NGB_DANRE
ID NGB_DANRE Reviewed; 159 AA.
AC Q90YJ2; B0R176;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Neuroglobin;
GN Name=ngb; ORFNames=si:ch211-233n24.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
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 [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=15140880; DOI=10.1074/jbc.m402011200;
RA Fuchs C., Heib V., Kiger L., Haberkamp M., Roesner A., Schmidt M.,
RA Hamdane D., Marden M.C., Hankeln T., Burmester T.;
RT "Zebrafish reveals different and conserved features of vertebrate
RT neuroglobin gene structure, expression pattern, and ligand binding.";
RL J. Biol. Chem. 279:24116-24122(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY HYPOXIA.
RX PubMed=16709914; DOI=10.1242/jeb.02243;
RA Roesner A., Hankeln T., Burmester T.;
RT "Hypoxia induces a complex response of globin expression in zebrafish
RT (Danio rerio).";
RL J. Exp. Biol. 209:2129-2137(2006).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18416560; DOI=10.1021/bi800286m;
RA Watanabe S., Wakasugi K.;
RT "Zebrafish neuroglobin is a cell-membrane-penetrating globin.";
RL Biochemistry 47:5266-5270(2008).
RN [7]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-3; LYS-7; LYS-9; ARG-13;
RP LYS-21 AND LYS-23.
RX PubMed=20417633; DOI=10.1016/j.febslet.2010.04.054;
RA Watanabe S., Wakasugi K.;
RT "Identification of residues critical for the cell-membrane-penetrating
RT activity of zebrafish neuroglobin.";
RL FEBS Lett. 584:2467-2472(2010).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=21614507; DOI=10.1007/s00360-011-0588-9;
RA Tiedke J., Gerlach F., Mitz S.A., Hankeln T., Burmester T.;
RT "Ontogeny of globin expression in zebrafish (Danio rerio).";
RL J. Comp. Physiol. B 181:1011-1021(2011).
CC -!- FUNCTION: Involved in oxygen transport in the brain (By similarity).
CC Hexacoordinate globin, displaying competitive binding of oxygen or the
CC distal His residue to the iron atom. Capable of penetrating cell
CC membranes. {ECO:0000250, ECO:0000269|PubMed:15140880,
CC ECO:0000269|PubMed:18416560}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:15140880}.
CC Cytoplasm {ECO:0000305}. Note=Located in the soma (perikaryon) of most
CC nerve cells in brain. Has ability to penetrate cell membranes and
CC translocate into cells. {ECO:0000269|PubMed:15140880,
CC ECO:0000269|PubMed:18416560, ECO:0000269|PubMed:20417633}.
CC -!- TISSUE SPECIFICITY: Detected in brain, eye and gill, but not in muscle
CC and blood (at protein level). Particularly high expression in the
CC periventral zone of tectum opticum, with significant expression
CC detected in white matter, preglomerular nucleus, posterior tubular
CC nucleus, torus longitudinalis, hypothalamus, pituitary gland, posterior
CC tuberculum, hypothalamus, synencephalon and formatio reticularis.
CC Detected also in brain regions of the visual system, predominantly in
CC parts of tectum opticum and torus semicircularis, area dorsalis
CC telencephali and medulla oblongata. Strong expression observed in
CC sensory epithelium of peripheral olfactory organ, and outer and inner
CC nuclear layers and ganglion cell layer of retina.
CC {ECO:0000269|PubMed:15140880, ECO:0000269|PubMed:16709914}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels during the early stages of
CC development, with levels increasing strongly around hatching period at
CC 72 hours post-fertilization. Expression levels remain high in the adult
CC stage. {ECO:0000269|PubMed:21614507}.
CC -!- INDUCTION: By hypoxia. Expression is significantly up-regulated by
CC severe hypoxia in brain but not in eye. {ECO:0000269|PubMed:16709914}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; AJ315610; CAC59947.1; -; mRNA.
DR EMBL; AL953899; CAQ15066.1; -; Genomic_DNA.
DR EMBL; BC059416; AAH59416.1; -; mRNA.
DR RefSeq; NP_571928.1; NM_131853.1.
DR AlphaFoldDB; Q90YJ2; -.
DR SMR; Q90YJ2; -.
DR STRING; 7955.ENSDARP00000069992; -.
DR PaxDb; Q90YJ2; -.
DR Ensembl; ENSDART00000075510; ENSDARP00000069992; ENSDARG00000053475.
DR Ensembl; ENSDART00000165850; ENSDARP00000137134; ENSDARG00000053475.
DR Ensembl; ENSDART00000183612; ENSDARP00000150652; ENSDARG00000116651.
DR GeneID; 100000711; -.
DR KEGG; dre:100000711; -.
DR CTD; 58157; -.
DR ZFIN; ZDB-GENE-011102-1; ngb.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00510000048375; -.
DR HOGENOM; CLU_003827_13_5_1; -.
DR InParanoid; Q90YJ2; -.
DR OMA; DEMKEAW; -.
DR OrthoDB; 1529889at2759; -.
DR PhylomeDB; Q90YJ2; -.
DR TreeFam; TF333247; -.
DR Reactome; R-DRE-8981607; Intracellular oxygen transport.
DR PRO; PR:Q90YJ2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000053475; Expressed in brain and 4 other tissues.
DR ExpressionAtlas; Q90YJ2; baseline.
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; IDA:ZFIN.
DR GO; GO:0019825; F:oxygen binding; IDA:ZFIN.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0015671; P:oxygen transport; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IDA:ZFIN.
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 1: Evidence at protein level;
KW Cytoplasm; Heme; Iron; Metal-binding; Oxygen transport; Reference proteome;
KW Transport.
FT CHAIN 1..159
FT /note="Neuroglobin"
FT /id="PRO_0000053398"
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 SITE 9
FT /note="Essential for protein transduction into cells"
FT SITE 21
FT /note="Essential for protein transduction into cells"
FT SITE 23
FT /note="Essential for protein transduction into cells"
FT MUTAGEN 3
FT /note="K->A: Minor effect in protein transduction
FT efficiency."
FT /evidence="ECO:0000269|PubMed:20417633"
FT MUTAGEN 7
FT /note="K->A: Reduced protein transduction efficiency. Loss
FT of transduction ability; when associated with Q-9."
FT /evidence="ECO:0000269|PubMed:20417633"
FT MUTAGEN 9
FT /note="K->Q: Reduced protein transduction efficiency. Loss
FT of transduction ability; when associated with A-7."
FT /evidence="ECO:0000269|PubMed:20417633"
FT MUTAGEN 13
FT /note="R->A: Minor effect in protein transduction
FT efficiency."
FT /evidence="ECO:0000269|PubMed:20417633"
FT MUTAGEN 21
FT /note="K->Q: Reduced protein transduction efficiency. Loss
FT of transduction ability; when associated with Q-23."
FT /evidence="ECO:0000269|PubMed:20417633"
FT MUTAGEN 23
FT /note="K->Q: Reduced protein transduction efficiency. Loss
FT of transduction ability; when associated with Q-21."
FT /evidence="ECO:0000269|PubMed:20417633"
SQ SEQUENCE 159 AA; 17684 MW; 6408F865A66D6D37 CRC64;
MEKLSEKDKG LIRDSWESLG KNKVPHGIVL FTRLFELDPA LLTLFSYSTN CGDAPECLSS
PEFLEHVTKV MLVIDAAVSH LDDLHTLEDF LLNLGRKHQA VGVNTQSFAL VGESLLYMLQ
SSLGPAYTTS LRQAWLTMYS IVVSAMTRGW AKNGEHKSN
