UNAG_ANGJA
ID UNAG_ANGJA Reviewed; 139 AA.
AC P0DM59;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Bilirubin-inducible fluorescent protein UnaG;
DE AltName: Full=Unagi green fluorescent protein;
DE Short=UnaG;
OS Anguilla japonica (Japanese eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7937;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF WILD
RP TYPE AND MUTANTS ALA-57 AND GLN-57 IN COMPLEXES WITH BILIRUBIN, FUNCTION,
RP DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF ASN-57.
RX PubMed=23768684; DOI=10.1016/j.cell.2013.05.038;
RA Kumagai A., Ando R., Miyatake H., Greimel P., Kobayashi T., Hirabayashi Y.,
RA Shimogori T., Miyawaki A.;
RT "A bilirubin-inducible fluorescent protein from eel muscle.";
RL Cell 153:1602-1611(2013).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RA Hayashi S., Toda Y.;
RT "A novel fluorescent protein purified from eel muscle.";
RL Fish. Sci. 75:1461-1469(2009).
CC -!- FUNCTION: Beta-barrel protein that binds unconjugated bilirubin with
CC high affinity. Excitation of the bilirubin-bound protein gives rise to
CC green fluorescence, both under normoxia and hypoxia. The apoprotein is
CC not fluorescent. Does not emit fluorescence in the presence of ditauro-
CC bilirubin, urobilin or biliverdin. {ECO:0000269|PubMed:23768684}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=498 nm {ECO:0000269|PubMed:23768684, ECO:0000269|Ref.2};
CC Note=Excitation of the bilirubin-bound protein gives rise to green
CC fluorescence, with maximal fluorecence emission at 527 nm.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in small-diameter muscle fibers from the
CC white muscle layer from juvenile animals (glass eels) (at protein
CC level). Detected in small-diameter muscle fibers from juvenile animals
CC (glass eels). {ECO:0000269|PubMed:23768684, ECO:0000269|Ref.2}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates bilirubin in
CC its interior. {ECO:0000269|PubMed:23768684}.
CC -!- BIOTECHNOLOGY: Becomes fluorescent upon binding free, unconjugated
CC bilirubin, a heme metabolite. Can be used as diagnostic tool to detect
CC abnormally high levels of free bilirubin, which are indicative of
CC impaired liver function. Could also be used in research as fluorescent
CC marker in eukaryotic cells and animals. {ECO:0000269|PubMed:23768684}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; AB763906; BAN57322.1; -; mRNA.
DR PDB; 4I3B; X-ray; 1.20 A; A/B/C/D/E/F=1-139.
DR PDB; 4I3C; X-ray; 2.00 A; A/B=1-139.
DR PDB; 4I3D; X-ray; 2.30 A; A/B/C/D=1-139.
DR PDBsum; 4I3B; -.
DR PDBsum; 4I3C; -.
DR PDBsum; 4I3D; -.
DR AlphaFoldDB; P0DM59; -.
DR SMR; P0DM59; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Luminescence;
KW Photoprotein.
FT CHAIN 1..139
FT /note="Bilirubin-inducible fluorescent protein UnaG"
FT /id="PRO_0000423436"
FT BINDING 57
FT /ligand="bilirubin IXalpha"
FT /ligand_id="ChEBI:CHEBI:57977"
FT BINDING 61
FT /ligand="bilirubin IXalpha"
FT /ligand_id="ChEBI:CHEBI:57977"
FT BINDING 80
FT /ligand="bilirubin IXalpha"
FT /ligand_id="ChEBI:CHEBI:57977"
FT BINDING 112
FT /ligand="bilirubin IXalpha"
FT /ligand_id="ChEBI:CHEBI:57977"
FT BINDING 132..134
FT /ligand="bilirubin IXalpha"
FT /ligand_id="ChEBI:CHEBI:57977"
FT MUTAGEN 57
FT /note="N->A: Abolishes fluorescence emission."
FT /evidence="ECO:0000269|PubMed:23768684"
FT MUTAGEN 57
FT /note="N->Q: Reduces fluorescence emission."
FT /evidence="ECO:0000269|PubMed:23768684"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:4I3B"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:4I3B"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4I3B"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:4I3B"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:4I3B"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:4I3B"
SQ SEQUENCE 139 AA; 15581 MW; 1F6C6410DFE25009 CRC64;
MVEKFVGTWK IADSHNFGEY LKAIGAPKEL SDGGDATTPT LYISQKDGDK MTVKIENGPP
TFLDTQVKFK LGEEFDEFPS DRRKGVKSVV NLVGEKLVYV QKWDGKETTY VREIKDGKLV
VTLTMGDVVA VRSYRRATE
