NGB_TETNG
ID NGB_TETNG Reviewed; 159 AA.
AC Q90W04; Q4RLY5;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Neuroglobin;
GN Name=ngb; ORFNames=GSTENG00032294001;
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=11554744; DOI=10.1006/bbrc.2001.5614;
RA Awenius C., Hankeln T., Burmester T.;
RT "Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon
RT nigroviridis.";
RL Biochem. Biophys. Res. Commun. 287:418-421(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
CC -!- FUNCTION: Involved in oxygen transport in the brain. Hexacoordinate
CC globin, displaying competitive binding of oxygen or the distal His
CC residue to the iron atom. Capable of penetrating cell membranes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Located in the soma (perikaryon) of most nerve
CC cells in brain. Has ability to penetrate cell membranes and translocate
CC into cells (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG10597.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ315609; CAC59975.1; -; mRNA.
DR EMBL; AJ315608; CAC59974.1; -; Genomic_DNA.
DR EMBL; CAAE01015019; CAG10597.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q90W04; -.
DR SMR; Q90W04; -.
DR STRING; 99883.ENSTNIP00000020525; -.
DR Ensembl; ENSTNIT00000020757; ENSTNIP00000020525; ENSTNIG00000017387.
DR KEGG; tng:GSTEN00032294G001; -.
DR GeneTree; ENSGT00510000048375; -.
DR HOGENOM; CLU_003827_13_5_1; -.
DR InParanoid; Q90W04; -.
DR OMA; HQAVGVH; -.
DR TreeFam; TF333247; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098809; F:nitrite reductase activity; IEA:Ensembl.
DR GO; GO:0019825; F:oxygen binding; IEA:Ensembl.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR Pfam; PF00042; Globin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Heme; Iron; Metal-binding; Oxygen transport; Reference proteome;
KW Transport.
FT CHAIN 1..159
FT /note="Neuroglobin"
FT /id="PRO_0000053401"
FT REGION 2..151
FT /note="Globin"
FT BINDING 66
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 98
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT SITE 7
FT /note="Essential for protein transduction into cells"
FT /evidence="ECO:0000250"
FT SITE 9
FT /note="Essential for protein transduction into cells"
FT /evidence="ECO:0000250"
FT SITE 21
FT /note="Essential for protein transduction into cells"
FT /evidence="ECO:0000250"
FT SITE 23
FT /note="Essential for protein transduction into cells"
FT /evidence="ECO:0000250"
SQ SEQUENCE 159 AA; 17761 MW; 1C9386169E13484B CRC64;
MEKLSSKDKE LIRGSWDSLG KNKVPHGVIL FSRLFELDPE LLNLFHYTTN CGSTQDCLSS
PEFLEHVTKV MLVIDAAVSH LDDLHSLEDF LLNLGRKHQA VGVKPQSFAM VGESLLYMLQ
CSLGQAYTAS LRQAWLNMYS VVVASMSRGW AKNGEDKAD
