgBase
  • cellular response to linoleic acid 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
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 178158Extracellular fatty acid-binding proteinPRO_0000017958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Blocked amino end (Ala)
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

1
178
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 409Combined sources
Helixi44 – 496Combined sources
Helixi50 – 523Combined sources
Beta strandi56 – 638Combined sources
Turni64 – 663Combined sources
Beta strandi67 – 748Combined sources
Beta strandi81 – 888Combined sources
Beta strandi91 – 944Combined sources
Beta strandi96 – 994Combined sources
Turni100 – 1034Combined sources
Beta strandi104 – 1118Combined sources
Beta strandi113 – 12513Combined sources
Beta strandi128 – 14114Combined sources
Helixi144 – 15512Combined sources
Turni156 – 1583Combined sources
Helixi161 – 1633Combined sources
Beta strandi164 – 1663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SAOX-ray1.80A/B23-178[»]
ProteinModelPortaliP21760.
SMRiP21760. Positions 23-178.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41L → S in AAA48677 (PubMed:1737754).Curated
Sequence conflicti27 – 271R → S (PubMed:1737754).Curated
Sequence conflicti27 – 271R → S (PubMed:2229062).Curated
Sequence conflicti45 – 451F → S (PubMed:1737754).Curated
Sequence conflicti45 – 451F → S (PubMed:2229062).Curated
Sequence conflicti62 – 621F → S in AAA53371 (PubMed:2498647).Curated
Sequence conflicti96 – 961L → V in AAA53371 (PubMed:2498647).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3SAOX-ray1.80A/B23-178[»]
ProteinModelPortaliP21760.
SMRiP21760. Positions 23-178.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396393.
KEGGigga:396393.

Organism-specific databases

CTDi138307.

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...

Publicationsi

  1. "Rapid repression of quiescence-specific gene expression by epidermal growth factor, insulin, and pp60v-src."
    Bedard P.-A., Yannoni Y., Simmons D.L., Erikson R.L.
    Mol. Cell. Biol. 9:1371-1375(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Expression, regulation, and tissue distribution of the Ch21 protein during chicken embryogenesis."
    Dozin B., Descalzi F., Briata L., Hayashi M., Gentili C., Hayashi K., Quarto R., Cancedda R.
    J. Biol. Chem. 267:2979-2985(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Differentiation-dependent activation of the extracellular fatty acid binding protein (Ex-FABP) gene during chondrogenesis."
    Giannoni P., Zambotti A., Pagano A., Cancedda R., Dozin B.
    J. Cell. Physiol. 198:144-154(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Leghorn.
  4. Qiu X., Li N.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The Ch21 protein, developmentally regulated in chick embryo, belongs to the superfamily of lipophilic molecule carrier proteins."
    Cancedda F.D., Dozin B., Rossi F., Molina F., Cancedda R., Negri A., Ronchi S.
    J. Biol. Chem. 265:19060-19064(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-178, PARTIAL PROTEIN SEQUENCE.
  6. "The amino terminal sequence of the developmentally regulated Ch21 protein shows homology with amino terminal sequences of low molecular weight proteins binding hydrophobic molecules."
    Cancedda F.D., Asaro D., Molina F., Cancedda R., Caruso C., Camardella L., Negri A., Ronchi S.
    Biochem. Biophys. Res. Commun. 168:933-938(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-48.
  7. "Identification of genes differentially expressed in two types of v-myb-transformed avian myelomonocytic cells."
    Nakano T., Graf T.
    Oncogene 7:527-534(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 103-178.
    Strain: White leghorn.
    Tissue: Bone marrow.
  8. "The developmentally regulated avian Ch21 lipocalin is an extracellular fatty acid-binding protein."
    Cancedda F.D., Malpeli M., Gentili C., Di Marzo V., Bet P., Carlevaro M., Cermelli S., Cancedda R.
    J. Biol. Chem. 271:20163-20169(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Ex-FABP: a fatty acid binding lipocalin developmentally regulated in chicken endochondral bone formation and myogenesis."
    Descalzi Cancedda F., Dozin B., Zerega B., Cermelli S., Cancedda R.
    Biochim. Biophys. Acta 1482:127-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  10. "Galline Ex-FABP is an antibacterial siderocalin and a lysophosphatidic acid sensor functioning through dual ligand specificities."
    Correnti C., Clifton M.C., Abergel R.J., Allred B., Hoette T.M., Ruiz M., Cancedda R., Raymond K.N., Descalzi F., Strong R.K.
    Structure 19:1796-1806(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-178 IN COMPLEX WITH LPA, SUBUNIT, SIDEROPHORE-BINDING SITES, DISULFIDE BOND.

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: June 8, 2016
This is version 105 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.