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Extracellular fatty acid-binding protein (Ex-FABP) (Protein Ch21) (Quiescence-specific protein) (p20K)

 EXFAB_CHICK             Reviewed;         178 AA.
P21760; P21928; Q6E6M8; Q9PWN9;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
31-JAN-2018, entry version 110.
RecName: Full=Extracellular fatty acid-binding protein;
Short=Ex-FABP;
AltName: Full=Protein Ch21;
AltName: Full=Quiescence-specific protein;
AltName: Full=p20K;
Flags: Precursor;
Name=EXFABP;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2498647; DOI=10.1128/MCB.9.3.1371;
Bedard P.-A., Yannoni Y., Simmons D.L., Erikson R.L.;
"Rapid repression of quiescence-specific gene expression by epidermal
growth factor, insulin, and pp60v-src.";
Mol. Cell. Biol. 9:1371-1375(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1737754;
Dozin B., Descalzi F., Briata L., Hayashi M., Gentili C., Hayashi K.,
Quarto R., Cancedda R.;
"Expression, regulation, and tissue distribution of the Ch21 protein
during chicken embryogenesis.";
J. Biol. Chem. 267:2979-2985(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Leghorn;
PubMed=14584054; DOI=10.1002/jcp.10405;
Giannoni P., Zambotti A., Pagano A., Cancedda R., Dozin B.;
"Differentiation-dependent activation of the extracellular fatty acid
binding protein (Ex-FABP) gene during chondrogenesis.";
J. Cell. Physiol. 198:144-154(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Qiu X., Li N.;
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-178, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2229062;
Cancedda F.D., Dozin B., Rossi F., Molina F., Cancedda R., Negri A.,
Ronchi S.;
"The Ch21 protein, developmentally regulated in chick embryo, belongs
to the superfamily of lipophilic molecule carrier proteins.";
J. Biol. Chem. 265:19060-19064(1990).
[6]
PROTEIN SEQUENCE OF 21-48.
PubMed=2346493; DOI=10.1016/0006-291X(90)91118-C;
Cancedda F.D., Asaro D., Molina F., Cancedda R., Caruso C.,
Camardella L., Negri A., Ronchi S.;
"The amino terminal sequence of the developmentally regulated Ch21
protein shows homology with amino terminal sequences of low molecular
weight proteins binding hydrophobic molecules.";
Biochem. Biophys. Res. Commun. 168:933-938(1990).
[7]
NUCLEOTIDE SEQUENCE OF 103-178.
STRAIN=White leghorn; TISSUE=Bone marrow;
PubMed=1549365;
Nakano T., Graf T.;
"Identification of genes differentially expressed in two types of v-
myb-transformed avian myelomonocytic cells.";
Oncogene 7:527-534(1992).
[8]
CHARACTERIZATION.
PubMed=8702740; DOI=10.1074/jbc.271.33.20163;
Cancedda F.D., Malpeli M., Gentili C., Di Marzo V., Bet P.,
Carlevaro M., Cermelli S., Cancedda R.;
"The developmentally regulated avian Ch21 lipocalin is an
extracellular fatty acid-binding protein.";
J. Biol. Chem. 271:20163-20169(1996).
[9]
CHARACTERIZATION.
PubMed=11058755; DOI=10.1016/S0167-4838(00)00159-X;
Descalzi Cancedda F., Dozin B., Zerega B., Cermelli S., Cancedda R.;
"Ex-FABP: a fatty acid binding lipocalin developmentally regulated in
chicken endochondral bone formation and myogenesis.";
Biochim. Biophys. Acta 1482:127-135(2000).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-178 IN COMPLEX WITH LPA,
SUBUNIT, SIDEROPHORE-BINDING SITES, AND DISULFIDE BOND.
PubMed=22153502; DOI=10.1016/j.str.2011.09.019;
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.;
"Galline Ex-FABP is an antibacterial siderocalin and a
lysophosphatidic acid sensor functioning through dual ligand
specificities.";
Structure 19:1796-1806(2011).
-!- FUNCTION: 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.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22153502}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Preferentially synthesized in nonproliferating
cells.
-!- PTM: Does not seem to be glycosylated.
-!- MISCELLANEOUS: Developmentally regulated in chick embryo.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M25784; AAA53371.1; -; mRNA.
EMBL; M55644; AAA48677.1; -; mRNA.
EMBL; AF121346; AAD23569.1; -; Genomic_DNA.
EMBL; AY545055; AAT73770.1; -; Genomic_DNA.
EMBL; X61199; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A30230; A30230.
RefSeq; NP_990753.1; NM_205422.1.
UniGene; Gga.739; -.
PDB; 3SAO; X-ray; 1.80 A; A/B=23-178.
PDBsum; 3SAO; -.
ProteinModelPortal; P21760; -.
SMR; P21760; -.
GeneID; 396393; -.
KEGG; gga:396393; -.
CTD; 396393; -.
HOVERGEN; HBG096019; -.
InParanoid; P21760; -.
PhylomeDB; P21760; -.
PRO; PR:P21760; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0050544; F:arachidonic acid binding; IDA:AgBase.
GO; GO:0005504; F:fatty acid binding; IDA:AgBase.
GO; GO:0070539; F:linoleic acid binding; IDA:AgBase.
GO; GO:0070538; F:oleic acid binding; IDA:AgBase.
GO; GO:0070540; F:stearic acid binding; IDA:AgBase.
GO; GO:0006953; P:acute-phase response; IEP:AgBase.
GO; GO:0006915; P:apoptotic process; IDA:AgBase.
GO; GO:0030154; P:cell differentiation; IMP:AgBase.
GO; GO:0008283; P:cell proliferation; IMP:AgBase.
GO; GO:0044255; P:cellular lipid metabolic process; NAS:AgBase.
GO; GO:0071399; P:cellular response to linoleic acid; IDA:AgBase.
GO; GO:0002062; P:chondrocyte differentiation; IEP:AgBase.
GO; GO:0003415; P:chondrocyte hypertrophy; IEP:AgBase.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; TAS:AgBase.
GO; GO:0055089; P:fatty acid homeostasis; IMP:AgBase.
GO; GO:0015908; P:fatty acid transport; IMP:AgBase.
GO; GO:0007507; P:heart development; IEP:AgBase.
GO; GO:0006954; P:inflammatory response; IDA:AgBase.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0015909; P:long-chain fatty acid transport; TAS:AgBase.
GO; GO:0048747; P:muscle fiber development; TAS:AgBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:AgBase.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:AgBase.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:AgBase.
GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:AgBase.
GO; GO:0051412; P:response to corticosterone; IDA:AgBase.
GO; GO:0034097; P:response to cytokine; IEP:AgBase.
GO; GO:0042493; P:response to drug; IMP:AgBase.
GO; GO:0070543; P:response to linoleic acid; IDA:AgBase.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:AgBase.
GO; GO:0009636; P:response to toxic substance; TAS:AgBase.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR002345; Lipocalin.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11430; PTHR11430; 1.
Pfam; PF00061; Lipocalin; 1.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Antibiotic; Antimicrobial; Complete proteome;
Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
Iron; Reference proteome; Secreted; Signal; Transport.
SIGNAL 1 20 {ECO:0000269|PubMed:2346493}.
CHAIN 21 178 Extracellular fatty acid-binding protein.
/FTId=PRO_0000017958.
BINDING 104 104 Catecholate-type ferric siderophore.
BINDING 123 123 Catecholate-type ferric siderophore.
BINDING 134 134 Catecholate-type ferric siderophore.
MOD_RES 21 21 Blocked amino end (Ala).
DISULFID 80 173 {ECO:0000269|PubMed:22153502}.
CONFLICT 4 4 L -> S (in Ref. 2; AAA48677).
{ECO:0000305}.
CONFLICT 27 27 R -> S (in Ref. 2 and 5). {ECO:0000305}.
CONFLICT 45 45 F -> S (in Ref. 2 and 5). {ECO:0000305}.
CONFLICT 62 62 F -> S (in Ref. 1; AAA53371).
{ECO:0000305}.
CONFLICT 96 96 L -> V (in Ref. 1; AAA53371).
{ECO:0000305}.
STRAND 32 40 {ECO:0000244|PDB:3SAO}.
HELIX 44 49 {ECO:0000244|PDB:3SAO}.
HELIX 50 52 {ECO:0000244|PDB:3SAO}.
STRAND 56 63 {ECO:0000244|PDB:3SAO}.
TURN 64 66 {ECO:0000244|PDB:3SAO}.
STRAND 67 74 {ECO:0000244|PDB:3SAO}.
STRAND 81 88 {ECO:0000244|PDB:3SAO}.
STRAND 91 94 {ECO:0000244|PDB:3SAO}.
STRAND 96 99 {ECO:0000244|PDB:3SAO}.
TURN 100 103 {ECO:0000244|PDB:3SAO}.
STRAND 104 111 {ECO:0000244|PDB:3SAO}.
STRAND 113 125 {ECO:0000244|PDB:3SAO}.
STRAND 128 141 {ECO:0000244|PDB:3SAO}.
HELIX 144 155 {ECO:0000244|PDB:3SAO}.
TURN 156 158 {ECO:0000244|PDB:3SAO}.
HELIX 161 163 {ECO:0000244|PDB:3SAO}.
STRAND 164 166 {ECO:0000244|PDB:3SAO}.
SEQUENCE 178 AA; 20201 MW; 0DDBDC33C1A0C6B8 CRC64;
MRTLALSLAL ALLCLLHTEA AATVPDRSEV AGKWYIVALA SNTDFFLREK GKMKMVMARI
SFLGEDELEV SYAAPSPKGC RKWETTFKKT SDDGELYYSE EAEKTVEVLD TDYKSYAVIF
ATRVKDGRTL HMMRLYSRSR EVSPTAMAIF RKLARERNYT DEMVAVLPSQ EECSVDEV


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