EXFAB_COTJA
ID EXFAB_COTJA Reviewed; 178 AA.
AC Q9I9P7; Q98SI8;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Extracellular fatty acid-binding protein;
DE Short=Ex-FABP;
DE AltName: Full=Lipocalin Q83;
DE Flags: Precursor;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Siemeister G., Hartl M., Bister K.;
RT "High-level expression in v-myc-transformed avian fibroblasts of a gene
RT encoding a member of the lipocalin protein family.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STRUCTURE BY NMR OF 23-178, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=14516741; DOI=10.1016/j.jmb.2003.08.018;
RA Hartl M., Matt T., Schuler W., Siemeister G., Kontaxis G., Kloiber K.,
RA Konrat R., Bister K.;
RT "Cell transformation by the v-myc oncogene abrogates c-Myc/Max-mediated
RT suppression of a C/EBP beta-dependent lipocalin gene.";
RL J. Mol. Biol. 333:33-46(2003).
RN [3]
RP STRUCTURE BY NMR OF 23-178 IN COMPLEX WITH ENTEROBACTIN, FUNCTION, SUBUNIT,
RP AND DISULFIDE BOND.
RX PubMed=20826777; DOI=10.1074/jbc.m110.123331;
RA Coudevylle N., Geist L., Hotzinger M., Hartl M., Kontaxis G., Bister K.,
RA Konrat R.;
RT "The v-myc-induced Q83 lipocalin is a siderocalin.";
RL J. Biol. Chem. 285:41646-41652(2010).
RN [4]
RP STRUCTURE BY NMR OF 23-178, FUNCTION, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=21951132; DOI=10.1021/bi201115q;
RA Coudevylle N., Hoetzinger M., Geist L., Kontaxis G., Hartl M., Bister K.,
RA Konrat R.;
RT "Lipocalin Q83 reveals a dual ligand binding mode with potential
RT implications for the functions of siderocalins.";
RL Biochemistry 50:9192-9199(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. {ECO:0000269|PubMed:20826777,
CC ECO:0000269|PubMed:21951132}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14516741,
CC ECO:0000269|PubMed:20826777, ECO:0000269|PubMed:21951132}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; AF229030; AAF35894.1; -; mRNA.
DR EMBL; AY029238; AAK31634.1; -; Genomic_DNA.
DR PDB; 1JZU; NMR; -; A=22-178.
DR PDB; 2KT4; NMR; -; B=23-178.
DR PDB; 2LBV; NMR; -; A=23-178.
DR PDBsum; 1JZU; -.
DR PDBsum; 2KT4; -.
DR PDBsum; 2LBV; -.
DR AlphaFoldDB; Q9I9P7; -.
DR BMRB; Q9I9P7; -.
DR SMR; Q9I9P7; -.
DR EvolutionaryTrace; Q9I9P7; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050544; F:arachidonic acid binding; IDA:AgBase.
DR GO; GO:1903981; F:enterobactin binding; IDA:AgBase.
DR GO; GO:0070538; F:oleic acid binding; IDA:AgBase.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; Disulfide bond; Immunity;
KW Innate immunity; Iron; Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..178
FT /note="Extracellular fatty acid-binding protein"
FT /id="PRO_0000017959"
FT BINDING 43
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000250|UniProtKB:P21760"
FT BINDING 72
FT /ligand="1-tetradecanoyl-sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:72683"
FT /evidence="ECO:0000250|UniProtKB:P21760"
FT BINDING 104
FT /ligand="1-tetradecanoyl-sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:72683"
FT /evidence="ECO:0000250|UniProtKB:P21760"
FT BINDING 104
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000250|UniProtKB:P21760"
FT BINDING 123
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000250|UniProtKB:P21760"
FT BINDING 134..136
FT /ligand="1-tetradecanoyl-sn-glycerol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:72683"
FT /evidence="ECO:0000250|UniProtKB:P21760"
FT BINDING 134
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000250|UniProtKB:P21760"
FT DISULFID 80..173
FT /evidence="ECO:0000269|PubMed:14516741,
FT ECO:0000269|PubMed:20826777, ECO:0000269|PubMed:21951132"
FT CONFLICT 3
FT /note="T -> M (in Ref. 1; AAK31634)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="K -> E (in Ref. 1; AAK31634)"
FT /evidence="ECO:0000305"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1JZU"
FT STRAND 31..42
FT /evidence="ECO:0007829|PDB:1JZU"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1JZU"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1JZU"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:1JZU"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1JZU"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:1JZU"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:1JZU"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:1JZU"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1JZU"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1JZU"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:1JZU"
FT STRAND 114..125
FT /evidence="ECO:0007829|PDB:1JZU"
FT STRAND 128..141
FT /evidence="ECO:0007829|PDB:1JZU"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:1JZU"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1JZU"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2KT4"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1JZU"
SQ SEQUENCE 178 AA; 20179 MW; 5F6E7643FB68E99F CRC64;
MRTLALSLGL ALLCLLHAKA AATVPDRSEI AGKWYVVALA SNTEFFLREK DKMKMAMARI
SFLGEDELKV SYAVPKPNGC RKWETTFKKT SDDGEVYYSE EAKKKVEVLD TDYKSYAVIY
ATRVKDGRTL HMMRLYSRSP EVSPAATAIF RKLAGERNYT DEMVAMLPRQ EECTVDEV
