EXFAB_CHICK
ID EXFAB_CHICK Reviewed; 178 AA.
AC P21760; P21928; Q6E6M8; Q9PWN9;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Extracellular fatty acid-binding protein;
DE Short=Ex-FABP;
DE AltName: Full=Protein Ch21;
DE AltName: Full=Quiescence-specific protein;
DE AltName: Full=p20K;
DE Flags: Precursor;
GN Name=EXFABP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2498647; DOI=10.1128/mcb.9.3.1371-1375.1989;
RA Bedard P.-A., Yannoni Y., Simmons D.L., Erikson R.L.;
RT "Rapid repression of quiescence-specific gene expression by epidermal
RT growth factor, insulin, and pp60v-src.";
RL Mol. Cell. Biol. 9:1371-1375(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1737754; DOI=10.1016/s0021-9258(19)50683-4;
RA Dozin B., Descalzi F., Briata L., Hayashi M., Gentili C., Hayashi K.,
RA Quarto R., Cancedda R.;
RT "Expression, regulation, and tissue distribution of the Ch21 protein during
RT chicken embryogenesis.";
RL J. Biol. Chem. 267:2979-2985(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Leghorn;
RX PubMed=14584054; DOI=10.1002/jcp.10405;
RA Giannoni P., Zambotti A., Pagano A., Cancedda R., Dozin B.;
RT "Differentiation-dependent activation of the extracellular fatty acid
RT binding protein (Ex-FABP) gene during chondrogenesis.";
RL J. Cell. Physiol. 198:144-154(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Qiu X., Li N.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-178, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2229062; DOI=10.1016/s0021-9258(17)30624-5;
RA Cancedda F.D., Dozin B., Rossi F., Molina F., Cancedda R., Negri A.,
RA Ronchi S.;
RT "The Ch21 protein, developmentally regulated in chick embryo, belongs to
RT the superfamily of lipophilic molecule carrier proteins.";
RL J. Biol. Chem. 265:19060-19064(1990).
RN [6]
RP PROTEIN SEQUENCE OF 21-48.
RX PubMed=2346493; DOI=10.1016/0006-291x(90)91118-c;
RA Cancedda F.D., Asaro D., Molina F., Cancedda R., Caruso C., Camardella L.,
RA Negri A., Ronchi S.;
RT "The amino terminal sequence of the developmentally regulated Ch21 protein
RT shows homology with amino terminal sequences of low molecular weight
RT proteins binding hydrophobic molecules.";
RL Biochem. Biophys. Res. Commun. 168:933-938(1990).
RN [7]
RP PROTEIN SEQUENCE OF 27-49; 33-51; 59-79; 114-124; 128-135; 138-152; 140-152
RP AND 155-178, TISSUE SPECIFICITY, INDUCTION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Egg white {ECO:0000303|PubMed:25436390};
RX PubMed=25436390; DOI=10.1021/jf504469t;
RA Kim J., Choi Y.H.;
RT "Differential abundance of egg white proteins in laying hens treated with
RT corticosterone.";
RL J. Agric. Food Chem. 62:12346-12359(2014).
RN [8]
RP NUCLEOTIDE SEQUENCE OF 103-178.
RC STRAIN=White leghorn; TISSUE=Bone marrow;
RX PubMed=1549365;
RA Nakano T., Graf T.;
RT "Identification of genes differentially expressed in two types of v-myb-
RT transformed avian myelomonocytic cells.";
RL Oncogene 7:527-534(1992).
RN [9]
RP CHARACTERIZATION.
RX PubMed=8702740; DOI=10.1074/jbc.271.33.20163;
RA Cancedda F.D., Malpeli M., Gentili C., Di Marzo V., Bet P., Carlevaro M.,
RA Cermelli S., Cancedda R.;
RT "The developmentally regulated avian Ch21 lipocalin is an extracellular
RT fatty acid-binding protein.";
RL J. Biol. Chem. 271:20163-20169(1996).
RN [10]
RP CHARACTERIZATION.
RX PubMed=11058755; DOI=10.1016/s0167-4838(00)00159-x;
RA Descalzi Cancedda F., Dozin B., Zerega B., Cermelli S., Cancedda R.;
RT "Ex-FABP: a fatty acid binding lipocalin developmentally regulated in
RT chicken endochondral bone formation and myogenesis.";
RL Biochim. Biophys. Acta 1482:127-135(2000).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-178 IN COMPLEX WITH MYRISTOYL
RP LYSOPHOSPHATIDIC ACID AND 2,3-DIHYDROXYBENZOATE, SUBUNIT,
RP SIDEROPHORE-BINDING SITES, AND DISULFIDE BOND.
RX PubMed=22153502; DOI=10.1016/j.str.2011.09.019;
RA Correnti C., Clifton M.C., Abergel R.J., Allred B., Hoette T.M., Ruiz M.,
RA Cancedda R., Raymond K.N., Descalzi F., Strong R.K.;
RT "Galline Ex-FABP is an antibacterial siderocalin and a lysophosphatidic
RT acid sensor functioning through dual ligand specificities.";
RL Structure 19:1796-1806(2011).
CC -!- FUNCTION: Siderocalin-like lipocalin tightly binding a variety of
CC bacterial ferric siderophores, also binds long-chain unsaturated fatty
CC acids such as linoleic acid, oleic acid, arachidonic acid and, with a
CC lower affinity, long chain saturated fatty acids such as steraic acid.
CC May act as an antibacterial factor, through dual ligand specificity,
CC both as a siderophore-sequestrating molecule and a lysophosphatidic
CC acid (LPA) sensor.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22153502}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in egg white (at protein level).
CC Expressed in the magnum of the oviduct (at protein level)
CC (PubMed:25436390). Preferentially synthesized in nonproliferating
CC cells. {ECO:0000269|PubMed:25436390}.
CC -!- INDUCTION: Down-regulated by dietary stress. Significantly decreased
CC expression between days 0 to 5 in egg whites of eggs laid by
CC corticosterone-fed hens (at protein level). Decreased expression at day
CC 14 in the magnum of the oviduct in the corticosterone-fed laying hens.
CC {ECO:0000269|PubMed:25436390}.
CC -!- PTM: Does not seem to be glycosylated.
CC -!- MISCELLANEOUS: Developmentally regulated in chick embryo.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; M25784; AAA53371.1; -; mRNA.
DR EMBL; M55644; AAA48677.1; -; mRNA.
DR EMBL; AF121346; AAD23569.1; -; Genomic_DNA.
DR EMBL; AY545055; AAT73770.1; -; Genomic_DNA.
DR EMBL; X61199; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A30230; A30230.
DR RefSeq; NP_990753.1; NM_205422.1.
DR PDB; 3SAO; X-ray; 1.80 A; A/B=23-178.
DR PDBsum; 3SAO; -.
DR AlphaFoldDB; P21760; -.
DR SMR; P21760; -.
DR STRING; 9031.ENSGALP00000039691; -.
DR GeneID; 396393; -.
DR KEGG; gga:396393; -.
DR CTD; 396393; -.
DR VEuPathDB; HostDB:geneid_396393; -.
DR eggNOG; ENOG502S13A; Eukaryota.
DR InParanoid; P21760; -.
DR OrthoDB; 1107052at2759; -.
DR PhylomeDB; P21760; -.
DR PRO; PR:P21760; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0050544; F:arachidonic acid binding; IDA:AgBase.
DR GO; GO:0005504; F:fatty acid binding; IDA:AgBase.
DR GO; GO:0070539; F:linoleic acid binding; IDA:AgBase.
DR GO; GO:0070538; F:oleic acid binding; IDA:AgBase.
DR GO; GO:0070540; F:stearic acid binding; IDA:AgBase.
DR GO; GO:0006953; P:acute-phase response; IEP:AgBase.
DR GO; GO:0006915; P:apoptotic process; IDA:AgBase.
DR GO; GO:0030154; P:cell differentiation; IMP:AgBase.
DR GO; GO:0008283; P:cell population proliferation; IMP:WormBase.
DR GO; GO:0044255; P:cellular lipid metabolic process; NAS:AgBase.
DR GO; GO:0071399; P:cellular response to linoleic acid; IDA:AgBase.
DR GO; GO:0002062; P:chondrocyte differentiation; IEP:AgBase.
DR GO; GO:0003415; P:chondrocyte hypertrophy; IEP:AgBase.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; TAS:AgBase.
DR GO; GO:0055089; P:fatty acid homeostasis; IMP:AgBase.
DR GO; GO:0015908; P:fatty acid transport; IMP:AgBase.
DR GO; GO:0007507; P:heart development; IEP:AgBase.
DR GO; GO:0006954; P:inflammatory response; IDA:AgBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0015909; P:long-chain fatty acid transport; TAS:AgBase.
DR GO; GO:0055001; P:muscle cell development; TAS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:AgBase.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:AgBase.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:AgBase.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:AgBase.
DR GO; GO:0051412; P:response to corticosterone; IDA:AgBase.
DR GO; GO:0034097; P:response to cytokine; IEP:AgBase.
DR GO; GO:0070543; P:response to linoleic acid; IDA:AgBase.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:AgBase.
DR GO; GO:0009636; P:response to toxic substance; TAS:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:AgBase.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Immunity; Innate immunity; Iron; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:2346493"
FT CHAIN 21..178
FT /note="Extracellular fatty acid-binding protein"
FT /id="PRO_0000017958"
FT BINDING 43
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000305|PubMed:22153502,
FT ECO:0007744|PDB:3SAO"
FT BINDING 72
FT /ligand="1-tetradecanoyl-sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:72683"
FT /evidence="ECO:0000269|PubMed:22153502,
FT ECO:0007744|PDB:3SAO"
FT BINDING 104
FT /ligand="1-tetradecanoyl-sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:72683"
FT /evidence="ECO:0000269|PubMed:22153502,
FT ECO:0007744|PDB:3SAO"
FT BINDING 104
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000305|PubMed:22153502,
FT ECO:0007744|PDB:3SAO"
FT BINDING 123
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000305|PubMed:22153502,
FT ECO:0007744|PDB:3SAO"
FT BINDING 134..136
FT /ligand="1-tetradecanoyl-sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:72683"
FT /evidence="ECO:0000269|PubMed:22153502,
FT ECO:0007744|PDB:3SAO"
FT BINDING 134
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000305|PubMed:22153502,
FT ECO:0007744|PDB:3SAO"
FT MOD_RES 21
FT /note="Blocked amino end (Ala)"
FT DISULFID 80..173
FT /evidence="ECO:0000269|PubMed:22153502"
FT CONFLICT 4
FT /note="L -> S (in Ref. 2; AAA48677)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="R -> S (in Ref. 2 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="F -> S (in Ref. 2 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="F -> S (in Ref. 1; AAA53371)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="L -> V (in Ref. 1; AAA53371)"
FT /evidence="ECO:0000305"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:3SAO"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3SAO"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3SAO"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3SAO"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:3SAO"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3SAO"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:3SAO"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:3SAO"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:3SAO"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:3SAO"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3SAO"
FT STRAND 113..125
FT /evidence="ECO:0007829|PDB:3SAO"
FT STRAND 128..141
FT /evidence="ECO:0007829|PDB:3SAO"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:3SAO"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3SAO"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3SAO"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3SAO"
SQ 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
